|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
12-361 |
0e+00 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 654.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATCS 89
Cdd:cd07782 1 YYIGVDVGTGSARAGLFDLDGRLLATASQPITTWNPKPDFYEQSSEDIWQAVCEAVKEVLEgaGVDPEQVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREiCWDKAGHF 169
Cdd:cd07782 81 LVVLDAEGKPVSVSPSGDDERNVILWMDHRAVEEAERINATGHEVLKYVGGKISPEMEPPKLLWLKENLPE-TWAKAGHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 170 FDLPDFLSWKATGVTARSLCSLVCKWTYSA----EKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:cd07782 160 FDLPDFLTWKATGSLTRSLCSLVCKWTYLAhegsEGGWDDDFFKEIGLEDLVEDNFAKIGSVVLPPGEPVGGGLTAEAAK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVrgHGLTCEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07782 240 ELGLPEGTPVGVSLIDAHAGGLGTLGADV--GGLPCEADPLTRRLALICGTSSCHMAVSPEPVFVPGVWGPYYSAMLPGL 317
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720410215 326 WLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARNL 361
Cdd:cd07782 318 WLNEGGQSATGALLDHIIETHPAYPELKEEAKAAGK 353
|
|
| 5C_CHO_kinase |
TIGR01315 |
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of ... |
12-364 |
4.49e-158 |
|
FGGY-family pentulose kinase; This model represents a subfamily of the FGGY family of carbohydrate kinases. This subfamily is closely related to a set of ribulose kinases, and many members are designated ribitol kinase. However, the member from Klebsiella pneumoniae, from a ribitol catabolism operon, accepts D-ribulose and to a lesser extent D-arabinitol and ribitol (and JW Lengeler, personal communication); its annotation in GenBank as ribitol kinase is imprecise and may have affected public annotation of related proteins.
Pssm-ID: 273552 [Multi-domain] Cd Length: 541 Bit Score: 455.51 E-value: 4.49e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDATCS 89
Cdd:TIGR01315 1 HYIGVDVGTGSARACIIDSTGDILALAAQNIKTWTPSSGLEGQSSVYIWQAICNCVKQVLaeSKVDPNSVKGIGFDATCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 90 LVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHF 169
Cdd:TIGR01315 81 LVVLTHDGEPLPVSKNGGADQNIILWMDHRALAEAEKINATNHNLLRYVGGKMSVEMEIPKVLWLKNNMPPE-LFARCKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 170 FDLPDFLSWKATGVTARSLCSLVCKWTY----SAEKGWDDSFWKMIGLEDLIDDNYSKIGNLVLLPGAALGIGLTPEAAR 245
Cdd:TIGR01315 160 FDLTDFLTWRATGKEIRSFCSVVCKWGFvpvdGSNKGWQEDFYETIGLGELVTDNFIRMGGSWMSPGELVGGGLTAEAAQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGHGltcEGQPVTSRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:TIGR01315 240 ELGLPAGTAVGSGLIDAHAGWIGTVGAKVAENG---DVSQAFTRLAAVAGTSTCHMAMTKGPVFVPGVWGPYRDALIPGY 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1720410215 326 WLNEGGQSVTGKLIDHMVQGHPAFPEL--QAKATARNLQKH 364
Cdd:TIGR01315 317 WLAEGGQSAAGELMDHMLETHVAYDETvkEAEAAGKNIYDY 357
|
|
| AraB |
COG1069 |
Ribulose kinase [Carbohydrate transport and metabolism]; |
10-364 |
2.99e-130 |
|
Ribulose kinase [Carbohydrate transport and metabolism];
Pssm-ID: 440687 [Multi-domain] Cd Length: 532 Bit Score: 384.08 E-value: 2.99e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 10 SRYYVGIDVGTGSVRAALVDQR-GLLLAFAEQPIKKWEP---------QFnhhEQSSEDIWAACCLVTKEVVQ--GIDAH 77
Cdd:COG1069 1 EKYVIGVDFGTDSVRAVVVDAAdGEELASAVHPYPRWVIglylppppdQA---RQHPLDYLEALEAAVREALAqaGVDPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 78 RIRGLGFDAT-CSLVVLDKEFHPLPVNHE--GDSSRNVIMWLDHRAVSQVHRINE----TKHRVLQYVGGVMSVEMQAPK 150
Cdd:COG1069 78 DVVGIGVDATgCTPVPVDADGTPLALLPEfaENPHAMVILWKDHTAQEEAERINElakaRGEDYLRYVGGIISSEWFWPK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 151 LLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGW-DDSFWKMIG--LEDLIDdnysKIGN 226
Cdd:COG1069 158 ILHLLREDPEV-YEAADSFVELCDWITWQLTGSLKRSRCTAGHKALWHAhEGGYpSEEFFAALDplLDGLAD----RLGT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 227 LVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVIGAdvrghgltCEGQpvtsrLAVICGTSSCHMGISKD 306
Cdd:COG1069 233 EIYPLGEPAG-TLTAEWAARLGLPPGTAVAVGAIDAHAGAVGAGGV--------EPGT-----LVKVMGTSTCHMLVSPE 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410215 307 PVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKATARNLQKH 364
Cdd:COG1069 299 ERFVPGICGQVDGSIVPGMWGYEAGQSAVGDIFAWFVRLLVPPLEYEKEAEERGISLH 356
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
12-352 |
3.05e-102 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 312.25 E-value: 3.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE-PQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDAT 87
Cdd:cd07768 1 YGIGVDVGTSSARAGVYDlYAGLEMAQEPVPYYQDSsKKSWKFWQKSTEIIKALQKCVQKLNirEGVDAYEVKGCGVDAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 CSLVVLDKEFHPLPVNHEGDSSRNVIMWLDHRAVSQVHRINETKHRVLQ-YVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07768 81 CSLAIFDREGTPLMALIPYPNEDNVIFWMDHSAVNEAQWINMQCPQQLLdYLGGKISPEMGVPKLKYFLDEYSHL-RDKH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 167 GHFFDLPDFLSWKATGVTARSLCSLVCKWTYSA-EKGWDDSFWKMIGLEDLiDDNYSKIGNLVLLPGAALGIGLtPEAAR 245
Cdd:cd07768 160 FHIFDLHDYIAYELTRLYEWNICGLLGKENLDGeESGWSSSFFKNIDPRLE-HLTTTKNLPSNVPIGTTSGVAL-PEMAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 246 ELGLPSGIAVAASLIDAHAGGLGVIGADVRGhgltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGF 325
Cdd:cd07768 238 KMGLHPGTAVVVSCIDAHASWFAVASPHLET------------SLFMIAGTSSCHMYGTTISDRIPGVWGPFDTIIDPDY 305
|
330 340
....*....|....*....|....*..
