|
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: 571.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQ 80
Cdd:PRK11172 1 MSIPAFGLGTFRLKDQVVIDSVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLAKDKLIPSLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 81 ESLQKLRTDYVDLTLIHWPSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIATNQIELSPYLQ 160
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 NSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLD 240
Cdd:PRK11172 161 NRKVVAFAKEHGIHVTSYMTLAYGKVLKDPVIARIAAKHNATPAQVILAWAMQLGYSVIPSSTKRENLASNLLAQDLQLD 240
|
250 260
....*....|....*....|....*..
gi 1453082642 241 DEDRQAIAALDCNDRLVSPEGLAPQWD 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 |
5.12e-172 |
|
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: 474.53 E-value: 5.12e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19139 1 IPAFGLGTFRLKDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIDNLSKDKLLPSLEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIATNQIELSPYLQNS 162
Cdd:cd19139 81 LEKLRTDYVDLTLIHWPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPYLQNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDE 242
Cdd:cd19139 161 KLVAHCKQHGIHVTSYMTLAYGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTKREHLRSNLLALDLTLDAD 240
|
....*...
gi 1453082642 243 DRQAIAAL 250
Cdd:cd19139 241 DMAAIAAL 248
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
1-256 |
2.23e-140 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 394.81 E-value: 2.23e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQ 80
Cdd:COG0656 3 VEIPALGLGTWQLPGEEAAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIAASGVPREELFVTTKVWNDNHGYDDTLAAFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 81 ESLQKLRTDYVDLTLIHWPSPNDavaVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGaENIATNQIELSPYLQ 160
Cdd:COG0656 83 ESLERLGLDYLDLYLIHWPGPGP---YVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG-VKPAVNQVELHPYLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 NSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLD 240
Cdd:COG0656 159 QRELLAFCREHGIVVEAYSPLGRGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTPERIRENLDAFDFELS 238
|
250
....*....|....*.
gi 1453082642 241 DEDRQAIAALDCNDRL 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 |
4.36e-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: 350.42 E-value: 4.36e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19073 1 IPALGLGTWQLRGDDCANAVKEALELGYRHIDTAEIYNNEAEVGEAIAESGVPREDLFITTKVWRDHLRPEDLKKSVDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGaENIATNQIELSPYLQNS 162
Cdd:cd19073 81 LEKLGTDYVDLLLIHWPNP--TVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP-LPIAVNQVEFHPFLYQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDE 242
Cdd:cd19073 158 ELLEYCRENDIVITAYSPLARGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDHLKENLAIFDWELTSE 237
|
....*
gi 1453082642 243 DRQAI 247
Cdd:cd19073 238 DVAKI 242
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
3-250 |
1.32e-113 |
|
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: 326.91 E-value: 1.32e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19140 8 IPALGLGTYPLTGEECTRAVEHALELGYRHIDTAQMYGNEAQVGEAIAASGVPRDELFLTTKVWPDNYSPDDFLASVEES 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAEnIATNQIELSPYLQNS 162
Cdd:cd19140 88 LRKLRTDYVDLLLLHWPNKD--VPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEAP-LFTNQVEYHPYLDQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAM-GEGYAVIPSSTKRDNLASNLKALDLQLDD 241
Cdd:cd19140 165 KLLDAAREHGIALTAYSPLARGEVLKDPVLQEIGRKHGKTPAQVALRWLLqQEGVAAIPKATNPERLEENLDIFDFTLSD 244
|
....*....
gi 1453082642 242 EDRQAIAAL 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 |
6.73e-108 |
|
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: 312.11 E-value: 6.73e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAALEAGYRHIDTAAAYGNEAEVGEAIRESGVPREELFITTKLWPTDHGYERVREALEES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDAVAV-EEFMA---ALMEAKKLGLTRQIGISNFTIPLMERaIAAVGAENIATNQIELSPY 158
Cdd:cd19071 81 LKDLGLDYLDLYLIHWPVPGKEGGSkEARLEtwrALEELVDEGLVRSIGVSNFNVEHLEE-LLAAARIKPAVNQIELHPY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 159 LQNSKVVDWAREHGIHITSYMTLA--YGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALD 236
Cdd:cd19071 160 LQQKELVEFCKEHGIVVQAYSPLGrgRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPERIKENLDVFD 239
|
250
....*....|..
gi 1453082642 237 LQLDDEDRQAIA 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 |
1.13e-89 |
|
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: 266.16 E-value: 1.13e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQ 80
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEAASAVREALEVGYRSIDTAAIYGNEEGVGKAIRASGVPREELFITTKLWNSDQGYDSTLRAFD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 81 ESLQKLRTDYVDLTLIHWPSPNDAVAVEEFmAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENiATNQIELSPYLQ 160
Cdd:cd19131 88 ESLRKLGLDYVDLYLIHWPVPAQDKYVETW-KALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVP-VVNQIELHPRFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 NSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLD 240
Cdd:cd19131 166 QRELRAFHAKHGIQTESWSPLGQGGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTPSRIAENFDVFDFELD 245
|
250
....*....|.
gi 1453082642 241 DEDRQAIAALD 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 |
7.15e-87 |
|
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: 259.12 E-value: 7.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19132 7 IPAIGFGTYPLKGDEGVEAVVAALQAGYRLLDTAFNYENEGAVGEAVRRSGVPREELFVTTKLPGRHHGYEEALRTIEES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDAVAVEEFmAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGaENIATNQIELSPYLQNS 162
Cdd:cd19132 87 LYRLGLDYVDLYLIHWPNPSRDLYVEAW-QALIEAREEGLVRSIGVSNFLPEHLDRLIDETG-VTPAVNQIELHPYFPQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAYGKA-LKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDD 241
Cdd:cd19132 165 EQRAYHREHGIVTQSWSPLGRGSGlLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPERQRENLAIFDFELSD 244
|
250
....*....|
gi 1453082642 242 EDRQAIAALD 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 |
9.54e-84 |
|
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: 252.72 E-value: 9.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQALEAGYRHIDCAAIYGNEAEIGAALAEvfkeGKVKREDLWITSKLWNNSHAPEDVLPA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWP-----------SPNDAVA-----VEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAA 142
Cdd:cd19123 92 LEKTLADLQLDYLDLYLMHWPvalkkgvgfpeSGEDLLSlspipLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 vGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYG------------KALKDEVIARIAAKHNATPAQVILAW 210
Cdd:cd19123 172 -ARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGdrpaamkaegepVLLEDPVINKIAEKHGASPAQVLIAW 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1453082642 211 AMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLV 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 |
1.81e-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: 245.62 E-value: 1.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKD-DVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAES----GVPRDELFITTKIWIENLSKDKLIA 77
Cdd:cd19136 1 MPILGLGTFRLRGeEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLlpkyGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWP-----SPNDAVAVE---EFMAALMEAKKLGLTRQIGISNFTIPLMERAIA------AV 143
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAElrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKycevppAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 gaeniatNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYG--KALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPS 221
Cdd:cd19136 161 -------NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGdlRLLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPK 233
|
250 260
....*....|....*....|....*....
gi 1453082642 222 STKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19136 234 STNPERIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
3-251 |
1.11e-80 |
|
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: 243.25 E-value: 1.11e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVI-ASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQE 81
Cdd:cd19133 9 MPILGFGVFQIPDPEECeRAVLEAIKAGYRLIDTAAAYGNEEAVGRAIKKSGIPREELFITTKLWIQDAGYEKAKKAFER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPNdavaVEEFMAALMEAKKLGLTRQIGISNFTiplMERAIAAVGAENI--ATNQIELSPYL 159
Cdd:cd19133 89 SLKRLGLDYLDLYLIHQPFGD----VYGAWRAMEELYKEGKIRAIGVSNFY---PDRLVDLILHNEVkpAVNQIETHPFN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSKVVDWAREHGIHITSYMTLAYGK--ALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDL 237
Cdd:cd19133 162 QQIEAVEFLKKYGVQIEAWGPFAEGRnnLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVRPERIAENFDIFDF 241
|
250
....*....|....
gi 1453082642 238 QLDDEDRQAIAALD 251
Cdd:cd19133 242 ELSDEDMEAIAALD 255
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
2-251 |
4.17e-79 |
|
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: 239.43 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQE 81
Cdd:cd19130 9 SIPQLGYGVFKVPPADTQRAVATALEVGYRHIDTAAIYGNEEGVGAAIAASGIPRDELFVTTKLWNDRHDGDEPAAAFAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPNDAVAVEEFmAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENiATNQIELSPYLQN 161
Cdd:cd19130 89 SLAKLGLDQVDLYLVHWPTPAAGNYVHTW-EAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVP-AVNQIELHPAYQQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 162 SKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDD 241
Cdd:cd19130 167 RTIRDWAQAHDVKIEAWSPLGQGKLLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRRERMEDNLDVFDFDLTD 246
|
250
....*....|
gi 1453082642 242 EDRQAIAALD 251
Cdd:cd19130 247 TEIAAIDALD 256
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
3-255 |
2.68e-78 |
|
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: 237.67 E-value: 2.68e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDD-VVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQE 81
Cdd:cd19157 10 MPWLGLGVFKVEEGsEVVNAVKTALKNGYRSIDTAAIYGNEEGVGKGIKESGIPREELFITSKVWNADQGYDSTLKAFEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPNDAVaveEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAvgAENI-ATNQIELSPYLQ 160
Cdd:cd19157 90 SLERLGLDYLDLYLIHWPVKGKYK---ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLAD--AEIVpMVNQVEFHPRLT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 NSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLD 240
Cdd:cd19157 165 QKELRDYCKKQGIQLEAWSPLMQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHRIIENADVFDFELS 244
|
250
....*....|....*
gi 1453082642 241 DEDRQAIAALDCNDR 255
Cdd:cd19157 245 QEDMDKIDALNENLR 259
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
2-257 |
1.13e-77 |
|
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: 236.80 E-value: 1.13e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTFRLKDDV-VIASVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIENLSKDKLI 76
Cdd:cd19116 10 EIPAIALGTWKLKDDEgVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAirekIAEGVVKREDLFITTKLWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 77 ASLQESLQKLRTDYVDLTLIHWP---------------SPNDaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA 141
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPvafkenndsesngdgSLSD-IDYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 142 AVgaeNI--ATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA---------LKDEVIARIAAKHNATPAQVILAW 210
Cdd:cd19116 169 NC---NIkpAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPrgqtnppprLDDPTLVAIAKKYGKTTAQIVLRY 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1453082642 211 AMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLV 257
Cdd:cd19116 246 LIDRGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
3-251 |
2.09e-75 |
|
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: 230.02 E-value: 2.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKD-DVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQE 81
Cdd:cd19126 9 MPWLGLGVFQTPDgDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIRESGVPREELFVTTKLWNDDQRARRTEDAFQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPNDAV----AVEEFMAAlmeakklGLTRQIGISNFTIPLMERaIAAVGAENIATNQIELSP 157
Cdd:cd19126 89 SLDRLGLDYVDLYLIHWPGKDKFIdtwkALEKLYAS-------GKVKAIGVSNFQEHHLEE-LLAHADVVPAVNQVEFHP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 158 YLQNSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDL 237
Cdd:cd19126 161 YLTQKELRGYCKSKGIVVEAWSPLGQGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASRIKENADIFDF 240
|
250
....*....|....
gi 1453082642 238 QLDDEDRQAIAALD 251
Cdd:cd19126 241 ELSEDDMTAIDALN 254
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
3-256 |
6.67e-75 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 229.19 E-value: 6.67e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWieNLSKDKLIASLQES 82
Cdd:PRK11565 15 MPQLGLGVWQASNEEVITAIHKALEVGYRSIDTAAIYKNEEGVGKALKEASVAREELFITTKLW--NDDHKRPREALEES 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPndavAVEEFMAA---LMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENiATNQIELSPYL 159
Cdd:PRK11565 93 LKKLQLDYVDLYLMHWPVP----AIDHYVEAwkgMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTP-VINQIELHPLM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSKVVDWAREHGIHITSYMTLAY-GKALKD-EVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDL 237
Cdd:PRK11565 168 QQRQLHAWNATHKIQTESWSPLAQgGKGVFDqKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTPSRIAENFDVFDF 247
|
250
....*....|....*....
gi 1453082642 238 QLDDEDRQAIAALDCNDRL 256
Cdd:PRK11565 248 RLDKDELGEIAKLDQGKRL 266
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
3-256 |
3.02e-73 |
|
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: 224.73 E-value: 3.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19134 11 MPVIGLGVGELSDDEAERSVSAALEAGYRLIDTAAAYGNEAAVGRAIAASGIPRGELFVTTKLATPDQGFTASQAACRAS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDAVAVEEFmAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGaENIATNQIELSPYLQNS 162
Cdd:cd19134 91 LERLGLDYVDLYLIHWPAGREGKYVDSW-GGLMKLREEGLARSIGVSNFTAEHLENLIDLTF-FTPAVNQIELHPLLNQA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDE 242
Cdd:cd19134 169 ELRKVNAQHGIVTQAYSPLGVGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNPERIASNLDVFDFELTAD 248
|
250
....*....|....
