|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
10-315 |
0e+00 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 645.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMV 89
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHEKGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 90 KGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIER 169
Cdd:cd19107 81 KGACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLDESGNVIPSDTTFLDTWEAMEELVDEGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 170 ILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKEIAAKYNKTTAQVL 249
Cdd:cd19107 161 ILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168407 250 IRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVCALMSCAKHKDYPFHAE 315
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRACALLSCSSHKDYPFHAE 306
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
7-299 |
4.56e-163 |
|
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: 456.08 E-value: 4.56e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKE-QVVKRQDLFIVSKLWCTFHD 85
Cdd:cd19106 1 LHTGQKMPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKVGPgKAVPREDLFVTSKLWNTKHH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPL 165
Cdd:cd19106 81 PEDVEPALRKTLKDLQLDYLDLYLIHWPYAFERGDNPFPKNPDGTIRYDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 166 QIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKEIAAKYNKTT 245
Cdd:cd19106 161 QIDDILSVA--RIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDRPWAKPDEPVLLEEPKVKALAKKYNKSP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168407 246 AQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVC 299
Cdd:cd19106 239 AQILLRWQVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
12-315 |
3.71e-157 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 441.32 E-value: 3.71e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 12 KMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKG 91
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVKT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 92 ACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERIL 171
Cdd:cd19110 83 ACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRSGMVIPSDTDFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 172 NKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGspdrpwAKPEDPSLLEDPRIKEIAAKYNKTTAQVLIR 251
Cdd:cd19110 163 NKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG------GSCEGVDLIDDPVIQRIAKKHGKSPAQILIR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 252 FPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVCALMSCAKHKDYPFHAE 315
Cdd:cd19110 237 FQIQRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRLATFPITENHKDYPFHIE 300
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
5-297 |
2.28e-136 |
|
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: 388.51 E-value: 2.28e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKS---PPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWC 81
Cdd:cd19108 3 VKLNDGHFIPVLGFGTYAPeevPKSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIRSKIADGTVKREDIFYTSKLWC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 TFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSN 161
Cdd:cd19108 83 TFHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDENGKLIFDTVDLCATWEAMEKCKDAGLAKSIGVSN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 162 FNPLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKEIAAK 240
Cdd:cd19108 163 FNRRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQrDKEWVDQNSPVLLEDPVLCALAKK 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168407 241 YNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19108 243 HKRTPALIALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
7-299 |
2.27e-133 |
|
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: 380.47 E-value: 2.27e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKS-PPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHD 85
Cdd:cd19116 5 LNDGNEIPAIALGTWKLkDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYfplDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPL 165
Cdd:cd19116 85 REQVEPALRESLKRLGLDYVDLYLIHWPVAFKENNDS---ESNGDGSLSDIDYLETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 166 QIERILNkpGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSlLEDPRIKEIAAKYNKTT 245
Cdd:cd19116 162 QINRLLS--NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPR-LDDPTLVAIAKKYGKTT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168407 246 AQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVC 299
Cdd:cd19116 239 AQIVLRYLIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
13-289 |
5.83e-127 |
|
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: 362.57 E-value: 5.83e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 13 MPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLkeqvVKRQDLFIVSKLWCTFHDQSMVKGA 92
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESG----VPREELFITTKLWPTDHGYERVREA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 93 CQKTLSDLQLDYLDLYLIHWPTGFKPGPdyfpldasgnvipSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILN 172
Cdd:cd19071 77 LEESLKDLGLDYLDLYLIHWPVPGKEGG-------------SKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 173 KPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKEIAAKYNKTTAQVLIRF 252
Cdd:cd19071 144 AA--RIKPAVNQIELHPYLQQKELVEFCKEHGIVVQAYSPLGRGRRP--------LLDDPVLKEIAKKYGKTPAQVLLRW 213
|
250 260 270
....*....|....*....|....*....|....*..
gi 1168407 253 PIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19071 214 ALQRGVVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
10-312 |
1.18e-126 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 364.12 E-value: 1.18e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTW----KSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHD 85
Cdd:cd19109 1 GNSIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNTCHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPL 165
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEIYPRDENGKWLYHKTNLCATWEALEACKDAGLVKSIGVSNFNRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 166 QIERILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSP-DRPWAKPEDPSLLEDPRIKEIAAKYNKT 244
Cdd:cd19109 161 QLELILNKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCrDPIWVNVSSPPLLEDPLLNSIGKKYNKT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168407 245 TAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVCALMSCAKHKDYPF 312
Cdd:cd19109 241 AAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYVELLMWRDHPEYPF 308
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
5-297 |
8.79e-125 |
|
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: 359.03 E-value: 8.79e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFH 84
Cdd:cd19123 4 LPLSNGDLIPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGpdyFPLDASGNVIPSDTD--FVDTWTAMEQLVDEGLVKAIGVSNF 162
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPVALKKG---VGFPESGEDLLSLSPipLEDTWRAMEELVDKGLCRHIGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 163 NPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWA-KPED-PSLLEDPRIKEIAAK 240
Cdd:cd19123 161 SVKKLEDLLATA--RIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAmKAEGePVLLEDPVINKIAEK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168407 241 YNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19123 239 HGASPAQVLIAWAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
4-289 |
9.96e-122 |
|
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: 350.88 E-value: 9.96e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 4 HLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19125 2 FFKLNTGAKIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPdyfPLDASGNVIPsdTDFVDTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19125 82 HAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRLKKGA---HMPEPEEVLP--PDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEdpsLLEDPRIKEIAAKYNK 243
Cdd:cd19125 157 VKKLEDLLAVA--RVPPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPGTTWVKKN---VLKDPIVTKVAEKLGK 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168407 244 TTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19125 232 TPAQVALRWGLQRGTSVLPKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
2-299 |
2.03e-120 |
|
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: 347.86 E-value: 2.03e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 2 ASHLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWC 81
Cdd:cd19154 1 SASITLSNGVKMPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 TFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSN 161
Cdd:cd19154 81 HEHAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 162 FNPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPED-----PSLLEDPRIKE 236
Cdd:cd19154 161 FNNDQIQRILDNA--RVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPGRANFTKSTgvspaPNLLQDPIVKA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168407 237 IAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVC 299
Cdd:cd19154 239 IAEKHGKTPAQVLLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRLF 301
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-298 |
3.78e-116 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 335.49 E-value: 3.78e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 9 NGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTFHDQSM 88
Cdd:COG0656 1 NGVEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAI----AASGVPREELFVTTKVWNDNHGYDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 89 VKGACQKTlsdlqldyldlylIHWPtgfkpGPDyfpldasgnvipsdtDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIE 168
Cdd:COG0656 77 TLAAFEESlerlgldyldlylIHWP-----GPG---------------PYVETWRALEELYEEGLIRAIGVSNFDPEHLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 169 RILNKPGlkYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKEIAAKYNKTTAQV 248
Cdd:COG0656 137 ELLAETG--VKPAVNQVELHPYLQQRELLAFCREHGIVVEAYSPLGRGK----------LLDDPVLAEIAEKHGKTPAQV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168407 249 LIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRV 298
Cdd:COG0656 205 VLRWHLQRGVVVIPKSVTPERIRENLDAFDFELSDEDMAAIDALDRGERL 254
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
7-289 |
1.35e-103 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 304.72 E-value: 1.35e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQ-VVKRQDLFIVSKLWCTFHD 85
Cdd:cd19118 1 LNTGNKIPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEpGVKREDLFITSKLWNNSHR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPL---DASGNVIPSDTD--FVDTWTAMEQLVDEGLVKAIGVS 160
Cdd:cd19118 81 PEYVEPALDDTLKELGLDYLDLYLIHWPVAFKPTGDLNPLtavPTNGGEVDLDLSvsLVDTWKAMVELKKTGKVKSIGVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 161 NFNPLQIERILNKPGLkyKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSpdrpwAKPEDPSLLEDPRIKEIAAK 240
Cdd:cd19118 161 NFSIDHLQAIIEETGV--VPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGN-----NLAGLPLLVQHPEVKAIAAK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1168407 241 YNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKvfDFELSNEDMATL 289
Cdd:cd19118 234 LGKTPAQVLIAWGIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAV 280
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-297 |
5.30e-101 |
|
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: 298.26 E-value: 5.30e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMV 89
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 90 KGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDyfpldaSGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIER 169
Cdd:cd19111 81 EKSLEKSLENLKLPYVDLYLIHHPCGFVNKKD------KGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 170 ILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRP--WAKPEDPSLLEDPRIKEIAAKYNKTTAQ 247
Cdd:cd19111 155 ILAYA--KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRAnqSLWPDQPDLLEDPTVLAIAKELDKTPAQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168407 248 VLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19111 233 VLLRFVLQRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMK 282
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-299 |
1.59e-99 |
|
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: 295.20 E-value: 1.59e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 3 SHLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCT 82
Cdd:cd19155 2 NCVTFNNGEKMPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 83 FHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFK-PGPDYFPLDASGNV-IPSDTDFVDTWTAMEQLVDEGLVKAIGVS 160
Cdd:cd19155 82 GNRREKVEKFLLKSLEKLQLDYVDLYLIHFPVGSLsKEDDSGKLDPTGEHkQDYTTDLLDIWKAMEAQVDQGLTRSIGLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 161 NFNPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKP-------EDPSLLEDPR 233
