|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
35-326 |
0e+00 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 637.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19159 32 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd19159 112 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 274
Cdd:cd19159 192 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 326
Cdd:cd19159 272 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
35-314 |
0e+00 |
|
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381367 [Multi-domain] Cd Length: 310 Bit Score: 597.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19141 31 VAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd19141 111 QLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 274
Cdd:cd19141 191 QLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 314
Cdd:cd19141 271 IAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
35-326 |
0e+00 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 565.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19160 34 TAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd19160 114 QLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 274
Cdd:cd19160 194 QLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLA 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 326
Cdd:cd19160 274 IAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
36-322 |
0e+00 |
|
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.
Pssm-ID: 213602 [Multi-domain] Cd Length: 317 Bit Score: 536.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQ 115
Cdd:TIGR01293 31 AEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQ 195
Cdd:TIGR01293 111 LEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 275
Cdd:TIGR01293 191 LPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAI 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767927486 276 AWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 322
Cdd:TIGR01293 271 AWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
35-327 |
0e+00 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 530.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19158 32 MAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd19158 112 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 274
Cdd:cd19158 192 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPY 327
Cdd:cd19158 272 IAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
36-321 |
3.26e-165 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 462.84 E-value: 3.26e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAE--TERGLSRKHIIEGLKGSLQR 113
Cdd:cd19143 33 AKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPppNDRGLSRKHIVEGTKASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVE 193
Cdd:cd19143 113 LQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERiVSEEGRKQQNKLKDLSPIAERLGCTLPQL 273
Cdd:cd19143 193 VEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKDR-KEELGQEKIEKVRKLKPIAEELGCSLAQL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 321
Cdd:cd19143 272 AIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
35-326 |
2.06e-144 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 410.32 E-value: 2.06e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAEtERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19142 32 QAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKIYWSYGSE-ERGLSRKHIIESVRASLRRL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd19142 111 QLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMEL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLP 271
Cdd:cd19142 191 YMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLT 270
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 767927486 272 QLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 326
Cdd:cd19142 271 QLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
35-304 |
9.37e-141 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 400.04 E-value: 9.37e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKAE-TERGLSRKHIIEGLKGSLQR 113
Cdd:cd19074 23 DAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGPGpNDRGLSRKHIFESIHASLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVE 193
Cdd:cd19074 101 LQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 vQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 273
Cdd:cd19074 181 -EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQL 258
|
250 260 270
....*....|....*....|....*....|.
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 304
Cdd:cd19074 259 ALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
36-326 |
3.63e-87 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 264.73 E-value: 3.63e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:COG0667 35 AIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEV 194
Cdd:COG0667 113 GTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcyqWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQ 272
Cdd:COG0667 190 ELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT----NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQ 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 326
Cdd:COG0667 263 LALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
36-321 |
1.99e-77 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 239.40 E-value: 1.99e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19087 32 SFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATKVFGPmGDDPNDRGLSRRHIRRAVEASLRRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEV 194
Cdd:cd19087 109 QTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwlkERIVSEEGRKQqnkLKDLSPIAERLGCTLPQ 272
Cdd:cd19087 188 EILPAARAYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPAS 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 321
Cdd:cd19087 262 LALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
36-306 |
9.46e-72 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 225.18 E-value: 9.46e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19091 41 ADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEV 194
Cdd:cd19091 118 GTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQ 272
Cdd:cd19091 197 ELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQ 271
|
250 260 270
....*....|....*....|....*....|....
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19091 272 VALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
43-319 |
2.48e-68 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 215.85 E-value: 2.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 120
Cdd:cd19084 34 AIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 121 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAysvarqFNMIPPVCEQAEYHLFQREKVEVQLPeLY 200
Cdd:cd19084 111 LYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLP-YC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 201 HKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAW 277
Cdd:cd19084 184 RENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAW 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767927486 278 CLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 319
Cdd:cd19084 257 TLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
36-302 |
2.02e-67 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 211.22 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd06660 19 AFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSRSRLSPEHIRRDLEESLRRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 194
Cdd:cd06660 98 GTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgctLPQLA 274
Cdd:cd06660 178 ELLDWAEENGLPLLAYSPLARG-----------------------------------------------------PAQLA 204
|
250 260
....*....|....*....|....*...
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLG 302
Cdd:cd06660 205 LAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
33-308 |
8.99e-67 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 212.12 E-value: 8.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 33 FLVAERLMTIAYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVITTKL-Y--WGGKaeTERGLSRKHIIEG 106
Cdd:cd19089 28 PEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVISTKAgYgmWPGP--YGDGGSRKYLLAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 107 LKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHL 186
Cdd:cd19089 106 LDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 FQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERL 266
Cdd:cd19089 185 LDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKR 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767927486 267 GCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 308
Cdd:cd19089 260 GQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
45-319 |
1.72e-64 |
|
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).
Pssm-ID: 381307 [Multi-domain] Cd Length: 308 Bit Score: 206.30 E-value: 1.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 45 ESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLE 117
Cdd:cd19081 37 DAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVVIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLP 197
Cdd:cd19081 115 YIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 198 ELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqwlKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAV 275
Cdd:cd19081 195 PLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA-----AKRYLNERGLRI---LDALDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767927486 276 AWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 319
Cdd:cd19081 267 AWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
36-306 |
5.16e-63 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 202.43 E-value: 5.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19079 37 SRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEV 194
Cdd:cd19079 116 GTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-ER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKCYQWLKErivSEEGRKQQNKLKDlspIAERLGCTLPQL 273
Cdd:cd19079 195 EMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKYDYF---TEADKEIVDRVEE---VAKERGVSMAQV 268
|
250 260 270
....*....|....*....|....*....|...
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19079 269 ALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
39-305 |
1.73e-59 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 193.39 E-value: 1.73e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 39 LMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSLVITTKL--------Y--WGgkaeterglSRKHII 104
Cdd:cd19151 35 MLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELIISTKAgytmwpgpYgdWG---------SKKYLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 105 EGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEY 184
Cdd:cd19151 105 ASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 185 HLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAE 264
Cdd:cd19151 184 SMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQ 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767927486 265 RLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 305
Cdd:cd19151 259 ARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
36-322 |
1.97e-59 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 192.53 E-value: 1.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSRKHIIEGLKGSLQRLQ 115
Cdd:pfam00248 20 ALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWPSGGSKENIRKSLEESLKRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqREKVEVQ 195
Cdd:pfam00248 99 TDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQNKLKDLSPIAERLGCTLPQL 273
Cdd:pfam00248 174 LLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNLEALEALEEIAKEHGVSPAQV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 322
Cdd:pfam00248 244 ALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
36-321 |
9.28e-59 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 192.01 E-value: 9.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHI 103
Cdd:cd19094 20 AHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvagpgEGITWPRGGGTRLDRENI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 104 IEGLKGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 165
Cdd:cd19094 99 REAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVKAGKIRHIGLSNETPWGVMKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 166 YSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLkcYQWLKER 243
Cdd:cd19094 179 LELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldGAARPEGGRLNL--FPGYMAR 255
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927486 244 IVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV-LPKmtsHVVNEIDNI 321
Cdd:cd19094 256 YRSPQALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVpLSD---ELLAEIDAV 328
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
43-307 |
7.48e-57 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 186.51 E-value: 7.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQL 116
Cdd:cd19150 39 AFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELIISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 196
Cdd:cd19150 117 DYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 197 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyqwlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLA 274
Cdd:cd19150 196 LDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS-------KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMA 268
|
250 260 270
....*....|....*....|....*....|...