gi 1453082642 243 DRQAIAALDCNDRL 256
Cdd:cd19134 249 HMDALDGLDDGTRF 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
2-247 |
6.63e-73 |
|
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: 223.65 E-value: 6.63e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTFRL---------KDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIaeSGVPRDELFITTKIWIEN 69
Cdd:cd19072 3 EVPVLGLGTWGIgggmskdysDDKKAIEALRYAIELGINLIDTAEMYGGghaEELVGKAI--KGFDREDLFITTKVSPDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 70 LSKDKLIASLQESLQKLRTDYVDLTLIHWpsPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIA 149
Cdd:cd19072 81 LKYDDVIKAAKESLKRLGTDYIDLYLIHW--PNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGPIV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 150 TNQIELSPYLQN--SKVVDWAREHGIHITSYMTLAYGKALKDE---VIARIAAKHNATPAQVILAWAMG-EGYAVIPSST 223
Cdd:cd19072 159 ANQVEYNLFDREeeSGLLPYCQKNGIAIIAYSPLEKGKLSNAKgspLLDEIAKKYGKTPAQIALNWLISkPNVIAIPKAS 238
|
250 260
....*....|....*....|....
gi 1453082642 224 KRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19072 239 NIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-250 |
1.10e-71 |
|
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: 221.60 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWieNLSKDKLIASLQES 82
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVEAALKAGYRHIDTAAIYGNEEEVGQGIKDSGVPREEIFITTKLW--CTWHRRVEEALDQS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDAVAVE----------------EFMAALMEAKKL---GLTRQIGISNFTIPLMERAIAAV 143
Cdd:cd19117 92 LKKLGLDYVDLYLMHWPVPLDPDGNDflfkkddgtkdhepdwDFIKTWELMQKLpatGKVKAIGVSNFSIKNLEKLLASP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 GAENI-ATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA--LKDEVIARIAAKHNATPAQVILAWAMGEGYAVIP 220
Cdd:cd19117 172 SAKIVpAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTNAplLKEPVIIKIAKKHGKTPAQVIISWGLQRGYSVLP 251
|
250 260 270
....*....|....*....|....*....|
gi 1453082642 221 SSTKRDNLASNLKAldLQLDDEDRQAIAAL 250
Cdd:cd19117 252 KSVTPSRIESNFKL--FTLSDEEFKEIDEL 279
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
1-249 |
1.64e-71 |
|
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: 220.57 E-value: 1.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGT--FRLKDDVV----IASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIW--IENLSK 72
Cdd:cd19120 4 IPAIAFGTGTawYKSGDDDIqrdlVDSVKLALKAGFRHIDTAEMYGNEKEVGEALKESGVPREDLFITTKVSpgIKDPRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 73 dkliaSLQESLQKLRTDYVDLTLIHWP--SPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERaIAAVGAENIAT 150
Cdd:cd19120 84 -----ALRKSLAKLGVDYVDLYLIHSPffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEE-LLDTAKIKPAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 151 NQIELSPYLQN--SKVVDWAREHGIHITSYMTLA-----YGKALkDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSST 223
Cdd:cd19120 158 NQIEFHPYLYPqqPALLEYCREHGIVVSAYSPLSpltrdAGGPL-DPVLEKIAEKYGVTPAQVLLRWALQKGIVVVTTSS 236
|
250 260
....*....|....*....|....*.
gi 1453082642 224 KRDNLASNLKALDLQLDDEDRQAIAA 249
Cdd:cd19120 237 KEERMKEYLEAFDFELTEEEVEEIDK 262
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
3-251 |
2.47e-70 |
|
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: 217.27 E-value: 2.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQES 82
Cdd:cd19127 9 MPALGLGVFQTPPEETADAVATALADGYRLIDTAAAYGNEREVGEGIRRSGVDRSDIFVTTKLWISDYGYDKALRGFDAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDavaVEEFMAALMEAKKL---GLTRQIGISNFTIPLMERAIAAVGAENiATNQIELSPYL 159
Cdd:cd19127 89 LRRLGLDYVDLYLLHWPVPND---FDRTIQAYKALEKLlaeGRVRAIGVSNFTPEHLERLIDATTVVP-AVNQVELHPYF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSKVVDWAREHGIHITSYMTLA----YGKA--------LKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDN 227
Cdd:cd19127 165 SQKDLRAFHRRLGIVTQAWSPIGgvmrYGASgptgpgdvLQDPTITGLAEKYGKTPAQIVLRWHLQNGVSAIPKSVHPER 244
|
250 260
....*....|....*....|....
gi 1453082642 228 LASNLKALDLQLDDEDRQAIAALD 251
Cdd:cd19127 245 IAENIDIFDFALSAEDMAAIDALD 268
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
3-256 |
2.38e-69 |
|
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: 216.12 E-value: 2.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SGV-PRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19154 12 MPLIGLGTWQSKGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAElleEGVvKREDLFITTKLWTHEHAPEDVEEA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPSP-----------------NDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERaIA 141
Cdd:cd19154 92 LRESLKKLQLEYVDLYLIHAPAAfkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQR-IL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 142 AVGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAY-GKA--------------LKDEVIARIAAKHNATPAQV 206
Cdd:cd19154 171 DNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSpGRAnftkstgvspapnlLQDPIVKAIAEKHGKTPAQV 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1453082642 207 ILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRL 256
Cdd:cd19154 251 LLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEIEKSLRL 300
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
3-250 |
4.07e-69 |
|
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: 214.97 E-value: 4.07e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIENLSKDKLIA 77
Cdd:cd19118 7 IPAIGLGTWQAEPGEVGAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELlkeepGVKREDLFITSKLWNNSHRPEYVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWP--------------SPND--------AVAVEEFMAALMEAKKLGLTRQIGISNFTIPL 135
Cdd:cd19118 87 ALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltaVPTNggevdldlSVSLVDTWKAMVELKKTGKVKSIGVSNFSIDH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 136 MERAIAAVGaENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTL---AYGKAL--KDEVIARIAAKHNATPAQVILAW 210
Cdd:cd19118 167 LQAIIEETG-VVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLgnnLAGLPLlvQHPEVKAIAAKLGKTPAQVLIAW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1453082642 211 AMGEGYAVIPSSTKRDNLASNLKalDLQLDDEDRQAIAAL 250
Cdd:cd19118 246 GIQRGHSVIPKSVTPSRIRSNFE--QVELSDDEFNAVTAL 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
3-250 |
1.23e-68 |
|
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: 212.95 E-value: 1.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL---KDDVVIASVKtalELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASL 79
Cdd:cd19135 13 MPILGLGTSHSggySHEAVVYALK---ECGYRHIDTAKRYGCEELLGKAIKESGVPREDLFLTTKLWPSDYGYESTKQAF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 80 QESLQKLRTDYVDLTLIHWPSPNDAV-----AVEEFMAALMEAKKLGLTRQIGISNFTIP----LMERAiaavgaeNIA- 149
Cdd:cd19135 90 EASLKRLGVDYLDLYLLHWPDCPSSGknvkeTRAETWRALEELYDEGLCRAIGVSNFLIEhleqLLEDC-------SVVp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 150 -TNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNL 228
Cdd:cd19135 163 hVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLAKGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTKEERI 242
|
250 260
....*....|....*....|..
gi 1453082642 229 ASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19135 243 KENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
2-248 |
4.21e-68 |
|
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: 212.21 E-value: 4.21e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESG----VPRDELFITTKIWIENLSKDKLIA 77
Cdd:cd19125 10 KIPAVGLGTWQADPGVVGNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFedgvVKREDLFITSKLWCTDHAPEDVPP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWP---------------SPNDAVAVEEFMAALMEAkklGLTRQIGISNFTIPLMERAIAA 142
Cdd:cd19125 90 ALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeevLPPDIPSTWKAMEKLVDS---GKVRAIGVSNFSVKKLEDLLAV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 vgAENI-ATNQIELSPYLQNSKVVDWAREHGIHITSY-------MTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGE 214
Cdd:cd19125 167 --ARVPpAVNQVECHPGWQQDKLHEFCKSKGIHLSAYsplgspgTTWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQR 244
|
250 260 270
....*....|....*....|....*....|....
gi 1453082642 215 GYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIA 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 |
1.49e-65 |
|
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: 205.06 E-value: 1.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKD-DVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESGVPRDELFITTKIWIENLSKDKLIASLQE 81
Cdd:cd19156 9 MPRLGLGVWRVQDgAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIRESGVPREEVFVTTKLWNSDQGYESTLAAFEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPNDAVAVEEFMAALMEAKKLgltRQIGISNFTIPLMERAIAAVgaeNIA--TNQIELSPYL 159
Cdd:cd19156 89 SLEKLGLDYVDLYLIHWPVKGKFKDTWKAFEKLYKEKKV---RAIGVSNFHEHHLEELLKSC---KVApmVNQIELHPLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQL 239
Cdd:cd19156 163 TQEPLRKFCKEKNIAVEAWSPLGQGKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHEERIQENFDVFDFEL 242
|
250
....*....|....*..
gi 1453082642 240 DDEDRQAIAALDCNDRL 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 |
3.11e-65 |
|
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: 204.81 E-value: 3.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGT--FRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SGV--PRDELFITTKIWIENLSKDKL 75
Cdd:cd19124 5 MPVIGMGTasDPPSPEDIKAAVLEAIEVGYRHFDTAAAYGTEEALGEALAEalrLGLvkSRDELFVTSKLWCSDAHPDLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 76 IASLQESLQKLRTDYVDLTLIHWP------SPNDAVAVEEFM--------AALMEAKKLGLTRQIGISNFTIPLMER--A 139
Cdd:cd19124 85 LPALKKSLRNLQLEYVDLYLIHWPvslkpgKFSFPIEEEDFLpfdikgvwEAMEECQRLGLTKAIGVSNFSCKKLQEllS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 140 IAAVGAeniATNQIELSPYLQNSKVVDWAREHGIHITSYMTL-AYGKA------LKDEVIARIAAKHNATPAQVILAWAM 212
Cdd:cd19124 165 FATIPP---AVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLgAPGTKwgsnavMESDVLKEIAAAKGKTVAQVSLRWVY 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1453082642 213 GEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 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 |
1.06e-63 |
|
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: 200.55 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTFRLKDDV-----VIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTKIWIENLSK 72
Cdd:cd19138 9 TKVPALGQGTWYMGEDPakraqEIEALRAGIDLGMTLIDTAEMYGDggsEELVGEAIRGR---RDKVFLVSKVLPSNASR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 73 DKLIASLQESLQKLRTDYVDLTLIHWPSpndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIATNQ 152
Cdd:cd19138 86 QGTVRACERSLRRLGTDYLDLYLLHWRG---GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCAANQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 153 ---------IELSpylqnskVVDWAREHGIHITSYMTLAYG-----KALKDEVIARIAAKHNATPAQVILAWAMGEGYAV 218
Cdd:cd19138 163 vlynlgsrgIEYD-------LLPWCREHGVPVMAYSPLAQGgllrrGLLENPTLKEIAARHGATPAQVALAWVLRDGNVI 235
|
250 260 270
....*....|....*....|....*....|....
gi 1453082642 219 -IPSSTKRDNLASNLKALDLQLDDEDrqaIAALD 251
Cdd:cd19138 236 aIPKSGSPEHARENAAAADLELTEED---LAELD 266
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
3-256 |
5.87e-63 |
|
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: 199.26 E-value: 5.87e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIA---ESG-VPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19111 4 MPVIGLGTYQSPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKwwlKNGkLKREEVFITTKLPPVYLEFKDTEKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWP-----------SPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERaIAAVGAEN 147
Cdd:cd19111 84 LEKSLENLKLPYVDLYLIHHPcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK-ILAYAKVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 148 IATNQIELSPYLQNSKVVDWAREHGIHITSYMTL-AYGKA-----------LKDEVIARIAAKHNATPAQVILAWAMGEG 215
Cdd:cd19111 163 PSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLgSPGRAnqslwpdqpdlLEDPTVLAIAKELDKTPAQVLLRFVLQRG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1453082642 216 YAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRL 256
Cdd:cd19111 243 TGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
3-247 |
7.85e-63 |
|
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: 198.18 E-value: 7.85e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL---------KDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAEsgVPRDELFITTKIWIENL 70
Cdd:cd19137 4 IPALGLGTWGIggfltpdysRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKD--FPREDLFIVTKVWPTNL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 71 SKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVgAENIAT 150
Cdd:cd19137 82 RYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPN--IPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKS-QTPIVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 151 NQIELSPY---LQNSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAMGEGYAV-IPSSTKRD 226
Cdd:cd19137 159 NQVKYNLEdrdPERDGLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQKPNVVaIPKAGRVE 238
|
250 260
....*....|....*....|.
