|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
11-273 |
1.62e-149 |
|
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: 418.96 E-value: 1.62e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19136 1 MPILGLGTFRLRGEEEVRQAVDAALKAGYRLIDTASVYRNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGYEKARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSS-LKSENPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAV 169
Cdd:cd19136 81 ACLGSLERLGTDYLDLYLIHWPGVQgLKPSDPRNAELRRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCEVPPAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 170 NQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRkqLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPE 249
Cdd:cd19136 161 NQVEFHPHLVQKELLKFCKDHGIHLQAYSSLGSGDLR--LLEDPTVLAIAKKYGRTPAQVLLRWALQQGIGVIPKSTNPE 238
|
250 260
....*....|....*....|....
gi 17552492 250 HVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19136 239 RIAENIKVFDFELSEEDMAELNAL 262
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
11-270 |
8.93e-110 |
|
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: 317.89 E-value: 8.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLlpanGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19071 1 MPLIGLGTYKLKPEETAEAVLAA-LEAGYRHIDTAAAYGNEAEVGEAIRES----GVPREELFITTKLWPTDHGYERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSlksENPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAVN 170
Cdd:cd19071 76 ALEESLKDLGLDYLDLYLIHWPVPG---KEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAARIKPAVN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 171 QVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPtyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEH 250
Cdd:cd19071 153 QIELHPYLQQKELVEFCKEHGIVVQAYSPLGRG--RRPLLDDPVLKEIAKKYGKTPAQVLLRWALQRGVVVIPKSSNPER 230
|
250 260
....*....|....*....|
gi 17552492 251 VATNFKVTKLAITQEDIDRL 270
Cdd:cd19071 231 IKENLDVFDFELSEEDMAAI 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-284 |
9.59e-102 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 297.74 E-value: 9.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEiLRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKA 88
Cdd:COG0656 3 VEIPALGLGTWQLPGEE-AAAAVRTALEAGYRHIDTAAMYGNEEGVGEAIA----ASGVPREELFVTTKVWNDNHGYDDT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGSslksenpankKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:COG0656 78 LAAFEESLERLGLDYLDLYLIHWPGP----------GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETGVKPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:COG0656 148 VNQVELHPYLQQRELLAFCREHGIVVEAYSPLG----RGKLLDDPVLAEIAEKHGKTPAQVVLRWHLQRGVVVIPKSVTP 223
|
250 260 270
....*....|....*....|....*....|....*.
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLALTVEHKTCWDPR 284
Cdd:COG0656 224 ERIRENLDAFDFELSDEDMAAIDALDRGERLGPDPD 259
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
10-273 |
1.25e-76 |
|
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: 234.14 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTWQV--QKEEilrQVIDAGFKEGYRFIDTAQVYNNEAKIGrileKLLPANGLKREDIWITSKLAPSNAGVKK 87
Cdd:cd19135 12 EMPILGLGTSHSggYSHE---AVVYALKECGYRHIDTAKRYGCEELLG----KAIKESGVPREDLFLTTKLWPSDYGYES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 ARESIEESLSNLKVEYLDLLLIHWPGSSLKSENpaNKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVP 167
Cdd:cd19135 85 TKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKN--VKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 168 AVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTN 247
Cdd:cd19135 163 HVNQVEFHPFQNPVELIEYCRDNNIVFEGYCPLA----KGKALEEPTVTELAKKYQKTPAQILIRWSIQNGVVTIPKSTK 238
|
250 260
....*....|....*....|....*.
gi 17552492 248 PEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19135 239 EERIKENCQVFDFSLSEEDMATLDSL 264
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-280 |
1.28e-75 |
|
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: 232.56 E-value: 1.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKA 88
Cdd:cd19116 9 NEIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYGNEAEVGEAIREKIAEGVVKREDLFITTKLWNSYHEREQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGSSLKSENPANKKLR-------VESWNVMCEMMAEGKLRSVGVSNFEICHLEELKK 161
Cdd:cd19116 89 EPALRESLKRLGLDYVDLYLIHWPVAFKENNDSESNGDGslsdidyLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 162 DSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEP-----LIKELAQKYNVEIPVLLLGFAYC 236
Cdd:cd19116 169 NCNIKPAVNQIEVHPTLTQEKLVAYCQSNGIVVMAYSPFGRLVPRGQTNPPPrlddpTLVAIAKKYGKTTAQIVLRYLID 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17552492 237 QGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALTVEHKTC 280
Cdd:cd19116 249 RGVVPIPKSSNKKRIKENIDIFDFQLTPEEVAALNSFNTNQRVY 292
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
9-273 |
6.33e-75 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 229.38 E-value: 6.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQ-KEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKllpaNGLKREDIWITSKLAPSNAGVKK 87
Cdd:cd19133 7 VEMPILGFGVFQIPdPEECERAVLEA-IKAGYRLIDTAAAYGNEEAVGRAIKK----SGIPREELFITTKLWIQDAGYEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 ARESIEESLSNLKVEYLDLLLIHWPGSSLKsenpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVP 167
Cdd:cd19133 82 AKKAFERSLKRLGLDYLDLYLIHQPFGDVY-----------GAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNEVKP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 168 AVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPtyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTN 247
Cdd:cd19133 151 AVNQIETHPFNQQIEAVEFLKKYGVQIEAWGPFAEG--RNNLFENPVLTEIAEKYGKSVAQVILRWLIQRGIVVIPKSVR 228
|
250 260
....*....|....*....|....*.
gi 17552492 248 PEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19133 229 PERIAENFDIFDFELSDEDMEAIAAL 254
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-273 |
3.33e-74 |
|
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: 228.45 E-value: 3.33e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANG-LKREDIWITSKL-----APSN 82
Cdd:cd19118 5 NKIPAIGLGTWQAEPGEV-GAAVKIALKAGYRHLDLAKVYQNQHEVGQALKELLKEEPgVKREDLFITSKLwnnshRPEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 83 agVKKAresIEESLSNLKVEYLDLLLIHWP-------GSSLKSENPANKKLR--------VESWNVMCEMMAEGKLRSVG 147
Cdd:cd19118 84 --VEPA---LDDTLKELGLDYLDLYLIHWPvafkptgDLNPLTAVPTNGGEVdldlsvslVDTWKAMVELKKTGKVKSIG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 148 VSNFEICHLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRK-QLSEEPLIKELAQKYNVEI 226
Cdd:cd19118 159 VSNFSIDHLQAIIEETGVVPAVNQIEAHPLLLQDELVDYCKSKNIHITAYSPLGNNLAGLpLLVQHPEVKAIAAKLGKTP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17552492 227 PVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLaiTQEDIDRLLAL 273
Cdd:cd19118 239 AQVLIAWGIQRGHSVIPKSVTPSRIRSNFEQVEL--SDDEFNAVTAL 283
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
11-270 |
5.83e-74 |
|
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: 228.00 E-value: 5.83e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19125 11 IPAVGLGTWQADPGVV-GNAVKTAIKEGYRHIDCAAIYGNEKEIGKALKKLFEDGVVKREDLFITSKLWCTDHAPEDVPP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSLKSEN---PANK-KLRVES-WNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNV 165
Cdd:cd19125 90 ALEKTLKDLQLDYLDLYLIHWPVRLKKGAHmpePEEVlPPDIPStWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVARV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 166 VPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSP---TYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVL 242
Cdd:cd19125 170 PPAVNQVECHPGWQQDKLHEFCKSKGIHLSAYSPLGSPgttWVKKNVLKDPIVTKVAEKLGKTPAQVALRWGLQRGTSVL 249
|
250 260
....*....|....*....|....*...