Cdd:cd19155 162 NFNREQMARILKNA--RIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHFSPgtgspsgSSPDLLQDPV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168407 234 IKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRVC 299
Cdd:cd19155 240 VKAIAERHGKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRGR 305
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
5-289 |
3.39e-95 |
|
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: 283.23 E-value: 3.39e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTFH 84
Cdd:cd19117 6 FKLNTGAEIPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGI----KDSGVPREEIFITTKLWCTWH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQsmVKGACQKTLSDLQLDYLDLYLIHWPTGFKPG--PDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNF 162
Cdd:cd19117 82 RR--VEEALDQSLKKLGLDYVDLYLMHWPVPLDPDgnDFLFKKDDGTKDHEPDWDFIKTWELMQKLPATGKVKAIGVSNF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 163 NPLQIERILNKPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKEIAAKYN 242
Cdd:cd19117 160 SIKNLEKLLASPSAKIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAP--------LLKEPVIIKIAKKHG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168407 243 KTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVfdFELSNEDMATL 289
Cdd:cd19117 232 KTPAQVIISWGLQRGYSVLPKSVTPSRIESNFKL--FTLSDEEFKEI 276
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
5-287 |
1.70e-94 |
|
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: 280.41 E-value: 1.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTFH 84
Cdd:cd19131 2 ITLNDGNTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAI----RASGVPREELFITTKLWNSDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQSMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnviPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNP 164
Cdd:cd19131 78 GYDSTLRAFDESLRKLGLDYVDLYLIHWPV------------------PAQDKYVETWKALIELKKEGRVKSIGVSNFTI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 165 LQIERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKEIAAKYNKT 244
Cdd:cd19131 140 EHLQRLIDETGVV--PVVNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQG----------GLLSDPVIGEIAEKHGKT 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1168407 245 TAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19131 208 PAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELDADDMQ 250
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-292 |
1.46e-93 |
|
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: 278.36 E-value: 1.46e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 13 MPTLGLGTWK-SPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKG 91
Cdd:cd19136 1 MPILGLGTFRlRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 92 ACQKTLSDLQLDYLDLYLIHWptgfkPGPDYFPLDASGNVIPSdtdfVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERIL 171
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHW-----PGVQGLKPSDPRNAELR----RESWRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 172 NKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPdrpwakpeDPSLLEDPRIKEIAAKYNKTTAQVLIR 251
Cdd:cd19136 152 KYC--EVPPAVNQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSG--------DLRLLEDPTVLAIAKKYGRTPAQVLLR 221
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1168407 252 FPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSY 292
Cdd:cd19136 222 WALQQGIGVIPKSTNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
5-297 |
2.26e-93 |
|
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: 279.37 E-value: 2.26e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTfh 84
Cdd:cd19112 3 ITLNSGHKMPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNS-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKP---GPDYFPLDASGNV-IPSDTDFVDTWTAMEQLVDEGLVKAIGVS 160
Cdd:cd19112 81 DHGHVIEACKDSLKKLQLDYLDLYLVHFPVATKHtgvGTTGSALGEDGVLdIDVTISLETTWHAMEKLVSAGLVRSIGIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 161 NFNPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLG--SPDRPWAKPEDPslLEDPRIKEIA 238
Cdd:cd19112 161 NYDIFLTRDCLAYS--KIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGgaAANAEWFGSVSP--LDDPVLKDLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168407 239 AKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19112 237 KKYGKSAAQIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYR 295
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
1-297 |
2.98e-92 |
|
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: 276.61 E-value: 2.98e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 1 MASHLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLW 80
Cdd:cd19115 1 ASPTVKLNSGYDMPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 81 CTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFK---PGPDYFP--LDASGNVIPSDTDFVDTWTAMEQLVDEGLVK 155
Cdd:cd19115 81 NTFHDGERVEPICRKQLADWGIDYFDLFLIHFPIALKyvdPAVRYPPgwFYDGKKVEFSNAPIQETWTAMEKLVDKGLAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 156 AIGVSNFNPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGsP------DRPWAKpEDPSLL 229
Cdd:cd19115 161 SIGVSNFSAQLLMDLLRYA--RIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PqsflelDLPGAK-DTPPLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1168407 230 EDPRIKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19115 237 EHDVIKSIAEKHGKTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLR 304
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
5-297 |
3.01e-90 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 271.63 E-value: 3.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFH 84
Cdd:cd19113 3 IKLNSGYKMPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLWNNFH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGP---DYFPLDASG---NVIPSDTDFVDTWTAMEQLVDEGLVKAIG 158
Cdd:cd19113 83 DPKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVPieeKYPPGFYCGdgdNFVYEDVPILDTWKALEKLVDAGKIKSIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 159 VSNFNPLQIERILNkpGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSP-----DRPWAKpEDPSLLEDPR 233
Cdd:cd19113 163 VSNFPGALILDLLR--GATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQsfvelNQGRAL-NTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 234 IKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLR 303
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
14-286 |
7.46e-89 |
|
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: 266.70 E-value: 7.46e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKGAC 93
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 94 QKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNK 173
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 174 pgLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKpedpSLLEDPRIKEIAAKYNKTTAQVLIRFP 253
Cdd:cd19128 162 --CKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNL----TFLNDSELKALATKYNTTPPQVIIAWH 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 1168407 254 IQR---NLVVIPKSVTPARIAENFKVFDFELSNEDM 286
Cdd:cd19128 236 LQKwpkNYSVIPKSANKSRCQQNFDINDLALTKEDM 271
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
7-293 |
4.90e-88 |
|
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: 264.05 E-value: 4.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTE-AVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTFHD 85
Cdd:cd19133 3 LNNGVEMPILGFGVFQIPDPEECErAVLEAIKAGYRLIDTAAAYGNEEAVGRAI----KKSGIPREELFITTKLWIQDAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGfkpgpDYFpldasgnvipsdtdfvDTWTAMEQLVDEGLVKAIGVSNFNPL 165
Cdd:cd19133 79 YEKAKKAFERSLKRLGLDYLDLYLIHQPFG-----DVY----------------GAWRAMEELYKEGKIRAIGVSNFYPD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 166 QIERILnkPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDrpwakpedPSLLEDPRIKEIAAKYNKTT 245
Cdd:cd19133 138 RLVDLI--LHNEVKPAVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEGR--------NNLFENPVLTEIAEKYGKSV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1168407 246 AQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYN 293
Cdd:cd19133 208 AQVILRWLIQRGIVVIPKSVRPERIAENFDIFDFELSDEDMEAIAALD 255
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
5-289 |
1.92e-87 |
|
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: 262.37 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTE-AVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19126 1 VTLNNGTRMPWLGLGVFQTPDGDETErAVQTALENGYRSIDTAAIYKNEEGVGEAI----RESGVPREELFVTTKLWNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPtgfkpGPDyfpldasgnvipsdtDFVDTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19126 77 QRARRTEDAFQESLDRLGLDYVDLYLIHWP-----GKD---------------KFIDTWKALEKLYASGKVKAIGVSNFQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKEIAAKYNK 243
Cdd:cd19126 137 EHHLEELLAHA--DVVPAVNQVEFHPYLTQKELRGYCKSKGIVVEAWSPLGQG----------GLLSNPVLAAIGEKYGK 204
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168407 244 TTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19126 205 SAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSEDDMTAI 250
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
5-298 |
1.92e-87 |
|
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: 262.71 E-value: 1.92e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQ-VTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19157 2 VTLNNGVKMPWLGLGVFKVEEGSeVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGI----KESGIPREELFITSKVWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKpgpdyfpldasgnvipsdtdFVDTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19157 78 QGYDSTLKAFEASLERLGLDYLDLYLIHWPVKGK--------------------YKETWKALEKLYKDGRVRAIGVSNFQ 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKEIAAKYNK 243
Cdd:cd19157 138 VHHLEDLLADA--EIVPMVNQVEFHPRLTQKELRDYCKKQGIQLEAWSPLMQGQ----------LLDNPVLKEIAEKYNK 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1168407 244 TTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRV 298
Cdd:cd19157 206 SVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELSQEDMDKIDALNENLRV 260
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
7-292 |
4.25e-87 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 262.47 E-value: 4.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLkEQVVKRQDLFIVSKLWCTFHDQ 86
Cdd:cd19121 6 LNTGASIPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYHRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 smVKGACQKTLSDLQLDYLDLYLIHWPTGFKP--GPDYFPL--DASGNVIPsDTDFVDTWTAMEQLVDEGLVKAIGVSNF 162
Cdd:cd19121 85 --VELCLDRSLKSLGLDYVDLYLVHWPVLLNPngNHDLFPTlpDGSRDLDW-DWNHVDTWKQMEKVLKTGKTKAIGVSNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 163 NPLQIERILnkPGLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIKEIAAKYN 242
Cdd:cd19121 162 SIPYLEELL--KHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSP--------LISDEPVVEIAKKHN 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1168407 243 KTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFElsNEDMATLLSY 292
Cdd:cd19121 232 VGPGTVLISYQVARGAVVLPKSVTPDRIKSNLEIIDLD--DEDMNKLNDI 279
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
4-289 |
1.55e-83 |
|
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: 253.02 E-value: 1.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 4 HLELNNGTKMPTLGLGTWKSPpGQVTEAVKVAI-DMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCT 82
Cdd:cd19135 4 TVRLSNGVEMPILGLGTSHSG-GYSHEAVVYALkECGYRHIDTAKRYGCEELLGKAI----KESGVPREDLFLTTKLWPS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 83 FHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDAsgnvipsdtdfvDTWTAMEQLVDEGLVKAIGVSNF 162
Cdd:cd19135 79 DYGYESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETRA------------ETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 163 NPLQIERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGspdrPWakpedpSLLEDPRIKEIAAKYN 242
Cdd:cd19135 147 LIEHLEQLLEDCSVV--PHVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KG------KALEEPTVTELAKKYQ 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168407 243 KTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19135 215 KTPAQILIRWSIQNGVVTIPKSTKEERIKENCQVFDFSLSEEDMATL 261
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
5-297 |
1.04e-82 |
|
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: 250.90 E-value: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWKSPPGQVTE-AVKVAIDMGYRHIDCAQVYQNEKEVGvalqEKLKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19156 1 VKLANGVEMPRLGLGVWRVQDGAEAEnAVKWAIEAGYRHIDTAAIYKNEEGVG----QGIRESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKpgpdyfpldasgnvipsdtdFVDTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19156 77 QGYESTLAAFEESLEKLGLDYVDLYLIHWPVKGK--------------------FKDTWKAFEKLYKEKKVRAIGVSNFH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKpgLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDrpwakpedpsLLEDPRIKEIAAKYNK 243
