|
Name |
Accession |
Description |
Interval |
E-value |
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
1-267 |
0e+00 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 574.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLK 80
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 81 ESLQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIATNQIELSPYLQ 160
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 161 NRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLD 240
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLD 240
|
250 260
....*....|....*....|....*..
gi 534608561 241 AEDKKAIAALDCNDRLVSPEGLAPEWD 267
Cdd:PRK11172 241 AEDMAAIAALDRNGRLVSPEGLAPEWD 267
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
3-250 |
1.58e-174 |
|
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: 480.70 E-value: 1.58e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIATNQIELSPYLQNR 162
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDAD 240
|
....*...
gi 534608561 243 DKKAIAAL 250
Cdd:cd19139 241 DMAAIAAL 248
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
1-256 |
1.78e-133 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 377.47 E-value: 1.78e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLK 80
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 81 ESLQKLRTDYVDLTLIHWPSPsdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGaENIATNQIELSPYLQ 160
Cdd:COG0656 83 ESLERLGLDYLDLYLIHWPGP---GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG-VKPAVNQVELHPYLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 161 NRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLD 240
Cdd:COG0656 159 QRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELS 238
|
250
....*....|....*.
gi 534608561 241 AEDKKAIAALDCNDRL 256
Cdd:COG0656 239 DEDMAAIDALDRGERL 254
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
3-247 |
5.37e-123 |
|
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: 350.03 E-value: 5.37e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGaENIATNQIELSPYLQNR 162
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNP--TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP-LPIAVNQVEFHPFLYQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19073 158 ELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 534608561 243 DKKAI 247
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
3-250 |
2.30e-106 |
|
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: 308.42 E-value: 2.30e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19140 8 IPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAEnIATNQIELSPYLQNR 162
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPNK--DVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP-LFTNQVEYHPYLDQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAM-GEGYSVIPSSTKRENLESNLKAQNLQLDA 241
Cdd:cd19140 165 KLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDFTLSD 244
|
....*....
gi 534608561 242 EDKKAIAAL 250
Cdd:cd19140 245 EEMARIAAL 253
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
3-248 |
2.46e-103 |
|
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: 300.55 E-value: 2.46e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVSAEEFM----QALLEAKKQGLTREIGISNFTIPLMEKaIAAVGAENIATNQIELSPY 158
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGSKEARletwRALEELVDEGLVRSIGVSNFNVEHLEE-LLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 159 LQNRKVVAWAKQHGIHITSYMTLA--YGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQN 236
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGrgRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|..
gi 534608561 237 LQLDAEDKKAIA 248
Cdd:cd19071 240 FELSEEDMAAID 251
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
1-251 |
8.83e-86 |
|
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: 256.53 E-value: 8.83e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLK 80
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 81 ESLQKLRTDYVDLTLIHWPSPSDEVSAEEFmQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENiATNQIELSPYLQ 160
Cdd:cd19131 88 ESLRKLGLDYVDLYLIHWPVPAQDKYVETW-KALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVP-VVNQIELHPRFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 161 NRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLD 240
Cdd:cd19131 166 QRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELD 245
|
250
....*....|.
gi 534608561 241 AEDKKAIAALD 251
Cdd:cd19131 246 ADDMQAIAGLD 256
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
3-251 |
1.29e-83 |
|
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: 250.65 E-value: 1.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19132 7 IPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALRTIEES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVSAEEFmQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGaENIATNQIELSPYLQNR 162
Cdd:cd19132 87 LYRLGLDYVDLYLIHWPNPSRDLYVEAW-QALIEAREEGLVRSIGVSNFLPEHLDRLIDETG-VTPAVNQIELHPYFPQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTLAYGNA-LKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDA 241
Cdd:cd19132 165 EQRAYHREHGIVTQSWSPLGRGSGlLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSD 244
|
250
....*....|
gi 534608561 242 EDKKAIAALD 251
Cdd:cd19132 245 EDMAAIAALD 254
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
3-257 |
7.87e-83 |
|
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: 250.41 E-value: 7.87e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE----SGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWP-----------SPSD-----EVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAA 142
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPvalkkgvgfpeSGEDllslsPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 vGAENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGN------------ALKDKVIARIAAKHNATPAQVILAW 210
Cdd:cd19123 172 -ARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDrpaamkaegepvLLEDPVINKIAEKHGASPAQVLIAW 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 534608561 211 AMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLV 257
Cdd:cd19123 251 AIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHRYV 297
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
3-250 |
8.13e-81 |
|
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: 244.08 E-value: 8.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKD-DVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAES----GVPRHELYITTKIWIENLSKDKLIP 77
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWP-----SPSDEVSAE---EFMQALLEAKKQGLTREIGISNFTIPLMEKAIA------AV 143
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAElrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKycevppAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 144 gaeniatNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYG--NALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPS 221
Cdd:cd19136 161 -------NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPK 233
|
250 260
....*....|....*....|....*....
gi 534608561 222 STKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19136 234 STNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
2-251 |
3.41e-76 |
|
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: 232.11 E-value: 3.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKE 81
Cdd:cd19130 9 SIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSPS--DEVSAEEFMQALLEAkkqGLTREIGISNFTIPLMEKAIAAVGAENiATNQIELSPYL 159
Cdd:cd19130 89 SLAKLGLDQVDLYLVHWPTPAagNYVHTWEAMIELRAA---GRTRSIGVSNFLPPHLERIVAATGVVP-AVNQIELHPAY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 160 QNRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQL 239
Cdd:cd19130 165 QQRTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDL 244
|
250
....*....|..
gi 534608561 240 DAEDKKAIAALD 251
Cdd:cd19130 245 TDTEIAAIDALD 256
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
3-251 |
1.04e-75 |
|
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: 230.54 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVI-SSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKE 81
Cdd:cd19133 9 MPILGFGVFQIPDPEECeRAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSpSDEVSAeefMQALLEAKKQGLTREIGISNFTiP--LMEkaIAAVGAENIATNQIELSPYL 159
Cdd:cd19133 89 SLKRLGLDYLDLYLIHQPF-GDVYGA---WRAMEELYKEGKIRAIGVSNFY-PdrLVD--LILHNEVKPAVNQIETHPFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 160 QNRKVVAWAKQHGIHITSYMTLAYG--NALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNL 237
Cdd:cd19133 162 QQIEAVEFLKKYGVQIEAWGPFAEGrnNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDF 241
|
250
....*....|....
gi 534608561 238 QLDAEDKKAIAALD 251
Cdd:cd19133 242 ELSDEDMEAIAALD 255
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-256 |
6.26e-74 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 226.88 E-value: 6.26e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWienlSKDKLIP--SLK 80
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLW----NDDHKRPreALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 81 ESLQKLRTDYVDLTLIHWPSPSDE--VSAeefMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENiATNQIELSPY 158
Cdd:PRK11565 91 ESLKKLQLDYVDLYLMHWPVPAIDhyVEA---WKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTP-VINQIELHPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 159 LQNRKVVAWAKQHGIHITSYMTLAYG--NALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQN 236
Cdd:PRK11565 167 MQQRQLHAWNATHKIQTESWSPLAQGgkGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFD 246
|
250 260
....*....|....*....|
gi 534608561 237 LQLDAEDKKAIAALDCNDRL 256
Cdd:PRK11565 247 FRLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-255 |
1.21e-73 |
|
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: 225.73 E-value: 1.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDD-VVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKE 81
Cdd:cd19157 10 MPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSPSdevSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAvgAENI-ATNQIELSPYLQ 160
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKG---KYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD--AEIVpMVNQVEFHPRLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 161 NRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLD 240
Cdd:cd19157 165 QKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELS 244
|
250
....*....|....*
gi 534608561 241 AEDKKAIAALDCNDR 255
Cdd:cd19157 245 QEDMDKIDALNENLR 259
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
3-251 |
1.56e-72 |
|
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: 222.70 E-value: 1.56e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKD-DVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKE 81
Cdd:cd19126 9 MPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKqglTREIGISNFTIPLMEKaIAAVGAENIATNQIELSPYLQN 161
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDKFIDTWKALEKLYASGK---VKAIGVSNFQEHHLEE-LLAHADVVPAVNQVEFHPYLTQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 162 RKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDA 241
Cdd:cd19126 165 KELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDFELSE 244
|
250
....*....|
gi 534608561 242 EDKKAIAALD 251
Cdd:cd19126 245 DDMTAIDALN 254
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
2-257 |
2.61e-72 |
|
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: 223.31 E-value: 2.61e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTFRLKDDV-VISSVKTALELDYRAIDTAQIYDNEAAVGQA----IAESGVPRHELYITTKIWIENLSKDKLI 76
Cdd:cd19116 10 EIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 77 PSLKESLQKLRTDYVDLTLIHWPSPSDEVSAEEFM--------------QALLEAKKQGLTREIGISNFTIPLMEKAIAA 142
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNgdgslsdidyletwRGMEDLVKLGLTRSIGVSNFNSEQINRLLSN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 VgaeNI--ATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA---------LKDKVIARIAAKHNATPAQVILAWA 211
Cdd:cd19116 170 C---NIkpAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppprLDDPTLVAIAKKYGKTTAQIVLRYL 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 534608561 212 MGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLV 257
Cdd:cd19116 247 IDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-256 |
4.38e-70 |
|
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: 216.65 E-value: 4.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19134 11 MPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACRAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVSAEEFmQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGaENIATNQIELSPYLQNR 162
Cdd:cd19134 91 LERLGLDYVDLYLIHWPAGREGKYVDSW-GGLMKLREEGLARSIGVSNFTAEHLENLIDLTF-FTPAVNQIELHPLLNQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19134 169 ELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTAD 248
|
250
....*....|....
gi 534608561 243 DKKAIAALDCNDRL 256
Cdd:cd19134 249 HMDALDGLDDGTRF 262
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-250 |
9.54e-70 |
|
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: 216.60 E-value: 9.54e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWieNLSKDKLIPSLKES 82
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLW--CTWHRRVEEALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDE----------------------VSAEEFMQALLeakKQGLTREIGISNFTIPLMEKAI 140
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdfIKTWELMQKLP---ATGKVKAIGVSNFSIKNLEKLL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 141 AAVGAENI-ATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA--LKDKVIARIAAKHNATPAQVILAWAMGEGYS 217
Cdd:cd19117 169 ASPSAKIVpAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAplLKEPVIIKIAKKHGKTPAQVIISWGLQRGYS 248
|
250 260 270
....*....|....*....|....*....|...
gi 534608561 218 VIPSSTKRENLESNLKAqnLQLDAEDKKAIAAL 250
Cdd:cd19117 249 VLPKSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
2-247 |
2.08e-67 |
|
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: 209.78 E-value: 2.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTFRL---------KDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIaeSGVPRHELYITTKIWIEN 69
Cdd:cd19072 3 EVPVLGLGTWGIgggmskdysDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 70 LSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIA 149
Cdd:cd19072 81 LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPS--IPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 150 TNQIELSpyLQNRKVVA----WAKQHGIHITSYMTLAYGNALKDK---VIARIAAKHNATPAQVILAWAMG-EGYSVIPS 221
Cdd:cd19072 159 ANQVEYN--LFDREEESgllpYCQKNGIAIIAYSPLEKGKLSNAKgspLLDEIAKKYGKTPAQIALNWLISkPNVIAIPK 236
|
250 260
....*....|....*....|....*.