gi 17552492 243 PRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19125 250 PKSTNEERIKENIDVFDWSIPEEDFAKF 277
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
11-278 |
2.03e-73 |
|
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: 226.91 E-value: 2.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19123 12 IPALGLGTWKSKPGEVGQAVKQA-LEAGYRHIDCAAIYGNEAEIGAALAEVFKEGKVKREDLWITSKLWNNSHAPEDVLP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPgSSLKSE--NPANKKLRV--------ESWNVMCEMMAEGKLRSVGVSNFEICHLEELK 160
Cdd:cd19123 91 ALEKTLADLQLDYLDLYLMHWP-VALKKGvgFPESGEDLLslspipleDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 161 KDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLS--------EEPLIKELAQKYNVEIPVLLLG 232
Cdd:cd19123 170 ATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSGDRPAAMKaegepvllEDPVINKIAEKHGASPAQVLIA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17552492 233 FAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALTVEHK 278
Cdd:cd19123 250 WAIQRGTVVIPKSVNPERIQQNLEAAEVELDASDMATIAALDRHHR 295
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
11-274 |
5.94e-73 |
|
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: 224.46 E-value: 5.94e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19132 7 IPAIGFGTYPLKGDEGVEAVVAA-LQAGYRLLDTAFNYENEGAVGEAVR----RSGVPREELFVTTKLPGRHHGYEEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPgsslkseNPaNKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAVN 170
Cdd:cd19132 82 TIEESLYRLGLDYVDLYLIHWP-------NP-SRDLYVEAWQALIEAREEGLVRSIGVSNFLPEHLDRLIDETGVTPAVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 171 QVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTyrkQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEH 250
Cdd:cd19132 154 QIELHPYFPQAEQRAYHREHGIVTQSWSPLGRGS---GLLDEPVIKAIAEKHGKTPAQVVLRWHVQLGVVPIPKSANPER 230
|
250 260
....*....|....*....|....
gi 17552492 251 VATNFKVTKLAITQEDIDRLLALT 274
Cdd:cd19132 231 QRENLAIFDFELSDEDMAAIAALD 254
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
9-273 |
1.11e-72 |
|
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: 223.79 E-value: 1.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKllpaNGLKREDIWITSKLAPSNAGVKKA 88
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEA-ASAVREALEVGYRSIDTAAIYGNEEGVGKAIRA----SGVPREELFITTKLWNSDQGYDST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGsslksenPANKKLrVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:cd19131 83 LRAFDESLRKLGLDYVDLYLIHWPV-------PAQDKY-VETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSptyrKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:cd19131 155 VNQIELHPRFQQRELRAFHAKHGIQTESWSPLGQ----GGLLSDPVIGEIAEKHGKTPAQVVIRWHLQNGLVVIPKSVTP 230
|
250 260
....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19131 231 SRIAENFDVFDFELDADDMQAIAGL 255
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
11-283 |
2.31e-71 |
|
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: 220.73 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGrileKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19157 10 MPWLGLGVFKVEEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGVG----KGIKESGIPREELFITSKVWNADQGYDSTLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGsslksenpanKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAVN 170
Cdd:cd19157 86 AFEASLERLGLDYLDLYLIHWPV----------KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 171 QVEYHPHFHQDDLVKYCNENNIHFQAYSSLgsptYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEH 250
Cdd:cd19157 156 QVEFHPRLTQKELRDYCKKQGIQLEAWSPL----MQGQLLDNPVLKEIAEKYNKSVAQVILRWDLQNGVVTIPKSIKEHR 231
|
250 260 270
....*....|....*....|....*....|...
gi 17552492 251 VATNFKVTKLAITQEDIDRLLALTVEHKTCWDP 283
Cdd:cd19157 232 IIENADVFDFELSQEDMDKIDALNENLRVGPDP 264
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
11-270 |
3.53e-70 |
|
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: 216.75 E-value: 3.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVqKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGrileKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19073 1 IPALGLGTWQL-RGDDCANAVKEALELGYRHIDTAEIYNNEAEVG----EAIAESGVPREDLFITTKVWRDHLRPEDLKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAVN 170
Cdd:cd19073 76 SVDRSLEKLGTDYVDLLLIHWPNPTVPLE---------ETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLPIAVN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 171 QVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEH 250
Cdd:cd19073 147 QVEFHPFLYQAELLEYCRENDIVITAYSPLA----RGEVLRDPVIQEIAEKYDKTPAQVALRWLVQKGIVVIPKASSEDH 222
|
250 260
....*....|....*....|
gi 17552492 251 VATNFKVTKLAITQEDIDRL 270
Cdd:cd19073 223 LKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
11-273 |
5.34e-69 |
|
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: 214.22 E-value: 5.34e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19126 9 MPWLGLGVFQTPDGDETERAVQTALENGYRSIDTAAIYKNEEGVGEAIR----ESGVPREELFVTTKLWNDDQRARRTED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGsslksenpanKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAVN 170
Cdd:cd19126 85 AFQESLDRLGLDYVDLYLIHWPG----------KDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADVVPAVN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 171 QVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEH 250
Cdd:cd19126 155 QVEFHPYLTQKELRGYCKSKGIVVEAWSPLG----QGGLLSNPVLAAIGEKYGKSAAQVVLRWDIQHGVVTIPKSVHASR 230
|
250 260
....*....|....*....|...
gi 17552492 251 VATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19126 231 IKENADIFDFELSEDDMTAIDAL 253
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
11-273 |
1.07e-68 |
|
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: 215.35 E-value: 1.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVqKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19154 12 MPLIGLGTWQS-KGAEGITAVRTALKAGYRLIDTAFLYQNEEAIGEALAELLEEGVVKREDLFITTKLWTHEHAPEDVEE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSLKSENPANKKLR----------VESWNVMCEMMAEGKLRSVGVSNFEICHLEELK 160
Cdd:cd19154 91 ALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENgmsihdavdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 161 KDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSP-----------TYRKQLSEEPLIKELAQKYNVEIPVL 229
Cdd:cd19154 171 DNARVKPHNNQVECHLYFPQKELVEFCKKHNISVTSYATLGSPgranftkstgvSPAPNLLQDPIVKAIAEKHGKTPAQV 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 17552492 230 LLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19154 251 LLRYLLQRGIAVIPKSATPSRIKENFNIFDFSLSEEDMATLEEI 294
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
11-280 |
3.63e-67 |
|
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: 211.47 E-value: 3.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRIL-EKLLPANGLKREDIWITSKLAPSNAGVKKAR 89
Cdd:cd19106 7 MPLIGLGTWKSKPGQV-KAAVKYALDAGYRHIDCAAVYGNEQEVGEALkEKVGPGKAVPREDLFVTSKLWNTKHHPEDVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 90 ESIEESLSNLKVEYLDLLLIHWPGSSLKSENP----ANKKLR------VESWNVMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd19106 86 PALRKTLKDLQLDYLDLYLIHWPYAFERGDNPfpknPDGTIRydsthyKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSP--TYRK----QLSEEPLIKELAQKYNVEIPVLLLGF 233
Cdd:cd19106 166 LSVARIKPAVLQVECHPYLAQNELIAHCKARGLVVTAYSPLGSPdrPWAKpdepVLLEEPKVKALAKKYNKSPAQILLRW 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 17552492 234 AYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALTVEHKTC 280
Cdd:cd19106 246 QVQRGVVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDALNRNWRYI 292
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
11-270 |
6.77e-67 |
|
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: 210.43 E-value: 6.77e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQ-VQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAgvKKAR 89
Cdd:cd19119 12 IPALGLGTASpHEDRAEVKEAVEAAIKEGYRHIDTAYAYETEDFVGEAIKRAIDDGSIKREELFITTKVWPTFY--DEVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 90 ESIEESLSNLKVEYLDLLLIHWPGSSLKSENPANK---------KLR-------VESWNVMCEMMAEGKLRSVGVSNFEI 153
Cdd:cd19119 90 RSLDESLKALGLDYVDLLLVHWPVCFEKDSDDSGKpftpvnddgKTRyaasgdhITTYKQLEKIYLDGRAKAIGVSNYSI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 154 CHLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSptYRKQLSEEPLIKELAQKYNVEIPVLLLGF 233
Cdd:cd19119 170 VYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGS--HGAPNLKNPLVKKIAEKYNVSTGDILISY 247
|
250 260 270
....*....|....*....|....*....|....*..