Cdd:cd19156 137 EHHLEELLKS--CKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQGK----------LLSNPVLKAIGKKYGK 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168407 244 TTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19156 205 SAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFELTAEEIRQIDGLNTDHR 258
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
8-276 |
6.11e-82 |
|
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: 250.07 E-value: 6.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQS 87
Cdd:cd19129 1 NGSGAIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 88 MVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDASGNVIPSD-TDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:cd19129 81 RVKPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANGNVIYDDgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRpwakpedPSLLEDPRIKEIAAKYNKTTA 246
Cdd:cd19129 161 LREIFEAA--RIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGME-------PKLLEDPVITAIARRVNKTPA 231
|
250 260 270
....*....|....*....|....*....|
gi 1168407 247 QVLIRFPIQRNLVVIPKSVTPARIAENFKV 276
Cdd:cd19129 232 QVLLAWAIQRGTALLTTSKTPSRIRENFDI 261
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
13-289 |
8.28e-82 |
|
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: 247.57 E-value: 8.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 13 MPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGvalqEKLKEQVVKRQDLFIVSKLWCTFHDQSMVKGA 92
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVG----EAIAESGVPREDLFITTKVWRDHLRPEDLKKS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 93 CQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnvipSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILN 172
Cdd:cd19073 77 VDRSLEKLGTDYVDLLLIHWPN-------------------PTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 173 KPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLgspdrpwAKPEdpsLLEDPRIKEIAAKYNKTTAQVLIRF 252
Cdd:cd19073 138 ISPLP--IAVNQVEFHPFLYQAELLEYCRENDIVITAYSPL-------ARGE---VLRDPVIQEIAEKYDKTPAQVALRW 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 1168407 253 PIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19073 206 LVQKGIVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-286 |
1.34e-81 |
|
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: 248.34 E-value: 1.34e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 9 NGTKMPTLGLGTWKSPPG--QVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVK-RQDLFIVSKLWCTFHD 85
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSpeDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEALRLGLVKsRDELFVTSKLWCSDAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFPLDAsGNVIPsdTDFVDTWTAMEQLVDEGLVKAIGVSNFNPL 165
Cdd:cd19124 81 PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEE-EDFLP--FDIKGVWEAMEECQRLGLTKAIGVSNFSCK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 166 QIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAkpeDPSLLEDPRIKEIAAKYNKTT 245
Cdd:cd19124 158 KLQELLSFA--TIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKWG---SNAVMESDVLKEIAAAKGKTV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1168407 246 AQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDM 286
Cdd:cd19124 233 AQVSLRWVYEQGVSLVVKSFNKERMKQNLDIFDWELTEEDL 273
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
7-289 |
9.25e-80 |
|
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: 243.47 E-value: 9.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGvalqEKLKEQVVKRQDLFIVSKLWCTFHDQ 86
Cdd:cd19127 3 LNNGVEMPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVG----EGIRRSGVDRSDIFVTTKLWISDYGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 SMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgPDYFpldasgnvipSDTdfVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:cd19127 79 DKALRGFDASLRRLGLDYVDLYLLHWPV-----PNDF----------DRT--IQAYKALEKLLAEGRVRAIGVSNFTPEH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAK--PEDPSLLEDPRIKEIAAKYNKT 244
Cdd:cd19127 142 LERLIDATTVV--PAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGVMRYGASgpTGPGDVLQDPTITGLAEKYGKT 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1168407 245 TAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19127 220 PAQIVLRWHLQNGVSAIPKSVHPERIAENIDIFDFALSAEDMAAI 264
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-287 |
3.19e-77 |
|
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: 236.75 E-value: 3.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGT----WKSPPG----QVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLkeqvVKRQDLFIVSKLWC 81
Cdd:cd19120 1 GSKIPAIAFGTgtawYKSGDDdiqrDLVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESG----VPREDLFITTKVSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 TFHDqsmVKGACQKTLSDLQLDYLDLYLIHWPTGFKPGpdyfpldasgnvipsDTDFVDTWTAMEQLVDEGLVKAIGVSN 161
Cdd:cd19120 77 GIKD---PREALRKSLAKLGVDYVDLYLIHSPFFAKEG---------------GPTLAEAWAELEALKDAGLVRSIGVSN 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 162 FNPLQIERILNKPglKYKPAVNQIECHPYLT--QEKLIEYCHCKGIVVTAYSPLGspdrPWAKPEDPSLleDPRIKEIAA 239
Cdd:cd19120 139 FRIEDLEELLDTA--KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLS----PLTRDAGGPL--DPVLEKIAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1168407 240 KYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19120 211 KYGVTPAQVLLRWALQKGIVVVTTSSKEERMKEYLEAFDFELTEEEVE 258
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
9-289 |
5.11e-77 |
|
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: 235.62 E-value: 5.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 9 NGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVAlqekLKEQVVKRQDLFIVSKLWctFHDQSM 88
Cdd:cd19140 4 NGVRIPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEA----IAASGVPRDELFLTTKVW--PDNYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 89 --VKGACQKTLSDLQLDYLDLYLIHWPtgfkpgpdyfpldasgnviPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:cd19140 78 ddFLASVEESLRKLRTDYVDLLLLHWP-------------------NKDVPLAETLGALNEAQEAGLARHIGVSNFTVAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPGLKYkpAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGspdrpwakpeDPSLLEDPRIKEIAAKYNKTTA 246
Cdd:cd19140 139 LREAVELSEAPL--FTNQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----------RGEVLKDPVLQEIGRKHGKTPA 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1168407 247 QVLIRFPIQR-NLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19140 207 QVALRWLLQQeGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
7-289 |
6.49e-75 |
|
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: 230.62 E-value: 6.49e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLkeqvVKRQDLFIVSKLWCTFHDQ 86
Cdd:cd19132 1 LNDGTQIPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSG----VPREELFVTTKLPGRHHGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 SMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnviPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:cd19132 77 EEALRTIEESLYRLGLDYVDLYLIHWPN------------------PSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRpwakpedpsLLEDPRIKEIAAKYNKTTA 246
Cdd:cd19132 139 LDRLIDETGVT--PAVNQIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGSG---------LLDEPVIKAIAEKHGKTPA 207
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1168407 247 QVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19132 208 QVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSDEDMAAI 250
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
5-289 |
1.48e-74 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 230.85 E-value: 1.48e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 5 LELNNGTKMPTLGLGTWkSPP---GQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWC 81
Cdd:cd19119 4 FKLNTGASIPALGLGTA-SPHedrAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 TFHDQsmVKGACQKTLSDLQLDYLDLYLIHWPTGFK-----PGPDYFPLDASGNVIPSDT-DFVDTWTAMEQLVDEGLVK 155
Cdd:cd19119 83 TFYDE--VERSLDESLKALGLDYVDLLLVHWPVCFEkdsddSGKPFTPVNDDGKTRYAASgDHITTYKQLEKIYLDGRAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 156 AIGVSNFNPLQIERILNKpgLKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPwakpedpsLLEDPRIK 235
Cdd:cd19119 161 AIGVSNYSIVYLERLIKE--CKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGAP--------NLKNPLVK 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1168407 236 EIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVfdFELSNEDMATL 289
Cdd:cd19119 231 KIAEKYNVSTGDILISYHVRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQKL 282
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
10-297 |
1.74e-74 |
|
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: 230.91 E-value: 1.74e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQVVKRQDLFIVSKLWCTFHDQSMV 89
Cdd:cd19114 1 GDKMPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGKDHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 90 KGACQKTLSDLQLDYLDLYLIHWPTGFK---PGPDYFPLDASGNVIPSDTDFV---DTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19114 81 REAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLWKDKELKKFPLEQSpmqECWREMEKLVDAGLVRNIGIANFN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSP---DRPWAKPEDPSLLEDPRIKEIAAK 240
Cdd:cd19114 161 VQLILDLLTYA--KIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAvytKVTKHLKHFTNLLEHPVVKKLADK 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1168407 241 YNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:cd19114 239 HKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANAR 295
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
4-289 |
5.92e-74 |
|
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: 228.26 E-value: 5.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 4 HLELNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19130 1 SIVLNDGNSIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnviPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFN 163
Cdd:cd19130 77 HDGDEPAAAFAESLAKLGLDQVDLYLVHWPT------------------PAAGNYVHTWEAMIELRAAGRTRSIGVSNFL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 164 PLQIERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKEIAAKYNK 243
Cdd:cd19130 139 PPHLERIVAATGVV--PAVNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQG----------KLLGDPPVGAIAAAHGK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1168407 244 TTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19130 207 TPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
7-294 |
5.83e-72 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 223.80 E-value: 5.83e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKlkeqVVKRQDLFIVSKLWCTfhDQ 86
Cdd:PRK11565 9 LQDGNVMPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEA----SVAREELFITTKLWND--DH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 SMVKGACQKTLSDLQLDYLDLYLIHWPtgfkpgpdyfpldasgnvIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:PRK11565 83 KRPREALEESLKKLQLDYVDLYLMHWP------------------VPAIDHYVEAWKGMIELQKEGLIKSIGVCNFQIHH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPGLKykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRpwakpedpSLLEDPRIKEIAAKYNKTTA 246
Cdd:PRK11565 145 LQRLIDETGVT--PVINQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGGK--------GVFDQKVIRDLADKYGKTPA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1168407 247 QVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNED---MATLLSYNR 294
Cdd:PRK11565 215 QIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDFRLDKDElgeIAKLDQGKR 265
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
7-285 |
4.29e-66 |
|
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: 209.40 E-value: 4.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKS--PPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQEKLKEQ-VVKRQDLFIVSKLWCTF 83
Cdd:cd19122 3 LNNGVKIPAVGFGTFANegAKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGF--------KPGPD--YFPL-DASGNVIPsdtdfvdTWTAMEQLVDEG 152
Cdd:cd19122 83 HEPEDVKWSIDNSLKNLKLDYIDLFLVHWPIAAekndqrspKLGPDgkYVILkDLTENPEP-------TWRAMEEIYESG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 153 LVKAIGVSNFNPLQIERILNKPglKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDPSllEDP 232
Cdd:cd19122 156 KAKAIGVSNWTIPGLKKLLSFA--KVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVPSTGERVS--ENP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1168407 233 RIKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVfdFELSNED 285
Cdd:cd19122 232 TLNEVAEKGGYSLAQVLIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDED 282
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-298 |
1.14e-61 |
|
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: 197.00 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 7 LNNGTKMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALqeklKEQVVKRQDLFIVSKLWCTFHDQ 86
Cdd:cd19134 5 LNDDNTMPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAI----AASGIPRGELFVTTKLATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 SMVKGACQKTLSDLQLDYLDLYLIHWPtgfkpgpdyfpldasgnvIPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQ 166