gi 1720410215 326 WLNEGGQSVTGKLIDHMVQGHPAFPEL 352
Cdd:cd07768 306 SVYEAGQSATGKLIEHLFESHPCARKF 332
|
|
| ASKHA_NBD_FGGY_L-RBK |
cd07781 |
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; ... |
12-356 |
2.82e-95 |
|
nucleotide-binding domain (NBD) of ribulokinase (RBK) and similar proteins; RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466799 [Multi-domain] Cd Length: 504 Bit Score: 293.67 E-value: 2.82e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--PQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA 86
Cdd:cd07781 1 YVIGIDFGTQSVRAGLVDlADGEELASAVVPYPTGYipPRPGWAEQNPADYWEALEEAVRGALAeaGVDPEDVVGIGVDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 87 TCS-LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRV----LQYVGGVMSVEMQAPKLLWLKENLREI 161
Cdd:cd07781 81 TSStVVPVDEDGNPL---------APAILWMDHRAQEEAAEINETAHPAleyyLAYYGGVYSSEWMWPKALWLKRNAPEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 162 cWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDLidDNYSKIGNLVLLPGAALGiGLT 240
Cdd:cd07781 152 -YDAAYTIVEACDWINARLTGRWVRSRCAAGHKWMYNEWGGgPPREFLAALDPGLL--KLREKLPGEVVPVGEPAG-TLT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 241 PEAARELGLPSGIAVAASLIDAHAGglgVIGADVRGHGltcegqpvtsRLAVICGTSSCHMGISKDPVFVPGVWGPYYSA 320
Cdd:cd07781 228 AEAAERLGLPAGIPVAQGGIDAHMG---AIGAGVVEPG----------TLALIMGTSTCHLMVSPKPVDIPGICGPVPDA 294
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1720410215 321 MVPGFWLNEGGQSVTGKLI----DHMV-----QGHPAFPELQAKA 356
Cdd:cd07781 295 VVPGLYGLEAGQSAVGDIFawfvRLFVppaeeRGDSIYALLSEEA 339
|
|
| ASKHA_NBD_FGGY_MPA43-like |
cd07778 |
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; ... |
13-353 |
4.26e-67 |
|
nucleotide-binding domain (NBD) of Saccharomyces cerevisiae protein MPA43 and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Saccharomyces cerevisiae protein MPA43. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466797 [Multi-domain] Cd Length: 544 Bit Score: 221.51 E-value: 4.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPI--KKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATCSL 90
Cdd:cd07778 2 GIGIDVGSTSVRIGIFDYHGTLLATSERPIsyKQDPKDLWFVTQSSTEIWKAIKTALKELIEELSDYIVSGIGVSATCSM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 91 VVLDKE-----FHPLPVNHE-GDSSRNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICW 163
Cdd:cd07778 82 VVMQRDsdtsyLVPYNVIHEkSNPDQDIIFWMDHRASEETQWLNNiLPDDILDYLGGGFIPEMAIPKLKYLIDLIKEDTF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 164 DKAgHFFDLPDFLSWKatgvtarsLCSLVCKW--TYSAE------------KGWDDSFWKMIGLEDLIDDNYSKIGNLVL 229
Cdd:cd07778 162 KKL-EVFDLHDWISYM--------LATNLGHSniVPVNAppsigigidgslKGWSKDFYSKLKISTKVCNVGNTFKEAPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 230 LPGAALGIG-LTPEAARELGLPSGIAVAASLIDAHAGGLGVIgadvrghgltCEGQPVTSRLAVICGTSSCHMGISKDPV 308
Cdd:cd07778 233 LPYAGIPIGkVNVILASYLGIDKSTVVGHGCIDCYAGWFSTF----------AAAKTLDTTLFMVAGTSTCFLYATSSSQ 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1720410215 309 --FVPGVWGPyYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQ 353
Cdd:cd07778 303 vgPIPGIWGP-FDQLLKNYSVYEGGQSATGKLIEKLFNSHPAIIELL 348
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
11-340 |
3.59e-59 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 199.67 E-value: 3.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT- 87
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEQDPEDWWEAVVEAIRELLAkaGVDPEEIAAIGVSGQm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 CSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:COG1070 81 HGLVLLDADGEPL---------RPAILWNDTRAAAEAAELREElgEEALYEITGNPLHPGFTAPKLLWLKENEPEI-FAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 166 AGHFFDLPDFLSWKATG--VTARSLCSlvckWT--YSAEKG-WDDSFWKMIGLEDLIddnyskignL--VLLPGAALGiG 238
Cdd:COG1070 151 IAKVLLPKDYLRYRLTGefVTDYSDAS----GTglLDVRTRdWSDELLEALGIDREL---------LpeLVPPGEVAG-T 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 239 LTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYY 318
Cdd:COG1070 217 LTAEAAAETGLPAGTPVVAGAGDNAAAALGA--------GAVEPGD-----AAVSLGTSGVVFVVSDKPLPDPEGRVHTF 283
|
330 340
....*....|....*....|..