gi 17552492 234 AYCQGISVLPRTTNPEHVATNFKVTKLaiTQEDIDRL 270
Cdd:cd19119 248 HVRQGVIVLPKSLKPVRIVSNGKIVSL--TKEDLQKL 282
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
9-283 |
2.91e-66 |
|
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: 207.76 E-value: 2.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKA 88
Cdd:cd19156 7 VEMPRLGLGVWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKNEEGVGQGIR----ESGVPREEVFVTTKLWNSDQGYEST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGsslksenpanKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:cd19156 83 LAAFEESLEKLGLDYVDLYLIHWPV----------KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCKVAPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSptyrKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:cd19156 153 VNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQ----GKLLSNPVLKAIGKKYGKSAAQVIIRWDIQHGIITIPKSVHE 228
|
250 260 270
....*....|....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLALTVEHKTCWDP 283
Cdd:cd19156 229 ERIQENFDVFDFELTAEEIRQIDGLNTDHRYGPDP 263
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
11-270 |
6.68e-66 |
|
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: 206.70 E-value: 6.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGT----WQVQKEEILRQVID---AGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPsna 83
Cdd:cd19120 4 IPAIAFGTgtawYKSGDDDIQRDLVDsvkLALKAGFRHIDTAEMYGNEKEVGEALK----ESGVPREDLFITTKVSP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 84 GVKKARESIEESLSNLKVEYLDLLLIHWPGSSlksenPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDS 163
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSPFFA-----KEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 164 NVVPAVNQVEYHPHFH--QDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISV 241
Cdd:cd19120 152 KIKPAVNQIEFHPYLYpqQPALLEYCREHGIVVSAYSPLSPLTRDAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIVV 231
|
250 260
....*....|....*....|....*....
gi 17552492 242 LPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19120 232 VTTSSKEERMKEYLEAFDFELTEEEVEEI 260
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
11-278 |
7.68e-66 |
|
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: 207.35 E-value: 7.68e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIdAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLApsNAGVKKARE 90
Cdd:cd19117 14 IPAVGLGTWQSKPNEVAKAVE-AALKAGYRHIDTAAIYGNEEEVGQGIK----DSGVPREEIFITTKLW--CTWHRRVEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPgSSLKSENPANKKLR-------------VESWNVMCEMMAEGKLRSVGVSNFEICHLE 157
Cdd:cd19117 87 ALDQSLKKLGLDYVDLYLMHWP-VPLDPDGNDFLFKKddgtkdhepdwdfIKTWELMQKLPATGKVKAIGVSNFSIKNLE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 158 ELKKDSN--VVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTyrKQLSEEPLIKELAQKYNVEIPVLLLGFAY 235
Cdd:cd19117 166 KLLASPSakIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLGSTN--APLLKEPVIIKIAKKHGKTPAQVIISWGL 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17552492 236 CQGISVLPRTTNPEHVATNFKVTKLaiTQEDIDRLLALTVEHK 278
Cdd:cd19117 244 QRGYSVLPKSVTPSRIESNFKLFTL--SDEEFKEIDELHKEYG 284
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-273 |
2.89e-65 |
|
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: 204.80 E-value: 2.89e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTWQVQKEEILRqVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKAR 89
Cdd:cd19140 7 RIPALGLGTYPLTGEECTR-AVEHALELGYRHIDTAQMYGNEAQVGEAIA----ASGVPRDELFLTTKVWPDNYSPDDFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 90 ESIEESLSNLKVEYLDLLLIHWPGsslkSENPANKKLRveswnVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPAV 169
Cdd:cd19140 82 ASVEESLRKLRTDYVDLLLLHWPN----KDVPLAETLG-----ALNEAQEAGLARHIGVSNFTVALLREAVELSEAPLFT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 170 NQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQ-GISVLPRTTNP 248
Cdd:cd19140 153 NQVEYHPYLDQRKLLDAAREHGIALTAYSPLA----RGEVLKDPVLQEIGRKHGKTPAQVALRWLLQQeGVAAIPKATNP 228
|
250 260
....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19140 229 ERLEENLDIFDFTLSDEEMARIAAL 253
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
11-273 |
3.22e-65 |
|
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: 205.81 E-value: 3.22e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQvQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19111 4 MPVIGLGTYQ-SPPEEVRAAVDYALFVGYRHIDTALSYQNEKAIGEALKWWLKNGKLKREEVFITTKLPPVYLEFKDTEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWP-GSSLKSENPANKKLR---VESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVV 166
Cdd:cd19111 83 SLEKSLENLKLPYVDLYLIHHPcGFVNKKDKGERELASsdvTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAKVK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 167 PAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLS--------EEPLIKELAQKYNVEIPVLLLGFAYCQG 238
Cdd:cd19111 163 PSNLQLECHAYLQQRELRKFCNKKNIVVTAYAPLGSPGRANQSLwpdqpdllEDPTVLAIAKELDKTPAQVLLRFVLQRG 242
|
250 260 270
....*....|....*....|....*....|....*
gi 17552492 239 ISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19111 243 TGVLPKSTNKERIEENFEVFDFELTEEHFKKLKTL 277
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
11-270 |
1.63e-64 |
|
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: 203.53 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLpANGLKREDIWITSKLAPSNAgvKKARE 90
Cdd:cd19121 12 IPAVGLGTWQAKAGEV-KAAVAHALKIGYRHIDGALCYQNEDEVGEGIKEAI-AGGVKREDLFVTTKLWSTYH--RRVEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWP------GSSLK-------SENPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLE 157
Cdd:cd19121 88 CLDRSLKSLGLDYVDLYLVHWPvllnpnGNHDLfptlpdgSRDLDWDWNHVDTWKQMEKVLKTGKTKAIGVSNYSIPYLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 158 ELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSpTYRKQLSEEPLIkELAQKYNVEIPVLLLGFAYCQ 237
Cdd:cd19121 168 ELLKHATVVPAVNQVENHPYLPQQELVDFCKEKGILIEAYSPLGS-TGSPLISDEPVV-EIAKKHNVGPGTVLISYQVAR 245
|
250 260 270
....*....|....*....|....*....|...