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 307
Cdd:cd19150 269 LAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
39-307 |
1.13e-52 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 177.10 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 39 LMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAETerGLSRKHIIEGLKGSLQ 112
Cdd:PRK09912 48 ILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 113 RLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKV 192
Cdd:PRK09912 126 RMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 193 EVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--KCYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTL 270
Cdd:PRK09912 205 KSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegNKVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSM 281
|
250 260 270
....*....|....*....|....*....|....*..
gi 767927486 271 PQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 307
Cdd:PRK09912 282 AQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
36-306 |
8.71e-52 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 173.56 E-value: 8.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG--GKAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19080 33 ARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLATKYTMNrrPGDPNAGGNHRKNLRRSVEASLRR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVE 193
Cdd:cd19080 110 LQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPELYHKIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQL 273
Cdd:cd19080 189 RELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGFGKLTERNWAIVDVVAA---VAEELGRSAAQV 263
|
250 260 270
....*....|....*....|....*....|...
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19080 264 ALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
43-324 |
5.40e-50 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 168.15 E-value: 5.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19085 32 ALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS-------PDNLTPEDVRKSCERSLKRLGTDYIDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmipPVCEQAEYHLFQREKVEVQLPEL-YH 201
Cdd:cd19085 102 QIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCrEH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 202 KIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVA 276
Cdd:cd19085 176 GIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFEPGaeEETFEALEKLKEIADELGVTMAQLALA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767927486 277 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 324
Cdd:cd19085 246 WVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
38-321 |
2.20e-42 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 148.72 E-value: 2.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 38 RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19083 37 DLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVVIATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQ 195
Cdd:cd19083 114 TDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDI 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPELyHKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQWLKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQL 273
Cdd:cd19083 188 LPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDLRNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHL 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 321
Cdd:cd19083 261 ALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-322 |
9.36e-42 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 147.05 E-value: 9.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 120
Cdd:cd19102 35 ALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 121 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImeaysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPel 199
Cdd:cd19102 112 LYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM-------KRCQAIHPIASlQPPYSLLRRGIEAEILP-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 200 Y---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK-ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLA 274
Cdd:cd19102 183 FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767927486 275 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 322
Cdd:cd19102 257 IAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
42-303 |
9.97e-42 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 146.60 E-value: 9.97e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 42 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLywggkAETERGLSRKHIIEGLKGSLQRLQLEYVDV 121
Cdd:cd19093 34 AALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-----APLPWRLTRRSVVKALKASLERLGLDSIDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 122 VFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELY 200
Cdd:cd19093 108 YQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQNGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 201 HKIGVGAMTWSPLACGIISGKYG--NGVPESSRASLKCYQWLKERIVseegrkqqnkLKDLSPIAERLGCTLPQLAVAWC 278
Cdd:cd19093 187 DELGITLIAYSPLAQGLLTGKYSpeNPPPGGRRRLFGRKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWL 256
|
250 260
....*....|....*....|....*
gi 767927486 279 LRNEGVssVLLGSSTPEQLIENLGA 303
Cdd:cd19093 257 IAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
38-322 |
1.08e-41 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 146.99 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 38 RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW----GGKAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19078 29 ELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFkidgGKPGPLGLDSRPEHIRKAVEGSLKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVE 193
Cdd:cd19078 106 LQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC------PVTAVQSEYSMMWREPEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPELyHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYqwlkerivSEEGRKQQNKLKDL-SPIAERLGCT 269
Cdd:cd19078 180 EVLPTL-EELGIGFVPFSPLGKGFLTGKIDENtkfDEGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGAT 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767927486 270 LPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 322
Cdd:cd19078 251 PAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDAL 301
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
35-306 |
1.61e-40 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 144.34 E-value: 1.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETE----------RGLSRKH 102
Cdd:cd19149 34 ESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVLATKcgLRWDREGGSFffvrdgvtvyKNLSPES 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 103 IIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaYSVARQFNMIppvceQA 182
Cdd:cd19149 111 IREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKE-YVKAGQLDII-----QE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 183 EYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivsEEGRKQQNKLKD- 258
Cdd:cd19149 185 KYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefDAGDARSGIPWFS--------PENREKVLALLEk 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 767927486 259 LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19149 256 WKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
43-318 |
5.21e-40 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 142.35 E-value: 5.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLE 117
Cdd:cd19076 41 ALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP 197
Cdd:cd19076 116 VIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 198 ---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRASLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 274
Cdd:cd19076 190 tcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPEDD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767927486 275 VAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 318
Cdd:cd19076 262 LAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
36-303 |
1.32e-38 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 136.84 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YWGGKAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19086 26 AIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRFDGGPERPQDFSPEYIREAVEASLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIMEAYSVArqfnmippvCEQAEYHLFQR 189
Cdd:cd19086 103 LGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALRRGGID---------VVQVIYNLLDQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 190 EKVEVQLPELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgct 269
Cdd:cd19086 174 RPEEELFPLA-EEHGVGVIARVPLASGLLTGK------------------------------------------------ 204
|
250 260 270
....*....|....*....|....*....|....
gi 767927486 270 LPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19086 205 LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
43-305 |
1.80e-38 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 137.36 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19072 35 AIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS-------PDHLKYDDVIKAAKESLKRLGTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHK 202
Cdd:cd19072 106 LIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 203 IGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivseegrkqqnkLKDLSPIAERLGCTLPQLAVAWCLRNE 282
Cdd:cd19072 182 NGIAIIAYSPLEKGKLSNAKG--------------------------------SPLLDEIAKKYGKTPAQIALNWLISKP 229
|
250 260
....*....|....*....|...