gi 534608561 222 STKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19072 237 ASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
1-249 |
2.44e-67 |
|
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: 209.78 E-value: 2.44e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGT--FRLKDDVV----ISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIW--IENLSK 72
Cdd:cd19120 4 IPAIAFGTGTawYKSGDDDIqrdlVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSpgIKDPRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 73 dklipSLKESLQKLRTDYVDLTLIHWP--SPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKaIAAVGAENIAT 150
Cdd:cd19120 84 -----ALRKSLAKLGVDYVDLYLIHSPffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEE-LLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 151 NQIELSPYLQNR--KVVAWAKQHGIHITSYMTLA----YGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTK 224
Cdd:cd19120 158 NQIEFHPYLYPQqpALLEYCREHGIVVSAYSPLSpltrDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSSK 237
|
250 260
....*....|....*....|....*
gi 534608561 225 RENLESNLKAQNLQLDAEDKKAIAA 249
Cdd:cd19120 238 EERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
3-256 |
1.45e-66 |
|
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: 208.81 E-value: 1.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE---SGV-PRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPSP-----------------SDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEkAIA 141
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQ-RIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 142 AVGAENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAY---------------GNALKDKVIARIAAKHNATPAQV 206
Cdd:cd19154 171 DNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpgranftkstgvspaPNLLQDPIVKAIAEKHGKTPAQV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 534608561 207 ILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRL 256
Cdd:cd19154 251 LLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
3-251 |
6.81e-66 |
|
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: 206.10 E-value: 6.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKES 82
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENiATNQIELSPYLQNR 162
Cdd:cd19127 89 LRRLGLDYVDLYLLHWPVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTVVP-AVNQVELHPYFSQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 KVVAWAKQHGIHITSYMTL------------AYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLES 230
Cdd:cd19127 168 DLRAFHRRLGIVTQAWSPIggvmrygasgptGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPERIAE 247
|
250 260
....*....|....*....|.
gi 534608561 231 NLKAQNLQLDAEDKKAIAALD 251
Cdd:cd19127 248 NIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
3-250 |
1.84e-65 |
|
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: 205.34 E-value: 1.84e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAES-----GVPRHELYITTKIWIENLSKDKLIP 77
Cdd:cd19118 7 IPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHRPEYVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWP--------------SPSD--------EVSAEEFMQALLEAKKQGLTREIGISNFTIPL 135
Cdd:cd19118 87 ALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltaVPTNggevdldlSVSLVDTWKAMVELKKTGKVKSIGVSNFSIDH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 136 MEKAIAAVGaENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLayGNALK-------DKVIARIAAKHNATPAQVIL 208
Cdd:cd19118 167 LQAIIEETG-VVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPL--GNNLAglpllvqHPEVKAIAAKLGKTPAQVLI 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 534608561 209 AWAMGEGYSVIPSSTKRENLESNLkaQNLQLDAEDKKAIAAL 250
Cdd:cd19118 244 AWGIQRGHSVIPKSVTPSRIRSNF--EQVELSDDEFNAVTAL 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
3-243 |
2.50e-65 |
|
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: 204.48 E-value: 2.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL---KDDVVISSVKtalELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSL 79
Cdd:cd19135 13 MPILGLGTSHSggySHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 80 KESLQKLRTDYVDLTLIHWP-SPSDEVSA----EEFMQALLEAKKQGLTREIGISNFTIP----LMEKAiaavgaeNIA- 149
Cdd:cd19135 90 EASLKRLGVDYLDLYLLHWPdCPSSGKNVketrAETWRALEELYDEGLCRAIGVSNFLIEhleqLLEDC-------SVVp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 150 -TNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENL 228
Cdd:cd19135 163 hVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERI 242
|
250
....*....|....*
gi 534608561 229 ESNLKAQNLQLDAED 243
Cdd:cd19135 243 KENCQVFDFSLSEED 257
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
2-248 |
4.62e-65 |
|
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: 204.50 E-value: 4.62e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESG----VPRHELYITTKIWIENLSKDKLIP 77
Cdd:cd19125 10 KIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPEDVPP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWP----SPSDEVSAEEF-----------MQALLEAkkqGLTREIGISNFTIPLMEKAIAA 142
Cdd:cd19125 90 ALEKTLKDLQLDYLDLYLIHWPvrlkKGAHMPEPEEVlppdipstwkaMEKLVDS---GKVRAIGVSNFSVKKLEDLLAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 vgAENI-ATNQIELSPYLQNRKVVAWAKQHGIHITSY-------MTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGE 214
Cdd:cd19125 167 --ARVPpAVNQVECHPGWQQDKLHEFCKSKGIHLSAYsplgspgTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQR 244
|
250 260 270
....*....|....*....|....*....|....
gi 534608561 215 GYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIA 248
Cdd:cd19125 245 GTSVLPKSTNEERIKENIDVFDWSIPEEDFAKFS 278
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
3-256 |
1.88e-63 |
|
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: 199.67 E-value: 1.88e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKD-DVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESGVPRHELYITTKIWIENLSKDKLIPSLKE 81
Cdd:cd19156 9 MPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKqglTREIGISNFTIPLMEKAIAAVgaeNIA--TNQIELSPYL 159
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKK---VRAIGVSNFHEHHLEELLKSC---KVApmVNQIELHPLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 160 QNRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQL 239
Cdd:cd19156 163 TQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFEL 242
|
250
....*....|....*..
gi 534608561 240 DAEDKKAIAALDCNDRL 256
Cdd:cd19156 243 TAEEIRQIDGLNTDHRY 259
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
3-250 |
1.06e-60 |
|
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: 193.25 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGT--FRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE---SGV--PRHELYITTKIWIENLSKDKL 75
Cdd:cd19124 5 MPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 76 IPSLKESLQKLRTDYVDLTLIHWP------SPSDEVSAEEFM--------QALLEAKKQGLTREIGISNFTIPLMEK--A 139
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPvslkpgKFSFPIEEEDFLpfdikgvwEAMEECQRLGLTKAIGVSNFSCKKLQEllS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 140 IAAVGAeniATNQIELSPYLQNRKVVAWAKQHGIHITSYMTL-AYGNA------LKDKVIARIAAKHNATPAQVILAWAM 212
Cdd:cd19124 165 FATIPP---AVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgAPGTKwgsnavMESDVLKEIAAAKGKTVAQVSLRWVY 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 534608561 213 GEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19124 242 EQGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKISEI 279
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
1-251 |
3.18e-60 |
|
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: 191.31 E-value: 3.18e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTFRLKDDV-----VISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESgvpRHELYITTKIWIENLSK 72
Cdd:cd19138 9 TKVPALGQGTWYMGEDPakraqEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLPSNASR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 73 DKLIPSLKESLQKLRTDYVDLTLIHWPSpsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIATNQ 152
Cdd:cd19138 86 QGTVRACERSLRRLGTDYLDLYLLHWRG---GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAANQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 153 IELSpyLQNR----KVVAWAKQHGIHITSYMTLAYGN-----ALKDKVIARIAAKHNATPAQVILAWAMGEGYSV-IPSS 222
Cdd:cd19138 163 VLYN--LGSRgieyDLLPWCREHGVPVMAYSPLAQGGllrrgLLENPTLKEIAARHGATPAQVALAWVLRDGNVIaIPKS 240
|
250 260
....*....|....*....|....*....
gi 534608561 223 TKRENLESNLKAQNLQLDAEDkkaIAALD 251
Cdd:cd19138 241 GSPEHARENAAAADLELTEED---LAELD 266
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
3-247 |
4.03e-60 |
|
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: 191.24 E-value: 4.03e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL---------KDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAEsgVPRHELYITTKIWIENL 70
Cdd:cd19137 4 IPALGLGTWGIggfltpdysRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 71 SKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVgAENIAT 150
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNP--NIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKS-QTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 151 NQIELSPY---LQNRKVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAMGEGYSV-IPSSTKRE 226
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVE 238
|
250 260
....*....|....*....|.
gi 534608561 227 NLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19137 239 HLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
3-256 |
1.21e-57 |
|
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: 185.39 E-value: 1.21e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIA---ESG-VPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19111 4 MPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWP--------------SPSDEVSAEEFMQALLEAkkqGLTREIGISNFTIPLMEKaIAAVG 144
Cdd:cd19111 84 LEKSLENLKLPYVDLYLIHHPcgfvnkkdkgerelASSDVTSVWRAMEALVSE---GKVKSIGLSNFNPRQINK-ILAYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 145 AENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTL-AYGNA-----------LKDKVIARIAAKHNATPAQVILAWAM 212
Cdd:cd19111 160 KVKPSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgSPGRAnqslwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 534608561 213 GEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRL 256
Cdd:cd19111 240 QRGTGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
3-259 |
3.86e-55 |
|
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: 179.89 E-value: 3.86e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAES-----GVPRHELYITTKIWIENLSKDKLIP 77
Cdd:cd19106 7 MPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWPS---------PS--------DEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKaI 140
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPYafergdnpfPKnpdgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDD-I 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 141 AAVGAENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGN----------ALKDKVIARIAAKHNATPAQVILAW 210
Cdd:cd19106 166 LSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPDrpwakpdepvLLEEPKVKALAKKYNKSPAQILLRW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 534608561 211 AMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLVSP 259
Cdd:cd19106 246 QVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVP 294
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
3-247 |
4.68e-54 |
|
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: 176.18 E-value: 4.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAES---GVPRHELYITTKIWieNLSKDKLIPSL 79
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLW--STYHRRVELCL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 80 KESLQKLRTDYVDLTLIHWPSP-SDEVSAEEF----------------------MQALLeakKQGLTREIGISNFTIPLM 136
Cdd:cd19121 90 DRSLKSLGLDYVDLYLVHWPVLlNPNGNHDLFptlpdgsrdldwdwnhvdtwkqMEKVL---KTGKTKAIGVSNYSIPYL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 137 EKAIAAvgAENI-ATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA--LKDKVIARIAAKHNATPAQVILAWAMG 213
Cdd:cd19121 167 EELLKH--ATVVpAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGSTGSplISDEPVVEIAKKHNVGPGTVLISYQVA 244
|
250 260 270
....*....|....*....|....*....|....