gi 17552492 238 GISVLPRTTNPEHVATNFKVTKLaiTQEDIDRL 270
Cdd:cd19121 246 GAVVLPKSVTPDRIKSNLEIIDL--DDEDMNKL 276
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
12-268 |
2.45e-64 |
|
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: 203.14 E-value: 2.45e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 12 PLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARES 91
Cdd:cd19128 2 PRLGFGTYKITESES-KEAVKNAIKAGYRHIDCAYYYGNEAFIGIAFSEIFKDGGVKREDLFITSKLWPTMHQPENVKEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 92 IEESLSNLKVEYLDLLLIHWP-------GSSLKSENPANKKLRV---ESWNVMCEMMAEGKLRSVGVSNFEICHLEELKK 161
Cdd:cd19128 81 LLITLQDLQLEYLDLFLIHWPlafdmdtDGDPRDDNQIQSLSKKpleDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 162 DSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLS--EEPLIKELAQKYNVEIPVLLLGF---AYC 236
Cdd:cd19128 161 YCKIKPFMNQIECHPYFQNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTflNDSELKALATKYNTTPPQVIIAWhlqKWP 240
|
250 260 270
....*....|....*....|....*....|..
gi 17552492 237 QGISVLPRTTNPEHVATNFKVTKLAITQEDID 268
Cdd:cd19128 241 KNYSVIPKSANKSRCQQNFDINDLALTKEDMD 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
9-273 |
2.92e-61 |
|
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: 194.93 E-value: 2.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NN---MPLIGIGTWQVQKEEILrQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGV 85
Cdd:cd19127 4 NNgveMPALGLGVFQTPPEETA-DAVATALADGYRLIDTAAAYGNEREVGEGIR----RSGVDRSDIFVTTKLWISDYGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 86 KKARESIEESLSNLKVEYLDLLLIHWPgsslkseNPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNV 165
Cdd:cd19127 79 DKALRGFDASLRRLGLDYVDLYLLHWP-------VPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATTV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 166 VPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGS--------PTYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQ 237
Cdd:cd19127 152 VPAVNQVELHPYFSQKDLRAFHRRLGIVTQAWSPIGGvmrygasgPTGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQN 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 17552492 238 GISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19127 232 GVSAIPKSVHPERIAENIDIFDFALSAEDMAAIDAL 267
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
9-273 |
3.44e-61 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 194.69 E-value: 3.44e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEILRQViDAGFKEGYRFIDTAQVYNNEAKIGRILEKllpaNGLKREDIWITSKLAPSNAGVKKA 88
Cdd:cd19134 9 NTMPVIGLGVGELSDDEAERSV-SAALEAGYRLIDTAAAYGNEAAVGRAIAA----SGIPRGELFVTTKLATPDQGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGsslksenPANKKLrVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:cd19134 84 QAACRASLERLGLDYVDLYLIHWPA-------GREGKY-VDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLTFFTPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:cd19134 156 VNQIELHPLLNQAELRKVNAQHGIVTQAYSPLG----VGRLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNVVISRSSNP 231
|
250 260
....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19134 232 ERIASNLDVFDFELTADHMDALDGL 256
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
11-273 |
2.23e-60 |
|
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: 193.90 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19155 12 MPVVGLGTWQSSPEEI-ETAVDTALEAGYRHIDTAYVYRNEAAIGNVLKKWIDSGKVKREELFIVTKLPPGGNRREKVEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSLKSE------NPANKKLR------VESWNVMCEMMAEGKLRSVGVSNFEICHLEE 158
Cdd:cd19155 91 FLLKSLEKLQLDYVDLYLIHFPVGSLSKEddsgklDPTGEHKQdyttdlLDIWKAMEAQVDQGLTRSIGLSNFNREQMAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 159 LKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRK-------------QLSEEPLIKELAQKYNVE 225
Cdd:cd19155 171 ILKNARIKPANLQVELHVYLQQKDLVDFCSTHSITVTAYAPLGSPGAAHfspgtgspsgsspDLLQDPVVKAIAERHGKS 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 17552492 226 IPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19155 251 PAQVLLRWLMQRGVVVIPKSTNAARIKENFQVFDFELTEADMAKLSSL 298
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
11-273 |
4.81e-59 |
|
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: 188.72 E-value: 4.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVqKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19139 1 IPAFGLGTFRL-KDDVVIDSVRTALELGYRHIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLSKDKLLP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPgsSLKSENPAnkklrVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKK---DSNVvp 167
Cdd:cd19139 76 SLEESLEKLRTDYVDLTLIHWP--SPNDEVPV-----EEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAvvgAGAI-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 168 AVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptyRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTN 247
Cdd:cd19139 147 ATNQIELSPYLQNRKLVAHCKQHGIHVTSYMTLA----YGKVLDDPVLAAIAERHGATPAQIALAWAMARGYAVIPSSTK 222
|
250 260
....*....|....*....|....*.
gi 17552492 248 PEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19139 223 REHLRSNLLALDLTLDADDMAAIAAL 248
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
11-270 |
6.02e-59 |
|
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: 189.40 E-value: 6.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGT--WQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLpANGL--KREDIWITSKLAPSNAGVK 86
Cdd:cd19124 5 MPVIGMGTasDPPSPEDIKAAVLEA-IEVGYRHFDTAAAYGTEEALGEALAEAL-RLGLvkSRDELFVTSKLWCSDAHPD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 87 KARESIEESLSNLKVEYLDLLLIHWPGSSLK--SENPANKK----LRVES-WNVMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd19124 83 LVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkFSFPIEEEdflpFDIKGvWEAMEECQRLGLTKAIGVSNFSCKKLQEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYR---KQLSEEPLIKELAQKYNVEIPVLLLGFAYC 236
Cdd:cd19124 163 LSFATIPPAVNQVEMNPAWQQKKLREFCKANGIHVTAYSPLGAPGTKwgsNAVMESDVLKEIAAAKGKTVAQVSLRWVYE 242
|
250 260 270
....*....|....*....|....*....|....