gi 767927486 283 GVsSVLLGSSTPEQLIENLGAIQ 305
Cdd:cd19072 230 NV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-303 |
5.47e-38 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 136.91 E-value: 5.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-----KAETERgLSRKHIIEG 106
Cdd:cd19082 19 AFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhpdleDMSRSR-LSPEDIRAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 107 LKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHL 186
Cdd:cd19082 94 LEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 FqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLKCYQwlkerivSEEGRKQQN 254
Cdd:cd19082 174 A--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRRVYY-------SEENFERLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767927486 255 KLKDLspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19082 244 RAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
36-321 |
2.61e-37 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 135.38 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterGLSRKHIIEGLKGSLQRL 114
Cdd:cd19075 22 AAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----GLSPENVRKQLETSLKRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEV 194
Cdd:cd19075 93 KVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITR-QVET 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEegrkqqnkLKDLSPIAER 265
Cdd:cd19075 172 ELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA--------LEKVEEAAEK 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927486 266 LGCTLPQLAVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 321
Cdd:cd19075 244 EGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-303 |
4.29e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 121.28 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHI 103
Cdd:cd19752 19 SFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgagpRDPDGGPESPEGLSAETI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 104 IEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAE 183
Cdd:cd19752 98 EQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 184 YHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRASLKCYqwlkerivseEGRKQ 252
Cdd:cd19752 178 HSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPLPEQY----------DGPDS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767927486 253 QNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19752 239 DARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
45-319 |
2.72e-31 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 118.51 E-value: 2.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 45 ESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFA 124
Cdd:cd19138 40 DLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL-------PSNASRQGTVRACERSLRRLGTDYLDLYLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 125 NRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMippVCEQAEYHLFQReKVEVQLPELYHKIG 204
Cdd:cd19138 110 HWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC---AANQVLYNLGSR-GIEYDLLPWCREHG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 205 VGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGV 284
Cdd:cd19138 185 VPVMAYSPLAQG---GLLRRGLLENP---------------------------TLKEIAARHGATPAQVALAWVLRDGNV 234
|
250 260 270
....*....|....*....|....*....|....*
gi 767927486 285 SSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 319
Cdd:cd19138 235 IAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
36-303 |
3.42e-30 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 115.02 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19095 22 AARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-GRDRKDFSPAAIRASIERSLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqFNMIppvceQAEYHLFQREKVE 193
Cdd:cd19095 97 LGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-FDVV-----QLPYNVLDREEEE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VqLPELY-HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrkqqnklkdLSPIAERLGCTLPQ 272
Cdd:cd19095 170 L-LPLAAeAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR---------------PEFAAEIGGATWAQ 222
|
250 260 270
....*....|....*....|....*....|.
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19095 223 AALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
41-297 |
5.96e-30 |
|
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381374 [Multi-domain] Cd Length: 302 Bit Score: 115.87 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 41 TI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQL 116
Cdd:cd19148 30 TIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLEWDEGGEVVRNSSPARIRKEVEDSLRRLQT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIMEAY-SVARQFNMIPPvceqaeYHLFQREKVEVQ 195
Cdd:cd19148 109 DYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQMETFrKVAPLHTVQPP------YNLFEREIEKDV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LP-ELYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKCYQwlkerivseEGRKQQ-----NKLKDLSpiA 263
Cdd:cd19148 182 LPyARKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPKFQ---------EPRFSQylaavEELDKLA--Q 245
|
250 260 270
....*....|....*....|....*....|....
gi 767927486 264 ERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 297
Cdd:cd19148 246 ERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
36-311 |
1.47e-29 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 114.19 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKG 109
Cdd:cd19092 26 LLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRLGDDPRPGRIKhydTSKEHILASVEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 110 SLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNM------IPPVCEQAE 183
Cdd:cd19092 106 SLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS----------QIELlqsyldQPLVTNQIE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 184 YHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessraslkcyqwlkeRIVSEEGRKQQNKLKDL 259
Cdd:cd19092 176 LSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGG--------------------------RLFGGFDERFQRLRAAL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767927486 260 SPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 311
Cdd:cd19092 226 EELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
39-306 |
1.51e-29 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 113.82 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 39 LMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEY 118
Cdd:cd19137 31 LLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW-------PTNLRYDDLLRSLQNSLRRLDTDY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmiPPVCEQAEYHLFQREKVEVQLPE 198
Cdd:cd19137 102 IDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT----PIVCNQVKYNLEDRDPERDGLLE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 199 LYHKIGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWC 278
Cdd:cd19137 178 YCQKNGITVVAYSPLRRGLE---------------------KTNRTLEE--------------IAKNYGKTIAQIALAWL 222
|
250 260
....*....|....*....|....*...
gi 767927486 279 LRNEGVSSVLLgSSTPEQLIENLGAIQV 306
Cdd:cd19137 223 IQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
36-303 |
6.27e-29 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 112.07 E-value: 6.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQ 115
Cdd:COG0656 20 AAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDNH------GYDDTLAAFEESLERLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREkvevq 195
Cdd:COG0656 90 LDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 lPEL--YHK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQ 272
Cdd:COG0656 160 -RELlaFCReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE--------------IAEKHGKTPAQ 203
|
250 260 270
....*....|....*....|....*....|.
gi 767927486 273 LAVAWCLRNeGVsSVLLGSSTPEQLIENLGA 303
Cdd:COG0656 204 VVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
43-323 |
3.38e-28 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 111.87 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLywGGKAET-------ERGLSRKHIIEGLK 108
Cdd:PRK10625 39 AVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SREKLIIASKV--SGPSRNndkgirpNQALDRKNIREALH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 109 GSLQRLQLEYVD---VVFANRP-----------DSNTP---MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 171
Cdd:PRK10625 116 DSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavsLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 172 FNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGR 250
Cdd:PRK10625 196 HDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGE 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767927486 251 KQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILR 323
Cdd:PRK10625 269 QTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-304 |
2.15e-27 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 107.67 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19105 34 ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 F---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME--IMEA-----YSVArqfnMIPpvceqaeY-HLFQREK 191
Cdd:cd19105 107 QlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNMAevLQAAiesgwFDVI----MVA-------YnFLNQPAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 192 VEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessraslkcyqwlkerivSEEGRKQQNKLKDLSpiaerlgctL 270
Cdd:cd19105 176 LEEALAAAAeKGIGVVAMK--TLAGGY----------------------------LQPALLSVLKAKGFS---------L 216
|
250 260 270
....*....|....*....|....*....|....
gi 767927486 271 PQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 304
Cdd:cd19105 217 PQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
40-319 |
3.15e-27 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 108.48 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 40 MTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITTKlywGGKAET--ERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19077 31 MKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSVK---GGLDPDtlRPDGSPEAVRKSIENILRAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 -QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVE 193
Cdd:cd19077 108 gGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREIEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 273
Cdd:cd19077 182 NGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL----DRFNGENFEKNLKLVDALQELAEKKGCTPAQL 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767927486 274 AVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 319
Cdd:cd19077 258 ALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
43-305 |
3.92e-27 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 107.64 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19090 29 ALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV--GRLPEDTADYSADRVRRSVEESLERLGRDRIDLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQFNMIPPVCeqaEYHLFQREKVEVQLP 197
Cdd:cd19090 103 MIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGDFDVVLTAN---RYTLLDQSAADELLP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 198 ELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrkQQNKLKDLSPIAERLGCTLPQLAVAW 277
Cdd:cd19090 179 AAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE--------LLDRAKRLYELCDEHGVPLPALALRF 242
|
250 260
....*....|....*....|....*...