gi 534608561 214 EGYSVIPSSTKRENLESNLkaQNLQLDAEDKKAI 247
Cdd:cd19121 245 RGAVVLPKSVTPDRIKSNL--EIIDLDDEDMNKL 276
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
4-250 |
6.56e-54 |
|
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: 175.79 E-value: 6.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE----SGVPRHELYITTKIWIENLSKDKLIPSL 79
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 80 KESLQKLRTDYVDLTLIHWP---------SPSDE--------VSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAA 142
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlafdmdtdgDPRDDnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 VGAENIaTNQIELSPYLQNRKVVAWAKQHGIHITSYMTL----AYGNA--LKDKVIARIAAKHNATPAQVILAWAMGE-- 214
Cdd:cd19128 162 CKIKPF-MNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNLtfLNDSELKALATKYNTTPPQVIIAWHLQKwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 534608561 215 -GYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19128 241 kNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-260 |
1.22e-53 |
|
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: 176.14 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAESG----VPRHELYITTKIWieNLSKDKLIPS 78
Cdd:cd19112 11 MPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLW--NSDHGHVIEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPSPS-------------DEVSAEEF-----------MQALLEAkkqGLTREIGISNFTIP 134
Cdd:cd19112 89 CKDSLKKLQLDYLDLYLVHFPVATkhtgvgttgsalgEDGVLDIDvtislettwhaMEKLVSA---GLVRSIGISNYDIF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 135 LMEKAIAAVGAENiATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA----------LKDKVIARIAAKHNATPA 204
Cdd:cd19112 166 LTRDCLAYSKIKP-AVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAAnaewfgsvspLDDPVLKDLAKKYGKSAA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 534608561 205 QVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLVSPE 260
Cdd:cd19112 245 QIVLRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
3-267 |
8.50e-53 |
|
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: 173.79 E-value: 8.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQ----AIAESGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSKLWNNFHDPKNVETA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWP------------------SPSDEVSAE-----EFMQALLEAKKQGLTREIGISNFTIPL 135
Cdd:cd19113 91 LNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycGDGDNFVYEdvpilDTWKALEKLVDAGKIKSIGVSNFPGAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 136 MEKAIAavGAE-NIATNQIELSPYLQNRKVVAWAKQHGIHITSY--------MTLAYGNAL------KDKVIARIAAKHN 200
Cdd:cd19113 171 ILDLLR--GATiKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYssfgpqsfVELNQGRALntptlfEHDTIKSIAAKHN 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 534608561 201 ATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLVSPeglapeWD 267
Cdd:cd19113 249 KTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIGLRFNDP------WD 309
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
5-251 |
1.51e-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: 172.50 E-value: 1.51e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 5 AFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYD---NEAAVGQAIAESGVPRHELYITTKI------WIENLSKDKL 75
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGGSKENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 76 IPSLKESLQKLRTDYVDLTLIHWPSPSDEVsaEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAEnIATNQIEL 155
Cdd:pfam00248 87 RKSLEESLKRLGTDYIDLYYLHWPDPDTPI--EETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIP-IVAVQVEY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 156 SPY--LQNRKVVAWAKQHGIHITSYMTLAYG---------------------------NALKDKVIARIAAKHNATPAQV 206
Cdd:pfam00248 164 NLLrrRQEEELLEYCKKNGIPLIAYSPLGGGlltgkytrdpdkgpgerrrllkkgtplNLEALEALEEIAKEHGVSPAQV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 534608561 207 ILAWAMGE--GYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALD 251
Cdd:pfam00248 244 ALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
3-260 |
1.72e-51 |
|
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: 170.43 E-value: 1.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVG----QAIAESGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPSPSDEVSAEE---FMQALLEAKK--------------------QGLTREIGISNFTIPL 135
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAAYVDPAEnypFLWKDKELKKfpleqspmqecwremeklvdAGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 136 MEKAIAAVGAENiATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLA-------------YGNALKDKVIARIAAKHNAT 202
Cdd:cd19114 164 ILDLLTYAKIKP-AVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkhlkhFTNLLEHPVVKKLADKHKRD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 203 PAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLVSPE 260
Cdd:cd19114 243 TGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPV 300
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
3-250 |
2.70e-51 |
|
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: 169.97 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL-------KDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAesGVPRHELYITTKI------- 65
Cdd:COG0667 13 VSRLGLGTMTFggpwggvDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgrrmgpg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 -WIENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIA-AV 143
Cdd:COG0667 91 pNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDP--DTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAiAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 144 GAENIATNQIELSpyLQNRK----VVAWAKQHGIHITSYMTLAYG------------------------------NALKD 189
Cdd:COG0667 169 GLPPIVAVQNEYS--LLDRSaeeeLLPAARELGVGVLAYSPLAGGlltgkyrrgatfpegdraatnfvqgylterNLALV 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 534608561 190 KVIARIAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:COG0667 247 DALRAIAAEHGVTPAQLALAWLLAQPGvtSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-256 |
6.98e-51 |
|
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: 168.86 E-value: 6.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE---SG-VPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWP----------------------SPSDEVSAEEFMQALLEakkQGLTREIGISNFTIPLM 136
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqdYTTDLLDIWKAMEAQVD---QGLTRSIGLSNFNREQM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 137 EKaIAAVGAENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTL-----------------AYGNALKDKVIARIAAKH 199
Cdd:cd19155 169 AR-ILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVKAIAERH 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 534608561 200 NATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRL 256
Cdd:cd19155 248 GKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
3-259 |
2.34e-48 |
|
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: 162.20 E-value: 2.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQ----AIAESGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQgvarAIKEGIVKREDLFIVSKLWNTFHDGERVEPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWP-----------------SPSDEV-----SAEEFMQALLEAKKQGLTREIGISNFTIPLM 136
Cdd:cd19115 93 CRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfYDGKKVefsnaPIQETWTAMEKLVDKGLARSIGVSNFSAQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 137 EKAI--AAVGAeniATNQIELSPYLQNRKVVAWAKQHGIHIT--------SYMTLAYGNA------LKDKVIARIAAKHN 200
Cdd:cd19115 173 MDLLryARIRP---ATLQIEHHPYLTQPRLVKYAQKEGIAVTayssfgpqSFLELDLPGAkdtpplFEHDVIKSIAEKHG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 534608561 201 ATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLVSP 259
Cdd:cd19115 250 KTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNNP 308
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
3-247 |
3.69e-47 |
|
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: 158.52 E-value: 3.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL---------KDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAEsgvPRHELYITTKIWIENL 70
Cdd:cd19085 1 VSRLGLGCWQFgggywwgdqDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 71 SKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVgaeNIAT 150
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG---RIDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 151 NQIelsPY-LQNR----KVVAWAKQHGIHITSYMTLAYG----------------------------------NALkdKV 191
Cdd:cd19085 153 NQL---PYnLLWRaieyEILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhfepgaeeetfEAL--EK 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 192 IARIAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19085 228 LKEIADELGVTMAQLALAWVLQQPGvtSVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
3-244 |
1.91e-46 |
|
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: 156.89 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDD--VVISSVKTALELDYRAIDTAQIYDNEAAVGQAI----AESGVPRHELYITTKIWieNLSKDKLI 76
Cdd:cd19119 12 IPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIkraiDDGSIKREELFITTKVW--PTFYDEVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 77 PSLKESLQKLRTDYVDLTLIHWPSPSDEVSAE-----------------------EFMQALLEAKKQGLTREIGISNFTI 133
Cdd:cd19119 90 RSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpftpvnddgktryaasgdhiTTYKQLEKIYLDGRAKAIGVSNYSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 134 PLMEKAIAAVGAENiATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA--LKDKVIARIAAKHNATPAQVILAWA 211
Cdd:cd19119 170 VYLERLIKECKVVP-AVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGApnLKNPLVKKIAEKYNVSTGDILISYH 248
|
250 260 270
....*....|....*....|....*....|...
gi 534608561 212 MGEGYSVIPSSTKRENLESNLKAQNLQLDAEDK 244
Cdd:cd19119 249 VRQGVIVLPKSLKPVRIVSNGKIVSLTKEDLQK 281
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
3-255 |
7.21e-46 |
|
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: 155.65 E-value: 7.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIA----ESGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQekikEQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPS---------PSDE-----------VSAEEFMQALLEakkQGLTREIGISNFTIPLMEK 138
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPTgfkpgkelfPLDEsgnvipsdttfLDTWEAMEELVD---EGLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 139 AIAAVGAE-NIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGN----------ALKDKVIARIAAKHNATPAQVI 207
Cdd:cd19107 161 ILNKPGLKyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpwakpedpsLLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 534608561 208 LAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDR 255
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-255 |
1.59e-45 |
|
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: 154.70 E-value: 1.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKD---DVVISSVKTALELDYRAIDTAQIYDNEAAVGQAI----AESGVPRHELYITTKIWIENLSKDKL 75
Cdd:cd19108 11 IPVLGFGTYAPEEvpkSKALEATKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTFHRPELV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 76 IPSLKESLQKLRTDYVDLTLIHWP---------SPSDE--------VSAEEFMQALLEAKKQGLTREIGISNFTIPLMEK 138
Cdd:cd19108 91 RPALEKSLKKLQLDYVDLYLIHFPvalkpgeelFPKDEngklifdtVDLCATWEAMEKCKDAGLAKSIGVSNFNRRQLEM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 139 AIAAVGAENIAT-NQIELSPYLQNRKVVAWAKQHGIHITSYMTLA---YGN--------ALKDKVIARIAAKHNATPAQV 206
Cdd:cd19108 171 ILNKPGLKYKPVcNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGsqrDKEwvdqnspvLLEDPVLCALAKKHKRTPALI 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 534608561 207 ILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDR 255
Cdd:cd19108 251 ALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
2-257 |
3.17e-45 |
|
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: 154.19 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTF----RLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQA----IAESGVPRHELYITTKIWIENLSKD 73
Cdd:cd19109 3 SIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCHPPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 74 KLIPSLKESLQKLRTDYVDLTLIHWPS---------PSDEVSAEEF--------MQALLEAKKQGLTREIGISNFTIPLM 136
Cdd:cd19109 83 LVRPTLERTLKVLQLDYVDLYIIEMPMafkpgdeiyPRDENGKWLYhktnlcatWEALEACKDAGLVKSIGVSNFNRRQL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 137 EKAIAAVGAE-NIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNA-----------LKDKVIARIAAKHNATPA 204
Cdd:cd19109 163 ELILNKPGLKhKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvsspplLEDPLLNSIGKKYNKTAA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 534608561 205 QVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRLV 257
Cdd:cd19109 243 QVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
4-233 |
9.56e-44 |
|
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: 148.05 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRLKDDV----VISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAESGVpRHELYITTKI--------WIE 68
Cdd:cd06660 1 SRLGLGTMTFGGDGdeeeAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGghppggdpSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAEN- 147
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPS--TPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 148 --IATNQIELS---PYLQNRKVVAWAKQHGIHITSYMTLAYGnalkdkviariaakhnatPAQVILAWAMGEGY--SVIP 220
Cdd:cd06660 158 pgFAAVQPQYSlldRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFvtVPIV 219
|
250
....*....|...
gi 534608561 221 SSTKRENLESNLK 233
Cdd:cd06660 220 GARSPEQLEENLA 232
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
2-229 |
2.19e-43 |
|
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: 149.14 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 2 AIPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAI----AESGVPRHELYITTKIWIENLSKDKLIP 77
Cdd:cd19129 5 AIPALGFGTLIPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMqevfKAGKIRREDLFVTTKLWNTNHRPERVKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWP---SPSDE---------------VSAEEFMQALLEAKKQGLTREIGISNFTIPLMeKA 139
Cdd:cd19129 85 AFEASLKRLQLDYLDLYLIHTPfafQPGDEqdprdangnviyddgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKL-RE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 140 IAAVGAENIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYG---NALKDKVIARIAAKHNATPAQVILAWAMGEGY 216
Cdd:cd19129 164 IFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAWAIQRGT 243
|
250
....*....|....*..