gi 17552492 237 QGISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19124 243 QGVSLVVKSFNKERMKQNLDIFDWELTEEDLEKI 276
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
8-280 |
7.33e-58 |
|
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: 187.63 E-value: 7.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 8 KNNMPLIGIGTWQV---QKEEILRQVIDAGfkegYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAG 84
Cdd:cd19107 1 GAKMPILGLGTWKSppgQVTEAVKVAIDAG----YRHIDCAYVYQNENEVGEAIQEKIKEQVVKREDLFIVSKLWCTFHE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 85 VKKARESIEESLSNLKVEYLDLLLIHWP-----GSSL--KSEN----PANKKLrVESWNVMCEMMAEGKLRSVGVSNFEI 153
Cdd:cd19107 77 KGLVKGACQKTLSDLKLDYLDLYLIHWPtgfkpGKELfpLDESgnviPSDTTF-LDTWEAMEELVDEGLVKAIGVSNFNH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 154 CHLEEL--KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPT--YRK----QLSEEPLIKELAQKYNVE 225
Cdd:cd19107 156 LQIERIlnKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDrpWAKpedpSLLEDPKIKEIAAKHNKT 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 17552492 226 IPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALTVEHKTC 280
Cdd:cd19107 236 TAQVLIRFPIQRNLVVIPKSVTPERIAENFKVFDFELSSEDMATILSFNRNWRAC 290
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
11-273 |
5.61e-55 |
|
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: 179.99 E-value: 5.61e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVkkARE 90
Cdd:cd19112 11 MPVIGLGVWRMEPGEI-KELILNAIKIGYRHFDCAADYKNEKEVGEALAEAFKTGLVKREDLFITTKLWNSDHGH--VIE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWP-----------GSSLKSENPANKKLRV---ESWNVMCEMMAEGKLRSVGVSNFEICHL 156
Cdd:cd19112 88 ACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttGSALGEDGVLDIDVTIsleTTWHAMEKLVSAGLVRSIGISNYDIFLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 157 EELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQL------SEEPLIKELAQKYNVEIPVLL 230
Cdd:cd19112 168 RDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGISVTAHTPLGGAAANAEWfgsvspLDDPVLKDLAKKYGKSAAQIV 247
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17552492 231 LGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19112 248 LRWGIQRNTAVIPKSSKPERLKENIDVFDFQLSKEDMKLIKSL 290
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
9-273 |
2.33e-54 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 177.57 E-value: 2.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNNEAKIGrileKLLPANGLKREDIWITSKLApsNAGVKKA 88
Cdd:PRK11565 13 NVMPQLGLGVWQASNEEV-ITAIHKALEVGYRSIDTAAIYKNEEGVG----KALKEASVAREELFITTKLW--NDDHKRP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPgsslkseNPAnKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:PRK11565 86 REALEESLKKLQLDYVDLYLMHWP-------VPA-IDHYVEAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDETGVTPV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTyrKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:PRK11565 158 INQIELHPLMQQRQLHAWNATHKIQTESWSPLAQGG--KGVFDQKVIRDLADKYGKTPAQIVIRWHLDSGLVVIPKSVTP 235
|
250 260
....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:PRK11565 236 SRIAENFDVFDFRLDKDELGEIAKL 260
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
11-273 |
3.02e-54 |
|
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: 178.38 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKARE 90
Cdd:cd19115 13 MPLVGFGLWKVNNDTCADQVYNA-IKAGYRLFDGACDYGNEVEAGQGVARAIKEGIVKREDLFIVSKLWNTFHDGERVEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPgSSLKSENPA----------NKKLRV------ESWNVMCEMMAEGKLRSVGVSNFEIC 154
Cdd:cd19115 92 ICRKQLADWGIDYFDLFLIHFP-IALKYVDPAvryppgwfydGKKVEFsnapiqETWTAMEKLVDKGLARSIGVSNFSAQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsPTYRKQLS-----------EEPLIKELAQKYN 223
Cdd:cd19115 171 LLMDLLRYARIRPATLQIEHHPYLTQPRLVKYAQKEGIAVTAYSSFG-PQSFLELDlpgakdtpplfEHDVIKSIAEKHG 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17552492 224 VEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19115 250 KTPAQVLLRWATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISAL 299
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
8-270 |
1.16e-53 |
|
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: 175.11 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 8 KNNMPLIGIGTWQV------------QKEEILRQVIDAGFkegyRFIDTAQVYNN---EAKIGRILEkllpanGLKREDI 72
Cdd:cd19072 1 GEEVPVLGLGTWGIgggmskdysddkKAIEALRYAIELGI----NLIDTAEMYGGghaEELVGKAIK------GFDREDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 73 WITSKLAPSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFE 152
Cdd:cd19072 71 FITTKVSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIE---------ETLRAMEELVEEGKIRYIGVSNFS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 153 ICHLEELKKDSNVVP-AVNQVEYHPHF--HQDDLVKYCNENNIHFQAYSSLGSpTYRKQLSEEPLIKELAQKYNVEIPVL 229
Cdd:cd19072 142 LEELEEAQSYLKKGPiVANQVEYNLFDreEESGLLPYCQKNGIAIIAYSPLEK-GKLSNAKGSPLLDEIAKKYGKTPAQI 220
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17552492 230 LLGF-AYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19072 221 ALNWlISKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
11-276 |
3.10e-53 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 175.71 E-value: 3.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKL-----APSNagV 85
Cdd:cd19113 11 MPSVGFGCWKLDNATAADQIYQA-IKAGYRLFDGAEDYGNEKEVGEGVNRAIDEGLVKREELFLTSKLwnnfhDPKN--V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 86 KKAresIEESLSNLKVEYLDLLLIHWP--------------------GSSLKSEN-PAnkklrVESWNVMCEMMAEGKLR 144
Cdd:cd19113 88 ETA---LNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdGDNFVYEDvPI-----LDTWKALEKLVDAGKIK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 145 SVGVSNFEICHLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTY----------RKQLSEEPL 214
Cdd:cd19113 160 SIGVSNFPGALILDLLRGATIKPAVLQIEHHPYLQQPKLIEYAQKAGITITAYSSFGPQSFvelnqgralnTPTLFEHDT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552492 215 IKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALTVE 276
Cdd:cd19113 240 IKSIAAKHNKTPAQVLLRWATQRGIAVIPKSNLPERLLQNLSVNDFDLTKEDFEEIAKLDIG 301
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
9-273 |
4.63e-52 |
|
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: 170.86 E-value: 4.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILekllPANGLKREDIWITSKLAPSNAGVKKA 88
Cdd:cd19130 8 NSIPQLGYGVFKVPPADTQRAVATA-LEVGYRHIDTAAIYGNEEGVGAAI----AASGIPRDELFVTTKLWNDRHDGDEP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGSSlksenpanKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVPA 168
Cdd:cd19130 83 AAAFAESLAKLGLDQVDLYLVHWPTPA--------AGNYVHTWEAMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTyrkqLSEEPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNP 248
Cdd:cd19130 155 VNQIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGK----LLGDPPVGAIAAAHGKTPAQIVLRWHLQKGHVVFPKSVRR 230
|
250 260
....*....|....*....|....*
gi 17552492 249 EHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19130 231 ERMEDNLDVFDFDLTDTEIAAIDAL 255
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
14-270 |
1.47e-51 |
|
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: 170.57 E-value: 1.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQ-------VQKEEILRqVIDAGFKEGYRFIDTAQVYN---NEAKIGRILEKLLPanglKREDIWITSKL----A 79
Cdd:pfam00248 1 IGLGTWQlgggwgpISKEEALE-ALRAALEAGINFIDTAEVYGdgkSEELLGEALKDYPV----KRDKVVIATKVpdgdG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 PSNAGVKKA--RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLE 157
Cdd:pfam00248 76 PWPSGGSKEniRKSLEESLKRLGTDYIDLYYLHWPDPDTPIE---------ETWDALEELKKEGKIRAIGVSNFDAEQIE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 158 ELKKDSNVVPAVNQVEYHP--HFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEP---------------------- 213
Cdd:pfam00248 147 KALTKGKIPIVAVQVEYNLlrRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPdkgpgerrrllkkgtplnleal 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 214 -LIKELAQKYNVEIPVLLLGFAYCQ--GISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:pfam00248 227 eALEEIAKEHGVSPAQVALRWALSKpgVTIPIPGASNPEQLEDNLGALEFPLSDEEVARI 286
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
10-273 |
4.13e-50 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 166.35 E-value: 4.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTWQVQKEeilrQVIDA---GFKEGYRFIDTAQVYNNEAKIGRILEkllpANGLKREDIWITSKLAPSNAGVK 86
Cdd:PRK11172 2 SIPAFGLGTFRLKDQ----VVIDSvktALELGYRAIDTAQIYDNEAAVGQAIA----ESGVPRDELFITTKIWIDNLAKD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 87 KARESIEESLSNLKVEYLDLLLIHWPgsslkseNPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEE----LKKD 162
Cdd:PRK11172 74 KLIPSLKESLQKLRTDYVDLTLIHWP-------SPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQaiaaVGAE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 163 SnvvPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGsptYRKQLSeEPLIKELAQKYNVEIPVLLLGFAYCQGISVL 242
Cdd:PRK11172 147 N---IATNQIELSPYLQNRKVVAFAKEHGIHVTSYMTLA---YGKVLK-DPVIARIAAKHNATPAQVILAWAMQLGYSVI 219
|
250 260 270
....*....|....*....|....*....|.