gi 767927486 278 CLRNEGVSSVLLGSSTPEQLIENLGAIQ 305
Cdd:cd19090 243 LLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
38-326 |
8.69e-27 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 107.53 E-value: 8.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 38 RLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQ 112
Cdd:cd19144 38 AVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATK--FGIEKNVETGEysvdgSPEYVKKACETSLK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 113 RLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QRE 190
Cdd:cd19144 114 RLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVH------PIAAVQIEYSPFslDIE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 191 KVEVQLPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRASLKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGC 268
Cdd:cd19144 188 RPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDDFEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNV 261
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 767927486 269 TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 326
Cdd:cd19144 262 TAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEEEKEIREIAEEAE 317
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
36-311 |
1.35e-26 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 106.77 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKG 109
Cdd:COG4989 33 AAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcgiRLPSEARDNRVKhydTSKEHIIASVEG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 110 SLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNMI------PPVCEQAE 183
Cdd:COG4989 113 SLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPS----------QFELLqsaldqPLVTNQIE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 184 YHLFQREKVE------VQLpelyHKIGVgaMTWSPLACGIISGKYgngvpessraslkcyqwlkerivSEEGRKQQNKLK 257
Cdd:COG4989 183 LSLLHTDAFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF-----------------------DEQFPRLRAALD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767927486 258 DlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 311
Cdd:COG4989 234 E---LAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDI--ELT 282
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
43-318 |
2.22e-26 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 106.36 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYV 119
Cdd:cd19145 42 AFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLATKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 120 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPEL 199
Cdd:cd19145 119 DLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 200 YHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQWLKeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 279
Cdd:cd19145 192 CRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSHP-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVL 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767927486 280 -RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 318
Cdd:cd19145 268 hQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
36-303 |
7.93e-26 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 103.45 E-value: 7.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW--GGKAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19088 26 AIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvrTGPGWWGPDGSPEYLRQAVEASLRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIppVCEQAEYHLFQREKVE 193
Cdd:cd19088 103 LGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----I--VSVQNRYNLANRDDEG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQlpELYHKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQL 273
Cdd:cd19088 177 VL--DYCEAAGIAFIPWFPLG--------GGDLAQPGG--------------------------LLAEVAARLGATPAQV 220
|
250 260 270
....*....|....*....|....*....|
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19088 221 ALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
43-303 |
2.00e-22 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 95.12 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWGGKAETER--GLSRKHIIEGLKGSLQR 113
Cdd:cd19162 28 AWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAGRPAGADRrfDFSADGIRRSIEASLER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeimeAYSVARQFN----MIPpvceqAEYH 185
Cdd:cd19162 106 LGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA-----LLRAARRADvdvvMVA-----GRYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 186 LFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQWLKERIVSeegRKQQnklkdLSPIAER 265
Cdd:cd19162 176 LLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRPATPEVLA---RARR-----LAAVCRR 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 767927486 266 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19162 240 YGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-321 |
3.75e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 95.02 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRSSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19104 41 ALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FA-NRPDSNTP--------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL- 186
Cdd:cd19104 115 QLhNRIGDERDkpvggtlsttdvlgLGGVADAFERLRSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 -----FQREKVEV-----QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnkl 256
Cdd:cd19104 190 npsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA---- 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767927486 257 KDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEIDNI 321
Cdd:cd19104 257 AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
44-322 |
7.15e-22 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 94.03 E-value: 7.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 44 YESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL---YWGGKAETER----GLSRKHIIEGLKGSLQRLQL 116
Cdd:cd19146 45 YEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKYttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKV 192
Cdd:cd19146 124 SYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDIL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 193 EVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLKCYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQ 272
Cdd:cd19146 204 PMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITS 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 322
Cdd:cd19146 268 VALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEIQEIEDAY 315
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
36-301 |
2.94e-20 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 88.31 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19071 16 TAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDHGYERVREALEESLKDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVV-----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF-- 187
Cdd:cd19071 86 LDYLDLYlihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELHPYlq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 188 QREKVEvqlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseegrkqqnklKDLSPIAERL 266
Cdd:cd19071 162 QKELVE------FcKEHGIVVQAYSPLGRG-------------RRPLLDD--------------------PVLKEIAKKY 202
|
250 260 270
....*....|....*....|....*....|....*
gi 767927486 267 GCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 301
Cdd:cd19071 203 GKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-309 |
6.78e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 87.58 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19097 28 AKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL---PPLKEDKKEDEAAIEASVEASLKRLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSvARQFNMIppvceQAEYHLF-QREKVE 193
Cdd:cd19097 99 VDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFKIDII-----QLPFNILdQRFLKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPELyHKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCYQWlkerivseegrkqQNKLKDLSPIAERLGCTLPQL 273
Cdd:cd19097 173 GLLAKL-KKKGIEIHARSVFLQGLL-------LMEPDKLPAKFAPA-------------KPLLKKLHELAKKLGLSPLEL 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 767927486 274 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK 309
Cdd:cd19097 232 ALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
38-303 |
1.14e-19 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 86.56 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 38 RLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQLE 117
Cdd:cd19073 18 NAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------LRPEDLKKSVDRSLEKLGTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVEVQ 195
Cdd:cd19073 88 YVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHpfLYQAELLEYC 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPelyHKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnklkdlspIAERLGCTLPQLAV 275
Cdd:cd19073 164 RE---NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------------IAEKYDKTPAQVAL 203
|
250 260
....*....|....*....|....*...
gi 767927486 276 AWCLRnEGVsSVLLGSSTPEQLIENLGA 303
Cdd:cd19073 204 RWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
36-301 |
1.45e-18 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 83.46 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19140 23 CTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-------YSPDDFLASVEESLRKLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQRekve 193
Cdd:cd19140 93 TDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHpyLDQR---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 vQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQL 273
Cdd:cd19140 165 -KLLDAAREHGIALTAYSPLARG---------------------EVLKDPVLQE--------------IGRKHGKTPAQV 208
|
250 260
....*....|....*....|....*...