Cdd:cd19134 81 TASQAACRASLERLGLDYVDLYLIHWP------------------AGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 167 IERILNKPGlkYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPdrpwakpedpSLLEDPRIKEIAAKYNKTTA 246
Cdd:cd19134 143 LENLIDLTF--FTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG----------RLLDNPAVTAIAAAHGRTPA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1168407 247 QVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWRV 298
Cdd:cd19134 211 QVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTADHMDALDGLDDGTRF 262
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-287 |
2.34e-58 |
|
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: 187.95 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 13 MPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQeklkEQVVKRQDLFIVSKLWCTFHDQSMVKGA 92
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLSKDKLLPS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 93 CQKTLSDLQLDYLDLYLIHWPtgfkpgpdyfpldASGNVIPSDtdfvDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILN 172
Cdd:cd19139 77 LEESLEKLRTDYVDLTLIHWP-------------SPNDEVPVE----EYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 173 KPGlKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKEIAAKYNKTTAQVLIRF 252
Cdd:cd19139 140 VVG-AGAIATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA-----YGK-----VLDDPVLAAIAERHGATPAQIALAW 208
|
250 260 270
....*....|....*....|....*....|....*
gi 1168407 253 PIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19139 209 AMARGYAVIPSSTKREHLRSNLLALDLTLDADDMA 243
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-289 |
5.03e-54 |
|
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: 177.04 E-value: 5.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWK---------SPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEklkeqvVKRQDLFIVS 77
Cdd:cd19072 1 GEEVPVLGLGTWGigggmskdySDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAIKG------FDREDLFITT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 78 KLW---CTFHDqsmVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnvipSDTDFVDTWTAMEQLVDEGLV 154
Cdd:cd19072 75 KVSpdhLKYDD---VIKAAKESLKRLGTDYIDLYLIHWPN-------------------PSIPIEETLRAMEELVEEGKI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 155 KAIGVSNFNPLQIERILNKPGlKYKPAVNQIECHpYLTQE---KLIEYCHCKGIVVTAYSPLGSPDRPWAKPedpslleD 231
Cdd:cd19072 133 RYIGVSNFSLEELEEAQSYLK-KGPIVANQVEYN-LFDREeesGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------S 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168407 232 PRIKEIAAKYNKTTAQVLIRFPIQR-NLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19072 204 PLLDEIAKKYGKTPAQIALNWLISKpNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-289 |
1.13e-52 |
|
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: 174.42 E-value: 1.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 16 LGLGTW-------KSPPGQVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGvalqEKLKEQVVKRQDLFIVSKLWC---- 81
Cdd:pfam00248 1 IGLGTWqlgggwgPISKEEALEALRAALEAGINFIDTAEVYgdgKSEELLG----EALKDYPVKRDKVVIATKVPDgdgp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 ---TFHDQSMVKgACQKTLSDLQLDYLDLYLIHWPTGfkpgpdyfpldasgnvipsDTDFVDTWTAMEQLVDEGLVKAIG 158
Cdd:pfam00248 77 wpsGGSKENIRK-SLEESLKRLGTDYIDLYYLHWPDP-------------------DTPIEETWDALEELKKEGKIRAIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 159 VSNFNPLQIERILNKPglKYKPAVNQIECHPY--LTQEKLIEYCHCKGIVVTAYSPLGS-----------------PDRP 219
Cdd:pfam00248 137 VSNFDAEQIEKALTKG--KIPIVAVQVEYNLLrrRQEEELLEYCKKNGIPLIAYSPLGGglltgkytrdpdkgpgeRRRL 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168407 220 WAKPEDPSLLEDPRIKEIAAKYNKTTAQVLIRFPIQ--RNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:pfam00248 215 LKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSkpGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
12-297 |
1.06e-51 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 171.36 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 12 KMPTLGLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVYQNEKEVGVALQeklkEQVVKRQDLFIVSKLWCTFHDQSMVKG 91
Cdd:PRK11172 2 SIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKDKLIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 92 ACQKTLSDLQLDYLDLYLIHWPtgfkpgpdyfpldASGNVIPSDtdfvdtwTAMEQLVD---EGLVKAIGVSNFNPLQIE 168
Cdd:PRK11172 78 SLKESLQKLRTDYVDLTLIHWP-------------SPNDEVSVE-------EFMQALLEakkQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 169 RILNKPGlKYKPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGspdrpWAKpedpsLLEDPRIKEIAAKYNKTTAQV 248
Cdd:PRK11172 138 QAIAAVG-AENIATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA-----YGK-----VLKDPVIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1168407 249 LIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATLLSYNRNWR 297
Cdd:PRK11172 207 ILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLDAEDMAAIAALDRNGR 255
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
4-289 |
1.34e-46 |
|
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: 158.18 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 4 HLELNNGTKMPTLGLGTW-----KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEKlkeqvvkRQDLFI 75
Cdd:cd19138 2 TVTLPDGTKVPALGQGTWymgedPAKRAQEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR-------RDKVFL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 76 VSKLWCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGfkpgpdyFPLDasgnvipsdtdfvDTWTAMEQLVDEGLVK 155
Cdd:cd19138 75 VSKVLPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGG-------VPLA-------------ETVAAMEELKKEGKIR 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 156 AIGVSNFNPLQIERILNKPGLKyKPAVNQIECHpyLTQE----KLIEYCHCKGIVVTAYSPLGSPDRPwakpeDPSLLED 231
Cdd:cd19138 135 AWGVSNFDTDDMEELWAVPGGG-NCAANQVLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGLL-----RRGLLEN 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1168407 232 PRIKEIAAKYNKTTAQVLIRFPIQRNLVV-IPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19138 207 PTLKEIAARHGATPAQVALAWVLRDGNVIaIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-289 |
2.37e-43 |
|
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: 149.64 E-value: 2.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWK---------SPPGQVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALQEklkeqvVKRQDLFIVS 77
Cdd:cd19137 1 GEKIPALGLGTWGiggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD------FPREDLFIVT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 78 KLWCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgPDyFPLDasgnvipsdtdfvDTWTAMEQLVDEGLVKAI 157
Cdd:cd19137 75 KVWPTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPN-----PN-IPLE-------------ETLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 158 GVSNFNPLQIERILNKpgLKYKPAVNQIECHPY---LTQEKLIEYCHCKGIVVTAYSPLgspDRPWAKPEDpslledpRI 234
Cdd:cd19137 136 GVSNFNRRLLEEAISK--SQTPIVCNQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPL---RRGLEKTNR-------TL 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168407 235 KEIAAKYNKTTAQVLIRFPIQR-NLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19137 204 EEIAKNYGKTIAQIALAWLIQKpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-289 |
3.48e-39 |
|
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: 139.67 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 12 KMPTLGLGTWK-----------SPPGQVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvVKRQDLFIVS 77
Cdd:cd19093 1 EVSPLGLGTWQwgdrlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKEL-----GDRDEVVIAT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 78 KLWCTFHD---QSMVKgACQKTLSDLQLDYLDLYLIHWPTGFKPGPDYFpldasgnvipsdtdfvdtWTAMEQLVDEGLV 154
Cdd:cd19093 76 KFAPLPWRltrRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIEAL------------------MDGLADAVEEGLV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 155 KAIGVSNFNPLQIERI---LNKPGlkYKPAVNQIE---CHPYLTQEKLIEYCHCKGIVVTAYSPLG--------SPDRP- 219
Cdd:cd19093 137 RAVGVSNYSADQLRRAhkaLKERG--VPLASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPENPp 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 220 ----------WAKPEDPSLLEdpRIKEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19093 215 pggrrrlfgrKNLEKVQPLLD--ALEEIAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
8-289 |
4.72e-33 |
|
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: 123.75 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTWK--SPPGQVTEA-----VKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvvKRQDLFIVS 77
Cdd:COG0667 8 RSGLKVSRLGLGTMTfgGPWGGVDEAeaiaiLDAALDAGINFFDTADVYgpgRSEELLGEALKGR------PRDDVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 78 KLWCTFHDqsmvkgacqktlsdlqldyldlylihWPTGFKPGPDYFP--LDAS-----GNVI--------PSDTDFVDTW 142
Cdd:COG0667 82 KVGRRMGP--------------------------GPNGRGLSREHIRraVEASlrrlgTDYIdlyqlhrpDPDTPIEETL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 143 TAMEQLVDEGLVKAIGVSNFNPLQIERILNKPGLKYKPAVNQIEchpY--LTQ---EKLIEYCHCKGIVVTAYSPLGS-- 215
Cdd:COG0667 136 GALDELVREGKIRYIGVSNYSAEQLRRALAIAEGLPPIVAVQNE---YslLDRsaeEELLPAARELGVGVLAYSPLAGgl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 216 -------------PDR-------PWAKPEDPSLLEdpRIKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAEN 273
Cdd:COG0667 213 ltgkyrrgatfpeGDRaatnfvqGYLTERNLALVD--ALRAIAAEHGVTPAQLALAWLLAQPGVtsVIPGARSPEQLEEN 290
|
330
....*....|....*.
gi 1168407 274 FKVFDFELSNEDMATL 289
Cdd:COG0667 291 LAAADLELSAEDLAAL 306
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-289 |
3.23e-29 |
|
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: 113.07 E-value: 3.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGTW---------KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEKlkeqvvkRQDLFIVSKLW- 80
Cdd:cd19085 2 SRLGLGCWqfgggywwgDQDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKGR-------RDDVVIATKVSp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 81 CTFHDQSMVKgACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnvipSDTDFVDTWTAMEQLVDEGLVKAIGVS 160
Cdd:cd19085 75 DNLTPEDVRK-SCERSLKRLGTDYIDLYQIHWPS-------------------SDVPLEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 161 NFNPLQIERILnKPGlkyKPAVNQIECHPYLTQ-EK-LIEYCHCKGIVVTAYSPL------GSPDRPWAKPED------P 226
Cdd:cd19085 135 NFGPAQLEEAL-DAG---RIDSNQLPYNLLWRAiEYeILPFCREHGIGVLAYSPLaqglltGKFSSAEDFPPGdartrlF 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1168407 227 SLLEDP----------RIKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19085 211 RHFEPGaeeetfealeKLKEIADELGVTMAQLALAWVLQQPGVtsVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
12-287 |
1.09e-25 |
|
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: 103.76 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 12 KMPTLGLGTW--------KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEKlkeqvvkRQDLFIVSKL- 79
Cdd:cd19084 3 KVSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR-------RDDVVIATKCg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 80 ------WCTFHD---QSMVKgAC---------------QktlsdlqldyldlylIHWPtgfkpgpDYfpldasgnvipsD 135
Cdd:cd19084 76 lrwdggKGVTKDlspESIRK-EVeqslrrlqtdyidlyQ---------------IHWP-------DP------------N 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 136 TDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERIlnkpgLKY-KPAVNQIechPY--LTQ---EKLIEYCHCKGIVVTA 209
Cdd:cd19084 121 TPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-----RKYgPIVSLQP---PYsmLEReieEELLPYCRENGIGVLP 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 210 YSPLG--------------SPD---------RPWAKPEDPSLLEdpRIKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKS 264
Cdd:cd19084 193 YGPLAqglltgkykkeptfPPDdrrsrfpffRGENFEKNLEIVD--KLKEIAEKYGKSLAQLAIAWTLAQPGVtsAIVGA 270
|
330 340
....*....|....*....|...
gi 1168407 265 VTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19084 271 KNPEQLEENAGALDWELTEEELK 293
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-285 |
2.46e-25 |
|
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: 102.63 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTW-----KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGvalqEKLKEQVVKRQDLFIVSKl 79
Cdd:cd19092 1 PEGLEVSRLVLGCMrladwGESAEELLSLIEAALELGITTFDHADIYGGgkcEELFG----EALALNPGLREKIEIQTK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 80 wctfhdqsmvkgacqktlsdlqldyldlylihwpTGFKPGPDYFP-----LDASG-NVIPS--------DTDFVD----- 140
Cdd:cd19092 76 ----------------------------------CGIRLGDDPRPgrikhYDTSKeHILASvegslkrlGTDYLDllllh 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 141 ----------TWTAMEQLVDEGLVKAIGVSNFNPLQIErILNKpGLKYKPAVNQIEC---HPYLTQEKLIEYCHCKGIVV 207
Cdd:cd19092 122 rpdplmdpeeVAEAFDELVKSGKVRYFGVSNFTPSQIE-LLQS-YLDQPLVTNQIELsllHTEAIDDGTLDYCQLLDITP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 208 TAYSPLGSpdrpwAKPEDPSLLEDPRI----KEIAAKYNKTTAQV----LIRFPIQrnLVVIPKSVTPARIAENFKVFDF 279
Cdd:cd19092 200 MAWSPLGG-----GRLFGGFDERFQRLraalEELAEEYGVTIEAIalawLLRHPAR--IQPILGTTNPERIRSAVKALDI 272
|
....*.