gi 534608561 217 SVIPSSTK----RENLE 229
Cdd:cd19129 244 ALLTTSKTpsriRENFD 260
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
3-256 |
3.27e-43 |
|
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: 148.95 E-value: 3.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIA----ESGVPRHELYITTKIWIENLSKDKLIPS 78
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPS---------PSDE-----VSAEEFM---QALLEAKKQGLTREIGISNFTIPLMEKAIA 141
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPMgfkpgepdlPLDRsgmviPSDTDFLdtwEAMEDLVIEGLVKNIGVSNFNHEQLERLLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 142 AVGAE-NIATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAyGNA-----LKDKVIARIAAKHNATPAQVILAWAMGEG 215
Cdd:cd19110 164 KPGLRvKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG-GSCegvdlIDDPVIQRIAKKHGKSPAQILIRFQIQRN 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 534608561 216 YSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAALDCNDRL 256
Cdd:cd19110 243 VIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRL 283
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
3-247 |
1.36e-42 |
|
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: 146.90 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTF--------RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESgvpRHELYITTK---IWIE 68
Cdd:cd19084 4 VSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 ------NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAA 142
Cdd:cd19084 81 gkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPN--TPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 VgaeNIATNQIELSPYLQN--RKVVAWAKQHGIHITSYMTLAYG------------------NALKD------------- 189
Cdd:cd19084 159 G---PIVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrSRFPFfrgenfeknleiv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 190 KVIARIAAKHNATPAQVILAWAMG--EGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19084 236 DKLKEIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
8-243 |
8.11e-39 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 137.20 E-value: 8.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 8 LGTFRLKD-----DVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKIWIE----------- 68
Cdd:COG4989 18 LGCMRLGEwdlspAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKCGIRlpseardnrvk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 --NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSP---SDEVSAeefmqALLEAKKQGLTREIGISNFT---IPLMEKAI 140
Cdd:COG4989 98 hyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPlmdPEEVAE-----AFDELKASGKVRHFGVSNFTpsqFELLQSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 141 aavgAENIATNQIELSPY----LQNRkVVAWAKQHGIHITSYMTLAYGNALKD---------KVIARIAAKHNATPAQVI 207
Cdd:COG4989 173 ----DQPLVTNQIELSLLhtdaFDDG-TLDYCQLNGITPMAWSPLAGGRLFGGfdeqfprlrAALDELAEKYGVSPEAIA 247
|
250 260 270
....*....|....*....|....*....|....*...
gi 534608561 208 LAWAMGEGYSVIP--SSTKRENLESNLKAQNLQLDAED 243
Cdd:COG4989 248 LAWLLRHPAGIQPviGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
6-243 |
2.58e-38 |
|
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: 135.76 E-value: 2.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 6 FGLGTFRLKDDV-----VISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKIWIE--------- 68
Cdd:cd19092 9 LVLGCMRLADWGesaeeLLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKCGIRlgddprpgr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 ----NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEkAIAAVG 144
Cdd:cd19092 89 ikhyDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPL--MDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIE-LLQSYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 145 AENIATNQIELSPY---LQNRKVVAWAKQHGIHITSYMTLAYGNALKD---------KVIARIAAKHNATPAQVILAWAM 212
Cdd:cd19092 166 DQPLVTNQIELSLLhteAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGfderfqrlrAALEELAEEYGVTIEAIALAWLL 245
|
250 260 270
....*....|....*....|....*....|...
gi 534608561 213 GEGYSVIP--SSTKRENLESNLKAQNLQLDAED 243
Cdd:cd19092 246 RHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
3-250 |
3.42e-38 |
|
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: 135.44 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRLK--DDVVISSVKTALELDYRAIDTAQIYDNEAAVGQAIAE-----SGVPRHELYITTKIWIENLSKDKL 75
Cdd:cd19122 9 IPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 76 IPSLKESLQKLRTDYVDLTLIHWPSPSDEVS---------------------AEEFMQALLEAKKQGLTREIGISNFTIP 134
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDqrspklgpdgkyvilkdltenPEPTWRAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 135 LMEKAIAAVGAENiATNQIELSPYLQNRKVVAWAKQHGIHITSYMTLAYGNAL--------KDKVIARIAAKHNATPAQV 206
Cdd:cd19122 169 GLKKLLSFAKVKP-HVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSQNQVpstgervsENPTLNEVAEKGGYSLAQV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 534608561 207 ILAWAMGEGYSVIPSSTKRENLESNLKAqnLQLDAEDKKAIAAL 250
Cdd:cd19122 248 LIAWGLRRGYVVLPKSSTPSRIESNFKS--IELSDEDFEAINQV 289
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
3-251 |
4.91e-38 |
|
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: 135.05 E-value: 4.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTF-----------RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGvPRHELYITTKIWIE 68
Cdd:cd19093 2 VSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 --NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSDEvSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAE 146
Cdd:cd19093 81 pwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYS-QIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 147 NI--ATNQIE---LSPYLQNRKVVAWAKQHGIHITSYMTLAYG-----------------------NALKDK----VIAR 194
Cdd:cd19093 160 GVplASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrkNLEKVQplldALEE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 534608561 195 IAAKHNATPAQVILAWAMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDkkaIAALD 251
Cdd:cd19093 240 IAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEE---VAELD 293
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
3-240 |
6.76e-38 |
|
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: 133.50 E-value: 6.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL----------KDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAesgvPRHE-LYITTKI--- 65
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwgppaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALH----PYPDdVVIATKGglv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 ------WIENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKA 139
Cdd:cd19088 77 rtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDP--KVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 140 IAAVGaenIATNQIELSPYlqNRK---VVAWAKQHGIHITSYMTLAYGNALKDKV-IARIAAKHNATPAQVILAW--AMG 213
Cdd:cd19088 155 RAIVR---IVSVQNRYNLA--NRDdegVLDYCEAAGIAFIPWFPLGGGDLAQPGGlLAEVAARLGATPAQVALAWllARS 229
|
250 260
....*....|....*....|....*..
gi 534608561 214 EGYSVIPSSTKRENLESNLKAQNLQLD 240
Cdd:cd19088 230 PVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-250 |
1.56e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 120.86 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 15 DDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAESgvpRHELYITTK---IWIEN------LSKDKLIPSLKES 82
Cdd:cd19102 25 DRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWDEEgrirrsLKPASIRAECEAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 83 LQKLRTDYVDLTLIHWPSPSDEVsaEEFMQALLEAKKQGLTREIGISNFTIPLMeKAIAAVGAenIATNQIELSpyLQNR 162
Cdd:cd19102 102 LRRLGVDVIDLYQIHWPDPDEPI--EEAWGALAELKEEGKVRAIGVSNFSVDQM-KRCQAIHP--IASLQPPYS--LLRR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 ----KVVAWAKQHGIHITSYMTLAYGnALKDKV----IAR------------------------------IAAKHNATPA 204
Cdd:cd19102 175 gieaEILPFCAEHGIGVIVYSPMQSG-LLTGKMtperVASlpaddwrrrspffqepnlarnlalvdalrpIAERHGRTVA 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 534608561 205 QVILAWAMG--EGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19102 254 QLAIAWVLRrpEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-247 |
1.21e-30 |
|
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: 115.78 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL-------KDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAEsgvPRHELYITTKIWIENLSK 72
Cdd:cd19076 12 VSALGLGCMGMsafygpaDEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKFGIVRDPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 73 DKLIP----------SLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKA--- 139
Cdd:cd19076 89 SGFRGvdgrpeyvraACEASLKRLGTDVIDLYYQHRVDP--NVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAhav 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 140 --IAAVgaeniatnQIELSPYLQN--RKVVAWAKQHGIHITSYMTLAYG---NALKD----------------------- 189
Cdd:cd19076 167 hpITAV--------QSEYSLWTRDieDEVLPTCRELGIGFVAYSPLGRGfltGAIKSpedlpeddfrrnnprfqgenfdk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 534608561 190 -----KVIARIAAKHNATPAQVILAWAMGEGYSV--IPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19076 239 nlklvEKLEAIAAEKGCTPAQLALAWVLAQGDDIvpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
22-247 |
1.27e-30 |
|
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: 116.14 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 22 VKTALELDYRAIDTAQIYDN---EAAVGQAIAESGvPRHELYITTKIWI--------ENLSKDKLIPSLKESLQKLRTDY 90
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKVYFpmgdgpngRGLSRKHIMAEVDASLKRLGTDY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 91 VDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIaavgaeNIATNQiELSPY--LQN------- 161
Cdd:cd19079 120 IDLYQIHRWDY--ETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKAL------HLAEKN-GWTKFvsMQNhynllyr 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 162 ---RKVVAWAKQHGIHITSYMTLA---------------------------YGNALKDKVIAR---IAAKHNATPAQVIL 208
Cdd:cd19079 191 eeeREMIPLCEEEGIGVIPWSPLArgrlarpwgdtterrrsttdtaklkydYFTEADKEIVDRveeVAKERGVSMAQVAL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 534608561 209 AWAMGEGYSVIP--SSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19079 271 AWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
1-249 |
3.71e-30 |
|
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: 114.68 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTF---------RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESgvpRHELYITTK---I 65
Cdd:cd19149 9 IEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 WIE----------------NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGIS 129
Cdd:cd19149 86 WDReggsfffvrdgvtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDV--ETPIEETMEALEELKRQGKIRAIGAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 130 NFTIplmEKAIAAVGAENIATNQIELSpyLQNRKV----VAWAKQHGIHITSYMTLAYG--------------------- 184
Cdd:cd19149 164 NVSV---EQIKEYVKAGQLDIIQEKYS--MLDRGIekelLPYCKKNNIAFQAYSPLEQGlltgkitpdrefdagdarsgi 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 185 -----------NALKDKvIARIAAKHNATPAQVILAWAMGEG--YSVIPSSTKRENLESNLKAQNLQLDAEDKKAIAA 249
Cdd:cd19149 239 pwfspenrekvLALLEK-WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-250 |
5.73e-30 |
|
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: 114.05 E-value: 5.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 13 LKDDVVISSVKTALELDYRAIDTAQIYD---NEAAVGQAIAESGvpRHELYITTK---------IWIENlSKDKLIPSLK 80
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATKgahkfggdgSVLNN-SPEFLRSAVE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 81 ESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTiplMEKAIAAVGAENIATNQIELSpyLQ 160
Cdd:cd19083 107 KSLKRLNTDYIDLYYIHFPDG--ETPKAEAVGALQELKDEGKIRAIGVSNFS---LEQLKEANKDGYVDVLQGEYN--LL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 161 NRKVVA----WAKQHGIHITSYMTLAYG--------------NALK---------------DKV--IARIAAKHNATPAQ 205
Cdd:cd19083 180 QREAEEdilpYCVENNISFIPYFPLASGllagkytkdtkfpdNDLRndkplfkgerfsenlDKVdkLKSIADEKGVTVAH 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 534608561 206 VILAWAMGEGY--SVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19083 260 LALAWYLTRPAidVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
31-251 |
2.75e-29 |
|
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: 112.31 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 31 RAIDTAQIY----------DNEAAVGQAIAESGvPRHELYITTKI--WI----ENLSKDKLIPSLKESLQKLRTDYVDLT 94
Cdd:cd19081 41 NFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMgpngPGLSRKHIRRAVEASLRRLQTDYIDLY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 95 LIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENiatnqieLSPY--LQ------NRKVVA 166
Cdd:cd19081 120 QAHWDDP--ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHG-------LPRYvsLQpeynlvDRESFE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 167 W-----AKQHGIHITSYMTLAYG-----------------------NALKDK------VIARIAAKHNATPAQVILAWAM 212
Cdd:cd19081 191 GellplCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakRYLNERglrildALDEVAAEHGATPAQVALAWLL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 534608561 213 GEGY--SVIPSSTKRENLESNLKAQNLQLDAEDkkaIAALD 251
Cdd:cd19081 271 ARPGvtAPIAGARTVEQLEDLLAAAGLRLTDEE---VARLD 308
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
4-234 |
3.30e-29 |
|
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: 110.79 E-value: 3.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRLKDDVVISSVK-------TALELDYRAIDTAQIYDN-EAAVGQAIaeSGVPRHELYITTKIWIEN------ 69
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAeaarllnTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGeggrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 70 --LSKDKLIPSLKESLQKLRTDYVDLTLIHwpSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTiPLMEKAIAavgAEN 147
Cdd:cd19095 79 kdFSPAAIRASIERSLRRLGTDYIDLLQLH--GPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG-EELEAAIA---SGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 148 IATNQIELSPYLQ-NRKVVAWAKQHGIHITSYMTLAYGNALKD-----------KVIARIAAKHNATPAQVILAWAMGEG 215
Cdd:cd19095 153 FDVVQLPYNVLDReEEELLPLAAEAGLGVIVNRPLANGRLRRRvrrrplyadyaRRPEFAAEIGGATWAQAALRFVLSHP 232
|
250 260
....*....|....*....|.