gi 767927486 274 AVAWCLRNEGVsSVLLGSSTPEQLIENL 301
Cdd:cd19140 209 ALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
36-303 |
2.20e-18 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 82.99 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkaeteRGLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19096 23 AIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW------SVKSAEDFRRILEESLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDvVFA----NRPD------SNTPMEEIVRAMT-----HVinqGMamywgTSRWSA---MEIMEAYsvarQFNMIpp 177
Cdd:cd19096 95 VDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDSPellKEILDSY----DFDFV-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 178 vceQAEYHLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessraslkcyqwlkerivseegrkqqNKL 256
Cdd:cd19096 160 ---QLQYNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA----------------------------------NNP 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767927486 257 KDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19096 203 PEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
36-304 |
5.61e-17 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 79.90 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKL--YwGGKAETERGLSRKHIIEGLKGSLQR 113
Cdd:cd19163 35 AIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYLATKVgrY-GLDPDKMFDFSAERITKSVEESLKR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVV------FAnrPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMeAYSVARQFNMIPPVCEQAEYHLF 187
Cdd:cd19163 112 LGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIGITGYP-LDVL-KEVLERSPVKIDTVLSYCHYTLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 188 QREKVEvqLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASlkcyQWLKERIvseegrkqqnklKDLSPIAERLG 267
Cdd:cd19163 188 DTSLLE--LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPAS----PEIKEAC------------AKAAAYCKSRG 246
|
250 260 270
....*....|....*....|....*....|....*..
gi 767927486 268 CTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 304
Cdd:cd19163 247 VDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
36-301 |
6.19e-17 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 80.63 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKaeterglSRKHIIEGLKGSLQRLQ 115
Cdd:COG1453 31 AEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILATKLPPWVR-------DPEDMRKDLEESLKRLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFanrpdsntpmeeIvramtHVINQGMAMYWGTSRWSAMEIMEAysvARQ----------FNMIPPVCEQA-E- 183
Cdd:COG1453 99 TDYIDLYL------------I-----HGLNTEEDLEKVLKPGGALEALEK---AKAegkirhigfsTHGSLEVIKEAiDt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 184 ----------YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqq 253
Cdd:COG1453 159 gdfdfvqlqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG------------------------------------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767927486 254 nKLKDLSPIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 301
Cdd:COG1453 202 -RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-301 |
5.73e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 77.36 E-value: 5.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywGG----------------KAETE 95
Cdd:cd19099 23 YREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---AGyipgdgdeplrplkylEEKLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 96 RGLSRKHIIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSNTPMEEIVRAMTHVINQGMAMYW 152
Cdd:cd19099 100 RGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFYDRLEEAFEALEEAVAEGKIRYY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 153 GTSRWSAmeiMEAYSVARQFNMIPPVCE---------------QAEYHLFQREKVEVQ---------LPELYHKIGVGAM 208
Cdd:cd19099 180 GISTWDG---FRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEKntvkgealsLLEAAKELGLGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 209 TWSPLAcgiiSGKYGNGVPESSRAslkcyqwlkerivseegrkqqnklkdlspiAERLGCTLPQLAVAWCLRNEGVSSVL 288
Cdd:cd19099 257 ASRPLN----QGQLLGELRLADLL------------------------------ALPGGATLAQRALQFARSTPGVDSAL 302
|
330
....*....|...
gi 767927486 289 LGSSTPEQLIENL 301
Cdd:cd19099 303 VGMRRPEHVDENL 315
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
40-301 |
7.66e-16 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 76.68 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 40 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQR 113
Cdd:cd19154 31 VRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITTKLWTHE-------HAPEDVEEALRESLKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 114 LQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnm 174
Cdd:cd19154 99 LQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 175 IPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCYQWlkerivseegrKQQN 254
Cdd:cd19154 175 VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------GSPGRANFTKSTGVS-----------PAPN 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 767927486 255 KLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 301
Cdd:cd19154 230 LLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
40-327 |
8.01e-16 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 76.12 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 40 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterglsrkHIIEGLKGSLQRLQLEYV 119
Cdd:cd19120 31 VKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK----------DPREALRKSLAKLGVDYV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 120 DVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqrekVEVQ 195
Cdd:cd19120 98 DLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPY----LYPQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRKQQNKLKDlspIAERLGCTLPQL 273
Cdd:cd19120 170 QPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGPLDPVLEK---IAEKYGVTPAQV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767927486 274 AVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 327
Cdd:cd19120 220 LLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
43-279 |
8.29e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.60 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGGkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19103 41 AMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI-----AGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPEL 199
Cdd:cd19103 114 WIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 200 YHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIVSEEGRKQQnkLKDLSP----IAERLGCTLPQL 273
Cdd:cd19103 187 CKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAETYNPLLPQ--LEELTAvmaeIGAKHGASIAQV 253
|
....*.
gi 767927486 274 AVAWCL 279
Cdd:cd19103 254 AIAWAI 259
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-303 |
1.73e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 75.71 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYWGGKAETergLSRKHIIEGLKGSLQ 112
Cdd:cd19101 25 AVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVPDPGELT---MTRAYVEAAIDRSLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 113 RLQLEYVDVV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEIMEAysvarqfnMIPPVCEQAEYHL 186
Cdd:cd19101 100 RLGVDRLDLVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EILDA--------GVPIVSNQVQYSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 FQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCYQwlkeRIVSEEG--RKQQNKLKDL 259
Cdd:cd19101 170 LDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKYK----LMIDEWGgwDLFQELLRTL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767927486 260 SPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 303
Cdd:cd19101 244 KAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
36-307 |
3.37e-15 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 74.88 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQ 115
Cdd:cd19153 35 AVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRDSEFD--YSAERVRASVATSLERLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWsAMEIMEaySVARQFNMIPPVCEQAEYHL-FQREK 191
Cdd:cd19153 113 TTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDAR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 192 VEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPE----------SSRASLKcyqWLKERIVSeegrkqqnklkdlsp 261
Cdd:cd19153 190 LESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgelrhYAAAADA---VCASVEAS--------------- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767927486 262 iaerlgctLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQVL 307
Cdd:cd19153 249 --------LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAV 287
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-306 |
3.98e-15 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 74.57 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETERGLSRKHIIEGLKG------------- 109
Cdd:cd19152 29 AWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQEVEPTFEPGFWNPLPfdavfdysydgil 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 110 -----SLQRLQLEYVDVVFANRPDSNTP-----------MEEIVRAMTHVINQGMAMYW--GTSRWS-AMEIME-----A 165
Cdd:cd19152 107 rsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIglGVNDWEvILRILEeadldW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 166 YSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgIISGKYGNGVpessRASLKCYQWLKERIV 245
Cdd:cd19152 187 VMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VNAGPFNSGF----LAGGDNFDYYEYGPA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927486 246 SEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19152 241 PPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
42-327 |
1.16e-14 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 73.21 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 42 IAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYV 119
Cdd:cd19123 33 QALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE------DVLPALEKTLADLQLDYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 120 D-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 181
Cdd:cd19123 105 DlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 182 AEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQWLKERIVSEegrkqqnklkdlsp 261
Cdd:cd19123 181 VELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPVLLEDPVINK-------------- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927486 262 IAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 327
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
36-301 |
2.04e-14 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 71.84 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQ 115
Cdd:cd19133 25 CERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQDAGYEK------AKKAFERSLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAYSvarqFNMIPPVCEQAEYHLFQRE 190
Cdd:cd19133 95 LDYLDLYLIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLIL----HNEVKPAVNQIETHPFNQQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 191 KVEVqlpELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQ--QNKLkdLSPIAERLGC 268
Cdd:cd19133 164 IEAV---EFLKKYGVQIEAWGPFA---------------------------------EGRNNlfENPV--LTEIAEKYGK 205
|
250 260 270
....*....|....*....|....*....|...