gi 1168407 280 ELSNED 285
Cdd:cd19092 273 ELTREE 278
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-289 |
1.42e-23 |
|
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: 98.13 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 15 TLGLGTWKSPPGQ------------VTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvvkRQDLFIVSK- 78
Cdd:cd19102 3 TIGLGTWAIGGGGwgggwgpqddrdSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 79 --LW------CTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTGfkpgpdyfpldasgnvipsDTDFVDTWTAMEQLVD 150
Cdd:cd19102 76 glLWdeegriRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDP-------------------DEPIEEAWGALAELKE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 151 EGLVKAIGVSNFNPLQIERIlnkpgLKYKP-AVNQIechPYLTQEKLIE-----YCHCKGIVVTAYSPLGS--------P 216
Cdd:cd19102 137 EGKVRAIGVSNFSVDQMKRC-----QAIHPiASLQP---PYSLLRRGIEaeilpFCAEHGIGVIVYSPMQSglltgkmtP 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 217 DRPWAKPED-----------PSLLEDPRI----KEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDF 279
Cdd:cd19102 209 ERVASLPADdwrrrspffqePNLARNLALvdalRPIAERHGRTVAQLAIAWVLRRPEVtsAIVGARRPDQIDETVGAADL 288
|
330
....*....|
gi 1168407 280 ELSNEDMATL 289
Cdd:cd19102 289 RLTPEELAEI 298
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
17-285 |
5.16e-21 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 90.98 E-value: 5.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 17 GLGTWKSPPGQVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALqeklKEQVVKRQDLFIVSKlwCTfhdqsmvkgac 93
Cdd:COG4989 22 RLGEWDLSPAEAAALIEAALELGITTFDHADIYggyTCEALFGEAL----KLSPSLREKIELQTK--CG----------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 94 qktlsdlqldyldlylIHWPTGFKP-GPDYFPLDASgNVIPS--------DTDFVDTW---------------TAMEQLV 149
Cdd:COG4989 85 ----------------IRLPSEARDnRVKHYDTSKE-HIIASvegslrrlGTDYLDLLllhrpdplmdpeevaEAFDELK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 150 DEGLVKAIGVSNFNPLQIErILNKpGLKYKPAVNQIECHPYLTQ---EKLIEYCHCKGIVVTAYSPLGSPDrpWAKPEDP 226
Cdd:COG4989 148 ASGKVRHFGVSNFTPSQFE-LLQS-ALDQPLVTNQIELSLLHTDafdDGTLDYCQLNGITPMAWSPLAGGR--LFGGFDE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1168407 227 sllEDPRIK----EIAAKYNKTTAQVLI----RFPIqrNLVVIPKSVTPARIAENFKVFDFELSNED 285
Cdd:COG4989 224 ---QFPRLRaaldELAEKYGVSPEAIALawllRHPA--GIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-215 |
9.46e-20 |
|
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: 86.03 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGTWK-SPPGQVTEAVKV---AIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvVKRQDLFIVSKLWctfhdq 86
Cdd:cd06660 1 SRLGLGTMTfGGDGDEEEAFALldaALEAGGNFFDTADVYgdgRSERLLGRWLKGR-----GNRDDVVIATKGG------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 smvkgacqktlsdlqldyldlyliHWPTGFKPGPDYFP------LDAS----GnvipsdTDFVD---------------T 141
Cdd:cd06660 70 ------------------------HPPGGDPSRSRLSPehirrdLEESlrrlG------TDYIDlyylhrddpstpveeT 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1168407 142 WTAMEQLVDEGLVKAIGVSNFNPLQIERILN--KPGLKYKPAVNQIE---CHPYLTQEKLIEYCHCKGIVVTAYSPLGS 215
Cdd:cd06660 120 LEALNELVREGKIRYIGVSNWSAERLAEALAyaKAHGLPGFAAVQPQyslLDRSPMEEELLDWAEENGLPLLAYSPLAR 198
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-282 |
2.27e-18 |
|
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: 82.65 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 13 MPTLGLGTWKSPPGQvTEAVKV---AIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvvkRQDLFIVSKLwctfhdq 86
Cdd:cd19088 9 MRLTGPGIWGPPADR-EEAIAVlrrALELGVNFIDTADSYgpdVNERLIAEALHPY-------PDDVVIATKG------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 87 smvkGAcqktlsdlqldyldlylihwptgFKPGPDYFPLDAS----------------GNVIP--------SDTDFVDTW 142
Cdd:cd19088 74 ----GL-----------------------VRTGPGWWGPDGSpeylrqaveaslrrlgLDRIDlyqlhridPKVPFEEQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 143 TAMEQLVDEGLVKAIGVSNFNPLQIERILNKPGLkykpAVNQIECHPYLTQ-EKLIEYCHCKGIVVTAYSPLGSpdRPWA 221
Cdd:cd19088 127 GALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI----VSVQNRYNLANRDdEGVLDYCEAAGIAFIPWFPLGG--GDLA 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168407 222 KPEDPslledprIKEIAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPARIAENFKVFDFELS 282
Cdd:cd19088 201 QPGGL-------LAEVAARLGATPAQVALAWLLARspVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
32-291 |
8.14e-15 |
|
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: 73.61 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 32 VKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvvKRQDLFIVSKLWCTFHDQSMV--------KGACQKTLSDL 100
Cdd:cd19083 39 VREALDNGVNLLDTAFIYglgRSEELVGEVLKEY------NRNEVVIATKGAHKFGGDGSVlnnspeflRSAVEKSLKRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 101 QLDYLDLYLIHWPTGfkpgpdyfpldasgnvipsDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERiLNKPGlkykp 180
Cdd:cd19083 113 NTDYIDLYYIHFPDG-------------------ETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE-ANKDG----- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 181 AVNQIEcHPY-LTQ----EKLIEYCHCKGIVVTAYSPLGS-------------PDRPWAKpeDPSLLEDP---------- 232
Cdd:cd19083 168 YVDVLQ-GEYnLLQreaeEDILPYCVENNISFIPYFPLASgllagkytkdtkfPDNDLRN--DKPLFKGErfsenldkvd 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168407 233 RIKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFELSNEDMATLLS 291
Cdd:cd19083 245 KLKSIADEKGVTVAHLALAWYLTRPAIdvVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDA 305
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
140-291 |
2.88e-14 |
|
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: 71.92 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 140 DTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNkpglKYKPAVNQIechPY-----LTQEKLIEYCHCKGIVVTAYSPLG 214
Cdd:cd19149 143 ETMEALEELKRQGKIRAIGASNVSVEQIKEYVK----AGQLDIIQE---KYsmldrGIEKELLPYCKKNNIAFQAYSPLE 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 215 S--------PDR-----------PWAKPEDPS----LLEdpRIKEIAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPAR 269
Cdd:cd19149 216 QglltgkitPDRefdagdarsgiPWFSPENREkvlaLLE--KWKPLCEKYGCTLAQLVIAWTLAQpgITSALCGARKPEQ 293
|
170 180
....*....|....*....|..
gi 1168407 270 IAENFKVFDFELSNEDMATLLS 291
Cdd:cd19149 294 AEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
140-289 |
5.12e-14 |
|
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: 71.12 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 140 DTWTAMEQLVDEGLVKAIGVSNFNPLQIERILnkpglKYKP-AVNQIECHPyLTQEKL----IEYCHCKGIVVTAYSPL- 213
Cdd:cd19077 129 ETIKALKELVKEGKIRGIGLSEVSAETIRRAH-----AVHPiAAVEVEYSL-FSREIEengvLETCAELGIPIIAYSPLg 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 214 -----GSPDRPWAKPEDPSLLEDPR---------------IKEIAAKYNKTTAQVLIRFPIQRN---LVVIPKSVTPARI 270
Cdd:cd19077 203 rglltGRIKSLADIPEGDFRRHLDRfngenfeknlklvdaLQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERV 282
|
170
....*....|....*....
gi 1168407 271 AENFKVFDFELSNEDMATL 289
Cdd:cd19077 283 EENLKAANVELTDEELKEI 301
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
8-289 |
1.08e-13 |
|
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: 70.31 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGT----------WKSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEklkeqVVKRQDLF 74
Cdd:cd19079 7 NSGLKVSRLCLGCmsfgdpkwrpWVLDEEESRPIIKRALDLGINFFDTANVYSGgasEEILGRALKE-----FAPRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 75 IVSKLWCTFHDQSMVKG--------ACQKTLSDLQLDYLDLYLIHWptgfkpgPDYfpldasgnvipsDTDFVDTWTAME 146
Cdd:cd19079 82 IATKVYFPMGDGPNGRGlsrkhimaEVDASLKRLGTDYIDLYQIHR-------WDY------------ETPIEETLEALH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 147 QLVDEGLVKAIGVSNFNPLQIERILN---KPGLKyKPAVNQiecHPY--LTQE---KLIEYCHCKGIVVTAYSPL----- 213
Cdd:cd19079 143 DVVKSGKVRYIGASSMYAWQFAKALHlaeKNGWT-KFVSMQ---NHYnlLYREeerEMIPLCEEEGIGVIPWSPLargrl 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 214 -----GSPDRPWAKPEDPSLLED----------PRIKEIAAKYNKTTAQVLIRFPIQRNLVVIP--KSVTPARIAENFKV 276
Cdd:cd19079 219 arpwgDTTERRRSTTDTAKLKYDyfteadkeivDRVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAA 298
|
330
....*....|...