gi 1720410215 319 SAMVPGFWLNEGGQSVTGKLID 340
Cdd:COG1070 284 CHAVPGRWLPMGATNNGGSALR 305
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
12-359 |
2.05e-49 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 172.02 E-value: 2.05e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEPYPTSRPGPGWVEQDPEDWWEALRSLLRELPAELRPRRVVAIAVDGTSgTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGHFF 170
Cdd:cd07783 81 VLVDREGEPL---------RPAIMYNDARAVAEAEELAEAAGAVAPRTGLAVSPSSSLAKLLWLKRHEPEV-LAKTAKFL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 171 DLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGL-EDLIddnyskigNLVLLPGAALGIgLTPEAARELG 248
Cdd:cd07783 151 HQADWLAGRLTGDRGVTDYNNALKLGYDPETGrWPSWLLALLGIpPDLL--------PRVVAPGTVIGT-LTAEAAEELG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 249 LPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVFVPGvwGPYYSAMVP-GFWL 327
Cdd:cd07783 222 LPAGTPVVAGTTDSIAAFLAS-GAVRPGDAVT------------SLGTTLVLKLLSDKRVPDPG--GGVYSHRHGdGYWL 286
|
330 340 350
....*....|....*....|....*....|..
gi 1720410215 328 NEGGQSVTGKLIDHMVQGHPaFPELQAKATAR 359
Cdd:cd07783 287 VGGASNTGGAVLRWFFSDDE-LAELSAQADPP 317
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
12-268 |
6.29e-48 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 169.62 E-value: 6.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07805 1 YILAIDLGTSGVKAALVDLDGELVASAFAPYPTYYPKPGWAEQDPEDWWDAVCRATRALLEksGIDPSDIAAIAFSGQmQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQY---VGGVMSVEMQAPKLLWLKENLREIcWDK 165
Cdd:cd07805 81 GVVPVDKDGNPL---------RNAIIWSDTRAAEEAEEIAGGLGGIEGYrlgGGNPPSGKDPLAKILWLKENEPEI-YAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 166 AGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLE-DLIDDnyskignlvLLPGAALgIG-LTPE 242
Cdd:cd07805 151 THKFLDAKDYLNFRLTGRAATDPSTASTTGLMDLRKRrWSEELLRAAGIDpDKLPE---------LVPSTEV-VGeLTPE 220
|
250 260
....*....|....*....|....*.
gi 1720410215 243 AARELGLPSGIAVAASLIDAHAGGLG 268
Cdd:cd07805 221 AAAELGLPAGTPVVGGGGDAAAAALG 246
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
12-329 |
9.55e-46 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 162.72 E-value: 9.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAERDMDELWQATAEAIRELLEksGVDPSDIAGVGVTGHgN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:cd07802 81 GLYLVDKDGKPV---------RNAILSNDSRAADIVDRWEEdgTLEKVYPLTGQPLWPGQPVALLRWLKENEPER-YDRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 167 GHFFDLPDFLSWKATGVtarslcsLVCKWT-YSA------EKGWDDSFWKMIGLEDLIDdnysKIGNLVllPGAALGIGL 239
Cdd:cd07802 151 RTVLFCKDWIRYRLTGE-------ISTDYTdAGSslldldTGEYDDELLDLLGIEELKD----KLPPLV--PSTEIAGRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 240 TPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGpYYS 319
Cdd:cd07802 218 TAEAAALTGLPEGTPVAAGAFDVVASALGA--------GAVDEGQ-----LCVILGTWSINEVVTDEPVVPDSVGS-NSL 283
|
330
....*....|
gi 1720410215 320 AMVPGFWLNE 329
Cdd:cd07802 284 HADPGLYLIV 293
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
12-351 |
3.91e-44 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 159.24 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVV--QGIDAHRIRGLGFDA-TC 88
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAEYPTSSPKPGWAEQDPEDWWQATKEALRELLakAGISPSDIAAIGLTGqMH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07808 81 GLVLLDKNGRPL---------RPAILWNDQRSAAECEELEARlGDEILIITGNPPLPGFTLPKLLWLKENEPEI-FARIR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 168 HFFdLP-DFLSWKATGVTAR-------SLCslvckwtYSAEKG-WDDSFWKMIGLEdliddnyskIGNL--VLLPGAALG 236
Cdd:cd07808 151 KIL-LPkDYLRYRLTGELATdpsdasgTLL-------FDVEKReWSEELLEALGLD---------PSILppIVESTEIVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 237 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPV----TSrlAVICGTSSCHMGISKDPVF--- 309
Cdd:cd07808 214 -TLTPEAAEELGLPEGTPVVAGAGDNAAAALGA--------GVVEPGDALislgTS--GVVFAPTDKPVPDPKGRLHtfp 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1720410215 310 --VPGVWgpYYSAMVPGF-----WLNE--GGQSVTGKLIDHMVQGHPAFPE 351
Cdd:cd07808 283 haVPGKW--YAMGVTLSAglslrWLRDlfGPDRESFDELDAEAAKVPPGSE 331
|
|
| PRK04123 |
PRK04123 |
ribulokinase; Provisional |
12-364 |
4.49e-44 |
|
ribulokinase; Provisional
Pssm-ID: 235221 [Multi-domain] Cd Length: 548 Bit Score: 160.40 E-value: 4.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKW---------EPQFNHHEQSSEDIWAAcclVTKEVVQ--GIDAHRI 79