gi 1453082642 227 NLASNLKALDLQLDDEDRQAI 247
Cdd:cd19137 239 HLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
3-247 |
5.17e-61 |
|
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: 193.90 E-value: 5.17e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAES---GVPRDELFITTKIWieNLSKDKLIASL 79
Cdd:cd19121 12 IPAVGLGTWQAKAGEVKAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAiagGVKREDLFVTTKLW--STYHRRVELCL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 80 QESLQKLRTDYVDLTLIHWPSPNDAVAVEEFMA-------------------ALMEA-KKLGLTRQIGISNFTIPLMERA 139
Cdd:cd19121 90 DRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPtlpdgsrdldwdwnhvdtwKQMEKvLKTGKTKAIGVSNYSIPYLEEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 140 IAAvgAENI-ATNQIELSPYLQNSKVVDWAREHGIHITSYMTL--AYGKALKDEVIARIAAKHNATPAQVILAWAMGEGY 216
Cdd:cd19121 170 LKH--ATVVpAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLgsTGSPLISDEPVVEIAKKHNVGPGTVLISYQVARGA 247
|
250 260 270
....*....|....*....|....*....|.
gi 1453082642 217 AVIPSSTKRDNLASNLKALDlqLDDEDRQAI 247
Cdd:cd19121 248 VVLPKSVTPDRIKSNLEIID--LDDEDMNKL 276
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
3-259 |
4.61e-59 |
|
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: 189.90 E-value: 4.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAES-----GVPRDELFITTKIWIENLSKDKLIA 77
Cdd:cd19106 7 MPLIGLGTWKSKPGQVKAAVKYALDAGYRHIDCAAVYGNEQEVGEALKEKvgpgkAVPREDLFVTSKLWNTKHHPEDVEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWPS---------PNDA--------VAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERaI 140
Cdd:cd19106 87 ALRKTLKDLQLDYLDLYLIHWPYafergdnpfPKNPdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDD-I 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 141 AAVGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTL-----AYGKA-----LKDEVIARIAAKHNATPAQVILAW 210
Cdd:cd19106 166 LSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLgspdrPWAKPdepvlLEEPKVKALAKKYNKSPAQILLRW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1453082642 211 AMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSP 259
Cdd:cd19106 246 QVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYIVP 294
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
3-267 |
2.20e-58 |
|
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: 188.04 E-value: 2.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQ----AIAESGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEVGEgvnrAIDEGLVKREELFLTSKLWNNFHDPKNVETA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPSPNDAVAVEE-----FMA------------------ALMEAKKLGLTRQIGISNFTIPL 135
Cdd:cd19113 91 LNKTLSDLKLDYVDLFLIHFPIAFKFVPIEEkyppgFYCgdgdnfvyedvpildtwkALEKLVDAGKIKSIGVSNFPGAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 136 MERAIAavGAE-NIATNQIELSPYLQNSKVVDWAREHGIHITSY--------MTLAYGKAL------KDEVIARIAAKHN 200
Cdd:cd19113 171 ILDLLR--GATiKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYssfgpqsfVELNQGRALntptlfEHDTIKSIAAKHN 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1453082642 201 ATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSPeglapqWD 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 |
9.50e-58 |
|
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: 185.98 E-value: 9.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 5 AFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKI------WIENLSKDKL 75
Cdd:pfam00248 7 QLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPVKRDKVVIATKVpdgdgpWPSGGSKENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 76 IASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAEnIATNQIEL 155
Cdd:pfam00248 87 RKSLEESLKRLGTDYIDLYYLHWPDPD--TPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKIP-IVAVQVEY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 156 SPY--LQNSKVVDWAREHGIHITSYMTLAYGKALK---------------------------DEVIARIAAKHNATPAQV 206
Cdd:pfam00248 164 NLLrrRQEEELLEYCKKNGIPLIAYSPLGGGLLTGkytrdpdkgpgerrrllkkgtplnleaLEALEEIAKEHGVSPAQV 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1453082642 207 ILAWAMGE--GYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALD 251
Cdd:pfam00248 244 ALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
3-260 |
3.53e-57 |
|
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: 185.00 E-value: 3.53e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAESG----VPRDELFITTKIWieNLSKDKLIAS 78
Cdd:cd19112 11 MPVIGLGVWRMEPGEIKELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFktglVKREDLFITTKLW--NSDHGHVIEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPSPNDAVAVEEFMAALMEAKKL---------------------GLTRQIGISNFTIPLMe 137
Cdd:cd19112 89 CKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDGVLdidvtislettwhameklvsaGLVRSIGISNYDIFLT- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 138 RAIAAVGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA----------LKDEVIARIAAKHNATPAQVI 207
Cdd:cd19112 168 RDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAAnaewfgsvspLDDPVLKDLAKKYGKSAAQIV 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1453082642 208 LAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSPE 260
Cdd:cd19112 248 LRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSLDRKYRTNQPA 300
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
4-250 |
9.87e-56 |
|
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: 180.41 E-value: 9.87e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE----SGVPRDELFITTKIWIENLSKDKLIASL 79
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEifkdGGVKREDLFITSKLWPTMHQPENVKEQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 80 QESLQKLRTDYVDLTLIHWP---------SPNDA--------VAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAA 142
Cdd:cd19128 82 LITLQDLQLEYLDLFLIHWPlafdmdtdgDPRDDnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 VGAENIaTNQIELSPYLQNSKVVDWAREHGIHITSYMTL----AYGKA--LKDEVIARIAAKHNATPAQVILAWAMGE-- 214
Cdd:cd19128 162 CKIKPF-MNQIECHPYFQNDKLIKFCIENNIHVTAYRPLggsyGDGNLtfLNDSELKALATKYNTTPPQVIIAWHLQKwp 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1453082642 215 -GYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19128 241 kNYSVIPKSANKSRCQQNFDINDLALTKEDMDAINTL 277
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
3-250 |
1.69e-55 |
|
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: 180.76 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL-------KDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAesGVPRDELFITTKI------- 65
Cdd:COG0667 13 VSRLGLGTMTFggpwggvDEAEAIAILDAALDAGINFFDTADVYgpgRSEELLGEALK--GRPRDDVVIATKVgrrmgpg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 -WIENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA-AV 143
Cdd:COG0667 91 pNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPD--TPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAiAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 GAENIATNQIELSPYLQNS--KVVDWAREHGIHITSYMTLAYG----KALKD--------------------------EV 191
Cdd:COG0667 169 GLPPIVAVQNEYSLLDRSAeeELLPAARELGVGVLAYSPLAGGlltgKYRRGatfpegdraatnfvqgylternlalvDA 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1453082642 192 IARIAAKHNATPAQVILAWAMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:COG0667 249 LRAIAAEHGVTPAQLALAWLLAQPGvtSVIPGARSPEQLEENLAAADLELSAEDLAALDAA 309
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
3-260 |
2.83e-55 |
|
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: 180.06 E-value: 2.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVG----QAIAESGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19114 4 MPLVGFGTAKIKANETEEVIYNAIKVGYRLIDGALLYGNEAEVGrgirKAIQEGLVKREDLFIVTKLWNNFHGKDHVREA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPSPN---DAVAVEEFMAALMEAKKL--------------------GLTRQIGISNFTIPL 135
Cdd:cd19114 84 FDRQLKDYGLDYIDLYLIHFPIPAayvDPAENYPFLWKDKELKKFpleqspmqecwremeklvdaGLVRNIGIANFNVQL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 136 MERAIAAVGAENiATNQIELSPYLQNSKVVDWAREHGIHITSYMTLA-------------YGKALKDEVIARIAAKHNAT 202
Cdd:cd19114 164 ILDLLTYAKIKP-AVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGnavytkvtkhlkhFTNLLEHPVVKKLADKHKRD 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 203 PAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSPE 260
Cdd:cd19114 243 TGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYELEANARFNDPV 300
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
3-256 |
2.30e-53 |
|
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: 175.41 E-value: 2.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE---SG-VPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19155 12 MPVVGLGTWQSSPEEIETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKwidSGkVKREELFIVTKLPPGGNRREKVEKF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWP----------------------SPNDAVAVEEFMAALMEAkklGLTRQIGISNFTIPLM 136
Cdd:cd19155 92 LLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqdYTTDLLDIWKAMEAQVDQ---GLTRSIGLSNFNREQM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 137 ERaIAAVGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTL-----------------AYGKALKDEVIARIAAKH 199
Cdd:cd19155 169 AR-ILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLgspgaahfspgtgspsgSSPDLLQDPVVKAIAERH 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1453082642 200 NATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRL 256
Cdd:cd19155 248 GKSPAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSLDKNIRG 304
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
3-255 |
7.08e-52 |
|
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: 171.45 E-value: 7.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19107 4 MPILGLGTWKSPPGQVTEAVKVAIDAGYRHIDCAYVYQNENEVGEAIQekikEQVVKREDLFIVSKLWCTFHEKGLVKGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPS------------------PNDAVAVE--EFMAALMEAkklGLTRQIGISNFTIPLMER 138
Cdd:cd19107 84 CQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnviPSDTTFLDtwEAMEELVDE---GLVKAIGVSNFNHLQIER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 139 AIAAVGAE-NIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLA-----YGKA-----LKDEVIARIAAKHNATPAQVI 207
Cdd:cd19107 161 ILNKPGLKyKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGspdrpWAKPedpslLEDPKIKEIAAKHNKTTAQVL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1453082642 208 LAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDR 255
Cdd:cd19107 241 IRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWR 288
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
3-247 |
9.39e-51 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 168.15 E-value: 9.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL---------KDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAEsgvPRDELFITTKIWIENL 70
Cdd:cd19085 1 VSRLGLGCWQFgggywwgdqDDEESIATIHAALDAGINFFDTAEAYGDghsEEVLGKALKG---RRDDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 71 SKDKLIASLQESLQKLRTDYVDLTLIHWPSPndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVgaeNIAT 150
Cdd:cd19085 78 TPEDVRKSCERSLKRLGTDYIDLYQIHWPSS--DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG---RIDS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 151 NQIelsPY--LQNSK---VVDWAREHGIHITSYMTLAYG----------------------------------KALkdEV 191
Cdd:cd19085 153 NQL---PYnlLWRAIeyeILPFCREHGIGVLAYSPLAQGlltgkfssaedfppgdartrlfrhfepgaeeetfEAL--EK 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 192 IARIAAKHNATPAQVILAWAMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19085 228 LKEIADELGVTMAQLALAWVLQQPGvtSVIVGARNPEQLEENAAAVDLELSPSVLERL 285
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
3-259 |
1.42e-50 |
|
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: 167.98 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQ----AIAESGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNAIKAGYRLFDGACDYGNEVEAGQgvarAIKEGIVKREDLFIVSKLWNTFHDGERVEPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWP-----------------SPNDAVA-----VEEFMAALMEAKKLGLTRQIGISNFTIPLM 136
Cdd:cd19115 93 CRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfYDGKKVEfsnapIQETWTAMEKLVDKGLARSIGVSNFSAQLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 137 ERAI--AAVGAeniATNQIELSPYLQNSKVVDWAREHGIHIT--------SYMTLAYGKA------LKDEVIARIAAKHN 200
Cdd:cd19115 173 MDLLryARIRP---ATLQIEHHPYLTQPRLVKYAQKEGIAVTayssfgpqSFLELDLPGAkdtpplFEHDVIKSIAEKHG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1453082642 201 ATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLVSP 259
Cdd:cd19115 250 KTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISALDIGLRFNNP 308
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
3-245 |
3.52e-50 |
|
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: 166.52 E-value: 3.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDD--VVIASVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWieNLSKDKLI 76
Cdd:cd19119 12 IPALGLGTASPHEDraEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIkraiDDGSIKREELFITTKVW--PTFYDEVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 77 ASLQESLQKLRTDYVDLTLIHWPSPNDAVAVE-----------------------EFMAALMEAKKLGLTRQIGISNFTI 133
Cdd:cd19119 90 RSLDESLKALGLDYVDLLLVHWPVCFEKDSDDsgkpftpvnddgktryaasgdhiTTYKQLEKIYLDGRAKAIGVSNYSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 134 PLMERAIAAVGAENiATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA--LKDEVIARIAAKHNATPAQVILAWA 211
Cdd:cd19119 170 VYLERLIKECKVVP-AVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSHGApnLKNPLVKKIAEKYNVSTGDILISYH 248
|
250 260 270
....*....|....*....|....*....|....