gi 1168407 277 FDFELSNEDMATL 289
Cdd:cd19079 299 LDIKLSEEEIKYL 311
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
35-289 |
1.95e-12 |
|
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: 66.47 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 35 AIDMGYRHIDCAQVYQ---NEKEVGVALQEKlkeqvvkRQDLFIVSKlwctfhdqsmvkgacqktlsdlqldyldlylih 111
Cdd:cd19076 41 ALELGVTFLDTADMYGpgtNEELLGKALKDR-------RDEVVIATK--------------------------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 112 WPTGFKPGPDYFPLDAS-GNV-----------------------IPSDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQI 167
Cdd:cd19076 81 FGIVRDPGSGFRGVDGRpEYVraaceaslkrlgtdvidlyyqhrVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 168 ERilnkpGLKYKP--AVnQIEchpYLTQEKLIE-----YCHCKGIVVTAYSPL------GSPDRPWAKPEDPSLLEDPR- 233
Cdd:cd19076 161 RR-----AHAVHPitAV-QSE---YSLWTRDIEdevlpTCRELGIGFVAYSPLgrgfltGAIKSPEDLPEDDFRRNNPRf 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168407 234 --------------IKEIAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19076 232 qgenfdknlklvekLEAIAAEKGCTPAQLALAWVLAQgdDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
8-289 |
9.05e-12 |
|
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: 64.77 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGT-----WKSPPGQVTEAVKV---AIDMGYRHIDCAQVYQ-NEKEVGVALqeklKEQVVKRQDLFIVSK 78
Cdd:cd19144 8 RNGPSVPALGFGAmglsaFYGPPKPDEERFAVldaAFELGCTFWDTADIYGdSEELIGRWF----KQNPGKREKIFLATK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 79 L----------WCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHwptgfkpgpdyfPLDASgnvIPSDTdfvdTWTAMEQL 148
Cdd:cd19144 84 FgieknvetgeYSVDGSPEYVKKACETSLKRLGVDYIDLYYQH------------RVDGK---TPIEK----TVAAMAEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 149 VDEGLVKAIGVSNFNPLQIERilnkpGLKYKP--AVnQIECHPYLT-----QEKLIEYCHCKGIVVTAYSPLG------- 214
Cdd:cd19144 145 VQEGKIKHIGLSECSAETLRR-----AHAVHPiaAV-QIEYSPFSLdierpEIGVLDTCRELGVAIVAYSPLGrgfltga 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 215 --SPD----------RPWAKPED-PSLLE--DpRIKEIAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPARIAENFKVF 277
Cdd:cd19144 219 irSPDdfeegdfrrmAPRFQAENfPKNLElvD-KIKAIAKKKNVTAGQLTLAWLLAQgdDIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|..
gi 1168407 278 DFELSNEDMATL 289
Cdd:cd19144 298 KVKLTEEEEKEI 309
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
17-213 |
1.01e-11 |
|
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: 64.64 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 17 GLGTWK--------SPPGQVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALqeklkEQVVKRQDLFIVSKLWCTFHD 85
Cdd:cd19148 8 ALGTWAiggwmwggTDEKEAIETIHKALDLGINLIDTAPVYgfgLSEEIVGKAL-----KEYGKRDRVVIATKVGLEWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKGACQKTLSDLQLDYLDL---------YLIHWPTgfkpgpdyfpldasgnvipSDTDFVDTWTAMEQLVDEGLVKA 156
Cdd:cd19148 83 GGEVVRNSSPARIRKEVEDSLRrlqtdyidlYQVHWPD-------------------PLVPIEETAEALKELLDEGKIRA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168407 157 IGVSNFNPLQIERILNKPGLkykpAVNQIechPYLTQEKLIE-----YCHCKGIVVTAYSPL 213
Cdd:cd19148 144 IGVSNFSPEQMETFRKVAPL----HTVQP---PYNLFEREIEkdvlpYARKHNIVTLAYGAL 198
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
134-289 |
3.17e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 63.00 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 134 SDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNKPglkYKPAVNQIEC-----HPyltQEKLIEYCHCKGIVVT 208
Cdd:cd19101 117 SDPGYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDAG---VPIVSNQVQYslldrRP---ENGMAALCEDHGIKLL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 209 AYSP----------LGSPDRPWAKPEDPSLLEDPRI-----------------KEIAAKYNKTTAQVLIRFPIQRNLV-- 259
Cdd:cd19101 191 AYGTlaggllsekyLGVPEPTGPALETRSLQKYKLMidewggwdlfqellrtlKAIADKHGVSIANVAVRWVLDQPGVag 270
|
170 180 190
....*....|....*....|....*....|....
gi 1168407 260 VIpksvTPAR----IAENFKVFDFELSNEDMATL 289
Cdd:cd19101 271 VI----VGARnsehIDDNVRAFSFRLDDEDRAAI 300
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-273 |
5.23e-11 |
|
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: 61.87 E-value: 5.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGTWK-------SPPGQVTEAVKVAIDMGYRHIDCAQVYQN-EKEVGVALQEklkeqvVKRQDLFIVSKLWCTFHD 85
Cdd:cd19095 1 SVLGLGTSGigrvwgvPSEAEAARLLNTALDLGINLIDTAPAYGRsEERLGRALAG------LRRDDLFIATKVGTHGEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 QSMVKgacqktlsdlqldyldlylihwptgfkpgpDYFP------LDAS---------------GNVIPSDTDfvDTWTA 144
Cdd:cd19095 75 GRDRK------------------------------DFSPaairasIERSlrrlgtdyidllqlhGPSDDELTG--EVLET 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 145 MEQLVDEGLVKAIGVSNFNPLqIERILNKPGLkykpAVNQIechPY----LTQEKLIEYCHCKGIVVTAYSPLGSPDRPW 220
Cdd:cd19095 123 LEDLKAAGKVRYIGVSGDGEE-LEAAIASGVF----DVVQL---PYnvldREEEELLPLAAEAGLGVIVNRPLANGRLRR 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1168407 221 AKPEDPSLLEDPRIKEIAAKYN-KTTAQVLIRFPIQRNLV--VIPKSVTPARIAEN 273
Cdd:cd19095 195 RVRRRPLYADYARRPEFAAEIGgATWAQAALRFVLSHPGVssAIVGTTNPEHLEEN 250
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
140-289 |
8.02e-11 |
|
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: 61.85 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 140 DTWTAMEQLVDEGLVKAIGVSNFNPLQIERILnkpGLKYKPAVNQIEC---HPYLTQEKLIEY-----CHCKGIVVTAYS 211
Cdd:cd19081 132 ETLGALNDLIRQGKVRYIGASNYSAWRLQEAL---ELSRQHGLPRYVSlqpEYNLVDRESFEGellplCREEGIGVIPYS 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 212 PLGS--------PDRPWAK----PEDPSLLEDPR-------IKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARI 270
Cdd:cd19081 209 PLAGgfltgkyrSEADLPGstrrGEAAKRYLNERglrildaLDEVAAEHGATPAQVALAWLLARPGVtaPIAGARTVEQL 288
|
170
....*....|....*....
gi 1168407 271 AENFKVFDFELSNEDMATL 289
Cdd:cd19081 289 EDLLAAAGLRLTDEEVARL 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
109-287 |
1.13e-10 |
|
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: 61.43 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 109 LIHWP---TGFKPGPDYFPLDASGNVIPsdtdFVDTWTAMEQLVDEGLVKAIGVSNFNP------LQIERILNKPglkyK 179
Cdd:cd19094 118 QLHWPdryTPLFGGGYYTEPSEEEDSVS----FEEQLEALGELVKAGKIRHIGLSNETPwgvmkfLELAEQLGLP----R 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 180 PAVNQiecHPY--LTQ---EKLIEYCHCKGIVVTAYSPLG----------SPDRpwakPEDPSLLEDPRI---------- 234
Cdd:cd19094 190 IVSIQ---NPYslLNRnfeEGLAEACHRENVGLLAYSPLAggvltgkyldGAAR----PEGGRLNLFPGYmaryrspqal 262
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1168407 235 ------KEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19094 263 eavaeyVKLARKHGLSPAQLALAWVRSRPFVtsTIIGATTLEQLKENIDAFDVPLSDELLA 323
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
8-289 |
1.25e-10 |
|
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: 61.48 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGT--------WKSPPGQVTEA-----VKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKlkeqvvkRQ 71
Cdd:cd19091 8 RSGLKVSELALGTmtfgggggFFGAWGGVDQEeadrlVDIALDAGINFFDTADVYsegESEEILGKALKGR-------RD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 72 DLFIVSKlwctfhdqsmvkgacqktlsdlqldyldlylihwpTGFKPGPDyfpLDASG----NVIPS--------DTDFV 139
Cdd:cd19091 81 DVLIATK-----------------------------------VRGRMGEG---PNDVGlsrhHIIRAveaslkrlGTDYI 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 140 D---------------TWTAMEQLVDEGLVKAIGVSNFNPLQIERIL---NKPGLKyKPAVNQI-----------ECHPY 190
Cdd:cd19091 123 DlyqlhgfdaltpleeTLRALDDLVRQGKVRYIGVSNFSAWQIMKALgisERRGLA-RFVALQAyysllgrdlehELMPL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 191 LTQEKLieychckGIVVtaYSPLG--------SPDRPwaKPEDPSL---------LEDPRI-------KEIAAKYNKTTA 246
Cdd:cd19091 202 ALDQGV-------GLLV--WSPLAggllsgkyRRGQP--APEGSRLrrtgfdfppVDRERGydvvdalREIAKETGATPA 270
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1168407 247 QVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:cd19091 271 QVALAWLLSRPTVssVIIGARNEEQLEDNLGAAGLSLTPEEIARL 315
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-284 |
4.65e-10 |
|
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: 59.53 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGTWKSPPGQVT-----EAVKVAIDMGYRHIDCAQVY---QNEKEVGVALQEklkeqvVKRQDLFIVSKLWC 81
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDdedakACVRKAYDLGINFFDTADVYaagQAEEVLGKALKG------WPRESYVISTKVFW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 82 TFHDQSMVKG--------ACQKTLSDLQLDYLDLYLIHwptgfKPGPdyfpldasgnvipsDTDFVDTWTAMEQLVDEGL 153
Cdd:cd19074 75 PTGPGPNDRGlsrkhifeSIHASLKRLQLDYVDIYYCH-----RYDP--------------ETPLEETVRAMDDLIRQGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 154 VKAIGVSNFNPLQIE---RILNKPGLkYKPAVNQIECHpYLTQEK---LIEYCHCKGIVVTAYSPLGS------------ 215
Cdd:cd19074 136 ILYWGTSEWSAEQIAeahDLARQFGL-IPPVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQglltgkyrdgip 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 216 -PDRPWAKPEDP-----SLLEDPRI------KEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFEL 281
Cdd:cd19074 214 pPSRSRATDEDNrdkkrRLLTDENLekvkklKPIADELGLTLAQLALAWCLRNPAVssAIIGASRPEQLEENVKASGVKL 293
|
...