Cdd:PRK04123 4 YVIGLDFGTDSVRALLVDcATGEELATAVVEYPHWvkgryldlpPNQALQHPLDYIESLEA---AIPAVLKeaGVDPAAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 80 RGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR-----VLQYVGGVMSVEMQAPKL 151
Cdd:PRK04123 81 VGIGVDFTgSTPAPVDADGTPLALLPEFAENPHamVKLWKDHTAQEEAEEINRLAHErgeadLSRYIGGIYSSEWFWAKI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 152 LWLKENLREIcWDKAGHFFDLPDFLSWKATGVTA-----RSLCSLVCKWTYSAEKG--WDDSFWKMI--GLEDLIDDnys 222
Cdd:PRK04123 161 LHVLREDPAV-YEAAASWVEACDWVVALLTGTTDpqdivRSRCAAGHKALWHESWGglPSADFFDALdpLLARGLRD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 223 KIGNLVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAgglGVIGADVRGHGLTcegqpvtsrlAVIcGTSSCHMG 302
Cdd:PRK04123 237 KLFTETWTAGEPAG-TLTAEWAQRLGLPEGVAVSVGAFDAHM---GAVGAGAEPGTLV----------KVM-GTSTCDIL 301
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410215 303 ISKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKL----IDHMVQghpafPELQAKATARNLQKH 364
Cdd:PRK04123 302 LADKQRAVPGICGQVDGSIVPGLIGYEAGQSAVGDIfawfARLLVP-----PEYKDEAEARGKQLL 362
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
12-336 |
1.59e-40 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 147.71 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPQPGWAEQDPEDWWQAVVEAIREVLAkaGIDPSDIAAIGISGQmP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAvsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd00366 81 GVVLVDADGNPL---------RPAIIWLDRRA-----------------------------------------------K 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 169 FFDLPDFLSWKATGVTA--RSLCSLVCKWTYsAEKGWDDSFWKMIGLEDliddnySKIGNLVlLPGAALGiGLTPEAARE 246
Cdd:cd00366 105 FLQPNDYIVFRLTGEFAidYSNASGTGLYDI-KTGDWSEELLDALGIPR------EKLPPIV-ESGEVVG-RVTPEAAEE 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 247 LGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVtsrlaVICGTSSCHMGISKDPVFVPGVWGPYYSAmVPGFW 326
Cdd:cd00366 176 TGLPAGTPVVAGGGDTAAAALGA--------GVVEPGDAV-----DSTGTSSVLSVCTDEPVPPDPRLLNRCHV-VPGLW 241
|
330
....*....|
gi 1720410215 327 LNEGGQSVTG 336
Cdd:cd00366 242 LLEGAINTGG 251
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
12-340 |
1.05e-37 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 141.19 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFdAT--CS 89
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAELDPEELWEAVKEAIREAAAQAGPDPIAAISV-SSqgES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 90 LVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAG 167
Cdd:cd07773 80 GVPVDRDGEPL---------GPAIVWFDPRGKEEAEELAEriGAEELYRITGLPPSPMYSLAKLLWLREHEPEI-FAKAA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 168 HFFDLPDFLSWKATGVTARSLcSLVCKWTY--SAEKGWDDSfwkmigLEDLIDDNYSKIGNLVlLPGAALGIgLTPEAAR 245
Cdd:cd07773 150 KWLSVADYIAYRLTGEPVTDY-SLASRTMLfdIRKRTWSEE------LLEAAGIDASLLPELV-PSGTVIGT-VTPEAAE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 246 ELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYS---AMV 322
Cdd:cd07773 221 ELGLPAGTPVVVGGHDHLCAALGA--------GVIEPGD-----VLDSTGTAEALLAVVDEPPLDEMLAEGGLSyghHVP 287
|
330
....*....|....*...
gi 1720410215 323 PGFWLNEGGQSvTGKLID 340
Cdd:cd07773 288 GGYYYLAGSLP-GGALLE 304
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
12-342 |
7.43e-37 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 138.81 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFA--EQPIKKwePQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDA- 86
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASAsiEHDLLT--PKPGWAEHDPEVWWGAVCEIIRELLAkaGISPKEIAAIGVSGl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 87 TCSLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET--KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWD 164
Cdd:cd07804 79 VPALVPVDENGKPL---------RPAILYGDRRATEEIEWLNENigEDRIFEITGNPLDSQSVGPKLLWIKRNEPEV-FK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 165 KAGHFFDLPDFLSWKATG--VTARSLCSLvckwtYS-----AEKGWDDSFWKMIGL-EDLIDDNYSkignlvllPGAALG 236
Cdd:cd07804 149 KTRKFLGAYDYIVYKLTGeyVIDYSSAGN-----EGglfdiRKRTWDEELLEALGIdPDLLPELVP--------STEIVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 237 iGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGP 316
Cdd:cd07804 216 -EVTKEAAEETGLAEGTPVVAGTVDAAASALSA--------GVVEPGD-----LLLMLGTAGDIGVVTDKLPTDPRLWLD 281
|
330 340
....*....|....*....|....*.