gi 17552492 243 PRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:PRK11172 220 PSSTKRENLASNLLAQDLQLDAEDMAAIAAL 250
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
10-273 |
1.60e-49 |
|
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: 165.90 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTWQVQKEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKAR 89
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKVA-IDAGYRHFDCAYLYHNESEVGAGIREKIKEGVVRREDLFIVSKLWCTCHKKSLVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 90 ESIEESLSNLKVEYLDLLLIHWPGSSLKSEN--PANKKLRV--------ESWNVMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd19110 82 TACTRSLKALKLNYLDLYLIHWPMGFKPGEPdlPLDRSGMVipsdtdflDTWEAMEDLVIEGLVKNIGVSNFNHEQLERL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 --KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQ 237
Cdd:cd19110 162 lnKPGLRVKPVTNQIECHPYLTQKKLISFCQSRNVSVTAYRPLGGSCEGVDLIDDPVIQRIAKKHGKSPAQILIRFQIQR 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 17552492 238 GISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19110 242 NVIVIPKSVTPSRIKENIQVFDFELTEHDMDNLLSL 277
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
11-261 |
4.83e-49 |
|
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: 164.33 E-value: 4.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQ--KEEILRQVIDAgFKEGYRFIDTAQVYNNEAKIGRILEKLLPAN-GLKREDIWITSKLAPSNAGVKK 87
Cdd:cd19122 9 IPAVGFGTFANEgaKGETYAAVTKA-LDVGYRHLDCAWFYLNEDEVGDAVRDFLKENpSVKREDLFICTKVWNHLHEPED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 ARESIEESLSNLKVEYLDLLLIHWPGSSLKSE------NPANKKLRVE--------SWNVMCEMMAEGKLRSVGVSNFEI 153
Cdd:cd19122 88 VKWSIDNSLKNLKLDYIDLFLVHWPIAAEKNDqrspklGPDGKYVILKdltenpepTWRAMEEIYESGKAKAIGVSNWTI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 154 CHLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGS----PTYRKQLSEEPLIKELAQKYNVEIPVL 229
Cdd:cd19122 168 PGLKKLLSFAKVKPHVNQIEIHPFLPNEELVDYCFSNDILPEAYSPLGSqnqvPSTGERVSENPTLNEVAEKGGYSLAQV 247
|
250 260 270
....*....|....*....|....*....|..
gi 17552492 230 LLGFAYCQGISVLPRTTNPEHVATNFKVTKLA 261
Cdd:cd19122 248 LIAWGLRRGYVVLPKSSTPSRIESNFKSIELS 279
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
11-270 |
3.37e-48 |
|
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: 161.26 E-value: 3.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQV--------QKEEILRQVIDAGFkegyRFIDTAQVYNN---EAKIGRILEKLlpanglkREDIWITSKLA 79
Cdd:cd19138 11 VPALGQGTWYMgedpakraQEIEALRAGIDLGM----TLIDTAEMYGDggsEELVGEAIRGR-------RDKVFLVSKVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 PSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSENpankklrVESwnvMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd19138 80 PSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAET-------VAA---MEELKKEGKIRAWGVSNFDTDDMEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 ---KKDSNVvpAVNQVEYH-----PHFhqdDLVKYCNENNIHFQAYSSLGS-PTYRKQLSEEPLIKELAQKYNVEIPVLL 230
Cdd:cd19138 150 wavPGGGNC--AANQVLYNlgsrgIEY---DLLPWCREHGVPVMAYSPLAQgGLLRRGLLENPTLKEIAARHGATPAQVA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 17552492 231 LGFAY-CQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19138 225 LAWVLrDGNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
9-273 |
1.03e-47 |
|
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: 161.19 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQV---QKEEILRQVIdagfKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGV 85
Cdd:cd19114 2 DKMPLVGFGTAKIkanETEEVIYNAI----KVGYRLIDGALLYGNEAEVGRGIRKAIQEGLVKREDLFIVTKLWNNFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 86 KKARESIEESLSNLKVEYLDLLLIHWPgSSLKSENPAN-----------KKLRVES------WNVMCEMMAEGKLRSVGV 148
Cdd:cd19114 78 DHVREAFDRQLKDYGLDYIDLYLIHFP-IPAAYVDPAEnypflwkdkelKKFPLEQspmqecWREMEKLVDAGLVRNIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 149 SNFEICHLEELKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRK---------QLSEEPLIKELA 219
Cdd:cd19114 157 ANFNVQLILDLLTYAKIKPAVLQIEHHPYLQQKRLIDWAKKQGIQITAYSSFGNAVYTKvtkhlkhftNLLEHPVVKKLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 17552492 220 QKYNVEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19114 237 DKHKRDTGQVLLRWAVQRNITVIPKSVNVERMKTNLDITSYKLDEEDMEALYEL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
14-274 |
4.64e-46 |
|
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: 156.59 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQ---------VQKEEILRqVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpanglKREDIWITSKLAPS 81
Cdd:cd19085 4 LGLGCWQfgggywwgdQDDEESIA-TIHAALDAGINFFDTAEAYGDghsEEVLGKALKG-------RRDDVVIATKVSPD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 82 NAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEELKK 161
Cdd:cd19085 76 NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLE---------ETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 162 DSNVVpaVNQVEYHPHFHQ--DDLVKYCNENNIHFQAYSSLG----------------------------SPTYRKQLSE 211
Cdd:cd19085 147 AGRID--SNQLPYNLLWRAieYEILPFCREHGIGVLAYSPLAqglltgkfssaedfppgdartrlfrhfePGAEEETFEA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552492 212 EPLIKELAQKYNVEIPVLLLGFAYCQ-GI-SVLPRTTNPEHVATNFKVTKLAITQEDIDRLLALT 274
Cdd:cd19085 225 LEKLKEIADELGVTMAQLALAWVLQQpGVtSVIVGARNPEQLEENAAAVDLELSPSVLERLDEIS 289
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-260 |
9.08e-45 |
|
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: 153.38 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTWqVQKEEILRQVIDAGFKEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPSNAGVKKAR 89
Cdd:cd19129 5 AIPALGFGTL-IPDPSATRNAVKAALEAGFRHFDCAERYRNEAEVGEAMQEVFKAGKIRREDLFVTTKLWNTNHRPERVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 90 ESIEESLSNLKVEYLDLLLIHWPGSSLKSEN--PANKKLRV---------ESWNVMCEMMAEGKLRSVGVSNFEICHLEE 158
Cdd:cd19129 84 PAFEASLKRLQLDYLDLYLIHTPFAFQPGDEqdPRDANGNViyddgvtllDTWRAMERLVDEGRCKAIGLSDVSLEKLRE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 159 LKKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSpTYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQG 238
Cdd:cd19129 164 IFEAARIKPAVVQVESHPYLPEWELLDFCKNHGIVLQAFAPLGH-GMEPKLLEDPVITAIARRVNKTPAQVLLAWAIQRG 242
|
250 260
....*....|....*....|..