gi 1168407 282 SNE 284
Cdd:cd19074 294 SPE 296
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-289 |
1.08e-09 |
|
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: 58.50 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 11 TKMPTLGLGTWK--SP-------------PGQVTEAVKVAIDMGYRHIDCAQVYqnekevGVALQEKLKEQVVK---RQD 72
Cdd:cd19103 2 KKLPKIALGTWSwgSGgaggdqvfgnhldEDTLKAVFDKAMAAGLNLWDTAAVY------GMGASEKILGEFLKrypRED 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 73 LFIVSKLWCTFHDQS------MVKGACQKTlsdlqldyldlylihwptgfkpGPDYFPLDASGNviPSDtdfVDTWTamE 146
Cdd:cd19103 76 YIISTKFTPQIAGQSadpvadMLEGSLARL----------------------GTDYIDIYWIHN--PAD---VERWT--P 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 147 QLVD---EGLVKAIGVSNFNPLQIER---ILNKPGLKykpaVNQIECH---PYLTQEK--LIEYCHCKGIVVTAYSPL-- 213
Cdd:cd19103 127 ELIPllkSGKVKHVGVSNHNLAEIKRaneILAKAGVS----LSAVQNHyslLYRSSEEagILDYCKENGITFFAYMVLeq 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 214 ----GSPDRPWAKPEDPSLLED-----PRI-------KEIAAKYNKTTAQVLIRFPIQRNLVVIPKSVTPARIAENFKVF 277
Cdd:cd19103 203 galsGKYDTKHPLPEGSGRAETynpllPQLeeltavmAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAA 282
|
330
....*....|..
gi 1168407 278 DFELSNEDMATL 289
Cdd:cd19103 283 SITLTDDEIKEL 294
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
16-276 |
2.53e-09 |
|
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: 56.72 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 16 LGLGTW--------KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEKlkeqvvkRQDLFIVSKLWCTFH 84
Cdd:cd19086 6 IGFGTWglggdwwgDVDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKGR-------RDKVVIATKFGNRFD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 85 DQ---------SMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpdyfpldasgnviPSDTDFVDTWTAMEQLVDEGLVK 155
Cdd:cd19086 79 GGperpqdfspEYIREAVEASLKRLGTDYIDLYQLHNPP------------------DEVLDNDELFEALEKLKQEGKIR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 156 AIGVSNFNPLQIERILNKPGLKykpAV----NQIECHPYltqEKLIEYCHCKGIVVTAYSPLGSpdrpwakpedpSLLED 231
Cdd:cd19086 141 AYGVSVGDPEEALAALRRGGID---VVqviyNLLDQRPE---EELFPLAEEHGVGVIARVPLAS-----------GLLTG 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1168407 232 prikeiaakynkTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKV 276
Cdd:cd19086 204 ------------KLAQAALRFILSHPAVstVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
135-273 |
5.48e-09 |
|
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: 56.19 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 135 DTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIER---ILNKPGLKYKPAVNQIecHPYL--------------TQEkLI 197
Cdd:cd19752 124 DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERarqIARQQGWAEFSAIQQR--HSYLrprpgadfgvqrivTDE-LL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 198 EYCHCKG-IVVTAYSPL--GSPDRPWAKPEDPSLLEDPR-----IKEIAAKYNKTTAQVLIRFPIQRNLVVIP--KSVTP 267
Cdd:cd19752 201 DYASSRPdLTLLAYSPLlsGAYTRPDRPLPEQYDGPDSDarlavLEEVAGELGATPNQVVLAWLLHRTPAIIPllGASTV 280
|
....*.
gi 1168407 268 ARIAEN 273
Cdd:cd19752 281 EQLEEN 286
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-78 |
5.45e-08 |
|
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: 53.48 E-value: 5.45e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1168407 15 TLGLGTWKSPPG-----QVTEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEKLKEQVVKRQDLFIVSK 78
Cdd:cd19099 5 SLGLGTYRGDSDdetdeEYREALKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTK 76
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
8-276 |
5.48e-08 |
|
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: 52.97 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTWKSPPGQVtEAVKVAIDMGYRHIDCAQVYQN---EKEVGVALQEklkeqvVKRQDLFIVSKLWCT-- 82
Cdd:cd19105 8 KTGLKVSRLGFGGGGLPRESP-ELLRRALDLGINYFDTAEGYGNgnsEEIIGEALKG------LRRDKVFLATKASPRld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 83 FHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpGPDYFPLDasGNVIPsdtdfvdtwtAMEQLVDEGLVKAIGVSNF 162
Cdd:cd19105 81 KKDKAELLKSVEESLKRLQTDYIDIYQLHGVD----TPEERLLN--EELLE----------ALEKLKKEGKVRFIGFSTH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 163 NPLQ--IERILNKPG-----LKYKPAvnqiecHPYLTQEKLIEYCHCKGIVVTAYSPLGS-PDRPWAKPEDPSLLEDPri 234
Cdd:cd19105 145 DNMAevLQAAIESGWfdvimVAYNFL------NQPAELEEALAAAAEKGIGVVAMKTLAGgYLQPALLSVLKAKGFSL-- 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1168407 235 keiaakynkttAQVLIRFPIQRNLV--VIPKSVTPARIAENFKV 276
Cdd:cd19105 217 -----------PQAALKWVLSNPRVdtVVPGMRNFAELEENLAA 249
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
27-289 |
5.55e-07 |
|
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: 50.31 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 27 QVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALqEKLKEQVVkrqdlfIVSKLWCTFHDQSMvkgacqktlsdlqld 103
Cdd:cd19078 26 EMIELIRKAVELGITFFDTAEVYgpyTNEELVGEAL-KPFRDQVV------IATKFGFKIDGGKP--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 104 yldlyliHWPTgfkpgpdyfpLDASGNVIPS---------DTDFVDTW---------------TAMEQLVDEGLVKAIGV 159
Cdd:cd19078 84 -------GPLG----------LDSRPEHIRKavegslkrlQTDYIDLYyqhrvdpnvpieevaGTMKELIKEGKIRHWGL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 160 SNFNPLQIERilnkpGLKYKP--AVnQIECH-----PyltQEKLIEYCHCKGIVVTAYSPLGS--------PDRPWAKPE 224
Cdd:cd19078 147 SEAGVETIRR-----AHAVCPvtAV-QSEYSmmwreP---EKEVLPTLEELGIGFVPFSPLGKgfltgkidENTKFDEGD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 225 DPSLLedPR---------------IKEIAAKYNKTTAQV-----LIRFPiqrNLVVIPKSVTPARIAENFKVFDFELSNE 284
Cdd:cd19078 218 DRASL--PRftpealeanqalvdlLKEFAEEKGATPAQIalawlLAKKP---WIVPIPGTTKLSRLEENIGAADIELTPE 292
|
....*
gi 1168407 285 DMATL 289
Cdd:cd19078 293 ELREI 297
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-284 |
7.65e-07 |
|
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: 49.47 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGT--WKSPPGQVT-----EAVKVAIDMGYRHIDCAQVYQN-EKEVGVALQEklkeqvVKRQDLFIVSKLWC---T 82
Cdd:cd19090 1 SALGLGTagLGGVFGGVDddeavATIRAALDLGINYIDTAPAYGDsEERLGLALAE------LPREPLVLSTKVGRlpeD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 83 FHDQS--MVKGA---------------CQktlsdlqldyldlylIHwptgfkpGPDYFPLDAS---GNVIPsdtdfvdtw 142
Cdd:cd19090 75 TADYSadRVRRSveeslerlgrdridlLM---------------IH-------DPERVPWVDIlapGGALE--------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 143 tAMEQLVDEGLVKAIGVSNfNPLQIERILNKPGLkykpaVNQIECHPYLT------QEKLIEYCHCKGIVVTAYSPLGS- 215
Cdd:cd19090 124 -ALLELKEEGLIKHIGLGG-GPPDLLRRAIETGD-----FDVVLTANRYTlldqsaADELLPAAARHGVGVINASPLGMg 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 216 ------PDRPWAKPEDPSLLEDPR---IKEIAAKYNKTTAQVLIRFPIQRNLV--VIPKSVTPARIAENFKVFDFELSNE 284
Cdd:cd19090 197 llagrpPERVRYTYRWLSPELLDRakrLYELCDEHGVPLPALALRFLLRDPRIstVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
16-289 |
1.02e-06 |
|
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: 49.35 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 16 LGLGTWKSPPGQVTEAVKV---AIDMGYRHIDCAQVY---QNEKEVGVALQEKLKEQVVkrqdlfIVSKLWCTFHDQS-- 87
Cdd:cd19145 20 MGLSGDYGAPKPEEEGIALihhAFNSGVTFLDTSDIYgpnTNEVLLGKALKDGPREKVQ------LATKFGIHEIGGSgv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 88 -------MVKGACQKTLSDLQLDYLDLYLIHwptgfkpgpdyfPLDASgnvIPSDtdfvDTWTAMEQLVDEGLVKAIGVS 160
Cdd:cd19145 94 evrgdpaYVRAACEASLKRLDVDYIDLYYQH------------RIDTT---VPIE----ITMGELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 161 NFNPLQIERilnkpglkyKPAVN-----QIECHPYL--TQEKLIEYCHCKGIVVTAYSPLGspdRP--WAKPEDPSLLED 231
Cdd:cd19145 155 EASADTIRR---------AHAVHpitavQLEWSLWTrdIEEEIIPTCRELGIGIVPYSPLG---RGffAGKAKLEELLEN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 232 -------PRIKE---------------IAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPARIAENFKVFDFELSNEDMA 287
Cdd:cd19145 223 sdvrkshPRFQGenleknkvlyerveaLAKKKGCTPAQLALAWVLHQgeDVVPIPGTTKIKNLNQNIGALSVKLTKEDLK 302
|
..
gi 1168407 288 TL 289
Cdd:cd19145 303 EI 304
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
134-236 |
1.69e-06 |
|
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: 48.72 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 134 SDTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILN---KPGL--------KYKPAVNQIECHpyltqekLIEYCHC 202
Cdd:cd19087 123 RDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGiaaRRGLlrfvseqpMYNLLKRQAELE-------ILPAARA 195
|
90 100 110
....*....|....*....|....*....|....*....