gi 1720410215 317 YYSamVPGFWLNEGGQSVTGKLIDHM 342
Cdd:cd07804 282 YHD--IPGTYVLNGGMATSGSLLRWF 305
|
|
| L-ribulokinase |
TIGR01234 |
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely ... |
12-364 |
1.90e-32 |
|
ribulokinase; This enzyme catalyzes the second step in arabinose catabolism. The most closely related protein subfamily outside the scope of this model includes ribitol kinase from E. coli. [Energy metabolism, Sugars]
Pssm-ID: 130301 [Multi-domain] Cd Length: 536 Bit Score: 127.73 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWE--------------PQFNHHEQSSEDIWAAcclVTKEVVQ--GI 74
Cdd:TIGR01234 2 YAIGVDFGTLSGRALAVDvATGEEIATAVEWYRHWVkgqflpktgaklpnDQALQHPADYIEVLEA---AIPTVLAelGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 75 DAHRIRGLGFDAT-CSLVVLDKEFHPLPVNHEGDSSRN--VIMWLDHRAVSQVHRINETKHR----VLQYVGGVMSVEMQ 147
Cdd:TIGR01234 79 DPADVVGIGVDFTaCTPAPIDSDGNPLCLLPEFAENPHayFKLWKHHAAQEEADRINRLAHApgevDLSRYGGIISSEWF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 148 APKLLWLKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKGW-DDSFWKMI--GLEDLIDDNYSK- 223
Cdd:TIGR01234 159 WAKILQITEEDPAI-YQAADRWIELADWIVAQLSGDIRRGRCTAGYKALWHESWGYpSASFFDELnpILNRHLPDKLFTd 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 224 IGNLvllpGAALGiGLTPEAARELGLPSGIAVAASLIDAHaggLGVIGADVrghgltceGQPvtSRLAVICGTSSCHMGI 303
Cdd:TIGR01234 238 IWTA----GEPAG-TLTPEWAQRTGLPEGVVVAVGNFDAH---VGAVAAGI--------AQP--GALVKIMGTSTCHVLI 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720410215 304 SKDPVFVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQgHPAFPELQAKATARNLQKH 364
Cdd:TIGR01234 300 GDKQRAVPGMCGVVDGGIVPGFIGYEAGQSAVGDIFAWFGK-VCVPPELKTEANASQKQLH 359
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
12-358 |
4.77e-32 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 126.13 E-value: 4.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIDAHRIRGLGFDATC-SL 90
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGFSSAMhSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 91 VVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRI--NETKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKAGH 168
Cdd:cd07770 81 LGVDEDGEPL---------TPVITWADTRAAEEAERLrkEGDGSELYRRTGCPIHPMYPLAKLLWLKEERPEL-FAKAAK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 169 FFDLPDFLSWKATG--VTARSLCSlvckWT---YSAEKGWDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIGLTPEA 243
Cdd:cd07770 151 FVSIKEYLLYRLTGelVTDYSTAS----GTgllNIHTLDWDEEALELLGID---EEQLPE-----LVDPTEVLPGLKPEF 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 244 ARELGLPSGIAVAASLIDAHAGGLGViGADVRGhgltcegqpvtsRLAVICGTSschmG----ISKDPVFVP--GVWgPY 317
Cdd:cd07770 219 AERLGLLAGTPVVLGASDGALANLGS-GALDPG------------RAALTVGTS----GairvVSDRPVLDPpgRLW-CY 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1720410215 318 YSAmvPGFWL-----NEGGqSVTGKLIDHMVQGHPAFPELQAKATA 358
Cdd:cd07770 281 RLD--ENRWLvggaiNNGG-NVLDWLRDTLLLSGDDYEELDKLAEA 323
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
12-340 |
8.21e-32 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 124.55 E-value: 8.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDAT-C 88
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYREYPPYYPEPGWVEQDPDDWWDALCEALKEAVAkaGVDPEDIAAIGLTSQrS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVsqvhrinetkhrvlqyvggvmsvemqapkllwlkenlreicwdkagH 168
Cdd:cd07779 81 TFVPVDEDGRPL---------RPAISWQDKRTA----------------------------------------------K 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 169 FFDLPDFLSWKATGVTARSLCSLVCKWTYSAEKG-WDDSFWKMIGLEDliddnySKIGNLVlLPGAALGiGLTPEAAREL 247
Cdd:cd07779 106 FLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRdWSDDLLDAFGIDR------DKLPELV-PPGTVIG-TLTKEAAEET 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 248 GLPSGIAVAASlidAHAGGLGVIGAdvrghGLTCEGQpvtsrLAVICGTSSCHMGISKDPVFVPGVWGPYYSAMVPGFWL 327
Cdd:cd07779 178 GLPEGTPVVAG---GGDQQCAALGA-----GVLEPGT-----ASLSLGTAAVVIAVSDKPVEDPERRIPCNPSAVPGKWV 244
|
330
....*....|...
gi 1720410215 328 NEGGQSVTGKLID 340
Cdd:cd07779 245 LEGSINTGGSAVR 257
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
12-322 |
5.29e-29 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 116.96 E-value: 5.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGID--AHRIRGLGFDAT-- 87
Cdd:cd24121 1 ILIGIDAGTSVVKAVAFDLDGRELAVAARRNAVLYPQPGWAEQDMNETWQAVVATIREVVAKLDvlPDRVAAIGVTGQgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 -CSLVvlDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREICwD 164
Cdd:cd24121 81 gTWLV--DEDGRPV---------RDAILWLDGRAADIVERWQAdgIAEAVFEITGTGLFPGSQAAQLAWLKENEPERL-E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 165 KAGHFFDLPDFLSWKATGVTA--RSLCSLVCkwtYSAEKG-WDDSFWKMIGLEDLIDdnyskignlvLLPGAALGIG--- 238
Cdd:cd24121 149 RARTALHCKDWLFYKLTGEIAtdPSDASLTF---LDFRTRqYDDEVLDLLGLEELRH----------LLPPIRPGTEvig 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 239 -LTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHGLTcegqpvtsrlavICGTSSCHMGISKDPVF-------- 309
Cdd:cd24121 216 pLTPEAAAATGLPAGTPVVLGPFDVVATALGS-GAIEPGDACS------------ILGTTGVHEVVVDEPDLepegvgyt 282
|
330
....*....|....*..