gi 17552492 239 ISVLPRTTNPEHVATNFKVTKL 260
Cdd:cd19129 243 TALLTTSKTPSRIRENFDISTL 264
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
11-270 |
1.77e-41 |
|
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: 145.07 E-value: 1.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTW---QVQKEEILRQV---IDAGFkegyRFIDTAQVYNNEAKIGR-ILEKLlpANG-LKREDIWITSKLAPSN 82
Cdd:cd19108 11 IPVLGFGTYapeEVPKSKALEATklaIDAGF----RHIDSAYLYQNEEEVGQaIRSKI--ADGtVKREDIFYTSKLWCTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 83 AGVKKARESIEESLSNLKVEYLDLLLIHWPgSSLKSEN-----PANKKLRVES------WNVMCEMMAEGKLRSVGVSNF 151
Cdd:cd19108 85 HRPELVRPALEKSLKKLQLDYVDLYLIHFP-VALKPGEelfpkDENGKLIFDTvdlcatWEAMEKCKDAGLAKSIGVSNF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 152 EICHLEEL--KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRK-------QLSEEPLIKELAQKY 222
Cdd:cd19108 164 NRRQLEMIlnKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAYSALGSQRDKEwvdqnspVLLEDPVLCALAKKH 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17552492 223 NvEIPVLL-LGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQED---IDRL 270
Cdd:cd19108 244 K-RTPALIaLRYQLQRGVVVLAKSFNEKRIKENLQVFEFQLTSEDmkaLDGL 294
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
9-273 |
3.28e-41 |
|
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: 144.56 E-value: 3.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 9 NNMPLIGIGTWQVQKE-------EILRQVIDagfkEGYRFIDTAQVYNNEAKIGRILEKLLPANGLKREDIWITSKLAPS 81
Cdd:cd19109 2 NSIPIIGLGTYSEPKTtpkgacaEAVKVAID----TGYRHIDGAYIYQNEHEVGQAIREKIAEGKVKREDIFYCGKLWNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 82 NAGVKKARESIEESLSNLKVEYLDLLLIHW-----PGSSL--KSENPA---NKKLRVESWNVMCEMMAEGKLRSVGVSNF 151
Cdd:cd19109 78 CHPPELVRPTLERTLKVLQLDYVDLYIIEMpmafkPGDEIypRDENGKwlyHKTNLCATWEALEACKDAGLVKSIGVSNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 152 EICHLEEL--KKDSNVVPAVNQVEYHPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRK-------QLSEEPLIKELAQKY 222
Cdd:cd19109 158 NRRQLELIlnKPGLKHKPVSNQVECHPYFTQPKLLEFCQQHDIVIVAYSPLGTCRDPIwvnvsspPLLEDPLLNSIGKKY 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 17552492 223 NVEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19109 238 NKTAAQVVLRFNIQRGVVVIPKSFNPERIKENFQIFDFSLTEEEMKDIEAL 288
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
11-270 |
4.15e-39 |
|
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: 137.70 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQV--------QKEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKLlpanglKREDIWITSKLA 79
Cdd:cd19137 4 IPALGLGTWGIggfltpdySRDEEMVELLKTAIELGYTHIDTAEMYgggHTEELVGKAIKDF------PREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 PSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd19137 78 PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLE---------ETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 KKDSNVVPAVNQVEYHPHFH---QDDLVKYCNENNIHFQAYsslgSPTYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYC 236
Cdd:cd19137 149 ISKSQTPIVCNQVKYNLEDRdpeRDGLLEYCQKNGITVVAY----SPLRRGLEKTNRTLEEIAKNYGKTIAQIALAWLIQ 224
|
250 260 270
....*....|....*....|....*....|....*
gi 17552492 237 Q-GISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19137 225 KpNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
14-270 |
4.61e-38 |
|
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: 135.73 E-value: 4.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV-------QKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpanglKREDIWITSK--LAPS 81
Cdd:cd19084 7 IGLGTWAIggtwwgeVDDQESIEAIKAAIDLGINFFDTAPVYGFghsEEILGKALKG-------RRDDVVIATKcgLRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 82 NAGVKKA-------RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFeic 154
Cdd:cd19084 80 GGKGVTKdlspesiRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIE---------ETAEALEKLKKEGKIRYIGVSNF--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKKDSNVVP-AVNQVEYHPhFHQD---DLVKYCNENNIHFQAYSSLG----------------------SPTYRKQ 208
Cdd:cd19084 148 SVEQLEEARKYGPiVSLQPPYSM-LEREieeELLPYCRENGIGVLPYGPLAqglltgkykkeptfppddrrsrFPFFRGE 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17552492 209 LSEEPL-----IKELAQKYNVEIPVLLLGFAYCQ--GISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19084 227 NFEKNLeivdkLKEIAEKYGKSLAQLAIAWTLAQpgVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-256 |
2.92e-35 |
|
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: 126.86 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV---QKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLLpanglKREDIWITSKLAPSNAGVKK 87
Cdd:cd06660 3 LGLGTMTFggdGDEEEAFALLDAALEAGGNFFDTADVYGDgrsERLLGRWLKGRG-----NRDDVVIATKGGHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 A--------RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEEL 159
Cdd:cd06660 78 RsrlspehiRRDLEESLRRLGTDYIDLYYLHRDDPSTPVE---------ETLEALNELVREGKIRYIGVSNWSAERLAEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 160 ----KKDSNVVPAVNQVEY---HPHFHQDDLVKYCNENNIHFQAYSSLGSptyrkqlseeplikELAQkynveipvLLLG 232
Cdd:cd06660 149 layaKAHGLPGFAAVQPQYsllDRSPMEEELLDWAEENGLPLLAYSPLAR--------------GPAQ--------LALA 206
|
250 260
....*....|....*....|....*.
gi 17552492 233 FAYCQ--GISVLPRTTNPEHVATNFK 256
Cdd:cd06660 207 WLLSQpfVTVPIVGARSPEQLEENLA 232
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-270 |
1.01e-34 |
|
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: 127.60 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNNMPL--IGIGTWQ-------VQKEEiLRQVIDAGFKEGYRFIDTAQVYN---NEAKIGRILEkllpanGLK 68
Cdd:COG0667 1 MEYRRLGRSGLKVsrLGLGTMTfggpwggVDEAE-AIAILDAALDAGINFFDTADVYGpgrSEELLGEALK------GRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 69 REDIWITSKLA--------PSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAE 140
Cdd:COG0667 74 RDDVVIATKVGrrmgpgpnGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIE---------ETLGALDELVRE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 141 GKLRSVGVSNFEICHLEE-LKKDSNVVP-AVNQVEYHPhFHQD---DLVKYCNENNIHFQAYSSLG----SPTYRK---- 207
Cdd:COG0667 145 GKIRYIGVSNYSAEQLRRaLAIAEGLPPiVAVQNEYSL-LDRSaeeELLPAARELGVGVLAYSPLAggllTGKYRRgatf 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 208 -------------QLSEEPL-----IKELAQKYNVEIPVLLLGFAYCQG--ISVLPRTTNPEHVATNFKVTKLAITQEDI 267
Cdd:COG0667 224 pegdraatnfvqgYLTERNLalvdaLRAIAAEHGVTPAQLALAWLLAQPgvTSVIPGARSPEQLEENLAAADLELSAEDL 303
|
...