gi 767927486 269 TLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 301
Cdd:cd19133 206 SVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
43-322 |
4.24e-14 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 71.73 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:PLN02587 40 AFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDIL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEV 194
Cdd:PLN02587 117 HCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP-LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 qLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASLKcyqwLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQ 272
Cdd:PLN02587 191 -LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE----LKSacAAAATHCKEK--------------GKNISK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767927486 273 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--MTSHVVNEIDNIL 322
Cdd:PLN02587 248 LALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgIDEELLSEVEAIL 299
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
36-301 |
4.03e-13 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 68.70 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSL 111
Cdd:cd19128 16 SKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQPEN------VKEQLLITL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 112 QRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 172
Cdd:cd19128 86 QDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCK-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 173 nmIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRASLKCyqwlkerivseegrk 251
Cdd:cd19128 164 --IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTFLND--------------- 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767927486 252 qqnklKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 301
Cdd:cd19128 214 -----SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
45-300 |
7.61e-13 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 67.35 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 45 ESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVVFA 124
Cdd:cd19135 37 ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSDYGYES------TKQAFEASLKRLGVDYLDLYLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 125 NRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaysvARQFNMIPPVCEQAEYHLFQREKvevQLP 197
Cdd:cd19135 107 HWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ----LLEDCSVVPHVNQVEFHPFQNPV---ELI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 198 ELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAW 277
Cdd:cd19135 180 EYCRDNNIVFEGYCPLAKG---------------------KALEEPTVTE--------------LAKKYQKTPAQILIRW 224
|
250 260
....*....|....*....|...
gi 767927486 278 CLRNEGVssVLLGSSTPEQLIEN 300
Cdd:cd19135 225 SIQNGVV--TIPKSTKEERIKEN 245
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
43-301 |
1.21e-12 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 66.63 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 122
Cdd:cd19131 32 ALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL------RAFDESLRKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvev 194
Cdd:cd19131 102 LIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-------PVVNQIELHpRFQQR---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 195 QLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLA 274
Cdd:cd19131 168 ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--------------IAEKHGKTPAQVV 212
|
250 260
....*....|....*....|....*..
gi 767927486 275 VAWCLRNEGVssVLLGSSTPEQLIENL 301
Cdd:cd19131 213 IRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
43-301 |
1.37e-12 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 66.91 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLE 117
Cdd:cd19124 29 AIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL-WCSDAH------PDLVLPALKKSLRNLQLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 181
Cdd:cd19124 99 YVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 182 AEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPESsraslkcyQWLKErivseegrkqqnklkdl 259
Cdd:cd19124 175 VEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVMES--------DVLKE----------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767927486 260 spIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 301
Cdd:cd19124 224 --IAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
36-309 |
2.34e-12 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 66.58 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK----AETERGL------------- 98
Cdd:cd19161 22 ADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRllkpAREGSVPdpngfvdplpfei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 99 ----SRKHIIEGLKGSLQRLQLEYVDVVF---------ANRPDSN---TPMEEIVRAMTHVINQGM--AMYWGTSRWSAM 160
Cdd:cd19161 97 vydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKALEELKKAGVikAFGLGVNEVQIC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 161 -EIMEAYSVarQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgIISGKYGNGVPESSRASLKCYQW 239
Cdd:cd19161 177 lEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------VIGGVFNSGILATGTKSGAKFNY 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767927486 240 lkeRIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ-VLPK 309
Cdd:cd19161 240 ---GDAPAE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQtDIPE 304
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
43-324 |
2.95e-12 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 66.15 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLEY 118
Cdd:cd19116 34 AIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE------REQVEPALRESLKRLGLDY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQA 182
Cdd:cd19116 104 VDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN----IKPAVNQI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 183 EYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLkcyqwlkerivsEEGRKQQNKLKDlsp 261
Cdd:cd19116 180 EVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRGQTN------------PPPRLDDPTLVA--- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927486 262 IAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 324
Cdd:cd19116 230 IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKEN---IDIFDfQLTPEEVAALNSFNTN 288
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
23-301 |
3.15e-12 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 65.65 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 23 ERSDDlptfiflVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkAETERGLSRKh 102
Cdd:cd19134 20 ELSDD-------EAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGFTAS- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 103 iIEGLKGSLQRLQLEYVDVVFANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPPVCEQ 181
Cdd:cd19134 84 -QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTPAVNQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 182 AEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnklkdl 259
Cdd:cd19134 159 IELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVGRLLDN-----PAVTA---------------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767927486 260 spIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 301
Cdd:cd19134 201 --IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
43-327 |
3.86e-12 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 65.60 E-value: 3.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQL 116
Cdd:cd19111 26 ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKLP-------PVYLEFKDTEKSLEKSLENLKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAE 183
Cdd:cd19111 94 PYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK----VKPSNLQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 184 YHLF--QREKVEVQLPelyHKIGVGAmtWSPLacgiisgkygnGVPesSRASLkcYQWLKERIVSEEgrkqQNKLKdlsp 261
Cdd:cd19111 170 CHAYlqQRELRKFCNK---KNIVVTA--YAPL-----------GSP--GRANQ--SLWPDQPDLLED----PTVLA---- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927486 262 IAERLGCTLPQLAVAWCL-RNEGvssVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 327
Cdd:cd19111 222 IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--ELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
43-306 |
1.02e-11 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 63.91 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:cd19139 23 ALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNLSKDKLLPSLEESLEKLRTDYVDLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYhlFQREKVEVQLPEly 200
Cdd:cd19139 93 LIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 201 HKIGVGAmtWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQQNKLkdLSPIAERLGCTLPQLAVAWCLr 280
Cdd:cd19139 169 HGIHVTS--YMTLA---------------------------------YGKVLDDPV--LAAIAERHGATPAQIALAWAM- 210
|
250 260
....*....|....*....|....*.