gi 1453082642 212 MGEGYAVIPSSTKRDNLASNLKAldLQLDDEDRQ 245
Cdd:cd19119 249 VRQGVIVLPKSLKPVRIVSNGKI--VSLTKEDLQ 280
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-255 |
1.81e-47 |
|
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: 159.70 E-value: 1.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFR----LKDDVVIAsVKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIENLSKDK 74
Cdd:cd19108 11 IPVLGFGTYApeevPKSKALEA-TKLAIDAGFRHIDSAYLYQNEEEVGQAIrskiADGTVKREDIFYTSKLWCTFHRPEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 75 LIASLQESLQKLRTDYVDLTLIHWPSP----NDAVAVEE----------FMA---ALMEAKKLGLTRQIGISNFTIPLME 137
Cdd:cd19108 90 VRPALEKSLKKLQLDYVDLYLIHFPVAlkpgEELFPKDEngklifdtvdLCAtweAMEKCKDAGLAKSIGVSNFNRRQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 138 RAIAAVGAENIAT-NQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA-----------LKDEVIARIAAKHNATPAQ 205
Cdd:cd19108 170 MILNKPGLKYKPVcNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDkewvdqnspvlLEDPVLCALAKKHKRTPAL 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1453082642 206 VILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDR 255
Cdd:cd19108 250 IALRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDMKALDGLNRNLR 299
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
2-257 |
4.22e-47 |
|
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: 159.19 E-value: 4.22e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTF----RLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQA----IAESGVPRDELFITTKIWIENLSKD 73
Cdd:cd19109 3 SIPIIGLGTYsepkTTPKGACAEAVKVAIDTGYRHIDGAYIYQNEHEVGQAirekIAEGKVKREDIFYCGKLWNTCHPPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 74 KLIASLQESLQKLRTDYVDLTLIHWP---SPNDAV-----------------AVEEfmaALMEAKKLGLTRQIGISNFTI 133
Cdd:cd19109 83 LVRPTLERTLKVLQLDYVDLYIIEMPmafKPGDEIyprdengkwlyhktnlcATWE---ALEACKDAGLVKSIGVSNFNR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 134 PLMERAIAAVGAE-NIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYGKA-----------LKDEVIARIAAKHNA 201
Cdd:cd19109 160 RQLELILNKPGLKhKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDpiwvnvsspplLEDPLLNSIGKKYNK 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1453082642 202 TPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRLV 257
Cdd:cd19109 240 TAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEALNKNVRYV 295
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
3-247 |
1.70e-46 |
|
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: 156.92 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTF--------RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTK---IWIE 68
Cdd:cd19084 4 VSRIGLGTWaiggtwwgEVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKGR---RDDVVIATKcglRWDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 ------NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAA 142
Cdd:cd19084 81 gkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPN--TPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 VgaeNIATNQIELSPYLQN--SKVVDWAREHGIHITSYMTLAYG------------------------------KALKD- 189
Cdd:cd19084 159 G---PIVSLQPPYSMLEREieEELLPYCRENGIGVLPYGPLAQGlltgkykkeptfppddrrsrfpffrgenfeKNLEIv 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 190 EVIARIAAKHNATPAQVILAWAMG--EGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19084 236 DKLKEIAEKYGKSLAQLAIAWTLAqpGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
3-256 |
3.91e-46 |
|
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: 156.27 E-value: 3.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIENLSKDKLIAS 78
Cdd:cd19110 4 IPAVGLGTWKASPGEVTEAVKVAIDAGYRHFDCAYLYHNESEVGAGIRekikEGVVRREDLFIVSKLWCTCHKKSLVKTA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWP--------------------SPNDAVAVEEFMAALMEAkklGLTRQIGISNFTIPLMER 138
Cdd:cd19110 84 CTRSLKALKLNYLDLYLIHWPmgfkpgepdlpldrsgmvipSDTDFLDTWEAMEDLVIE---GLVKNIGVSNFNHEQLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 139 AIAAVGAE-NIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAyGKA-----LKDEVIARIAAKHNATPAQVILAWAM 212
Cdd:cd19110 161 LLNKPGLRvKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLG-GSCegvdlIDDPVIQRIAKKHGKSPAQILIRFQI 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1453082642 213 GEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAALDCNDRL 256
Cdd:cd19110 240 QRNVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSLDRNLRL 283
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
4-233 |
1.89e-45 |
|
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: 152.29 E-value: 1.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRLKDDV----VIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVpRDELFITTKI--------WIE 68
Cdd:cd06660 1 SRLGLGTMTFGGDGdeeeAFALLDAALEAGGNFFDTADVYgdgRSERLLGRWLKGRGN-RDDVVIATKGghppggdpSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAEN- 147
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPS--TPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGl 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 148 --IATNQIELS---PYLQNSKVVDWAREHGIHITSYMTLAYGkalkdeviariaakhnatPAQVILAWAMGEGY--AVIP 220
Cdd:cd06660 158 pgFAAVQPQYSlldRSPMEEELLDWAEENGLPLLAYSPLARG------------------PAQLALAWLLSQPFvtVPIV 219
|
250
....*....|...
gi 1453082642 221 SSTKRDNLASNLK 233
Cdd:cd06660 220 GARSPEQLEENLA 232
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
2-231 |
1.38e-44 |
|
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: 152.23 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 2 AIPAFGLGTFrLKDDVVIAS-VKTALELGYRAIDTAQIYDNEAAVGQAI----AESGVPRDELFITTKIWIENLSKDKLI 76
Cdd:cd19129 5 AIPALGFGTL-IPDPSATRNaVKAALEAGFRHFDCAERYRNEAEVGEAMqevfKAGKIRREDLFVTTKLWNTNHRPERVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 77 ASLQESLQKLRTDYVDLTLIHWP---------SPNDA---------VAVEEFMAALMEAKKLGLTRQIGISNFTIPLMeR 138
Cdd:cd19129 84 PAFEASLKRLQLDYLDLYLIHTPfafqpgdeqDPRDAngnviyddgVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKL-R 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 139 AIAAVGAENIATNQIELSPYLQNSKVVDWAREHGIHITSYMTLAYG---KALKDEVIARIAAKHNATPAQVILAWAMGEG 215
Cdd:cd19129 163 EIFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGHGmepKLLEDPVITAIARRVNKTPAQVLLAWAIQRG 242
|
250
....*....|....*.
gi 1453082642 216 YAVIPSSTKRDNLASN 231
Cdd:cd19129 243 TALLTTSKTPSRIREN 258
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
3-251 |
1.33e-43 |
|
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: 149.69 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTF-----------RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGvPRDELFITTKIWIE 68
Cdd:cd19093 2 VSPLGLGTWqwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYGTgrsERLLGRFLKELG-DRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 --NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNDAvAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAE 146
Cdd:cd19093 81 pwRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYS-QIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 147 NI--ATNQIE---LSPYLQNSKVVDWAREHGIHITSYMTLAYG----------------------KALKD-----EVIAR 194
Cdd:cd19093 160 GVplASNQVEyslLYRDPEQNGLLPACDELGITLIAYSPLAQGlltgkyspenpppggrrrlfgrKNLEKvqpllDALEE 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1453082642 195 IAAKHNATPAQVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDrqaIAALD 251
Cdd:cd19093 240 IAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEE---VAELD 293
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
8-243 |
3.91e-43 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 148.38 E-value: 3.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 8 LGTFRLKD-----DVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIE----------- 68
Cdd:COG4989 18 LGCMRLGEwdlspAEAAALIEAALELGITTFDHADIYGGytcEALFGEALKLSPSLREKIELQTKCGIRlpseardnrvk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 --NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMErAIAAVGAE 146
Cdd:COG4989 98 hyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDP--LMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE-LLQSALDQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 147 NIATNQIELSPY----LQNSkVVDWAREHGIHITSYMTLAYGKALKD---------EVIARIAAKHNATPAQVILAWAMG 213
Cdd:COG4989 175 PLVTNQIELSLLhtdaFDDG-TLDYCQLNGITPMAWSPLAGGRLFGGfdeqfprlrAALDELAEKYGVSPEAIALAWLLR 253
|
250 260 270
....*....|....*....|....*....|..
gi 1453082642 214 EGYAVIP--SSTKRDNLASNLKALDLQLDDED 243
Cdd:COG4989 254 HPAGIQPviGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
6-243 |
9.66e-43 |
|
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: 146.93 E-value: 9.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 6 FGLGTFRLKDDV-----VIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWIE--------- 68
Cdd:cd19092 9 LVLGCMRLADWGesaeeLLSLIEAALELGITTFDHADIYGGgkcEELFGEALALNPGLREKIEIQTKCGIRlgddprpgr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 ----NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSP-NDAvavEEFMAALMEAKKLGLTRQIGISNFTIPLMErAIAAV 143
Cdd:cd19092 89 ikhyDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPlMDP---EEVAEAFDELVKSGKVRYFGVSNFTPSQIE-LLQSY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 GAENIATNQIELSPY---LQNSKVVDWAREHGIHITSYMTLAYGKALKD---------EVIARIAAKHNATPAQVILAWA 211
Cdd:cd19092 165 LDQPLVTNQIELSLLhteAIDDGTLDYCQLLDITPMAWSPLGGGRLFGGfderfqrlrAALEELAEEYGVTIEAIALAWL 244
|
250 260 270
....*....|....*....|....*....|....
gi 1453082642 212 MGEGYAVIP--SSTKRDNLASNLKALDLQLDDED 243
Cdd:cd19092 245 LRHPARIQPilGTTNPERIRSAVKALDIELTREE 278
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
3-250 |
1.13e-40 |
|
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: 141.99 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLK--DDVVIASVKTALELGYRAIDTAQIYDNEAAVGQAIAE-----SGVPRDELFITTKIWIENLSKDKL 75
Cdd:cd19122 9 IPAVGFGTFANEgaKGETYAAVTKALDVGYRHLDCAWFYLNEDEVGDAVRDflkenPSVKREDLFICTKVWNHLHEPEDV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 76 IASLQESLQKLRTDYVDLTLIHWP-------------SPNDAVAVEEFMA--------ALMEAKKLGLTRQIGISNFTIP 134
Cdd:cd19122 89 KWSIDNSLKNLKLDYIDLFLVHWPiaaekndqrspklGPDGKYVILKDLTenpeptwrAMEEIYESGKAKAIGVSNWTIP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 135 LMERAIAAVGAENiATNQIELSPYLQNSKVVDWAREHGIHITSYMTL-------AYGKALKD-EVIARIAAKHNATPAQV 206
Cdd:cd19122 169 GLKKLLSFAKVKP-HVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLgsqnqvpSTGERVSEnPTLNEVAEKGGYSLAQV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1453082642 207 ILAWAMGEGYAVIPSSTKRDNLASNLKALDLQldDEDRQAIAAL 250
Cdd:cd19122 248 LIAWGLRRGYVVLPKSSTPSRIESNFKSIELS--DEDFEAINQV 289
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
3-240 |
7.77e-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: 7.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL----------KDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAesgvPRDE-LFITTKI--- 65
Cdd:cd19088 1 VSRLGYGAMRLtgpgiwgppaDREEAIAVLRRALELGVNFIDTADSYgpdVNERLIAEALH----PYPDdVVIATKGglv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 ------WIENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERA 139
Cdd:cd19088 77 rtgpgwWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPK--VPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 140 IAAVGaenIATNQIELSP-YLQNSKVVDWAREHGIHITSYMTLAYGKALKDEV-IARIAAKHNATPAQVILAW--AMGEG 215
Cdd:cd19088 155 RAIVR---IVSVQNRYNLaNRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGlLAEVAARLGATPAQVALAWllARSPV 231
|
250 260
....*....|....*....|....*
gi 1453082642 216 YAVIPSSTKRDNLASNLKALDLQLD 240
Cdd:cd19088 232 MLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-250 |
1.85e-36 |
|
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: 131.26 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 15 DDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAESgvpRDELFITTK---IWIEN------LSKDKLIASLQES 82
Cdd:cd19102 25 DRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL---RDRPIVATKcglLWDEEgrirrsLKPASIRAECEAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPSPNDavAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERaIAAVGAenIATNQIELS---PYL 159
Cdd:cd19102 102 LRRLGVDVIDLYQIHWPDPDE--PIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR-CQAIHP--IASLQPPYSllrRGI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSkVVDWAREHGIHITSYMTLAYG---KALKDEVIAR------------------------------IAAKHNATPAQV 206
Cdd:cd19102 177 EAE-ILPFCAEHGIGVIVYSPMQSGlltGKMTPERVASlpaddwrrrspffqepnlarnlalvdalrpIAERHGRTVAQL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1453082642 207 ILAWAMG--EGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19102 256 AIAWVLRrpEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-247 |
9.09e-36 |
|
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: 129.26 E-value: 9.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL-------KDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAEsgvPRDELFITTKIWIENLSK 72
Cdd:cd19076 12 VSALGLGCMGMsafygpaDEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD---RRDEVVIATKFGIVRDPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 73 DKLI----------ASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERA--- 139
Cdd:cd19076 89 SGFRgvdgrpeyvrAACEASLKRLGTDVIDLYYQHRVDPN--VPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAhav 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 140 --IAAVgaeniatnQIELSPYLQNSK--VVDWAREHGIHITSYMTLAYG------KALKD-------------------- 189
Cdd:cd19076 167 hpITAV--------QSEYSLWTRDIEdeVLPTCRELGIGFVAYSPLGRGfltgaiKSPEDlpeddfrrnnprfqgenfdk 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1453082642 190 -----EVIARIAAKHNATPAQVILAWAMGEGYAV--IPSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19076 239 nlklvEKLEAIAAEKGCTPAQLALAWVLAQGDDIvpIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
13-250 |
5.28e-35 |
|