gi 534608561 216 Y--SVIPSSTKRENLESNLKA 234
Cdd:cd19095 233 GvsSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-234 |
3.52e-29 |
|
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: 110.75 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 7 GLGTFRLkDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAesGVPRHELYITTKIWIENLSKDK--LIPSLKE 81
Cdd:cd19105 17 GFGGGGL-PRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPRLDKKDKaeLLKSVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 82 SLQKLRTDYVDLTLIHWPSPSDE-VSAEEFMQALLEAKKQGLTREIGIS--NFTIPLMEKAI------AAVGAENIATNQ 152
Cdd:cd19105 94 SLKRLQTDYIDIYQLHGVDTPEErLLNEELLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIesgwfdVIMVAYNFLNQP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 153 IELspylqnRKVVAWAKQHGIHITSYMTLAYGnaLKDKVIARIAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLES 230
Cdd:cd19105 174 AEL------EEALAAAAEKGIGVVAMKTLAGG--YLQPALLSVLKAKGFSLPQAALKWVLSNPRvdTVVPGMRNFAELEE 245
|
....
gi 534608561 231 NLKA 234
Cdd:cd19105 246 NLAA 249
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
3-250 |
5.24e-29 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 112.61 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFRL--KD-DVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAEsgvPRHELYITTKI--WIENlsKDKLI 76
Cdd:COG1453 13 VSVLGFGGMRLprKDeEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG---PRDKVILATKLppWVRD--PEDMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 77 PSLKESLQKLRTDYVDLTLIHWPSPSDE----VSAEEFMQALLEAKKQGLTREIGISNF-TIPLMEKAIAavgAENIATN 151
Cdd:COG1453 88 KDLEESLKRLQTDYIDLYLIHGLNTEEDlekvLKPGGALEALEKAKAEGKIRHIGFSTHgSLEVIKEAID---TGDFDFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 152 QIELSPYLQN----RKVVAWAKQHGIHITSyM-TLAYGN--ALKDKVIARIAAKhnATPAQVILAWAMG--EGYSVIPSS 222
Cdd:COG1453 165 QLQYNYLDQDnqagEEALEAAAEKGIGVII-MkPLKGGRlaNPPEKLVELLCPP--LSPAEWALRFLLShpEVTTVLSGM 241
|
250 260 270
....*....|....*....|....*....|
gi 534608561 223 TKRENLESNLKA--QNLQLDAEDKKAIAAL 250
Cdd:COG1453 242 STPEQLDENLKTadNLEPLTEEELAILERL 271
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
24-236 |
2.17e-27 |
|
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: 106.87 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 24 TALELDYRAIDTAQIY-------DNEAAVGQAIAESGVpRHELYITTK--------IWIENLSKDKLIPSLKESLQKLRT 88
Cdd:cd19082 25 AFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 89 DYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIA---AVGAENIATNQIELS------PYL 159
Cdd:cd19082 104 DYIDLYFLHRDDPS--VPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAyakAHGLPGFAASSPQWSlarpnePPW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 160 QNRKVV-------AWAKQHGIHITSYMTLAYG------------------------NALKDKVIARIAAKHNATPAQVIL 208
Cdd:cd19082 182 PGPTLVamdeemrAWHEENQLPVFAYSSQARGffskraaggaeddselrrvyyseeNFERLERAKELAEEKGVSPTQIAL 261
|
250 260 270
....*....|....*....|....*....|
gi 534608561 209 AWAMGEGYSVIP--SSTKRENLESNLKAQN 236
Cdd:cd19082 262 AYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-247 |
8.53e-27 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 105.99 E-value: 8.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTF--------RLKDDVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAESGVPRHELYITTKIWIE----- 68
Cdd:cd19144 13 VPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWFKQNPGKREKIFLATKFGIEknvet 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 69 -----NLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAav 143
Cdd:cd19144 93 geysvDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDG--KTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 144 gAENIATNQIELSPYL-----QNRKVVAWAKQHGIHITSYMTLAYG-------------------NA------------- 186
Cdd:cd19144 169 -VHPIAAVQIEYSPFSldierPEIGVLDTCRELGVAIVAYSPLGRGfltgairspddfeegdfrrMAprfqaenfpknle 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 534608561 187 LKDKvIARIAAKHNATPAQVILAW--AMGEGYSVIPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19144 248 LVDK-IKAIAKKKNVTAGQLTLAWllAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
7-234 |
9.73e-27 |
|
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: 103.71 E-value: 9.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 7 GLGTFRL--------KDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAEsgvPRHELYITTKI---------W 66
Cdd:cd19086 7 GFGTWGLggdwwgdvDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFgnrfdggpeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 67 IENLSKDKLIPSLKESLQKLRTDYVDLTLIHwpSPSDEVS-AEEFMQALLEAKKQGLTREIGISnfTIPLmEKAIAAVGA 145
Cdd:cd19086 84 PQDFSPEYIREAVEASLKRLGTDYIDLYQLH--NPPDEVLdNDELFEALEKLKQEGKIRAYGVS--VGDP-EEALAALRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 146 ENIATNQIELSPYLQN--RKVVAWAKQHGIHITSYMTLAYGnALKDKviariaakhnatPAQVILAWAMGEGY--SVIPS 221
Cdd:cd19086 159 GGIDVVQVIYNLLDQRpeEELFPLAEEHGVGVIARVPLASG-LLTGK------------LAQAALRFILSHPAvsTVIPG 225
|
250
....*....|...
gi 534608561 222 STKRENLESNLKA 234
Cdd:cd19086 226 ARSPEQVEENAAA 238
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
22-251 |
3.61e-26 |
|
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: 104.23 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 22 VKTALELDYRAIDTAQIYDN---EAAVGQAIAESgvpRHELYITTKI--WIEN------LSKDKLIPSLKESLQKLRTDY 90
Cdd:cd19091 45 VDIALDAGINFFDTADVYSEgesEEILGKALKGR---RDDVLIATKVrgRMGEgpndvgLSRHHIIRAVEASLKRLGTDY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 91 VDLTLIHWPSPSDEVsaEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIA---AVGAENIATNQIELSpyLQNR----K 163
Cdd:cd19091 122 IDLYQLHGFDALTPL--EETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGiseRRGLARFVALQAYYS--LLGRdlehE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 164 VVAWAKQHGIHITSYMTLAYGnALKDK---------------------------------VIARIAAKHNATPAQVILAW 210
Cdd:cd19091 198 LMPLALDQGVGLLVWSPLAGG-LLSGKyrrgqpapegsrlrrtgfdfppvdrergydvvdALREIAKETGATPAQVALAW 276
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 534608561 211 AMGEGY--SVIPSSTKRENLESNLKAQNLQLDAEDkkaIAALD 251
Cdd:cd19091 277 LLSRPTvsSVIIGARNEEQLEDNLGAAGLSLTPEE---IARLD 316
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
4-214 |
1.06e-25 |
|
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: 102.25 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRL-------KDDVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAEsgVPRHELYITTKI-----WIENL 70
Cdd:cd19090 1 SALGLGTAGLggvfggvDDDEAVATIRAALDLGINYIDTAPAYgDSEERLGLALAE--LPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 71 SKDKLIPSLKESLQKLRTDYVDLTLIH---WPSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAI------A 141
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIetgdfdV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 142 AVGAENI-ATNQIEL-----------------SPYLQN-------------------------RKVVAWAKQHGIHITsy 178
Cdd:cd19090 159 VLTANRYtLLDQSAAdellpaaarhgvgvinaSPLGMGllagrppervrytyrwlspelldraKRLYELCDEHGVPLP-- 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 534608561 179 mTLAYGNALKDKVIARI--AAkhnATPAQVI--LAWAMGE 214
Cdd:cd19090 237 -ALALRFLLRDPRISTVlvGA---SSPEELEqnVAAAEGP 272
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
7-242 |
1.17e-23 |
|
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: 96.89 E-value: 1.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 7 GLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAesGVPRHELYITTKI-WI-------ENL 70
Cdd:cd19074 8 SLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPtgpgpndRGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 71 SKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKA---IAAVGAEN 147
Cdd:cd19074 86 SRKHIFESIHASLKRLQLDYVDIYYCHRYDP--ETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdlARQFGLIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 148 IATNQIELSpYLQNRK---VVAWAKQHGIHITSYMTLAYG--------------------------------NALKDKV- 191
Cdd:cd19074 164 PVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrrlltDENLEKVk 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 534608561 192 -IARIAAKHNATPAQVILAWAMG--EGYSVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19074 243 kLKPIADELGLTLAQLALAWCLRnpAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-233 |
2.23e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 94.86 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGT---FRLKDDVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAEsgvPRHELYITTKIWieNLSKDKLIPS 78
Cdd:cd19100 11 VSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYgDSEEKIGKALKG---RRDKVFLATKTG--ARDYEGAKRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 79 LKESLQKLRTDYVDLTLIHWPSPSDEV----SAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAavgAENIATNQIE 154
Cdd:cd19100 86 LERSLKRLGTDYIDLYQLHAVDTEEDLdqvfGPGGALEALLEAKEEGKIRFIGISGHSPEVLLRALE---TGEFDVVLFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 155 LSP-YLQNR----KVVAWAKQHGIHITSYMTLAYGNALKDKVIARIAAkhnatpaqviLAWAMGEGY--SVIPSSTKREN 227
Cdd:cd19100 163 INPaGDHIDsfreELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA----------LRYALSLPPvdVVIVGMDSPEE 232
|
....*.