gi 1720410215 310 ----VPGVWGPYYSAMV 322
Cdd:cd24121 283 iclgVPGRWLRAMANMA 299
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
12-336 |
1.71e-26 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 110.01 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHH--EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgfdAT 87
Cdd:cd07798 1 YYLVIDIGTGGGRCALVDSEGKIVAIAYREWEYYTDDDYPDakEFDPEELWEKICEAIREALKkaGISPEDISAV---SS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 CS----LVVLDKEFHPL---PvNHegdssrnvimwlDHRAVSQVHRIN-ETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 159
Cdd:cd07798 78 TSqregIVFLDKDGRELyagP-NI------------DARGVEEAAEIDdEFGEEIYTTTGHWPTELFPAARLLWFKENRP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 160 EIcWDKAGHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEDLIddnyskignL--VL 229
Cdd:cd07798 145 EI-FERIATVLSISDWIGYRLTGE-------LVSEPSQASETQlfdikkreWSQELLEALGLPPEI---------LpeIV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 230 LPGAALGIgLTPEAARELGLPSGIAVAASLIDAHAGGLGViGADVRGHgltcegqpvtsrLAVICGTSSCHMGISKDPVF 309
Cdd:cd07798 208 PSGTVLGT-VSEEAARELGLPEGTPVVVGGADTQCALLGS-GAIEPGD------------IGIVAGTTTPVQMVTDEPII 273
|
330 340 350
....*....|....*....|....*....|
gi 1720410215 310 VP--GVW-GPYysaMVPGFWLNEGGQSVTG 336
Cdd:cd07798 274 DPerRLWtGCH---LVPGKWVLESNAGVTG 300
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
12-268 |
2.34e-26 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 105.88 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFDATC- 88
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPGWAEQDPDEIWQAVAQCIAKTLSqlGISLKQIKGIGISNQGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINE--TKHRVLQYVGGVMSVEMQAPKLLWLKENLREIcWDKA 166
Cdd:pfam00370 81 GTVLLDKNDKPL---------YNAILWKDRRTAEIVENLKEegNNQKLYEITGLPIWPGFTLSKLRWIKENEPEV-FEKI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 167 GHFFDLPDFLSWKATGVtarslcsLVCKWTYSAEKG--------WDDSFWKMIGLEdliDDNYSKignlvLLPGAALGIG 238
Cdd:pfam00370 151 HKFLTIHDYLRWRLTGV-------FVTDHTNASRSMmfnihkldWDPELLAALGIP---RDHLPP-----LVESSEIYGE 215
|
250 260 270
....*....|....*....|....*....|
gi 1720410215 239 LTPEAARELGLPSGIAVAASLIDAHAGGLG 268
Cdd:pfam00370 216 LNPELAAMWGLDEGVPVVGGGGDQQAAAFG 245
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
12-308 |
5.73e-26 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 108.41 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPikkWEPQFNHH---EQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD 85
Cdd:cd07809 1 LVLGIDLGTQSIKAVLIDaETGRVVASGSAP---HENILIDPgwaEQDPEDWWDALQAAFAQLLKdaGAELRDVAAIGIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 86 ATC-SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINET-KHRVLQYVGGVMSVEMQAPKLLWLKENLREIcW 163
Cdd:cd07809 78 GQMhGLVALDADGKVL---------RPAKLWCDTRTAPEAEELTEAlGGKKCLLVGLNIPARFTASKLLWLKENEPEH-Y 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 164 DKAgHFFDLP-DFLSWKATG--VTARSLCSLVckwtysaekGWDDSF-----WKMIGLEDLIDDNYSKIGNlVLLPGAAL 235
Cdd:cd07809 148 ARI-AKILLPhDYLNWKLTGekVTGLGDASGT---------FPIDPRtrdydAELLAAIDPSRDLRDLLPE-VLPAGEVA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720410215 236 GiGLTPEAARELGLPSGIAVAASLIDAHAG--GLGVIGadvrghgltcEGQPVTSrlaviCGTSSCHMGISKDPV 308
Cdd:cd07809 217 G-RLTPEGAEELGLPAGIPVAPGEGDNMTGalGTGVVN----------PGTVAVS-----LGTSGTAYGVSDKPV 275
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
290-356 |
1.43e-18 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 83.14 E-value: 1.43e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720410215 290 LAVICGTSSCHMGISKDPV-FVPGVWGPYYSAMVPGFWLNEGGQSVTGKLIDHMVQGHPAFPELQAKA 356
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVlSVHGVWGPYTNEMLPGYWGLEGGQSAAGSLLAWLLQFHGLREELRDAG 68
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
12-270 |
4.12e-16 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 79.68 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKWEPQFNHHEQSSEDI-----WAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:cd07775 1 YLLALDAGTGSGRAVIFDLEGNQIAVAQ---REWRHKEVPDVPGSMDFdteknWKLICECIREALKkaGIAPKSIAAI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 85 dATCS----LVVLDKEFHPLPVNHegdssrNVimwlDHRAVSQVHRINETKH---RVLQYVGGVMSVEMQAPKLLWLKEN 157
Cdd:cd07775 76 -STTSmregIVLYDNEGEEIWACA------NV----DARAAEEVSELKELYNtleEEVYRISGQTFALGAIPRLLWLKNN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 158 LREIcWDKAGHFFDLPDFLSWKATGVTAR--SLCSLVCKWTySAEKGWDDSFWKMIGLEDLIDDNyskignlVLLPGAAL 235
Cdd:cd07775 145 RPEI-YRKAAKITMLSDWIAYKLSGELAVepSNGSTTGLFD-LKTRDWDPEILEMAGLKADILPP-------VVESGTVI 215
|
250 260 270
....*....|....*....|....*....|....*..