gi 767927486 281 NEGVsSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19139 211 ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-301 |
1.07e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 63.66 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKAETERGLSRkhiieglkgSLQRLQ 115
Cdd:cd19100 29 AAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKTGARDYEGAKRDLER---------SLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVF----ANRPDSNTPMEE--IVRAMTHVINQGMAMYWGTS--RWSAM-EIMEAYsvarQFNMIPPVCEQAEYHl 186
Cdd:cd19100 95 TDYIDLYQlhavDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISghSPEVLlRALETG----EFDVVLFPINPAGDH- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 fQREKVEVQLPELY-HKIGVGAMtwSPLACGiisgkygngvpessraslkcyQWLKERIVSeegrkqqnklkdlspiaer 265
Cdd:cd19100 170 -IDSFREELLPLAReKGVGVIAM--KVLAGG---------------------RLLSGDPLD------------------- 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 767927486 266 lgctlPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 301
Cdd:cd19100 207 -----PEQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
52-301 |
1.22e-11 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 64.29 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 52 DTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FA 124
Cdd:cd19125 42 DCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-WCTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 125 NRPDSNTP---------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQ 195
Cdd:cd19125 114 LKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---K 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 196 LPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAV 275
Cdd:cd19125 187 LHEFCKSKGIHLSAYSPL-----------GSPGTTWVKKNV---LKDPIVTK--------------VAEKLGKTPAQVAL 238
|
250 260
....*....|....*....|....*.
gi 767927486 276 AWCLRnEGvSSVLLGSSTPEQLIENL 301
Cdd:cd19125 239 RWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
37-123 |
2.46e-11 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 63.45 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 37 ERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRL 114
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIITKV--GRYGPDDFDYSPEWIRASVERSLRRL 112
|
....*....
gi 767927486 115 QLEYVDVVF 123
Cdd:cd19164 113 HTDYLDLVY 121
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
36-223 |
4.37e-11 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 62.07 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQ 115
Cdd:cd19126 25 TERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQRARRTED------AFQESLDRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEV 194
Cdd:cd19126 95 LDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRG 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 767927486 195 QLPElyHKIGVGAmtWSPLACGI---------ISGKYG 223
Cdd:cd19126 170 YCKS--KGIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
43-301 |
9.69e-11 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 61.49 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGKAETErglsrkhiiEGLKGSLQRLQL 116
Cdd:cd19136 24 ALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGYEKAR---------AACLGSLERLGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SAMEIMEAYSvarqfnMIPPVCEQAEY 184
Cdd:cd19136 92 DYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRHLEELLKYC------EVPPAVNQVEF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 185 H--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCYQWLKERIVSEegrkqqnklkdlspI 262
Cdd:cd19136 166 HphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DLRLLEDPTVLA--------------I 207
|
250 260 270
....*....|....*....|....*....|....*....
gi 767927486 263 AERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 301
Cdd:cd19136 208 AKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
36-319 |
1.06e-10 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 61.76 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW--------GGKAETERGLSRKHIIEGL 107
Cdd:cd19147 36 AFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKFTTdykayevgKGKAVNYCGNHKRSLHVSV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 108 KGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLF 187
Cdd:cd19147 115 RDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 188 QREKVEVQLPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwLKERIVSEEGRK------QQNKL----- 256
Cdd:cd19147 195 NRDFERDIIPMARH-FGMALAPWDVL---------GGGKFQSKKA-------VEERKKNGEGLRsfvggtEQTPEevkis 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767927486 257 KDLSPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 319
Cdd:cd19147 258 EALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEIEYLE 319
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
43-303 |
1.73e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 60.81 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgLSRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:PRK11172 25 ALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-LAKDKLIPSLKESLQKLRTDYVDLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS------AMEIMEAYSVARQfnmippvceQAEYH-LFQREKVE 193
Cdd:PRK11172 95 LIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIATN---------QIELSpYLQNRKVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 194 VQLPElyHKIGVGA-MTwspLAcgiisgkYGngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQ 272
Cdd:PRK11172 166 AFAKE--HGIHVTSyMT---LA-------YG--------------KVLKDPVIAR--------------IAAKHNATPAQ 205
|
250 260 270
....*....|....*....|....*....|.
gi 767927486 273 LAVAWCLRnEGvSSVLLGSSTPEQLIENLGA 303
Cdd:PRK11172 206 VILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
36-301 |
5.10e-10 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 59.21 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkaeteRGlsRKH----IIEGLKGSL 111
Cdd:cd19132 22 GVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL---------PG--RHHgyeeALRTIEESL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 112 QRLQLEYVDVVFANRPD-SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM---EIMEAYSVArqfnmipPVCEQAEYH-L 186
Cdd:cd19132 88 YRLGLDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLIDETGVT-------PAVNQIELHpY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 187 FQREKVEVqlpelYHK-IGVGAMTWSPLacgiisGKyGNGVpessraslkcyqwLKERIVSEegrkqqnklkdlspIAER 265
Cdd:cd19132 161 FPQAEQRA-----YHReHGIVTQSWSPL------GR-GSGL-------------LDEPVIKA--------------IAEK 201
|
250 260 270
....*....|....*....|....*....|....*.
gi 767927486 266 LGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENL 301
Cdd:cd19132 202 HGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
41-301 |
6.00e-10 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 58.96 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 41 TIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--GKAETERGLSRkhiieglkgSLQRLQLEY 118
Cdd:cd19127 29 ATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyGYDKALRGFDA---------SLRRLGLDY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVarqfnmIPPVcEQAEYHLFQRE 190
Cdd:cd19127 97 VDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERLIDATTV------VPAV-NQVELHPYFSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 191 KvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlkerivseegrkqqnklkdLSPIAERLGCTL 270
Cdd:cd19127 167 K---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT--------------------ITGLAEKYGKTP 220
|
250 260 270
....*....|....*....|....*....|.
gi 767927486 271 PQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 301
Cdd:cd19127 221 AQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
43-318 |
6.96e-10 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 59.01 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEY 118
Cdd:cd19129 28 ALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER------VKPAFEASLKRLQLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 178
Cdd:cd19129 98 LDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR----IKPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 179 CEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLACGIisgkygngvpessraslkcyqwlkerivseegrkQQNKLKD 258
Cdd:cd19129 174 VVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGM----------------------------------EPKLLED 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767927486 259 --LSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGaIQVLPKMTSHVVNEI 318
Cdd:cd19129 217 pvITAIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
35-301 |
1.17e-09 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 58.69 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 35 VAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKLYWGGkaeterglSRKHIIEG-L 107
Cdd:cd19155 26 EIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKLPPGG--------NRREKVEKfL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 108 KGSLQRLQLEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAY 166
Cdd:cd19155 93 LKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARIL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 167 SVARqfnmIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYGNGVPESSRASLkcyqwLKERIV 245
Cdd:cd19155 173 KNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPGTGSPSGSSPDL-----LQDPVV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 767927486 246 SEegrkqqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 301
Cdd:cd19155 241 KA--------------IAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
43-301 |
2.58e-09 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 57.50 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLYwggkaETERGlsrkHIIEGLKGSLQRLQLEY 118
Cdd:cd19112 33 AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW-----NSDHG----HVIEACKDSLKKLQLDY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVVFANRP-----------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA--MEIMEAYSvarqfn 173
Cdd:cd19112 101 LDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIflTRDCLAYS------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 174 MIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGIISGKYGNGVpessraslkcyqwlkerivseegrkq 252
Cdd:cd19112 175 KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWFGSV-------------------------- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767927486 253 qNKLKD--LSPIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENL 301
Cdd:cd19112 225 -SPLDDpvLKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
43-226 |
6.45e-09 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 55.85 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaeterglsRKHIIEGLKGSLQRLQLEYVDVV 122
Cdd:PRK11565 37 ALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD--------HKRPREALEESLKKLQLDYVDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvEVQ 195
Cdd:PRK11565 105 LMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT-------PVINQIELHpLMQQR--QLH 173
|
170 180 190
....*....|....*....|....*....|.