gi 534608561 228 LESNLK 233
Cdd:cd19100 233 LDENLA 238
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-184 |
4.18e-23 |
|
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: 95.45 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 19 ISSVKTALELDYRAIDTAQIYD---NEAAVGQAIAESGvPRHELYITTKI---WIE------NLSKDKLIPSLKESLQKL 86
Cdd:cd19148 28 IETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEggevvrNSSPARIRKEVEDSLRRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 87 RTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLME--KAIAAvgaenIATNQielSPY-----L 159
Cdd:cd19148 107 QTDYIDLYQVHWPDPL--VPIEETAEALKELLDEGKIRAIGVSNFSPEQMEtfRKVAP-----LHTVQ---PPYnlferE 176
|
170 180
....*....|....*....|....*
gi 534608561 160 QNRKVVAWAKQHGIhitsyMTLAYG 184
Cdd:cd19148 177 IEKDVLPYARKHNI-----VTLAYG 196
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
33-251 |
1.33e-22 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 94.21 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIYDN---EAAVGQAIAESgvpRHELYITTKiWIENLSKDK----------LIPSLKESLQKLRTDYVDLTLIHWP 99
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN---RDRIVLATK-YTMNRRPGDpnaggnhrknLRRSVEASLRRLQTDYIDLLYVHAW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 100 spsDEV-SAEEFMQALLEAKKQGLTREIGISNFtiPLMEKAIAAVGAE-----NIATNQIELSpyLQNRKV----VAWAK 169
Cdd:cd19080 124 ---DFTtPVEEVMRALDDLVRAGKVLYVGISDT--PAWVVARANTLAElrgwsPFVALQIEYS--LLERTPerelLPMAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 170 QHGIHITSYMTLAYG------------------------NALKDK------VIARIAAKHNATPAQVILAWAMGEGYSVI 219
Cdd:cd19080 197 ALGLGVTPWSPLGGGlltgkyqrgeegrageakgvtvgfGKLTERnwaivdVVAAVAEELGRSAAQVALAWVRQKPGVVI 276
|
250 260 270
....*....|....*....|....*....|....
gi 534608561 220 PS--STKRENLESNLKAQNLQLDAEdkkAIAALD 251
Cdd:cd19080 277 PIigARTLEQLKDNLGALDLTLSPE---QLARLD 307
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-249 |
4.61e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 92.66 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 14 KDDVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAESG---------------VPRHELYITTKIWIENlskdklip 77
Cdd:cd19101 21 DEDAAVRAMAAYVDAGLTTFDCADIYgPAEELIGEFRKRLRrerdaaddvqihtkwVPDPGELTMTRAYVEA-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 78 SLKESLQKLRTDYVDLTLIHWPSPSDEvSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAvGAEnIATNQIELS- 156
Cdd:cd19101 93 AIDRSLKRLGVDRLDLVQFHWWDYSDP-GYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILDA-GVP-IVSNQVQYSl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 157 ----PylqNRKVVAWAKQHGIHITSYMTLA--------------------------YGNALKD-----------KVIARI 195
Cdd:cd19101 170 ldrrP---ENGMAALCEDHGIKLLAYGTLAggllsekylgvpeptgpaletrslqkYKLMIDEwggwdlfqellRTLKAI 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 534608561 196 AAKHNATPAQVILAWAM---GEGySVIPSSTKRENLESNLKAQNLQLDAEDKKAIAA 249
Cdd:cd19101 247 ADKHGVSIANVAVRWVLdqpGVA-GVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-250 |
1.02e-21 |
|
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: 91.63 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 22 VKTALELDYRAIDTAQIY---DNEAAVGQAIAEsgVPRHELYITTKI--WIENLSKDKLIPSLKESLQKLRTDYVDLTLI 96
Cdd:cd19103 38 FDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFtpQIAGQSADPVADMLEGSLARLGTDYIDIYWI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 97 HwpSPSDevsAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIATNQIELSPYLQNRK-----VVAWAKQH 171
Cdd:cd19103 116 H--NPAD---VERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAVQNHYSLLYRSseeagILDYCKEN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 172 GIHITSYMTLAYG----------------------NALKDK------VIARIAAKHNATPAQVILAWAMGEGYSVIPSST 223
Cdd:cd19103 191 GITFFAYMVLEQGalsgkydtkhplpegsgraetyNPLLPQleeltaVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVT 270
|
250 260
....*....|....*....|....*..
gi 534608561 224 KRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19103 271 KPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
6-247 |
2.16e-21 |
|
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: 90.76 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 6 FGLGTFRL-------KDDVVISSVKTALELDYRAIDTAQIY------DNEAAVGQAIAESGVPRHELYITTKI-WIENL- 70
Cdd:cd19077 8 IGLGLMGLtwrpnptPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKGgLDPDTl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 71 ----SKDKLIPSLKESLQKLR-TDYVDltlIHWPSPSDE-VSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAiAAVg 144
Cdd:cd19077 88 rpdgSPEAVRKSIENILRALGgTKKID---IFEPARVDPnVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA-HAV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 145 aENIATNQIELSPY----LQNrKVVAWAKQHGIHITSYMTLAYG---NALKD---------------------------- 189
Cdd:cd19077 163 -HPIAAVEVEYSLFsreiEEN-GVLETCAELGIPIIAYSPLGRGlltGRIKSladipegdfrrhldrfngenfeknlklv 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534608561 190 KVIARIAAKHNATPAQVILAWAMGEGYSVI---PSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19077 241 DALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-234 |
5.40e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 87.00 E-value: 5.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIY----------DNEAAVGQAIAESGVpRHELYITTK------------IWIENLSKDKLIPSLKESLQKLRTDY 90
Cdd:cd19752 34 LDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKvgagprdpdggpESPEGLSAETIEQEIDKSLRRLGTDY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 91 VDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKaiaavgAENIATNQ-------IELS-PYLQNR 162
Cdd:cd19752 113 IDLYYAHVDDR--DTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER------ARQIARQQgwaefsaIQQRhSYLRPR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 163 -------------KVVAWAKQHG-IHITSYMTLAYG-----------------NALKDKVIARIAAKHNATPAQVILAWA 211
Cdd:cd19752 185 pgadfgvqrivtdELLDYASSRPdLTLLAYSPLLSGaytrpdrplpeqydgpdSDARLAVLEEVAGELGATPNQVVLAWL 264
|
250 260
....*....|....*....|....*
gi 534608561 212 MGEGYSVIP--SSTKRENLESNLKA 234
Cdd:cd19752 265 LHRTPAIIPllGASTVEQLEENLAA 289
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
33-250 |
3.95e-19 |
|
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: 84.93 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIYDN---EAAVGQAIAESgvpRHELYITTK--------IWIENLSKDKLIPSLKESLQKLRTDYVDLTLIHwpSP 101
Cdd:cd19087 47 FDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKvfgpmgddPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMH--HF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 102 SDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAENIATNQIELSPY-LQNR----KVVAWAKQHGIHIT 176
Cdd:cd19087 122 DRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYnLLKRqaelEILPAARAYGLGVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 177 SYMTLA-------YGNALKDKV------------------------IARIAAKHNATPAQVILAWAMGEGY--SVIPSST 223
Cdd:cd19087 202 PYSPLAgglltgkYGKGKRPESgrlveraryqarygleeyrdiaerFEALAAEAGLTPASLALAWVLSHPAvtSPIIGPR 281
|
250 260
....*....|....*....|....*..
gi 534608561 224 KRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19087 282 TLEQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-247 |
1.16e-18 |
|
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: 83.44 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 19 ISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAEsgvPRHELYITTK--IWIENLSKDKLIP---------SLKESLQ 84
Cdd:cd19078 28 IELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKfgFKIDGGKPGPLGLdsrpehirkAVEGSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 85 KLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKA-----IAAVGAE-NIATNQIE--LS 156
Cdd:cd19078 105 RLQTDYIDLYYQHRVDPN--VPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAhavcpVTAVQSEySMMWREPEkeVL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 157 PYLQnrkvvawakQHGIHITSYMTLAYG--------NALKDK-----------------------VIARIAAKHNATPAQ 205
Cdd:cd19078 183 PTLE---------ELGIGFVPFSPLGKGfltgkideNTKFDEgddraslprftpealeanqalvdLLKEFAEEKGATPAQ 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 534608561 206 VILAWAMGEGYSV--IPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19078 254 IALAWLLAKKPWIvpIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
4-173 |
2.68e-18 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 81.45 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRLKD--------DVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAEsgVPRHELYITTKI-WIENLS 71
Cdd:cd19096 1 SVLGFGTMRLPEsdddsideEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 72 KDKLIPSLKESLQKLRTDYVDLTLIHWP-SPSDEVSAEEF--MQALLEAKKQGLTREIGISnF--TIPLMEKAIAavgAE 146
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLnSPEWLEKARKGglLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILD---SY 154
|
170 180 190
....*....|....*....|....*....|.
gi 534608561 147 NIATNQIELS----PYLQNRKVVAWAKQHGI 173
Cdd:cd19096 155 DFDFVQLQYNyldqENQAGRPGIEYAAKKGM 185
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
42-243 |
8.41e-18 |
|
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: 81.15 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 42 EAAVGQAIAESGVP-RHELYITTKIWIENL--------SKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQ 112
Cdd:cd19089 60 EENFGRILKRDLRPyRDELVISTKAGYGMWpgpygdggSRKYLLASLDQSLKRMGLDYVDIFYHHRYDP--DTPLEETMT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 113 ALLEAKKQGLTREIGISNFTIPLMEKAIA---AVGAEnIATNQI-----------ELSPYLQNRKV--VAW--------- 167
Cdd:cd19089 138 ALADAVRSGKALYVGISNYPGAKARRAIAllrELGVP-LIIHQPryslldrwaedGLLEVLEEAGIgfIAFsplaqgllt 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 168 -------------AKQHGIHITSYMTLAYGNALkdKVIARIAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLESNL 232
Cdd:cd19089 217 dkylngippdsrrAAESKFLTEEALTPEKLEQL--RKLNKIAAKRGQSLAQLALSWVLRDPRvtSVLIGASSPSQLEDNV 294
|
250
....*....|..