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: 127.54 E-value: 5.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 13 LKDDVVIASVKTALELGYRAIDTAQIYD---NEAAVGQAIAESGvpRDELFITTK---------IWIENlSKDKLIASLQ 80
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGlgrSEELVGEVLKEYN--RNEVVIATKgahkfggdgSVLNN-SPEFLRSAVE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 81 ESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAiAAVGAENIATNQIELSPYLQ 160
Cdd:cd19083 107 KSLKRLNTDYIDLYYIHFPDGE--TPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVLQGEYNLLQREA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 NSKVVDWAREHGIHITSYMTLAY----GKALKD---------------------------EVIARIAAKHNATPAQVILA 209
Cdd:cd19083 184 EEDILPYCVENNISFIPYFPLASgllaGKYTKDtkfpdndlrndkplfkgerfsenldkvDKLKSIADEKGVTVAHLALA 263
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1453082642 210 WAMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19083 264 WYLTRPAidVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
3-247 |
7.23e-32 |
|
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: 119.47 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTF--------RLKDDVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAESGVPRDELFITTKIWIE----- 68
Cdd:cd19144 13 VPALGFGAMglsafygpPKPDEERFAVLDAAFELGCTFWDTADIYgDSEELIGRWFKQNPGKREKIFLATKFGIEknvet 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 69 -----NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAav 143
Cdd:cd19144 93 geysvDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGK--TPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 gAENIATNQIELSPYLQNSK-----VVDWAREHGIHITSYMTLAYG--------------------------------KA 186
Cdd:cd19144 169 -VHPIAAVQIEYSPFSLDIErpeigVLDTCRELGVAIVAYSPLGRGfltgairspddfeegdfrrmaprfqaenfpknLE 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1453082642 187 LKDEvIARIAAKHNATPAQVILAW--AMGEGYAVIPSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19144 248 LVDK-IKAIAKKKNVTAGQLTLAWllAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEI 309
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
1-249 |
3.48e-31 |
|
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: 117.37 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTF---------RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTK---I 65
Cdd:cd19149 9 IEASVIGLGTWaigggpwwgGSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKGR---RDKVVLATKcglR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 WIE----------------NLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGIS 129
Cdd:cd19149 86 WDReggsfffvrdgvtvykNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVE--TPIEETMEALEELKRQGKIRAIGAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 130 NFTIplmERAIAAVGAENIATNQIE---LSPYLQNSkVVDWAREHGIHITSYMTLAYG----KALKD------------- 189
Cdd:cd19149 164 NVSV---EQIKEYVKAGQLDIIQEKysmLDRGIEKE-LLPYCKKNNIAFQAYSPLEQGlltgKITPDrefdagdarsgip 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1453082642 190 --------------EVIARIAAKHNATPAQVILAWAMGEG--YAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAA 249
Cdd:cd19149 240 wfspenrekvlallEKWKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
7-235 |
6.63e-31 |
|
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: 115.37 E-value: 6.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 7 GLGTFRLkDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAesGVPRDELFITTKIWIENLSKDK--LIASLQE 81
Cdd:cd19105 17 GFGGGGL-PRESPELLRRALDLGINYFDTAEGYGNgnsEEIIGEALK--GLRRDKVFLATKASPRLDKKDKaeLLKSVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 82 SLQKLRTDYVDLTLIHWPSPND-AVAVEEFMAALMEAKKLGLTRQIGIS--NFTIPLMERAI------AAVGAENIATNQ 152
Cdd:cd19105 94 SLKRLQTDYIDIYQLHGVDTPEeRLLNEELLEALEKLKKEGKVRFIGFSthDNMAEVLQAAIesgwfdVIMVAYNFLNQP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 153 IELspylqnSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKhnATPAQVILAWAMGEGY--AVIPSSTKRDNLAS 230
Cdd:cd19105 174 AEL------EEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLKAKG--FSLPQAALKWVLSNPRvdTVVPGMRNFAELEE 245
|
....*
gi 1453082642 231 NLKAL 235
Cdd:cd19105 246 NLAAA 250
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
22-251 |
7.33e-31 |
|
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: 116.53 E-value: 7.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 22 VKTALELGYRAIDTAQIYDN---EAAVGQAIAESGvPRDELFITTKIWI--------ENLSKDKLIASLQESLQKLRTDY 90
Cdd:cd19079 41 IKRALDLGINFFDTANVYSGgasEEILGRALKEFA-PRDEVVIATKVYFpmgdgpngRGLSRKHIMAEVDASLKRLGTDY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 91 VDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTiplmerAIAAVGAENIATNQiELSPY--LQN------- 161
Cdd:cd19079 120 IDLYQIHRWDYE--TPIEETLEALHDVVKSGKVRYIGASSMY------AWQFAKALHLAEKN-GWTKFvsMQNhynllyr 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 162 ---SKVVDWAREHGIHITSYMTLAYG--------------------KALKD-------EVIAR---IAAKHNATPAQVIL 208
Cdd:cd19079 191 eeeREMIPLCEEEGIGVIPWSPLARGrlarpwgdtterrrsttdtaKLKYDyfteadkEIVDRveeVAKERGVSMAQVAL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1453082642 209 AWAMGEGYAVIP--SSTKRDNLASNLKALDLQLDDEDrqaIAALD 251
Cdd:cd19079 271 AWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEE---IKYLE 312
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
4-234 |
1.24e-30 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 114.64 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRLKDDVVIASVK-------TALELGYRAIDTAQIYDN-EAAVGQAIaeSGVPRDELFITTKIWIEN------ 69
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAeaarllnTALDLGINLIDTAPAYGRsEERLGRAL--AGLRRDDLFIATKVGTHGeggrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 70 --LSKDKLIASLQESLQKLRTDYVDLTLIHwpSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTiplmERAIAAVGAEN 147
Cdd:cd19095 79 kdFSPAAIRASIERSLRRLGTDYIDLLQLH--GPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 148 IATNQIELSPYLQNSK-VVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNA-----------TPAQVILAWAMGEG 215
Cdd:cd19095 153 FDVVQLPYNVLDREEEeLLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARrpefaaeiggaTWAQAALRFVLSHP 232
|
250 260
....*....|....*....|.
gi 1453082642 216 Y--AVIPSSTKRDNLASNLKA 234
Cdd:cd19095 233 GvsSAIVGTTNPEHLEENLAA 253
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
3-250 |
1.36e-30 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 116.84 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRL--KD-DVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAEsgvPRDELFITTKI--WIENlsKDKLI 76
Cdd:COG1453 13 VSVLGFGGMRLprKDeEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKG---PRDKVILATKLppWVRD--PEDMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 77 ASLQESLQKLRTDYVDLTLIHwpSPNDAVAVE------EFMAALMEAKKLGLTRQIGISNFTIPlmERAIAAVGAENIAT 150
Cdd:COG1453 88 KDLEESLKRLQTDYIDLYLIH--GLNTEEDLEkvlkpgGALEALEKAKAEGKIRHIGFSTHGSL--EVIKEAIDTGDFDF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 151 NQIELSPYLQNS----KVVDWAREHGIHITSyM-TLAYGK--ALKDEVIARIAAKhnATPAQVILAWAMG--EGYAVIPS 221
Cdd:COG1453 164 VQLQYNYLDQDNqageEALEAAAEKGIGVII-MkPLKGGRlaNPPEKLVELLCPP--LSPAEWALRFLLShpEVTTVLSG 240
|
250 260 270
....*....|....*....|....*....|.
gi 1453082642 222 STKRDNLASNLKALDL--QLDDEDRQAIAAL 250
Cdd:COG1453 241 MSTPEQLDENLKTADNlePLTEEELAILERL 271
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
24-236 |
1.26e-29 |
|
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: 112.65 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 24 TALELGYRAIDTAQIY-------DNEAAVGQAIAESGVpRDELFITTK--------IWIENLSKDKLIASLQESLQKLRT 88
Cdd:cd19082 25 AFVELGGNFIDTARVYgdwvergASERVIGEWLKSRGN-RDKVVIATKgghpdledMSRSRLSPEDIRADLEESLERLGT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 89 DYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA---AVGAENIATNQIELS------PYL 159
Cdd:cd19082 104 DYIDLYFLHRDDPS--VPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAyakAHGLPGFAASSPQWSlarpnePPW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 QNSKVV-------DWAREHGIHITSYMTLAYG---KALK---------------DEVIAR------IAAKHNATPAQVIL 208
Cdd:cd19082 182 PGPTLVamdeemrAWHEENQLPVFAYSSQARGffsKRAAggaeddselrrvyysEENFERlerakeLAEEKGVSPTQIAL 261
|
250 260 270
....*....|....*....|....*....|
gi 1453082642 209 AWAMGEGYAVIP--SSTKRDNLASNLKALD 236
Cdd:cd19082 262 AYVLNQPFPTVPiiGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
27-251 |
1.76e-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: 112.69 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 27 ELGYRAIDTAQIY----------DNEAAVGQAIAESGvPRDELFITTKI--WI----ENLSKDKLIASLQESLQKLRTDY 90
Cdd:cd19081 37 DAGGNFIDTADVYsawvpgnaggESETIIGRWLKSRG-KRDRVVIATKVgfPMgpngPGLSRKHIRRAVEASLRRLQTDY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 91 VDLTLIHWPSPndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENiatnqieLSPY--LQ-------- 160
Cdd:cd19081 116 IDLYQAHWDDP--ATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHG-------LPRYvsLQpeynlvdr 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 161 ---NSKVVDWAREHGIHITSYMTLAYG-----------------------KALKD------EVIARIAAKHNATPAQVIL 208
Cdd:cd19081 187 esfEGELLPLCREEGIGVIPYSPLAGGfltgkyrseadlpgstrrgeaakRYLNErglrilDALDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1453082642 209 AWAMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDrqaIAALD 251
Cdd:cd19081 267 AWLLARPGvtAPIAGARTVEQLEDLLAAAGLRLTDEE---VARLD 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
22-251 |
2.76e-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: 104.62 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 22 VKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTKI--WIEN------LSKDKLIASLQESLQKLRTDY 90
Cdd:cd19091 45 VDIALDAGINFFDTADVYSEgesEEILGKALKGR---RDDVLIATKVrgRMGEgpndvgLSRHHIIRAVEASLKRLGTDY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 91 VDLTLIHWPspnDAVA-VEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA---AVGAENIATNQIELSpyLQNS---- 162
Cdd:cd19091 122 IDLYQLHGF---DALTpLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGiseRRGLARFVALQAYYS--LLGRdleh 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 163 KVVDWAREHGIHITSYMTLAY----GKALKD----------------------------EVIARIAAKHNATPAQVILAW 210
Cdd:cd19091 197 ELMPLALDQGVGLLVWSPLAGgllsGKYRRGqpapegsrlrrtgfdfppvdrergydvvDALREIAKETGATPAQVALAW 276
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1453082642 211 AMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDrqaIAALD 251
Cdd:cd19091 277 LLSRPTvsSVIIGARNEEQLEDNLGAAGLSLTPEE---IARLD 316
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
19-247 |
1.00e-25 |
|
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: 102.70 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 19 IASVKTALELGYRAIDTAQIY---DNEAAVGQAIAEsgvPRDELFITTKIWIE-----------NLSKDKLIASLQESLQ 84
Cdd:cd19078 28 IELIRKAVELGITFFDTAEVYgpyTNEELVGEALKP---FRDQVVIATKFGFKidggkpgplglDSRPEHIRKAVEGSLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 85 KLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERA-----IAAVgaeniatnQIELSPyl 159
Cdd:cd19078 105 RLQTDYIDLYYQHRVDPN--VPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAhavcpVTAV--------QSEYSM-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 160 qnskvvdWAREH-----------GIHITSYMTLAYG--------------------------KALKD-----EVIARIAA 197
Cdd:cd19078 173 -------MWREPekevlptleelGIGFVPFSPLGKGfltgkidentkfdegddraslprftpEALEAnqalvDLLKEFAE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1453082642 198 KHNATPAQVILAWAMGEG-YAV-IPSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19078 246 EKGATPAQIALAWLLAKKpWIVpIPGTTKLSRLEENIGAADIELTPEELREI 297
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
7-184 |
1.24e-25 |
|
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: 101.01 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 7 GLGTFRL--------KDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAEsgvPRDELFITTKI---------W 66
Cdd:cd19086 7 GFGTWGLggdwwgdvDDAEAIRALRAALDLGINFFDTADVYGDghsERLLGKALKG---RRDKVVIATKFgnrfdggpeR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 67 IENLSKDKLIASLQESLQKLRTDYVDLTLIHWPsPNDAVAVEEFMAALMEAKKLGLTRQIGISnfTIPLmERAIAAVGAE 146
Cdd:cd19086 84 PQDFSPEYIREAVEASLKRLGTDYIDLYQLHNP-PDEVLDNDELFEALEKLKQEGKIRAYGVS--VGDP-EEALAALRRG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1453082642 147 NIATNQIELSPYLQNS--KVVDWAREHGIHITSYMTLAYG 184
Cdd:cd19086 160 GIDVVQVIYNLLDQRPeeELFPLAEEHGVGVIARVPLASG 199
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
4-140 |
3.97e-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: 100.71 E-value: 3.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRL-------KDDVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAEsgVPRDELFITTKI-----WIENL 70
Cdd:cd19090 1 SALGLGTAGLggvfggvDDDEAVATIRAALDLGINYIDTAPAYgDSEERLGLALAE--LPREPLVLSTKVgrlpeDTADY 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1453082642 71 SKDKLIASLQESLQKLRTDYVDLTLIH---WPSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAI 140
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHdpeRVPWVDILAPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAI 151
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-236 |
4.05e-25 |
|
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: 100.87 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 26 LELGYRAIDTAQIY----------DNEAAVGQAIAESGVpRDELFITTK------------IWIENLSKDKLIASLQESL 83
Cdd:cd19752 27 VAAGGNFLDTANNYafwteggvggESERLIGRWLKDRGN-RDDVVIATKvgagprdpdggpESPEGLSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 84 QKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAiaavgaENIATNQ-------IELS 156
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRD--TPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA------RQIARQQgwaefsaIQQR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 157 -PYLQ-------------NSKVVDWAREHG-IHITSYMTLAYG------KALKD-----------EVIARIAAKHNATPA 204
Cdd:cd19752 178 hSYLRprpgadfgvqrivTDELLDYASSRPdLTLLAYSPLLSGaytrpdRPLPEqydgpdsdarlAVLEEVAGELGATPN 257
|
250 260 270
....*....|....*....|....*....|....