gi 767927486 196 LPELYHKIGVGAmtWSPLACGiisgkyGNGV 226
Cdd:PRK11565 174 AWNATHKIQTES--WSPLAQG------GKGV 196
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
43-223 |
1.05e-08 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 55.22 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQLEYVDVV 122
Cdd:cd19156 32 AIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSDQGYESTLA------AFEESLEKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEVQLPElyH 201
Cdd:cd19156 102 LIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--K 174
|
170 180 190
....*....|....*....|....*....|.
gi 767927486 202 KIGVGAmtWSPLACG---------IISGKYG 223
Cdd:cd19156 175 NIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
76-306 |
4.35e-08 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 53.78 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 76 RRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV------VFANRPDSNTPM---------------- 133
Cdd:cd19122 68 KREDLFICTKV-WNHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdlten 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 134 -EEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSP 212
Cdd:cd19122 141 pEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 213 LACGiisgkygNGVPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSS 292
Cdd:cd19122 214 LGSQ-------NQVPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSS 264
|
250
....*....|....
gi 767927486 293 TPEQLIENLGAIQV 306
Cdd:cd19122 265 TPSRIESNFKSIEL 278
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
43-324 |
1.23e-07 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 52.39 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAaGKAEVilGSIIKK-----KGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLE 117
Cdd:cd19106 29 ALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL-WNTKHHPE------DVEPALRKTLKDLQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 178
Cdd:cd19106 99 YLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 179 CEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVPEssRAslkcyqWLK--ERIVSEEGRkqqnkl 256
Cdd:cd19106 175 VLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSPD--RP------WAKpdEPVLLEEPK------ 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767927486 257 kdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 324
Cdd:cd19106 227 --VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQVFDfTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
43-302 |
2.91e-07 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 50.85 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 122
Cdd:cd19157 33 ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQGYDSTL------KAFEASLERLGLDYLDLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 123 FANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREkvevqLPELY 200
Cdd:cd19157 103 LIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 201 HKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 280
Cdd:cd19157 173 KKQGIQLEAWSPLMQG---------------------QLLDNPVLKE--------------IAEKYNKSVAQVILRWDLQ 217
|
250 260
....*....|....*....|..
gi 767927486 281 NEGVssVLLGSSTPEQLIENLG 302
Cdd:cd19157 218 NGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
36-321 |
7.52e-07 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 49.80 E-value: 7.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgkaeTERglsrKHIIEGLKGSLQRLQ 115
Cdd:cd19117 29 VAKAVEAALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC----TWH----RRVEEALDQSLKKLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 116 LEYVDVVFANRP-------DSNTPMEEIVRA--------------MTHVINQGMAMYWGTSRWSAMEIMEAysVARQFNM 174
Cdd:cd19117 97 LDYVDLYLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVKAIGVSNFSIKNLEKL--LASPSAK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 175 IPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpeSSRASLkcyqwLKERIVSEegrkqqn 254
Cdd:cd19117 175 IVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------STNAPL-----LKEPVIIK------- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767927486 255 klkdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGAIQvlpkMTSHVVNEIDNI 321
Cdd:cd19117 226 -------IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----LSDEEFKEIDEL 279
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-306 |
1.41e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 49.27 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 36 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHIIE 105
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 106 GLKGSLQRLQlEYVDV-----------VFANrpdsntpmEEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYS 167
Cdd:cd19098 113 QWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 168 VARQFNmippvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSE 247
Cdd:cd19098 182 GARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767927486 248 EGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 306
Cdd:cd19098 233 ELAP---LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
43-321 |
1.50e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.81 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 111
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 112 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 185
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 186 LFQREkvEVQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwlkerivseegrkqqnklkdLSPIAER 265
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPL---------GGFTPLQSST--------------------------LSDVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 767927486 266 LGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 321
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
43-193 |
4.71e-05 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 44.33 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYA----AGK--AEVILGSIIKkkgwrRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQL 116
Cdd:cd19115 35 AIKAGYRLFDGACDYGneveAGQgvARAIKEGIVK-----REDLFIVSKL-WNTFHDGE------RVEPICRKQLADWGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 117 EYVDVVFANRP------------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 172
Cdd:cd19115 103 DYFDLFLIHFPialkyvdpavryppgwfydgkkveFSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYAR-- 180
|
170 180
....*....|....*....|...
gi 767927486 173 nmIPPVCEQAEYH--LFQREKVE 193
Cdd:cd19115 181 --IRPATLQIEHHpyLTQPRLVK 201
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
42-187 |
1.30e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 42.99 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 42 IAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAETErgLSRKhiieGLKGSLQRLQLE 117
Cdd:cd19108 35 LAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRPE--LVRP----ALEKSLKKLQLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 118 YVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------IMEAYSVA----RQFNMI---P----- 176
Cdd:cd19108 105 YVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdagLAKSIGVSnfnrRQLEMIlnkPglkyk 180
|
170
....*....|.
gi 767927486 177 PVCEQAEYHLF 187
Cdd:cd19108 181 PVCNQVECHPY 191
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
37-220 |
1.82e-03 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 39.51 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 37 ERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSiikkkGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRL 114
Cdd:cd19130 26 QRAVATALEVGYRHIDTAAIYGneEGVGAAIAAS-----GIPRDELFVTTKL-WNDRHDGDEPAA------AFAESLAKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 115 QLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRW--SAMEIMEAYSVarqfnmIPPVCEQAEYH--L 186
Cdd:cd19130 94 GLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG------VVPAVNQIELHpaY 164
|
170 180 190
....*....|....*....|....*....|....
gi 767927486 187 FQREKVEVQlpelyHKIGVGAMTWSPLACGIISG 220
Cdd:cd19130 165 QQRTIRDWA-----QAHDVKIEAWSPLGQGKLLG 193
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
43-191 |
1.97e-03 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 39.46 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 43 AYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQLEY 118
Cdd:cd19114 26 AIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-WNNFH------GKDHVREAFDRQLKDYGLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767927486 119 VDVVFANRPDS-------------------------NTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 173
Cdd:cd19114 96 IDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYAK--- 172
|
170
....*....|....*....
gi 767927486 174 mIPPVCEQAEYHLF-QREK 191
Cdd:cd19114 173 -IKPAVLQIEHHPYlQQKR 190
|
|
| |