gi 1168407 203 KGIVVTAYSPLGS-----PDRPWAKPEDPSLLEDPRIKE 236
Cdd:cd19087 196 YGLGVIPYSPLAGglltgKYGKGKRPESGRLVERARYQA 234
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-226 |
4.84e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 46.71 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 10 GTKMPTLGLGT---WKSPPGQVTEAVKVAIDMGYRHIDCAQVYQN-EKEVGVALQEKlkeqvvkRQDLFIVSKLWCTfhd 85
Cdd:cd19100 8 GLKVSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYGDsEEKIGKALKGR-------RDKVFLATKTGAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 86 qsMVKGACQ---------KTLSDLqldyldLYLIHwptGFKPGPDYFPLDASGNVIpsdtdfvdtwTAMEQLVDEGLVKA 156
Cdd:cd19100 78 --DYEGAKRdlerslkrlGTDYID------LYQLH---AVDTEEDLDQVFGPGGAL----------EALLEAKEEGKIRF 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 157 IGVSNFNPLQIERILNKPG----LkykPAVNQIECHPYLTQEKLIEYCHCKGIVVTAYSPLGSPDRPWAKPEDP 226
Cdd:cd19100 137 IGISGHSPEVLLRALETGEfdvvL---FPINPAGDHIDSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP 207
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
143-289 |
6.62e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 46.89 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 143 TAMEQLVDEGLVKAIGVSNFNPLQIERilnkpGLKYKPAVNqIECHPYLTQ---EKLIEYCHCKGIVVTAYSPLG--SPd 217
Cdd:PRK10376 148 TVLAELQRQGLVRHIGLSNVTPTQVAE-----ARKIAEIVC-VQNHYNLAHradDALIDALARDGIAYVPFFPLGgfTP- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 218 rpwakpedpslLEDPRIKEIAAKYNKTTAQVLIRFPIQR--NLVVIPKSVTPARIAENFKVFDFELSNEDMATL 289
Cdd:PRK10376 221 -----------LQSSTLSDVAASLGATPMQVALAWLLQRspNILLIPGTSSVAHLRENLAAAELVLSEEVLAEL 283
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-252 |
8.60e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 46.37 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 16 LGLGTW-------------KSPPGQVTEAVKVAIDMGYRHIDCAQVYQN-EKEVGVALQEKlkeqvvkrQDLFIVSKL-- 79
Cdd:cd19097 3 LALGTAqfgldygianksgKPSEKEAKKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRL--------DKFKIITKLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 80 --WCTFHDQSMVKGACQKTLSDLQLDYLDLYLIHWPTgfkpgpDyfpLDASGNVIpsdtdfvdtWTAMEQLVDEGLVKAI 157
Cdd:cd19097 75 lkEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPD------D---LLKHGGKL---------VEALLELKKEGLIRKI 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 158 GVSNFNPLQIERILNkpglKYKPAVNQIechPY------LTQEKLIEYCHCKGIVVTAYSP------LGSPDRPWAKPED 225
Cdd:cd19097 137 GVSVYSPEELEKALE----SFKIDIIQL---PFnildqrFLKSGLLAKLKKKGIEIHARSVflqgllLMEPDKLPAKFAP 209
|
250 260
....*....|....*....|....*...
gi 1168407 226 -PSLLEdpRIKEIAAKYNKTTAQVLIRF 252
Cdd:cd19097 210 aKPLLK--KLHELAKKLGLSPLELALGF 235
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
8-287 |
1.68e-05 |
|
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: 45.71 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTWK-----SPPGQVTEAVKVAIDMGYRHIDCAQVY-----QNEKEVGVALQEKLKEqvvKRQDLFIVS 77
Cdd:cd19089 6 RSGLHLPAISLGLWHnfgdyTSPEEARELLRTAFDLGITHFDLANNYgpppgSAEENFGRILKRDLRP---YRDELVIST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 78 KlwctfhdqsmvkgacqktlsdlqldyldlylihwpTGFK--PGP--DY-------FPLDASgnVIPSDTDFVD------ 140
Cdd:cd19089 83 K-----------------------------------AGYGmwPGPygDGgsrkyllASLDQS--LKRMGLDYVDifyhhr 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 141 ---------TWTAMEQLVDEGLVKAIGVSNFNPLQIER---ILNKpgLKYKPAVNQIechPY--LTQ---EKLIEYCHCK 203
Cdd:cd19089 126 ydpdtpleeTMTALADAVRSGKALYVGISNYPGAKARRaiaLLRE--LGVPLIIHQP---RYslLDRwaeDGLLEVLEEA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 204 GIVVTAYSPL-----------GSPDRPWAKPEDPSLLED-------PRIK---EIAAKYNKTTAQVLIRFPIQRNLV--V 260
Cdd:cd19089 201 GIGFIAFSPLaqglltdkylnGIPPDSRRAAESKFLTEEaltpeklEQLRklnKIAAKRGQSLAQLALSWVLRDPRVtsV 280
|
330 340
....*....|....*....|....*...
gi 1168407 261 IPKSVTPARIAENFKVFD-FELSNEDMA 287
Cdd:cd19089 281 LIGASSPSQLEDNVAALKnLDFSEEELA 308
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
137-278 |
2.81e-05 |
|
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: 44.85 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 137 DFVDTwtaMEQLVDEGLVKAIGVSNFNplqIERIL---------NKPGlkykPAVNQI---------ECHPYLT----QE 194
Cdd:cd19082 122 EIVDT---LNELVRAGKIRAFGASNWS---TERIAeanayakahGLPG----FAASSPqwslarpnePPWPGPTlvamDE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 195 KLIEYcHCK-GIVVTAYSPLGS---PDRpwAKPEDPSLLEDP-------------RIKEIAAKYNKTTAQVLIRFPIQRN 257
Cdd:cd19082 192 EMRAW-HEEnQLPVFAYSSQARgffSKR--AAGGAEDDSELRrvyyseenferleRAKELAEEKGVSPTQIALAYVLNQP 268
|
170 180
....*....|....*....|...
gi 1168407 258 LVVIP--KSVTPARIAENFKVFD 278
Cdd:cd19082 269 FPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
8-289 |
4.33e-05 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 44.81 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 8 NNGTKMPTLGLGTW---KSPPGQVTEAVKVAIDMGYRHIDCAQVY-QNEKEVGVALQEKlkeqvvkRQDLFIVSKL---- 79
Cdd:COG1453 8 KTGLEVSVLGFGGMrlpRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILATKLppwv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 80 ------WCTFhDQSMVKgaCQktlsdlqldyldLYLIH-------WPTGFKPGpdyfpldasgnvipsdtdfvDTWTAME 146
Cdd:COG1453 81 rdpedmRKDL-EESLKR--LQtdy-------idLYLIHglnteedLEKVLKPG--------------------GALEALE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 147 QLVDEGLVKAIGVSNFNPLQ-IERILNkpglKYKPAVNQIECHPYLTQ----EKLIEYCHCKGIVVTAYSPLGspdrpwa 221
Cdd:COG1453 131 KAKAEGKIRHIGFSTHGSLEvIKEAID----TGDFDFVQLQYNYLDQDnqagEEALEAAAEKGIGVIIMKPLK------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1168407 222 kpeDPSLLEDP-RIKEIAAKyNKTTAQVLIRFPIQ--RNLVVIPKSVTPARIAENFKVFD-FE-LSNEDMATL 289
Cdd:COG1453 200 ---GGRLANPPeKLVELLCP-PLSPAEWALRFLLShpEVTTVLSGMSTPEQLDENLKTADnLEpLTEEELAIL 268
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-274 |
1.12e-04 |
|
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: 43.12 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 14 PTLGLGTwkSPPG--------QVTEAVKVAIDMGYRHIDCAQVY---QNEKEVGVALQEKLkeqvvkRQDLFIVSKLwct 82
Cdd:cd19162 1 PRLGLGA--ASLGnlaragedEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALARHP------RAEYVVSTKV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 83 fhDQSMVKGAcqktlsdlqldyldlylihwPTGFKPGPDYFPLDASG---NVIPSDT-------DFV------------- 139
Cdd:cd19162 70 --GRLLEPGA--------------------AGRPAGADRRFDFSADGirrSIEASLErlgldrlDLVflhdpdrhllqal 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 140 -DTWTAMEQLVDEGLVKAIGVSNFNPLQIERILNKPGLKykpAVNQIECHPYLTQE---KLIEYCHCKGIVVTAYSPLGS 215
Cdd:cd19162 128 tDAFPALEELRAEGVVGAIGVGVTDWAALLRAARRADVD---VVMVAGRYTLLDRRaatELLPLCAAKGVAVVAAGVFNS 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 216 ---------PDRPWAKPEDPSLLEDP-RIKEIAAKYNKTTAQVLIRFPIQRNLVVipkSV-----TPARIAENF 274
Cdd:cd19162 205 gilatddpaGDRYDYRPATPEVLARArRLAAVCRRYGVPLPAAALQFPLRHPAVA---SVvvgaaSPAELRDNL 275
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
9-214 |
8.61e-04 |
|
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: 40.41 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 9 NGTKMPTLGLGTWKSPPGQVTEAV-----KVAIDMGYRHIDCAQVYQNEKeVGVALQEKLKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19159 9 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYAAGK-AEVILGSIIKKKGWRRSSLVITTKLYWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMvKGACQKtlsdlqldyldlyliHWPTGFKPGPDYFPLD----ASGNVIPSDTDFVDTWTAMEQLVDEGLVKAIGV 159
Cdd:cd19159 88 KAETE-RGLSRK---------------HIIEGLKGSLQRLQLEyvdvVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 160 SNFNPLQI------ERILNkpglKYKPAVNQIECHPYLTQE---KLIEYCHCKGIVVTAYSPLG 214
Cdd:cd19159 152 SRWSAMEImeaysvARQFN----MIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLA 211
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
9-214 |
2.08e-03 |
|
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: 39.30 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 9 NGTKMPTLGLGTWKSPPGQVTEA-----VKVAIDMGYRHIDCAQVYQNEKeVGVALQEKLKEQVVKRQDLFIVSKLWCTF 83
Cdd:cd19158 9 SGLRVSCLGLGTWVTFGGQITDEmaehlMTLAYDNGINLFDTAEVYAAGK-AEVVLGNIIKKKGWRRSSLVITTKIFWGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 84 HDQSMvKGACQKtlsdlqldyldlyliHWPTGFKPGPDYFPLDASGNVIPS----DTDFVDTWTAMEQLVDEGLVKAIGV 159
Cdd:cd19158 88 KAETE-RGLSRK---------------HIIEGLKASLERLQLEYVDVVFANrpdpNTPMEETVRAMTHVINQGMAMYWGT 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1168407 160 SNFNPLQI------ERILNkpglKYKPAVNQIECHPYLTQE---KLIEYCHCKGIVVTAYSPLG 214
Cdd:cd19158 152 SRWSSMEImeaysvARQFN----LIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLA 211
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
135-215 |
4.54e-03 |
|
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: 38.31 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1168407 135 DTDFVDTWTAMEQLVDEGLVKAIGVSNFNPLQIERILN--------KP----GLkYKPAVNQIEchpyltqEKLIEYCHC 202
Cdd:cd19075 108 STPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvLPtvyqGM-YNAITRQVE-------TELFPCLRK 179
|
90
....*....|...
gi 1168407 203 KGIVVTAYSPLGS 215
Cdd:cd19075 180 LGIRFYAYSPLAG 192
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
10-80 |
5.29e-03 |
|
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: 38.20 E-value: 5.29e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1168407 10 GTKMPTLGLGTWKSPPGQVT-----EAVKVAIDMGYRHIDCAQVYQNEKeVGVALQEKLKEQVVKRQDLFIVSKLW 80
Cdd:cd19141 9 GLRVSCLGLGTWVTFGSQISdevaeELVTLAYENGINLFDTAEVYAAGK-AEIVLGKILKKKGWRRSSYVITTKIF 83
|
|
| |