gi 1453082642 205 QVILAWAMGEGYAVIP--SSTKRDNLASNLKALD 236
Cdd:cd19752 258 QVVLAWLLHRTPAIIPllGASTVEQLEENLAALD 291
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
7-242 |
4.96e-25 |
|
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: 100.74 E-value: 4.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 7 GLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAesGVPRDELFITTKI-WI-------ENL 70
Cdd:cd19074 8 SLGTWltfggQVDDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKALK--GWPRESYVISTKVfWPtgpgpndRGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 71 SKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERA---IAAVGAEN 147
Cdd:cd19074 86 SRKHIFESIHASLKRLQLDYVDIYYCHRYDPE--TPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAhdlARQFGLIP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 148 IATNQIELSpYLQNSK---VVDWAREHGIHITSYMTLAYG----------------------------KALKDEVIAR-- 194
Cdd:cd19074 164 PVVEQPQYN-MLWREIeeeVIPLCEKNGIGLVVWSPLAQGlltgkyrdgipppsrsratdednrdkkrRLLTDENLEKvk 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1453082642 195 ----IAAKHNATPAQVILAWAMG--EGYAVIPSSTKRDNLASNLKALDLQLDDE 242
Cdd:cd19074 243 klkpIADELGLTLAQLALAWCLRnpAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-233 |
8.60e-25 |
|
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: 98.71 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGT---FRLKDDVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAEsgvPRDELFITTKIWieNLSKDKLIAS 78
Cdd:cd19100 11 VSRLGFGGgplGRLSQEEAAAIIRRALDLGINYFDTAPSYgDSEEKIGKALKG---RRDKVFLATKTG--ARDYEGAKRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 79 LQESLQKLRTDYVDLTLIHWPS----PNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIplmERAIAAVGAENIATNQIE 154
Cdd:cd19100 86 LERSLKRLGTDYIDLYQLHAVDteedLDQVFGPGGALEALLEAKEEGKIRFIGISGHSP---EVLLRALETGEFDVVLFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 155 LSP-YLQNS----KVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAkhnatpaqviLAWAMGEGY--AVIPSSTKRDN 227
Cdd:cd19100 163 INPaGDHIDsfreELLPLAREKGVGVIAMKVLAGGRLLSGDPLDPEQA----------LRYALSLPPvdVVIVGMDSPEE 232
|
....*.
gi 1453082642 228 LASNLK 233
Cdd:cd19100 233 LDENLA 238
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-243 |
9.95e-25 |
|
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: 100.10 E-value: 9.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 5 AFGLGTF--RLKDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAEsgVPRDELFITTKI--WIENLSKDKLIA 77
Cdd:cd19103 19 AGGDQVFgnHLDEDTLKAVFDKAMAAGLNLWDTAAVYgmgASEKILGEFLKR--YPREDYIISTKFtpQIAGQSADPVAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWPSpnDAVAVEEFMAALMeakKLGLTRQIGISNFTIPLMERAIAAVGAENIATNQIE--- 154
Cdd:cd19103 97 MLEGSLARLGTDYIDIYWIHNPA--DVERWTPELIPLL---KSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAVQnhy 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 155 --LSPYLQNSKVVDWAREHGIHITSYMTL-------AYGKA-------------------LKD--EVIARIAAKHNATPA 204
Cdd:cd19103 172 slLYRSSEEAGILDYCKENGITFFAYMVLeqgalsgKYDTKhplpegsgraetynpllpqLEEltAVMAEIGAKHGASIA 251
|
250 260 270
....*....|....*....|....*....|....*....
gi 1453082642 205 QVILAWAMGEGYAVIPSSTKRDNLASNLKALDLQLDDED 243
Cdd:cd19103 252 QVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDE 290
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
19-184 |
1.91e-24 |
|
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: 99.30 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 19 IASVKTALELGYRAIDTAQIYD---NEAAVGQAIAESGvPRDELFITTKI---WIE------NLSKDKLIASLQESLQKL 86
Cdd:cd19148 28 IETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-KRDRVVIATKVgleWDEggevvrNSSPARIRKEVEDSLRRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 87 RTDYVDLTLIHWPSPndAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLME--RAIAAvgaenIATNQielSPY-----L 159
Cdd:cd19148 107 QTDYIDLYQVHWPDP--LVPIEETAEALKELLDEGKIRAIGVSNFSPEQMEtfRKVAP-----LHTVQ---PPYnlferE 176
|
170 180
....*....|....*....|....*
gi 1453082642 160 QNSKVVDWAREHGIhitsyMTLAYG 184
Cdd:cd19148 177 IEKDVLPYARKHNI-----VTLAYG 196
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
6-247 |
2.11e-24 |
|
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: 99.24 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 6 FGLGTFRL-------KDDVVIASVKTALELGYRAIDTAQIY------DNEAAVGQAIAESGVPRDELFITTKI-WIENL- 70
Cdd:cd19077 8 IGLGLMGLtwrpnptPDEEAFETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKYPEYADKVVLSVKGgLDPDTl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 71 ----SKDKLIASLQESLQKLR-TDYVDltlIHWPSPND-AVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAiAAVg 144
Cdd:cd19077 88 rpdgSPEAVRKSIENILRALGgTKKID---IFEPARVDpNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRA-HAV- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 145 aENIATNQIELSPY----LQNSkVVDWAREHGIHITSYMTLAYG------KALKD------------------------- 189
Cdd:cd19077 163 -HPIAAVEVEYSLFsreiEENG-VLETCAELGIPIIAYSPLGRGlltgriKSLADipegdfrrhldrfngenfeknlklv 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1453082642 190 EVIARIAAKHNATPAQVILAWAMGEGYAVI---PSSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19077 241 DALQELAEKKGCTPAQLALAWILAQSGPKIipiPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-249 |
2.12e-24 |
|
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: 99.21 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 14 KDDVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAESG---------------VPRDELFITTKIWIEnlskdkliA 77
Cdd:cd19101 21 DEDAAVRAMAAYVDAGLTTFDCADIYgPAEELIGEFRKRLRrerdaaddvqihtkwVPDPGELTMTRAYVE--------A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWPSPNDAVAVeEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAenIATNQIELS- 156
Cdd:cd19101 93 AIDRSLKRLGVDRLDLVQFHWWDYSDPGYL-DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGVP--IVSNQVQYSl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 157 ----PylqNSKVVDWAREHGIHITSYMTLAYG-------------------------KALKDE------------VIARI 195
Cdd:cd19101 170 ldrrP---ENGMAALCEDHGIKLLAYGTLAGGllsekylgvpeptgpaletrslqkyKLMIDEwggwdlfqellrTLKAI 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1453082642 196 AAKHNATPAQVILAWAM---GEGyAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAA 249
Cdd:cd19101 247 ADKHGVSIANVAVRWVLdqpGVA-GVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDA 302
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
33-251 |
3.42e-23 |
|
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: 95.75 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 33 IDTAQIYDN---EAAVGQAIAESgvpRDELFITTKiWIENLSKDK----------LIASLQESLQKLRTDYVDLTLIHWP 99
Cdd:cd19080 48 IDTANNYTNgtsERLLGEFIAGN---RDRIVLATK-YTMNRRPGDpnaggnhrknLRRSVEASLRRLQTDYIDLLYVHAW 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 100 spnDAVA-VEEFMAALMEAKKLGLTRQIGISNFTIPLMERA--IA-AVGAENIATNQIELSpYLQNS---KVVDWAREHG 172
Cdd:cd19080 124 ---DFTTpVEEVMRALDDLVRAGKVLYVGISDTPAWVVARAntLAeLRGWSPFVALQIEYS-LLERTperELLPMARALG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 173 IHITSYMTLAYGK-------------------------------ALKDEVIArIAAKHNATPAQVILAWAMGEGYAVIPS 221
Cdd:cd19080 200 LGVTPWSPLGGGLltgkyqrgeegrageakgvtvgfgklternwAIVDVVAA-VAEELGRSAAQVALAWVRQKPGVVIPI 278
|
250 260 270
....*....|....*....|....*....|..
gi 1453082642 222 --STKRDNLASNLKALDLQLDDEdrqAIAALD 251
Cdd:cd19080 279 igARTLEQLKDNLGALDLTLSPE---QLARLD 307
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
19-243 |
2.06e-21 |
|
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: 90.95 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 19 IASVKTALELGYRAIDTAQIY---DNEAAVGQAIaeSGVPRDELFITTKIWIENLSKDKLI---------ASLQESLQKL 86
Cdd:cd19145 36 IALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKAL--KDGPREKVQLATKFGIHEIGGSGVEvrgdpayvrAACEASLKRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 87 RTDYVDLTLIHwpSPNDAVAVEEFMAALmeaKKL---GLTRQIGISNFTIPLMERA-----IAAVgaeniatnQIELSPY 158
Cdd:cd19145 114 DVDYIDLYYQH--RIDTTVPIEITMGEL---KKLveeGKIKYIGLSEASADTIRRAhavhpITAV--------QLEWSLW 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 159 LQNSK--VVDWAREHGIHITSYMTLAYG----KALKDEV---------------------------IARIAAKHNATPAQ 205
Cdd:cd19145 181 TRDIEeeIIPTCRELGIGIVPYSPLGRGffagKAKLEELlensdvrkshprfqgenleknkvlyerVEALAKKKGCTPAQ 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1453082642 206 VILAWAMGEGYAV--IPSSTKRDNLASNLKALDLQLDDED 243
Cdd:cd19145 261 LALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKED 300
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-243 |
3.21e-21 |
|
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: 90.39 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDD-----VVIASVKTALELGYRAIDTAQIYDN-----EAAVGQAIAESGVP-RDELFITTKIWIENL- 70
Cdd:cd19089 11 LPAISLGLWHNFGDytspeEARELLRTAFDLGITHFDLANNYGPppgsaEENFGRILKRDLRPyRDELVISTKAGYGMWp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 71 -------SKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA-- 141
Cdd:cd19089 91 gpygdggSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPD--TPLEETMTALADAVRSGKALYVGISNYPGAKARRAIAll 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 142 -AVGAEnIATNQIELSPYLQNSK--VVDWAREHGIHITSYMTLAYG-------------------------------KAL 187
Cdd:cd19089 169 rELGVP-LIIHQPRYSLLDRWAEdgLLEVLEEAGIGFIAFSPLAQGlltdkylngippdsrraaeskflteealtpeKLE 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1453082642 188 KDEVIARIAAKHNATPAQVILAWAMGEGY--AVIPSSTKRDNLASNLKALD-LQLDDED 243
Cdd:cd19089 248 QLRKLNKIAAKRGQSLAQLALSWVLRDPRvtSVLIGASSPSQLEDNVAALKnLDFSEEE 306
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
5-250 |
3.50e-21 |
|
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: 90.32 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 5 AFGLGTF--RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTK--------IWIENLS 71
Cdd:cd19087 17 CLGTMNFggRTDEETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAGR---RDDIVLATKvfgpmgddPNDRGLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 72 KDKLIASLQESLQKLRTDYVDLTLIHwpSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAE----- 146
Cdd:cd19087 94 RRHIRRAVEASLRRLQTDYIDLYQMH--HFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRgllrf 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 147 -------NIATNQIELspylqnsKVVDWAREHGIHITSYMTLA-------YGKALKDEV--------------------- 191
Cdd:cd19087 172 vseqpmyNLLKRQAEL-------EILPAARAYGLGVIPYSPLAgglltgkYGKGKRPESgrlveraryqarygleeyrdi 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1453082642 192 ---IARIAAKHNATPAQVILAWAMGE---GYAVIPSSTKrDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19087 245 aerFEALAAEAGLTPASLALAWVLSHpavTSPIIGPRTL-EQLEDSLAALEITLTPELLAEIDEL 308
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
4-173 |
1.48e-19 |
|
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: 84.92 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRLKD--------DVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAEsgVPRDELFITTKI-WIENLS 71
Cdd:cd19096 1 SVLGFGTMRLPEsdddsideEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKE--GPREKFYLATKLpPWSVKS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 72 KDKLIASLQESLQKLRTDYVDLTLIHWP-SPNDAVAVEEF--MAALMEAKKLGLTRQIGISnF--TIPLMERAIAavgAE 146
Cdd:cd19096 79 AEDFRRILEESLKRLGVDYIDFYLLHGLnSPEWLEKARKGglLEFLEKAKKEGLIRHIGFS-FhdSPELLKEILD---SY 154
|
170 180 190
....*....|....*....|....*....|.