gi 1720410215 236 GIgLTPEAARELGLPSGIAVAASLIDAHAG--GLGVI 270
Cdd:cd07775 216 GK-VTKEAAEETGLKEGTPVVVGGGDVQLGclGLGVV 251
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
13-304 |
1.47e-13 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 71.92 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 13 YVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC-----CLVTKEVVQGIDAHRIRGLGFDAT 87
Cdd:PRK15027 2 YIGIDLGTSGVKVILLNEQGEVVASQTEKLTVSRPHPLWSEQDPEQWWQATdramkALGDQHSLQDVKALGIAGQMHGAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 cslvVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGVMSVEMQAPKLLWLKENLREICWDKAG 167
Cdd:PRK15027 82 ----LLDAQQRVL---------RPAILWNDGRCAQECALLEARVPQSRVITGNLMMPGFTAPKLLWVQRHEPEIFRQIDK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 168 HFfdLP-DFLSWKATGVTARSLCSLV-CKWTYSAEKGWDDSfwkMIGLEDLIDDNYSkignlVLLPGAALGIGLTPEAAR 245
Cdd:PRK15027 149 VL--LPkDYLRLRMTGEFASDMSDAAgTMWLDVAKRDWSDV---MLQACHLSRDQMP-----ALYEGSEITGALLPEVAK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720410215 246 ELGLPSgIAVAASLIDAHAGGLGVigadvrghGLTCEGQPVTSrlaviCGTSSCHMGIS 304
Cdd:PRK15027 219 AWGMAT-VPVVAGGGDNAAGAVGV--------GMVDANQAMLS-----LGTSGVYFAVS 263
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
12-314 |
4.18e-12 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 67.34 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEqpiKKW----EPQF-NHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLgf 84
Cdd:PRK10939 4 YLMALDAGTGSIRAVIFDLNGNQIAVGQ---AEWrhlaVPDVpGSMEFDLEKNWQLACQCIRQALQkaGIPASDIAAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 85 dATCSL----VVLDKEFHPLpvnhegdssrnvimW----LDHRAVSQV----HRINETKHRVLQYVGGVMSVEmQAPKLL 152
Cdd:PRK10939 79 -SATSMregiVLYDRNGTEI--------------WacanVDARASREVselkELHNNFEEEVYRCSGQTLALG-ALPRLL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 153 WLKENLREIcWDKAGHFFDLPDFLSWKATGVTA--------RSLCSLVckwtysaEKGWDDSFWKMIGledLIDDNYSKi 224
Cdd:PRK10939 143 WLAHHRPDI-YRQAHTITMISDWIAYMLSGELAvdpsnagtTGLLDLV-------TRDWDPALLEMAG---LRADILPP- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 225 gnlVLLPGAALGiGLTPEAARELGLPSGIAVAASLIDAHAGGLGVigadvrghGLTCEGQpvtsrLAVICGT-------- 296
Cdd:PRK10939 211 ---VKETGTVLG-HVTAKAAAETGLRAGTPVVMGGGDVQLGCLGL--------GVVRPGQ-----TAVLGGTfwqqvvnl 273
|
330 340
....*....|....*....|..
gi 1720410215 297 ----SSCHMGISKDPVFVPGVW 314
Cdd:PRK10939 274 papvTDPNMNIRINPHVIPGMV 295
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
12-158 |
2.26e-10 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 62.10 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdaTC- 88
Cdd:cd07769 1 YILAIDQGTTSTRAILFDEDGNIVASAQKEHEQIYPQPGWVEHDPEEIWENTLEVIREALAkaGISASDIAAIGI--TNq 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720410215 89 --SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINETKH--RVLQYVGGVMSVEMQAPKLLWLKENL 158
Cdd:cd07769 79 reTTVVWDK--------KTGKPLYNAIVWQDRRTADICEELKAKGLeeRIREKTGLPLDPYFSATKIKWILDNV 144
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
12-132 |
1.55e-09 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 59.43 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFD---A 86
Cdd:cd07786 1 YILAIDQGTTSSRAILFDHDGNIVAVAQREFTQIYPKPGWVEHDPEEIWESQLAVAREALAkaGIRASDIAAIGITnqrE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720410215 87 TCslVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHRINETKH 132
Cdd:cd07786 81 TT--VVWDRE--------TGKPVYNAIVWQDRRTADICEELKAEGH 116
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
12-182 |
1.92e-09 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 59.11 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGFdAT-- 87
Cdd:cd07793 1 YILAVDVGTTNIRCHIFDKKGKIIGSSSEKVEVLYPEPGWVEIDPEELWQQFVKVIKEALKnaGLTPEDIAAIGI-STqr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 88 CSLVVLDKE----FHplpvnhegdssrNVIMWLDHRAVSQVHRINE-TKHRVLQYVGGVM-----------------SVE 145
Cdd:cd07793 80 NTFLTWDKKtgkpLH------------NFITWQDLRAAELCESWNRsLLLKALRGGSKFLhfltrnkrflaasvlkfSTA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720410215 146 MQAPKLLWLKENLREICWDKAGH---FFDLPDFLSWKATG 182
Cdd:cd07793 148 HVSIRLLWILQNNPELKEAAEKGellFGTIDTWLLWKLTG 187
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
17-288 |
1.00e-07 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 53.49 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 17 DVGTGSVRAALVDQRGLLLAFAEQP----IKKWEPQFnhHEQSSEDIW---AACClvtKEVVQGIDAHRIRGL-----GF 84