gi 534608561 233 KA-QNLQLDAED 243
Cdd:cd19089 295 AAlKNLDFSEEE 306
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-233 |
1.78e-17 |
|
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: 80.44 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 5 AFGLGTFRL-----KDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAES----GVPRHELYITTKI------- 65
Cdd:cd19099 5 SLGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELiekgGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 --------WIENLSKDKLIP------------------SLKESLQKLRTDYVDLTLIHWPSPS-DEVSAEEFMQALLEA- 117
Cdd:cd19099 85 deplrplkYLEEKLGRGLIDvadsaglrhcispayledQIERSLKRLGLDTIDLYLLHNPEEQlLELGEEEFYDRLEEAf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 118 ------KKQGLTREIGISNFTIPLMEKA--------IAAVGAENIATN-------QIELSPYLQNRKVVAW--------- 167
Cdd:cd19099 165 ealeeaVAEGKIRYYGISTWDGFRAPPAlpghlsleKLVAAAEEVGGDnhhfkviQLPLNLLEPEALTEKNtvkgealsl 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 534608561 168 ---AKQHGIHITSYMTLAYGNALKDKVIARIAAKHNA-TPAQVILAWA---MGEGySVIPSSTKRENLESNLK 233
Cdd:cd19099 245 leaAKELGLGVIASRPLNQGQLLGELRLADLLALPGGaTLAQRALQFArstPGVD-SALVGMRRPEHVDENLA 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
33-250 |
1.84e-17 |
|
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: 80.30 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIY----------DNEAAVGQAIAESGvPRHELYITTKI--------WI----ENLSKDKLIPSLKESLQKLRTDY 90
Cdd:cd19094 35 IDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPrgggTRLDRENIREAVEGSLKRLGTDY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 91 VDLTLIHWPS----------------PSDEVSAEEFMQALLEAKKQGLTREIGISNFTiP--LME--KAIAAVGAENIAT 150
Cdd:cd19094 114 IDLYQLHWPDrytplfgggyytepseEEDSVSFEEQLEALGELVKAGKIRHIGLSNET-PwgVMKflELAEQLGLPRIVS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 151 NQIELSpyLQNRK-VVAWAKQ---HGIHITSYMTLA-------YGNALKDKVIAR------------------------- 194
Cdd:cd19094 193 IQNPYS--LLNRNfEEGLAEAchrENVGLLAYSPLAggvltgkYLDGAARPEGGRlnlfpgymaryrspqaleavaeyvk 270
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534608561 195 IAAKHNATPAQVILAWA-----MGegySVIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19094 271 LARKHGLSPAQLALAWVrsrpfVT---STIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-242 |
5.83e-17 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 78.36 E-value: 5.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGT------FRLKDDV-VISSVKTALELDYRAIDTAQIYDN---EAAVGQAIaeSGVPRHELYITTKI----- 65
Cdd:cd19163 11 LKVSKLGFGAsplggvFGPVDEEeAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKVgrygl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 -WIE--NLSKDKLIPSLKESLQKLRTDYVDLTLIHWP--SPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAI 140
Cdd:cd19163 89 dPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIefAPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 141 AAvgaeniATNQIE--LSpY----LQNR---KVVAWAKQHGIHITSYMTLAYGnALKD-------------KVIARIAAK 198
Cdd:cd19163 169 ER------SPVKIDtvLS-YchytLNDTsllELLPFFKEKGVGVINASPLSMG-LLTErgppdwhpaspeiKEACAKAAA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 534608561 199 H----NATPAQVILAWAMG--EGYSVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19163 241 YcksrGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
6-242 |
7.11e-17 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 78.47 E-value: 7.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 6 FGLGTF--RLKDDV----VISSVKTALELDYRAIDTAQIY-DNEAAVGQAIA--ESGVPRHELYITTK-----IWIENLS 71
Cdd:cd19164 18 FGAATFsyQYTTDPesipPVDIVRRALELGIRAFDTSPYYgPSEIILGRALKalRDEFPRDTYFIITKvgrygPDDFDYS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 72 KDKLIPSLKESLQKLRTDYVDLTLIHwpspsD-E-VSAEEFMQA---LLEAKKQGLTREIGISNFTIPLMEKAIAAVGAE 146
Cdd:cd19164 98 PEWIRASVERSLRRLHTDYLDLVYLH-----DvEfVADEEVLEAlkeLFKLKDEGKIRNVGISGYPLPVLLRLAELARTT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 147 NIATNQIELSpY----LQNRKVVAW-----AKQHGIHITSYMTLAYG--------------NALKDKVI--ARIAAKHNA 201
Cdd:cd19164 173 AGRPLDAVLS-YchytLQNTTLLAYipkflAAAGVKVVLNASPLSMGllrsqgppewhpasPELRAAAAkaAEYCQAKGT 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 534608561 202 TPAQVILAWAM----GEGYSVIPSSTKREnLESNLKAQNLQLDAE 242
Cdd:cd19164 252 DLADVALRYALrewgGEGPTVVGCSNVDE-LEEAVEAYWSVLAGA 295
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-247 |
8.82e-17 |
|
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: 78.24 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 19 ISSVKTALELDYRAIDTAQIY---DNEAAVGQAIaeSGVPRHELYITTKIWIENLSKDKLI---------PSLKESLQKL 86
Cdd:cd19145 36 IALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKAL--KDGPREKVQLATKFGIHEIGGSGVEvrgdpayvrAACEASLKRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 87 RTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKA-----IAAVgaeniatnQIELSPYLQN 161
Cdd:cd19145 114 DVDYIDLYYQHRIDTT--VPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAhavhpITAV--------QLEWSLWTRD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 162 --RKVVAWAKQHGIHITSYMTLAYG---------------------------NALKDKV----IARIAAKHNATPAQVIL 208
Cdd:cd19145 184 ieEEIIPTCRELGIGIVPYSPLGRGffagkakleellensdvrkshprfqgeNLEKNKVlyerVEALAKKKGCTPAQLAL 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 534608561 209 AWAMGEGYSV--IPSSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19145 264 AWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
10-247 |
9.45e-16 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 75.33 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 10 TF--RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKI-W-----IEN---LSKDKL 75
Cdd:cd19143 23 TFgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWggggpPPNdrgLSRKHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 76 IPSLKESLQKLRTDYVDLTLIHWPSPS------------------------DEVSAEEFMQALLEAKKQGLTReigisnf 131
Cdd:cd19143 103 VEGTKASLKRLQLDYVDLVFCHRPDPAtpieetvramndlidqgkafywgtSEWSAQQIEEAHEIADRLGLIP------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 132 tiPLMEkaiaavgaeniatnQIELSpYLQNRKV-VAWA---KQHGIHITSYMTLA-------YGNA-------------- 186
Cdd:cd19143 176 --PVME--------------QPQYN-LFHRERVeVEYAplyEKYGLGTTTWSPLAsglltgkYNNGipegsrlalpgyew 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 187 LKDKV-------------IARIAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLESNLKAQNL--QLDAEDKKAI 247
Cdd:cd19143 239 LKDRKeelgqekiekvrkLKPIAEELGCSLAQLAIAWCLKNPNvsTVITGATKVEQLEENLKALEVlpKLTPEVMEKI 316
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
6-251 |
2.28e-15 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 74.24 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 6 FGLGTFRL---------KD-DVVISSVKTALELDYRAIDTAQIYdNEAAVGQAIAESGVP-RHELYITTKI--------- 65
Cdd:PRK10376 20 LGYGAMQLagpgvfgppKDrDAAIAVLREAVALGVNHIDTSDFY-GPHVTNQLIREALHPyPDDLTIVTKVgarrgedgs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 WIENLSKDKLIPSLKESLQKLRT---DYVDLTLIHWPSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTiplmEKAIAA 142
Cdd:PRK10376 99 WLPAFSPAELRRAVHDNLRNLGLdvlDVVNLRLMGDGHGPAEGSIEEPLTVLAELQRQGLVRHIGLSNVT----PTQVAE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 143 vgAENIAT-----NQIELSPYLQNRKVVAWAKQhGIHITSYMTLAYGNALKDKVIARIAAKHNATPAQVILAWAM--GEG 215
Cdd:PRK10376 175 --ARKIAEivcvqNHYNLAHRADDALIDALARD-GIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLqrSPN 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 534608561 216 YSVIPSSTKRENLESNLKAQNLQLDAEdkkAIAALD 251
Cdd:PRK10376 252 ILLIPGTSSVAHLRENLAAAELVLSEE---VLAELD 284
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-234 |
5.58e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.56 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 12 RLKDDVVISSVKTALELDYRAIDTAQIY-DNEAAVGQAIAESgvprHELYITTKI----WIENLSKDKLIPSLKESLQKL 86
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYgDSEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEAAIEASVEASLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 87 RTDYVDLTLIHwpSPSDE-VSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGAE------NIATNQIELSPYL 159
Cdd:cd19097 98 KVDSLDGLLLH--NPDDLlKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDiiqlpfNILDQRFLKSGLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 160 QNrkvvawAKQHG--IHITS-------YMT----LAYGNALKDKV--IARIAAKHNATPAQVILAWAMGEGY--SVIPSS 222
Cdd:cd19097 176 AK------LKKKGieIHARSvflqgllLMEpdklPAKFAPAKPLLkkLHELAKKLGLSPLELALGFVLSLPEidKIVVGV 249
|
250
....*....|..
gi 534608561 223 TKRENLESNLKA 234
Cdd:cd19097 250 DSLEQLKEIIAA 261
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
6-132 |
8.34e-15 |
|
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: 72.59 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 6 FGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAiaesGVPRHELYITTKI--WIEN-LSKDK 74
Cdd:cd19075 5 LGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYpdgTSEELLGEL----GLGERGFKIDTKAnpGVGGgLSPEN 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 75 LIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFT 132
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLHAPDRS--TPLEETLAAIDELYKEGKFKEFGLSNYS 136
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
7-133 |
8.72e-15 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 72.57 E-value: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 7 GLGTFRLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKI-----WIENLSKDKLIPS 78
Cdd:cd19153 24 GVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEFDYSAERVRAS 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 79 LKESLQKLRTDYVDLTLIH---WPSPSDEVSaeEFMQALLEAKKQGLTREIGISNFTI 133
Cdd:cd19153 104 VATSLERLHTTYLDVVYLHdieFVDYDTLVD--EALPALRTLKDEGVIKRIGIAGYPL 159
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-250 |
9.49e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 69.88 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTFRLKDDVviSSVKTALELDY------RAIDTAQIYD----------NEAAVGQAIAESGvPRHELYITTK 64
Cdd:PRK10625 11 LEVSTLGLGTMTFGEQN--SEADAHAQLDYavaqgiNLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 65 IWIENLSKDKLI------------PSLKESLQKLRTDYVDLTLIHWP------------SPSDE---VSAEEFMQALLEA 117
Cdd:PRK10625 88 VSGPSRNNDKGIrpnqaldrknirEALHDSLKRLQTDYLDLYQVHWPqrptncfgklgySWTDSapaVSLLETLDALAEQ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 118 KKQGLTREIGISNFT-------IPLMEKAiaavGAENIATNQielSPY-LQNRKV---VAWAKQH-GIHITSYMTLAYG- 184
Cdd:PRK10625 168 QRAGKIRYIGVSNETafgvmryLHLAEKH----DLPRIVTIQ---NPYsLLNRSFevgLAEVSQYeGVELLAYSCLAFGt 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 185 ---------------NAL-----------KDKVIAR---IAAKHNATPAQVILAWAMGEGY--SVIPSSTKRENLESNLK 233
Cdd:PRK10625 241 ltgkylngakpagarNTLfsrftrysgeqTQKAVAAyvdIAKRHGLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNIE 320
|
330
....*....|....*..