gi 1453082642 147 NIATNQIELS----PYLQNSKVVDWAREHGI 173
Cdd:cd19096 155 DFDFVQLQYNyldqENQAGRPGIEYAAKKGM 185
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
6-144 |
3.67e-19 |
|
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: 84.64 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 6 FGLGTF--RLKDDV----VIASVKTALELGYRAIDTAQIY-DNEAAVGQAIA--ESGVPRDELFITTK-----IWIENLS 71
Cdd:cd19164 18 FGAATFsyQYTTDPesipPVDIVRRALELGIRAFDTSPYYgPSEIILGRALKalRDEFPRDTYFIITKvgrygPDDFDYS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 72 KDKLIASLQESLQKLRTDYVDLTLIHwpspnDA--VAVEEFMAALMEAKKL---GLTRQIGISNFTIP----LMERAIAA 142
Cdd:cd19164 98 PEWIRASVERSLRRLHTDYLDLVYLH-----DVefVADEEVLEALKELFKLkdeGKIRNVGISGYPLPvllrLAELARTT 172
|
..
gi 1453082642 143 VG 144
Cdd:cd19164 173 AG 174
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
13-184 |
5.99e-19 |
|
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: 84.12 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 13 LKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKI-----WIENLSKDKLIASLQESLQ 84
Cdd:cd19153 30 LEQDEAVAIVAEAFAAGINHFDTSPYYGAessEAVLGKALAALQVPRSSYTVATKVgryrdSEFDYSAERVRASVATSLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 85 KLRTDYVDLTLIHWPSPND-AVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVgaeNIATNQIELSpY----L 159
Cdd:cd19153 110 RLHTTYLDVVYLHDIEFVDyDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRC---SPGSLDAVLS-YchltL 185
|
170 180
....*....|....*....|....*....
gi 1453082642 160 QNSKVVDWAREH----GIHITSYMTLAYG 184
Cdd:cd19153 186 QDARLESDAPGLvrgaGPHVINASPLSMG 214
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
6-236 |
1.87e-18 |
|
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: 82.99 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 6 FGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAiaesGVPRDELFITTKI--WIEN-LSKDK 74
Cdd:cd19075 5 LGTMTFgsqgrFTTAEAAAELLDAFLERGHTEIDTARVYpdgTSEELLGEL----GLGERGFKIDTKAnpGVGGgLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 75 LIASLQESLQKLRTDYVDLTLIHwpSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA----------AV- 143
Cdd:cd19075 81 VRKQLETSLKRLKVDKVDVFYLH--APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwvlpTVy 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 -GAENIATNQIE--LSPYLqnskvvdwaREHGIHITSYMTLA-------------------------YGKALKD------ 189
Cdd:cd19075 159 qGMYNAITRQVEteLFPCL---------RKLGIRFYAYSPLAggfltgkykysedkagggrfdpnnaLGKLYRDrywkps 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1453082642 190 -----EVIARIAAKHNATPAQVILAWAM-------GEGYAVI--PSSTKRdnLASNLKALD 236
Cdd:cd19075 230 yfealEKVEEAAEKEGISLAEAALRWLYhhsaldgEKGDGVIlgASSLEQ--LEENLAALE 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
6-251 |
2.53e-18 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 82.32 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 6 FGLGTFRL---------KD-DVVIASVKTALELGYRAIDTAQIYdNEAAVGQAIAESGVP-RDELFITTKI--------- 65
Cdd:PRK10376 20 LGYGAMQLagpgvfgppKDrDAAIAVLREAVALGVNHIDTSDFY-GPHVTNQLIREALHPyPDDLTIVTKVgarrgedgs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 WIENLSKDKLIASLQESLQKLRTDYVDLT------LIHWPSPNDavaVEEFMAALMEAKKLGLTRQIGISNFTiplmERA 139
Cdd:PRK10376 99 WLPAFSPAELRRAVHDNLRNLGLDVLDVVnlrlmgDGHGPAEGS---IEEPLTVLAELQRQGLVRHIGLSNVT----PTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 140 IAAvgAENIAT-----NQIELSpYLQNSKVVDWAREHGIHITSYMTLAYGKALKDEVIARIAAKHNATPAQVILAWAM-- 212
Cdd:PRK10376 172 VAE--ARKIAEivcvqNHYNLA-HRADDALIDALARDGIAYVPFFPLGGFTPLQSSTLSDVAASLGATPMQVALAWLLqr 248
|
250 260 270
....*....|....*....|....*....|....*....
gi 1453082642 213 GEGYAVIPSSTKRDNLASNLKALDLQLDDEdrqAIAALD 251
Cdd:PRK10376 249 SPNILLIPGTSSVAHLRENLAAAELVLSEE---VLAELD 284
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-211 |
2.65e-18 |
|
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: 82.75 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 5 AFGLGTFRL-----KDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAES----GVPRDELFITTKI------- 65
Cdd:cd19099 5 SLGLGTYRGdsddeTDEEYREALKAALDSGINVIDTAINYrggRSERLIGKALRELiekgGIKRDEVVIVTKAgyipgdg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 --------WIEN------------------LSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNDAVAVEEFM-------- 111
Cdd:cd19099 85 deplrplkYLEEklgrglidvadsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFydrleeaf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 112 AALMEAKKLGLTRQIGISNFTIP-------------LMERAIAAVGAEN-------IATNQIELSPYLQNSKVVDW---- 167
Cdd:cd19099 165 EALEEAVAEGKIRYYGISTWDGFrappalpghlsleKLVAAAEEVGGDNhhfkviqLPLNLLEPEALTEKNTVKGEalsl 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1453082642 168 ---AREHGIHITSYMTLAYGKALKDEVIARIAAKHNA-TPAQVILAWA 211
Cdd:cd19099 245 leaAKELGLGVIASRPLNQGQLLGELRLADLLALPGGaTLAQRALQFA 292
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-245 |
3.58e-18 |
|
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: 81.83 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGT------FRLKDDV-VIASVKTALELGYRAIDTAQIYDN---EAAVGQAIaeSGVPRDELFITTKI----- 65
Cdd:cd19163 11 LKVSKLGFGAsplggvFGPVDEEeAIRTVHEALDSGINYIDTAPWYGQgrsETVLGKAL--KGIPRDSYYLATKVgrygl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 -WIE--NLSKDKLIASLQESLQKLRTDYVDLTLIHWP--SPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAI 140
Cdd:cd19163 89 dPDKmfDFSAERITKSVEESLKRLGLDYIDIIQVHDIefAPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 141 AAvgaeniATNQIE--LSpY----LQNS---KVVDWAREHGIHITSYMTLAYG--------------KALKDevIARIAA 197
Cdd:cd19163 169 ER------SPVKIDtvLS-YchytLNDTsllELLPFFKEKGVGVINASPLSMGlltergppdwhpasPEIKE--ACAKAA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1453082642 198 KH----NATPAQVILAWAMG--EGYAVIPSSTKRDNLASNLKALDLQLDDEDRQ 245
Cdd:cd19163 240 AYcksrGVDISKLALQFALSnpDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
10-247 |
5.04e-18 |
|
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: 81.87 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 10 TF--RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKI-W-----IEN---LSKDKL 75
Cdd:cd19143 23 TFgnQVDVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKELGWPRSDYVVSTKIfWggggpPPNdrgLSRKHI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 76 IASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEF--------------------------MAALMEAKKLGLTRqigis 129
Cdd:cd19143 103 VEGTKASLKRLQLDYVDLVFCHRPDPA--TPIEETvramndlidqgkafywgtsewsaqqiEEAHEIADRLGLIP----- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 130 nftiPLMEraiaavgaeniatnQIELSpYLQNSKV-VDWA---REHGIHITSYMTLAYG--------------------- 184
Cdd:cd19143 176 ----PVME--------------QPQYN-LFHRERVeVEYAplyEKYGLGTTTWSPLASGlltgkynngipegsrlalpgy 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 185 KALKDEV-------------IARIAAKHNATPAQVILAWAMGEGY--AVIPSSTKRDNLASNLKALDL--QLDDEDRQAI 247
Cdd:cd19143 237 EWLKDRKeelgqekiekvrkLKPIAEELGCSLAQLAIAWCLKNPNvsTVITGATKVEQLEENLKALEVlpKLTPEVMEKI 316
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
25-250 |
7.75e-18 |
|
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: 81.46 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 25 ALELGYRAIDTAQIY----------DNEAAVGQAIAESGvPRDELFITTKI--------WI----ENLSKDKLIASLQES 82
Cdd:cd19094 27 AFDEGVNFIDTAEMYpvppspetqgRTEEIIGSWLKKKG-NRDKVVLATKVagpgegitWPrgggTRLDRENIREAVEGS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 83 LQKLRTDYVDLTLIHWPS----------------PNDAVAVEEFMAALMEAKKLGLTRQIGISNFTiP--LME--RAIAA 142
Cdd:cd19094 106 LKRLGTDYIDLYQLHWPDrytplfgggyytepseEEDSVSFEEQLEALGELVKAGKIRHIGLSNET-PwgVMKflELAEQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 VGAENIATNQielSPY--LQNSKVVDWA---REHGIHITSYMTLAYG----KALKDEV---IAR---------------- 194
Cdd:cd19094 185 LGLPRIVSIQ---NPYslLNRNFEEGLAeacHRENVGLLAYSPLAGGvltgKYLDGAArpeGGRlnlfpgymaryrspqa 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 195 ---------IAAKHNATPAQVILAWA-----MGegyAVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19094 262 leavaeyvkLARKHGLSPAQLALAWVrsrpfVT---STIIGATTLEQLKENIDAFDVPLSDELLAEIDAV 328
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-199 |
2.09e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 77.31 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 14 KDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESgvpRDELFITTKIWIENLS----KDKLIASLQESLQKL 86
Cdd:cd19104 30 TREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL---PAGPYITTKVRLDPDDlgdiGGQIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 87 RTDYVDLTLIH-------------WPSPNDAVAVEEFMAALMEAKKLGLTRQIGISNF-TIPLMERAIA--AVGAENIAT 150
Cdd:cd19104 107 KRDSVDLLQLHnrigderdkpvggTLSTTDVLGLGGVADAFERLRSEGKIRFIGITGLgNPPAIRELLDsgKFDAVQVYY 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 151 NQIELSPYLQN---------SKVVDWAREHGIHITSYMTLAYGkALKDEVIARIAAKH 199
Cdd:cd19104 187 NLLNPSAAEARprgwsaqdyGGIIDAAAEHGVGVMGIRVLAAG-ALTTSLDRGREAPP 243
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-213 |
3.51e-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: 73.33 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 12 RLKDDVVIASVKTALELGYRAIDTAQIY-DNEAAVGQAIAESgvprDELFITTKI----WIENLSKDKLIASLQESLQKL 86
Cdd:cd19097 22 KPSEKEAKKILEYALKAGINTLDTAPAYgDSEKVLGKFLKRL----DKFKIITKLpplkEDKKEDEAAIEASVEASLKRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 87 RTDYVDLTLIHWPSPNDAVAvEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGAENIatnQIELSPY---LQNSK 163
Cdd:cd19097 98 KVDSLDGLLLHNPDDLLKHG-GKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDII---QLPFNILdqrFLKSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1453082642 164 VVDWAREHG--IHITS-------YMT----LAYGKALKDEV--IARIAAKHNATPAQVILAWAMG 213
Cdd:cd19097 174 LLAKLKKKGieIHARSvflqgllLMEpdklPAKFAPAKPLLkkLHELAKKLGLSPLELALGFVLS 238
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
20-250 |
1.09e-12 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 66.80 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 20 ASVKTALELGYRAIDTAQIYD----------NEAAVGQAIAESGvPRDELFITTKIWIENLSKDKLI------------A 77
Cdd:PRK10625 34 AQLDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAKRG-SREKLIIASKVSGPSRNNDKGIrpnqaldrknirE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 78 SLQESLQKLRTDYVDLTLIHWP---------------SPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAA 142
Cdd:PRK10625 113 ALHDSLKRLQTDYLDLYQVHWPqrptncfgklgyswtDSAPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 143 VGAEN---IATNQielSPY--LQNSKVVDWA---REHGIHITSYMTLAY----GKAL--------KDEVIAR-------- 194
Cdd:PRK10625 193 AEKHDlprIVTIQ---NPYslLNRSFEVGLAevsQYEGVELLAYSCLAFgtltGKYLngakpagaRNTLFSRftrysgeq 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 195 ----------IAAKHNATPAQVILAWAMGEGY--AVIPSSTKRDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:PRK10625 270 tqkavaayvdIAKRHGLDPAQMALAFVRRQPFvaSTLLGATTMEQLKTNIESLHLTLSEEVLAEIEAV 337
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
3-141 |
2.82e-12 |
|
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: 65.50 E-value: 2.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFRLKDDVVI-----ASVKTALELGYRAIDTAQIY-----DNEAAVGQAIAESGVP-RDELFITTK----IWI 67
Cdd:cd19151 12 LPAISLGLWHNFGDVDRyensrAMLRRAFDLGITHFDLANNYgpppgSAEENFGRILKEDLKPyRDELIISTKagytMWP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 68 ----ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIA 141
Cdd:cd19151 92 gpygDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPE--TPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAA 167
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
4-146 |
4.37e-12 |
|
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: 64.69 E-value: 4.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGT------FRLKDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAesGVPRDELFITTKI--------- 65
Cdd:cd19162 1 PRLGLGAaslgnlARAGEDEAAATLDAAWDAGIRYFDTAPLYglgLSERRLGAALA--RHPRAEYVVSTKVgrllepgaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 66 -------WIENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMER 138
Cdd:cd19162 79 grpagadRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
....*...