Cdd:PRK10331 8 DCGATNVRAIAVDRQGKIVARASTPnasdIAAENSDW--HQWSLDAILqrfADCC---RQINSELTECHIRGItvttfGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 85 DATcslvvldkefhplPVNHEGDSSRNVIMWLDHRAVSQVHRI-NETKHRVLQYVGGVMSVEMQAP-KLLWLKENLREIc 162
Cdd:PRK10331 83 DGA-------------LVDKQGNLLYPIISWKCPRTAAVMENIeRYISAQQLQQISGVGAFSFNTLyKLVWLKENHPQL- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 163 WDKAGHFFDLPDFLSWKATGV--TARSLCSlVCKWTYSAEKGWDDSFWKMIGL-EDL---IDDNYSKIGNlvllpgaalg 236
Cdd:PRK10331 149 LEQAHAWLFISSLINHRLTGEftTDITMAG-TSQMLDIQQRDFSPEILQATGLsRRLfprLVEAGEQIGT---------- 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1720410215 237 igLTPEAARELGLPSGIAVAASlidAHAGGLGVIGAdvrGHGLtceGQPVTS 288
Cdd:PRK10331 218 --LQPSAAALLGLPVGIPVISA---GHDTQFALFGS---GAGQ---NQPVLS 258
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
12-217 |
2.05e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 52.61 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 12 YYVGIDVGTGSVRAALVD-QRGLLLAFAEQPIKKWEPQ--FNHHEQSSEDIWAAcclvTKEVVQGIDAH---RIRGLGFd 85
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPAPISSddPGRSEQDPEKILEA----VRNLIDELPREylsDVTGIGI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 86 aTC---SLVVLDKEFHPLpvnhegdssRNVIMWLDHRAVSQVHRINETKHRVLQYVGGV-MSVEMQAPKLLWLKENLREI 161
Cdd:cd07777 76 -TGqmhGIVLWDEDGNPV---------SPLITWQDQRCSEEFLGGLSTYGEELLPKSGMrLKPGYGLATLFWLLRNGPLP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 162 cwDKAGHFFDLPDFLSWKATGvTARSLCSLVCK--WTY--SAEKGWDDSFWKMIGLEDLI 217
Cdd:cd07777 146 --SKADRAGTIGDYIVARLTG-LPKPVMHPTNAasWGLfdLETGTWNKDLLEALGLPVIL 202
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
13-161 |
3.97e-07 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 51.76 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAAC--CL---VTKEVVQGIDAHRIRGLGFda 86
Cdd:cd07792 2 LVGaIDQGTTSTRFIVFDSTGELVASHQVEHKQIYPKPGWVEHDPMEILESVyeCIeeaVEKLKALGISPSDIKAIGI-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 87 TC---SLVVLDKEfhplpvnhEGDSSRNVIMWLDHRAVSQVHR----INETKHRVLQYVGGVMSVEMQAPKLLWLKENLR 159
Cdd:cd07792 80 TNqreTTVVWDKS--------TGKPLYNAIVWLDTRTSDTVEElsakTPGGKDHFRKKTGLPISTYFSAVKLRWLLDNVP 151
|
..
gi 1720410215 160 EI 161
Cdd:cd07792 152 EV 153
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
16-261 |
1.90e-04 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 43.40 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 16 IDVGTGSVRAALVDQRGLLLAFAEQPIK-KWEPQFNHHEqsSEDIWAACCLVTKEVVQGidaHRIRGLGFdaTC---SLV 91
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPeIEEDGYPCED--VEAIWEWLLDSLAELAKR---HRIDAINF--TThgaTFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 92 VLDKEFHP-LPV---NHEGDSSrnvimwldhravsqvhrINEtkhrvlQY--------------VGGVMSVEMQapkLLW 153
Cdd:cd07772 78 LLDENGELaLPVydyEKPIPDE-----------------INE------AYyaergpfeetgsppLPGGLNLGKQ---LYW 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 154 LKENLREIcWDKAGHFFDLPDFLSWKATGVTARSLCSLVC--------KWTYS---AEKGWDDSFWKMigledliddnys 222
Cdd:cd07772 132 LKREKPEL-FARAKTILPLPQYWAWRLTGKAASEITSLGChtdlwdfeKNEYSslvKKEGWDKLFPPL------------ 198
|
250 260 270
....*....|....*....|....*....|....*....
gi 1720410215 223 kignlvLLPGAALGIgLTPEAARELGLPSGIAVAASLID 261
Cdd:cd07772 199 ------RKAWEVLGP-LRPDLARRTGLPKDIPVGCGIHD 230
|
|
| PTZ00294 |
PTZ00294 |
glycerol kinase-like protein; Provisional |
13-161 |
1.08e-03 |
|
glycerol kinase-like protein; Provisional
Pssm-ID: 240348 [Multi-domain] Cd Length: 504 Bit Score: 41.11 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 13 YVG-IDVGTGSVRAALVDQRGLLLAFAEQPIKKWEPQFNHHEQSSEDIWAACCLVTKEVVQGIdahRIRGLGFDATC--- 88
Cdd:PTZ00294 3 YIGsIDQGTTSTRFIIFDEKGNVVSSHQIPHEQITPHPGWLEHDPEEILRNVYKCMNEAIKKL---REKGPSFKIKAigi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720410215 89 -----SLVVLDKefhplpvnHEGDSSRNVIMWLDHRAVSQVHRINET--KHRVLQYVGG-VMSVEMQAPKLLWLKENLRE 160
Cdd:PTZ00294 80 tnqreTVVAWDK--------VTGKPLYNAIVWLDTRTYDIVNELTKKygGSNFFQKITGlPISTYFSAFKIRWMLENVPA 151
|
.
gi 1720410215 161 I 161
Cdd:PTZ00294 152 V 152
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
11-84 |
3.08e-03 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 39.11 E-value: 3.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720410215 11 RYYVGIDVGTGSVRAALVDQRGLLLAFAEQPIkkwepqfnHHEQSSEDIWAACCLVTKEVVQ--GIDAHRIRGLGF 84
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPT--------PAGAGPEAVLEAIAELIEELLAeaGISRGRILGIGI 72
|
|
| |