gi 534608561 234 AQNLQLDAEDKKAIAAL 250
Cdd:PRK10625 321 SLHLTLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-250 |
1.23e-13 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 69.60 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 14 KDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESgvpRHELYITTKIWIENLS----KDKLIPSLKESLQKL 86
Cdd:cd19104 30 TREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYITTKVRLDPDDlgdiGGQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 87 RTDYVDLTLIH-------------WPSPSDEVSAEEFMQALLEAKKQGLTREIGISNF-TIPLMEKAIA--AVGAENIAT 150
Cdd:cd19104 107 KRDSVDLLQLHnrigderdkpvggTLSTTDVLGLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLDsgKFDAVQVYY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 151 NQIELSPYLQN---------RKVVAWAKQHGIHITSYMTLAYGnALKDKVIAR-----------------------IAAK 198
Cdd:cd19104 187 NLLNPSAAEARprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAG-ALTTSLDRGreapptsdsdvaidfrraaafraLARE 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 534608561 199 HNATPAQVILAWAMG-EGYS-VIPSSTKRENLESNLKAQNL-QLDAEDKKAIAAL 250
Cdd:cd19104 266 WGETLAQLAHRFALSnPGVStVLVGVKNREELEEAVAAEAAgPLPAENLARLEAL 320
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-234 |
3.18e-12 |
|
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: 65.45 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAESGVPRHELYITTKIWI----- 67
Cdd:cd19159 11 LRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 68 --ENLSKDKLIPSLKESLQKLRTDYVDLTLIHwpSPSDEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGA 145
Cdd:cd19159 91 teRGLSRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 146 ENIATNQIELSPY--LQNRKV---------------VAWAK----------QHGIHITSYMTLAYGNALKDKVIAR---- 194
Cdd:cd19159 169 FNMIPPVCEQAEYhlFQREKVevqlpelyhkigvgaMTWSPlacgiisgkyGNGVPESSRASLKCYQWLKERIVSEegrk 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 534608561 195 ----------IAAKHNATPAQVILAWAM-GEGY-SVIPSSTKRENLESNLKA 234
Cdd:cd19159 249 qqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENLGA 300
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-234 |
4.66e-11 |
|
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: 62.08 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIYDNEAA---VGQAIAESGVPRHELYITTKI-W---IEN- 69
Cdd:cd19141 12 VSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGKAeivLGKILKKKGWRRSSYVITTKIfWggkAETe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 70 --LSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFT-IPLMEkAIAAVGAE 146
Cdd:cd19141 92 rgLSRKHIIEGLKASLERLQLEYVDIVFANRPDPN--TPMEEIVRAFTHVINQGMAMYWGTSRWSaMEIME-AYSVARQF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 147 NIATNQIELSPY--LQNRKV---------------VAWAKQ----------HGIHITSYMTLAYGNALKDKVIARIAAKH 199
Cdd:cd19141 169 NLIPPIVEQAEYhlFQREKVemqlpelfhkigvgaMTWSPLacgilsgkydDGVPEYSRASLKGYQWLKEKILSEEGRRQ 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 534608561 200 NA--------------TPAQVILAWAM-GEG-YSVIPSSTKRENLESNLKA 234
Cdd:cd19141 249 QAklkelqiiadrlgcTLPQLAIAWCLkNEGvSSVLLGASSTEQLYENLQA 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
33-247 |
9.45e-11 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 60.90 E-value: 9.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIY---DNEAAVGQAIAESGVpRHELYITTK--IWIENLSKDK------------LIPSLKESLQKLRTDYVDLTL 95
Cdd:cd19146 52 IDTANNYqgeESERWVGEWMASRGN-RDEMVLATKytTGYRRGGPIKiksnyqgnhaksLRLSVEASLKKLQTSYIDILY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 96 IHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAV------------GAENIATNQIElspylqnRK 163
Cdd:cd19146 131 VHWWDYT--TSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYArahgltqfvvyqGHWSAAFRDFE-------RD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 164 VVAWAKQHGIHITSYMTLAYG---------NALKD---------------KVIARIAAKHNATPAQVILAWAMGEGYSVI 219
Cdd:cd19146 202 ILPMCEAEGMALAPWGVLGQGqfrteeefkRRGRSgrkggpqtekerkvsEKLEKVAEEKGTAITSVALAYVMHKAPYVF 281
|
250 260 270
....*....|....*....|....*....|
gi 534608561 220 P--SSTKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19146 282 PivGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
4-129 |
3.94e-10 |
|
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: 58.91 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGT------FRLKDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAesGVPRHELYITTKI--------- 65
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 534608561 66 -------WIENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSDEVSAEEFMQALLEAKKQGLTREIGIS 129
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFPALEELRAEGVVGAIGVG 149
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
13-133 |
7.92e-10 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 58.25 E-value: 7.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 13 LKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKI--WIE--NLSKDKLIPSLKESLQK 85
Cdd:PLN02587 28 VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgrYGEgfDFSAERVTKSVDESLAR 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 534608561 86 LRTDYVDLTLIH---WPSPSDEVSaeEFMQALLEAKKQGLTREIGISNFTI 133
Cdd:PLN02587 108 LQLDYVDILHCHdieFGSLDQIVN--ETIPALQKLKESGKVRFIGITGLPL 156
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
3-141 |
1.63e-09 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 57.41 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLG---TFRLKDDVVISS--VKTALELDYRAIDTAQIY-----DNEAAVGQAIAESGVP-RHELYITTK----IWI 67
Cdd:cd19151 12 LPAISLGlwhNFGDVDRYENSRamLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKagytMWP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 534608561 68 ----ENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIA 141
Cdd:cd19151 92 gpygDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDP--ETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAA 167
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-234 |
3.95e-09 |
|
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: 56.25 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIY---DNEAAVGQAIAESGVPRHELYITTKIWI----- 67
Cdd:cd19158 11 LRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 68 --ENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSDEVsaEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGA 145
Cdd:cd19158 91 teRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPM--EETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 146 ENIATNQIELSPY--LQNRKV---------------VAWAK----------QHGIHITSYMTLAYGNALKDKVIAR---- 194
Cdd:cd19158 169 FNLIPPICEQAEYhmFQREKVevqlpelfhkigvgaMTWSPlacgivsgkyDSGIPPYSRASLKGYQWLKDKILSEegrr 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 534608561 195 ----------IAAKHNATPAQVILAWAM-GEGY-SVIPSSTKRENLESNLKA 234
Cdd:cd19158 249 qqaklkelqaIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNAEQLMENIGA 300
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
33-247 |
3.96e-09 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 56.37 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 33 IDTAQIYDNEAA---VGQAIAESGVpRHELYITTKIWIENLS---------------KDKLIPSLKESLQKLRTDYVDLT 94
Cdd:cd19147 51 IDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYKAyevgkgkavnycgnhKRSLHVSVRDSLRKLQTDWIDIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 95 LIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGIS----------NFTIPLMEKAIAAV--GAENIATNQIE-------- 154
Cdd:cd19147 130 YVHWWDYT--TSIEEVMDSLHILVQQGKVLYLGVSdtpawvvsaaNYYATAHGKTPFSVyqGRWNVLNRDFErdiipmar 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 155 -----LSPY-------LQNRKVVAWAKQHGIHITSYMTLAYGNALKDKV---IARIAAKHN-ATPAQVILAWAMGEGYSV 218
Cdd:cd19147 208 hfgmaLAPWdvlgggkFQSKKAVEERKKNGEGLRSFVGGTEQTPEEVKIseaLEKVAEEHGtESVTAIALAYVRSKAPNV 287
|
250 260 270
....*....|....*....|....*....|.
gi 534608561 219 IPS--STKRENLESNLKAQNLQLDAEDKKAI 247
Cdd:cd19147 288 FPLvgGRKIEHLKDNIEALSIKLTPEEIEYL 318
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-234 |
2.42e-08 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 53.84 E-value: 2.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 1 MAIPAFGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAESGVPRHELYITTKIWI----- 67
Cdd:cd19160 13 LRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWggqae 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 68 --ENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSDEVsaEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAVGA 145
Cdd:cd19160 93 teRGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPM--EEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 146 ENIATNQIELSPY--LQNRKVVAWAKQ--HGIHITS--YMTLAYG---------------------NALKDKVIAR---- 194
Cdd:cd19160 171 FNLIPPVCEQAEYhlFQREKVEMQLPElyHKIGVGSvtWSPLACGlitgkydgrvpdtcraavkgyQWLKEKVQSEegkk 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 534608561 195 ----------IAAKHNATPAQVILAWAM-GEGY-SVIPSSTKRENLESNLKA 234
Cdd:cd19160 251 qqakvkelhpIADRLGCTVAQLAIAWCLrSEGVsSVLLGVSSAEQLIENLGS 302
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
3-137 |
5.50e-08 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 52.85 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTF-----RLKDDVVISSVKTALELDYRAIDTAQIYDNEAA---VGQAIAESGVPRHELYITTKIWIEN----- 69
Cdd:cd19142 13 VSNVGLGTWstfstAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAeteLGRILKKKGWKRSSYIVSTKIYWSYgseer 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 70 -LSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPSdeVSAEEFMQALLEAKKQGLTREIGISNFT-IPLME 137
Cdd:cd19142 93 gLSRKHIIESVRASLRRLQLDYIDIVIIHKADPM--CPMEEVVRAMSYLIDNGLIMYWGTSRWSpVEIME 160
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
4-242 |
2.36e-07 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 50.69 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGT------FR-LKDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAEsgVPRHELYITTKI-WI----- 67
Cdd:cd19152 1 PKLGFGTaplgnlYEaVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgRLlvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 68 -------------------ENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPS--DEVSAEEFMQALLEA-------KK 119
Cdd:cd19152 79 eveptfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDlaGAESDEHFAQAIKGAfraleelRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 120 QGLTREIGI-SNFTIPLMEkaIAAVGAENIA-----------TNQIELSPYLQNRKVvawakqhGIHI------------ 175
Cdd:cd19152 159 EGVIKAIGLgVNDWEVILR--ILEEADLDWVmlagrytlldhSAARELLPECEKRGV-------KVVNagpfnsgflagg 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 534608561 176 TSYMTLAYGNA---LKDKV--IARIAAKHNATPAQVILAWAMG-EGY-SVIPSSTKRENLESNLKAQNLQLDAE 242
Cdd:cd19152 230 DNFDYYEYGPAppeLIARRdrIEALCEQHGVSLAAAALQFALApPAVaSVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
4-128 |
3.00e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 50.40 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 4 PAFGLGTFRL-------KDDVVISSVKTALELDYRAIDTAQIYDN---EAAVGQAIAEsgVPRHELYITTKI-------- 65
Cdd:cd19161 1 SELGLGTAGLgnlytavSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 66 ---------WIENL--------SKDKLIPSLKESLQKLRTDYVDLTLIHWPSP---SDEVSAEEFMQ-------ALLEAK 118
Cdd:cd19161 79 egsvpdpngFVDPLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVythGDRKERHHFAQlmsggfkALEELK 158
|
170
....*....|
gi 534608561 119 KQGLTREIGI 128
Cdd:cd19161 159 KAGVIKAFGL 168
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-243 |
5.19e-06 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 46.68 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 3 IPAFGLGTFR-LKDDVVISS----VKTALELDYRAIDTAQIY-----DNEAAVGQAIAESGVP-RHELYITTK----IWI 67
Cdd:cd19150 12 LPALSLGLWHnFGDDTPLETqraiLRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKagydMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 68 ----ENLSKDKLIPSLKESLQKLRTDYVDLTLIHWPSPsdEVSAEEFMQALLEAKKQGLTREIGISNFTIPLMEKAIAAV 143
Cdd:cd19150 92 gpygEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDP--DTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAIL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 534608561 144 GAENIATNQIELSPYLQNRkvvaWAKQHGIHIT---------SYMTLAYGnALKDKVIA--------------------- 193
Cdd:cd19150 170 RELGTPLLIHQPSYNMLNR----WVEESGLLDTlqelgvgciAFTPLAQG-LLTDKYLNgipegsraskerslspkmlte 244
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 534608561 194 ----------RIAAKHNATPAQVILAWAM--GEGYSVIPSSTKRENLESNLKA-QNLQLDAED 243
Cdd:cd19150 245 anlnsiralnEIAQKRGQSLAQMALAWVLrdGRVTSALIGASRPEQLEENVGAlDNLTFSADE 307
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| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
186-250 |
1.47e-03 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 39.25 E-value: 1.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 534608561 186 ALKDKVIARIAAKHNATPAQVILAWAMGEGYS--VIPSSTKRENLESNLKAQNLQLDAEDKKAIAAL 250
Cdd:cd19098 235 APLMAVLKAVADRLGVTPDALALAAVLAQPFVdvVLSGAATPEQLRSNLRALDVSLDLELLAALADL 301
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|
| |