gi 1453082642 139 AIAAVGAE 146
Cdd:cd19162 159 AARRADVD 166
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
33-247 |
1.20e-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: 63.60 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 33 IDTAQIY---DNEAAVGQAIAESGVpRDELFITTK--IWIENLSKDK------------LIASLQESLQKLRTDYVDLTL 95
Cdd:cd19146 52 IDTANNYqgeESERWVGEWMASRGN-RDEMVLATKytTGYRRGGPIKiksnyqgnhaksLRLSVEASLKKLQTSYIDILY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 96 IHWpsPNDAVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAV------------GAENIATNQIElspylqnSK 163
Cdd:cd19146 131 VHW--WDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYArahgltqfvvyqGHWSAAFRDFE-------RD 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 164 VVDWAREHGIHITSYMTLAYGKALKDE------------------------VIARIAAKHNATPAQVILAWAMGEGYAVI 219
Cdd:cd19146 202 ILPMCEAEGMALAPWGVLGQGQFRTEEefkrrgrsgrkggpqtekerkvseKLEKVAEEKGTAITSVALAYVMHKAPYVF 281
|
250 260 270
....*....|....*....|....*....|
gi 1453082642 220 P--SSTKRDNLASNLKALDLQLDDEDRQAI 247
Cdd:cd19146 282 PivGGRKVEHLKGNIEALGISLSDEEIQEI 311
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
13-133 |
1.77e-11 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 63.26 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 13 LKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKI--WIE--NLSKDKLIASLQESLQK 85
Cdd:PLN02587 28 VSEEDAIASVREAFRLGINFFDTSPYYGGtlsEKVLGKALKALGIPREKYVVSTKCgrYGEgfDFSAERVTKSVDESLAR 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1453082642 86 LRTDYVDLTLIH---WPSPnDAVaVEEFMAALMEAKKLGLTRQIGISNFTI 133
Cdd:PLN02587 108 LQLDYVDILHCHdieFGSL-DQI-VNETIPALQKLKESGKVRFIGITGLPL 156
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-237 |
2.34e-11 |
|
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: 62.75 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI----- 67
Cdd:cd19159 11 LRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkae 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 68 --ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTIPLMERAIAAVGA 145
Cdd:cd19159 91 teRGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSN--TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 146 ENIATNQIELSPY--LQNSKV---------------VDWA----------REHGIHITSYMTLAYGKALKDEVIAR---- 194
Cdd:cd19159 169 FNMIPPVCEQAEYhlFQREKVevqlpelyhkigvgaMTWSplacgiisgkYGNGVPESSRASLKCYQWLKERIVSEegrk 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1453082642 195 ----------IAAKHNATPAQVILAWAM-GEGY-AVIPSSTKRDNLASNLKALDL 237
Cdd:cd19159 249 qqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENLGAIQV 303
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-235 |
5.33e-10 |
|
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: 58.61 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIYDNEAA---VGQAIAESGVPRDELFITTKI-W---IEN- 69
Cdd:cd19141 12 VSCLGLGTWvtfgsQISDEVAEELVTLAYENGINLFDTAEVYAAGKAeivLGKILKKKGWRRSSYVITTKIfWggkAETe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 70 --LSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFT-IPLMErAIAAVGAE 146
Cdd:cd19141 92 rgLSRKHIIEGLKASLERLQLEYVDIVFANRPDPN--TPMEEIVRAFTHVINQGMAMYWGTSRWSaMEIME-AYSVARQF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 147 NIATNQIELSPY--LQNSKV---------------VDWA----------REHGIHITSYMTLAYGKALKDEVIARIAAKH 199
Cdd:cd19141 169 NLIPPIVEQAEYhlFQREKVemqlpelfhkigvgaMTWSplacgilsgkYDDGVPEYSRASLKGYQWLKEKILSEEGRRQ 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1453082642 200 NA--------------TPAQVILAWAM-GEG-YAVIPSSTKRDNLASNLKAL 235
Cdd:cd19141 249 QAklkelqiiadrlgcTLPQLAIAWCLkNEGvSSVLLGASSTEQLYENLQAI 300
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
4-242 |
1.97e-09 |
|
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: 57.23 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGT------FR-LKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAEsgVPRDELFITTKI-WI----- 67
Cdd:cd19152 1 PKLGFGTaplgnlYEaVSDEEAKATLVAAWDLGIRYFDTAPWYGAglsEERLGAALRE--LGREDYVISTKVgRLlvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 68 -------------------ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPND---------AVAVEEFMAALMEAKK 119
Cdd:cd19152 79 eveptfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLagaesdehfAQAIKGAFRALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 120 LGLTRQIGI-SNFTIPLMEraIAAVGAENIATNQIELSPYLQN--SKVVDWAREHGIHI--------------TSYMTLA 182
Cdd:cd19152 159 EGVIKAIGLgVNDWEVILR--ILEEADLDWVMLAGRYTLLDHSaaRELLPECEKRGVKVvnagpfnsgflaggDNFDYYE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1453082642 183 YGKAlKDEVIAR------IAAKHNATPAQVILAWAMG-EGYA-VIPSSTKRDNLASNLKALDLQLDDE 242
Cdd:cd19152 237 YGPA-PPELIARrdrieaLCEQHGVSLAAAALQFALApPAVAsVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-137 |
4.66e-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: 4.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI----- 67
Cdd:cd19158 11 LRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkae 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1453082642 68 --ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFT-IPLME 137
Cdd:cd19158 91 teRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSsMEIME 161
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
3-97 |
4.74e-09 |
|
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: 55.93 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIYDNEAA---VGQAIAESGVPRDELFITTKIWIEN----- 69
Cdd:cd19142 13 VSNVGLGTWstfstAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAeteLGRILKKKGWKRSSYIVSTKIYWSYgseer 92
|
90 100
....*....|....*....|....*....
gi 1453082642 70 -LSKDKLIASLQESLQKLRTDYVDLTLIH 97
Cdd:cd19142 93 gLSRKHIIESVRASLRRLQLDYIDIVIIH 121
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
27-243 |
8.56e-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: 55.22 E-value: 8.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 27 ELGYRAIDTAQIYDNEAA---VGQAIAESGVpRDELFITTKIWIENLS---------------KDKLIASLQESLQKLRT 88
Cdd:cd19147 45 EAGGNFIDTANNYQDEQSetwIGEWMKSRKN-RDQIVIATKFTTDYKAyevgkgkavnycgnhKRSLHVSVRDSLRKLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 89 DYVDLTLIHWpsPNDAVAVEEFMAALMEAKKLGLTRQIGISNftIPlmerAIAAVGAENIATNQ--IELSPYLQNSKVVD 166
Cdd:cd19147 124 DWIDILYVHW--WDYTTSIEEVMDSLHILVQQGKVLYLGVSD--TP----AWVVSAANYYATAHgkTPFSVYQGRWNVLN 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 167 ---------WAREHGIHITSYMTLAYGKALK------------------------------DEVIARIAAKHN-ATPAQV 206
Cdd:cd19147 196 rdferdiipMARHFGMALAPWDVLGGGKFQSkkaveerkkngeglrsfvggteqtpeevkiSEALEKVAEEHGtESVTAI 275
|
250 260 270
....*....|....*....|....*....|....*....
gi 1453082642 207 ILAWAMGEGYAVIPS--STKRDNLASNLKALDLQLDDED 243
Cdd:cd19147 276 ALAYVRSKAPNVFPLvgGRKIEHLKDNIEALSIKLTPEE 314
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-236 |
1.24e-08 |
|
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: 54.77 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 3 IPAFGLGTFR-LKDDVVIAS----VKTALELGYRAIDTAQIY-----DNEAAVGQAIAESGVP-RDELFITTK----IWI 67
Cdd:cd19150 12 LPALSLGLWHnFGDDTPLETqraiLRTAFDLGITHFDLANNYgpppgSAEENFGRILREDFAGyRDELIISTKagydMWP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 68 ----ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFTiPLMERAIAAV 143
Cdd:cd19150 92 gpygEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPD--TPLEETMGALDHAVRSGKALYVGISSYS-PERTREAAAI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 144 GAENIATNQIE------LSPYLQNSKVVDWAREHGIHITSYMTLAYG------------------------KALKDEVIA 193
Cdd:cd19150 169 LRELGTPLLIHqpsynmLNRWVEESGLLDTLQELGVGCIAFTPLAQGlltdkylngipegsraskerslspKMLTEANLN 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1453082642 194 R------IAAKHNATPAQVILAWAMGEG---YAVIPSStKRDNLASNLKALD 236
Cdd:cd19150 249 SiralneIAQKRGQSLAQMALAWVLRDGrvtSALIGAS-RPEQLEENVGALD 299
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-137 |
3.47e-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: 53.45 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 1 MAIPAFGLGTF-----RLKDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIWI----- 67
Cdd:cd19160 13 LRVSCLGLGTWvtfgsQISDETAEDLLTVAYEHGVNLFDTAEVYAAgkaERTLGNILKSKGWRRSSYVVTTKIYWggqae 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1453082642 68 --ENLSKDKLIASLQESLQKLRTDYVDLTLIHWPSPNDavAVEEFMAALMEAKKLGLTRQIGISNFT-IPLME 137
Cdd:cd19160 93 teRGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNS--PMEEIVRAMTYVINQGMAMYWGTSRWSaMEIME 163
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
4-97 |
1.07e-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: 51.94 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 4 PAFGLGTFRL-------KDDVVIASVKTALELGYRAIDTAQIYDN---EAAVGQAIAEsgVPRDELFITTKI-------- 65
Cdd:cd19161 1 SELGLGTAGLgnlytavSNADADATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE--KPRDEFVLSTKVgrllkpar 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1453082642 66 ---------WIENL--------SKDKLIASLQESLQKLRTDYVDLTLIH 97
Cdd:cd19161 79 egsvpdpngFVDPLpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVH 127
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-250 |
2.95e-07 |
|
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: 50.42 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 25 ALELGYRAIDTAQIY-DNEAAVGQAIAESGVPRDELFITTKiW----------------IENLSKDKLIASLQESLQKLr 87
Cdd:cd19098 44 AWAAGVRYFDAARSYgRAEEFLGSWLRSRNIAPDAVFVGSK-WgytytadwqvdaavheVKDHSLARLLKQWEETRSLL- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 88 TDYVDLTLIHWPSPNDAV-AVEEFMAALMEAKKLGltRQIGISNFTIP---LMERAIAA-VGAENI-----AT-NQIELS 156
Cdd:cd19098 122 GKHLDLYQIHSATLESGVlEDADVLAALAELKAEG--VKIGLSLSGPQqaeTLRRALEIeIDGARLfdsvqATwNLLEQS 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 157 PylqnSKVVDWAREHGIHITSYMTLAYGK----------ALKDEVIARIAAKHNATPAQVILAWAMGEGYA--VIPSSTK 224
Cdd:cd19098 200 A----GEALEEAHEAGMGVIVKEALANGRltdrnpspelAPLMAVLKAVADRLGVTPDALALAAVLAQPFVdvVLSGAAT 275
|
250 260
....*....|....*....|....*.
gi 1453082642 225 RDNLASNLKALDLQLDDEDRQAIAAL 250
Cdd:cd19098 276 PEQLRSNLRALDVSLDLELLAALADL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
20-132 |
3.08e-07 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 50.76 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1453082642 20 ASVKTALELGYRAIDTAQIY-----DNEAAVGQAIAESGVP-RDELFITTK----IWI----ENLSKDKLIASLQESLQK 85
Cdd:PRK09912 47 AILRKAFDLGITHFDLANNYgpppgSAEENFGRLLREDFAAyRDELIISTKagydMWPgpygSGGSRKYLLASLDQSLKR 126
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1453082642 86 LRTDYVDLTLIHWPSPNdaVAVEEFMAALMEAKKLGLTRQIGISNFT 132
Cdd:PRK09912 127 MGLEYVDIFYSHRVDEN--TPMEETASALAHAVQSGKALYVGISSYS 171
|
|
| |