gi 17552492 268 DRL 270
Cdd:COG0667 304 AAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
14-270 |
1.02e-33 |
|
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: 124.26 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQ----------VQKEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKLLPanglkREDIWITSKLAP 80
Cdd:cd19093 5 LGLGTWQwgdrlwwgygEYGDEDLQAAFDAALEAGVNLFDTAEVYgtgRSERLLGRFLKELGD-----RDEVVIATKFAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 81 snAGVKKARESI----EESLSNLKVEYLDLLLIHWPGSSLKSENpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHL 156
Cdd:cd19093 80 --LPWRLTRRSVvkalKASLERLGLDSIDLYQLHWPGPWYSQIE--------ALMDGLADAVEEGLVRAVGVSNYSADQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 157 EELK---KDSNVVPAVNQVEY---HPHFHQDDLVKYCNENNIHFQAYSSLG--------SPT-----------YRKQLSE 211
Cdd:cd19093 150 RRAHkalKERGVPLASNQVEYsllYRDPEQNGLLPACDELGITLIAYSPLAqglltgkySPEnpppggrrrlfGRKNLEK 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17552492 212 -EPLIKEL---AQKYNVEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19093 230 vQPLLDALeeiAEKYGKTPAQVALNWLIAKGVVPIPGAKNAEQAEENAGALGWRLSEEEVAEL 292
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
14-272 |
5.46e-30 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 115.06 E-value: 5.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV--------QKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpanglKREDIWITSKLA--- 79
Cdd:cd19149 14 IGLGTWAIgggpwwggSDDNESIRTIHAALDLGINLIDTAPAYGFghsEEIVGKAIKG-------RRDKVVLATKCGlrw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 ----------------PSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKL 143
Cdd:cd19149 87 dreggsfffvrdgvtvYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIE---------ETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 144 RSVGVSNFEICHLEELKKDSNVvpAVNQVEYH--PHFHQDDLVKYCNENNIHFQAYSSLG-------------------- 201
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAGQL--DIIQEKYSmlDRGIEKELLPYCKKNNIAFQAYSPLEqglltgkitpdrefdagdar 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 202 ------SPTYRKQLSE--EPlIKELAQKYNVEIPVLLLGFAYCQG--ISVLPRTTNPEHVATNFKVTKLAITQEDIDRLL 271
Cdd:cd19149 236 sgipwfSPENREKVLAllEK-WKPLCEKYGCTLAQLVIAWTLAQPgiTSALCGARKPEQAEENAKAGDIRLSAEDIATMR 314
|
.
gi 17552492 272 A 272
Cdd:cd19149 315 S 315
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
15-266 |
5.90e-30 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 114.48 E-value: 5.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 15 GIGTWQVQKEEiLRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEkllpANGLKREDIWITSKL------APSNAGV 85
Cdd:COG4989 22 RLGEWDLSPAE-AAALIEAALELGITTFDHADIYGGytcEALFGEALK----LSPSLREKIELQTKCgirlpsEARDNRV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 86 K-----KA--RESIEESLSNLKVEYLDLLLIHWPgSSLksenpankklrVESWNV---MCEMMAEGKLRSVGVSNFEICH 155
Cdd:COG4989 97 KhydtsKEhiIASVEGSLRRLGTDYLDLLLLHRP-DPL-----------MDPEEVaeaFDELKASGKVRHFGVSNFTPSQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 156 LEELKKDSNVVPAVNQVE----YHPHFHqDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEE-----PLIKELAQKYNVEI 226
Cdd:COG4989 165 FELLQSALDQPLVTNQIElsllHTDAFD-DGTLDYCQLNGITPMAWSPLAGGRLFGGFDEQfprlrAALDELAEKYGVSP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 17552492 227 PVLLLGF--AYCQGISVLPRTTNPEHVATNFKVTKLAITQED 266
Cdd:COG4989 244 EAIALAWllRHPAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
15-272 |
1.08e-25 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 102.63 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 15 GIGTWQVQKEEILRqVIDAGFKEGYRFIDTAQVYNN---EAKIGRILeKLLPAnglKREDIWITSKlapsnAGVKKA--- 88
Cdd:cd19092 15 RLADWGESAEELLS-LIEAALELGITTFDHADIYGGgkcEELFGEAL-ALNPG---LREKIEIQTK-----CGIRLGddp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 ---------------RESIEESLSNLKVEYLDLLLIHWPgsslkseNPAnkklrVESWNV---MCEMMAEGKLRSVGVSN 150
Cdd:cd19092 85 rpgrikhydtskehiLASVEGSLKRLGTDYLDLLLLHRP-------DPL-----MDPEEVaeaFDELVKSGKVRYFGVSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 151 FEICHLEELKKDSNVVPAVNQVE---YHPHFHQDDLVKYCNENNIHFQAYSSL-GSPTYRKQLSEEP----LIKELAQKY 222
Cdd:cd19092 153 FTPSQIELLQSYLDQPLVTNQIElslLHTEAIDDGTLDYCQLLDITPMAWSPLgGGRLFGGFDERFQrlraALEELAEEY 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 17552492 223 NVEIPVLLLGFAYCQGISVLP--RTTNPEHVATNFKVTKLAITQEDIDRLLA 272
Cdd:cd19092 233 GVTIEAIALAWLLRHPARIQPilGTTNPERIRSAVKALDIELTREEWYEIYE 284
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-192 |
1.91e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.75 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNN--MPLIGIGTW--QVQKEEILRQVIDAGFKEGYRFIDTAQVY-NNEAKIGRILEKLlpanglkREDIWIT 75
Cdd:COG1453 1 MQYRRLGKTGleVSVLGFGGMrlPRKDEEEAEALIRRAIDNGINYIDTARGYgDSEEFLGKALKGP-------RDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 76 SKLAPSNAGVKKARESIEESLSNLKVEYLDLLLIHwpgsSLKSENPANKKLR-VESWNVMCEMMAEGKLRSVGVSnfeiC 154
Cdd:COG1453 74 TKLPPWVRDPEDMRKDLEESLKRLQTDYIDLYLIH----GLNTEEDLEKVLKpGGALEALEKAKAEGKIRHIGFS----T 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 17552492 155 H--LEELKK--DSNVVPAVnQVEYHP--HFHQ--DDLVKYCNENNI 192
Cdd:COG1453 146 HgsLEVIKEaiDTGDFDFV-QLQYNYldQDNQagEEALEAAAEKGI 190
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
14-274 |
1.01e-24 |
|
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: 100.57 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQVQ--------KEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEkllpanGLKREDIWITSKLAPSN 82
Cdd:cd19083 14 IGLGTNAVGghnlypnlDEEEGKDLVREALDNGVNLLDTAFIYglgRSEELVGEVLK------EYNRNEVVIATKGAHKF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 83 AGVKKA--------RESIEESLSNLKVEYLDLLLIHWPgsslKSENPankklRVESWNVMCEMMAEGKLRSVGVSNFEIC 154
Cdd:cd19083 88 GGDGSVlnnspeflRSAVEKSLKRLNTDYIDLYYIHFP----DGETP-----KAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKKDSNVvpAVNQVEYH--PHFHQDDLVKYCNENNIHFQAYSSLGS---------------------------PTY 205
Cdd:cd19083 159 QLKEANKDGYV--DVLQGEYNllQREAEEDILPYCVENNISFIPYFPLASgllagkytkdtkfpdndlrndkplfkgERF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552492 206 RKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQ-GISVL-PRTTNPEHVATNFKVTKLAITQEDIDRLLALT 274
Cdd:cd19083 237 SENLDKVDKLKSIADEKGVTVAHLALAWYLTRpAIDVViPGAKRAEQVIDNLKALDVTLTEEEIAFIDALF 307
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
11-263 |
2.29e-24 |
|
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: 98.44 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQVQKEE-----ILRQVIDAGFkegyRFIDTAQVYN---NEAKIGRIL----EKLLPA--NGLKR--EDIWi 74
Cdd:cd19088 9 MRLTGPGIWGPPADReeaiaVLRRALELGV----NFIDTADSYGpdvNERLIAEALhpypDDVVIAtkGGLVRtgPGWW- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 75 tsklaPSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEIC 154
Cdd:cd19088 84 -----GPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFE---------EQLGALAELQDEGLIRHIGLSNVTVA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKKDSNVVpAVnQVEYHP-HFHQDDLVKYCNENNIHFQAYSSLGSptyRKQLSEEPLIKELAQKYNVEIPVLLLG- 232
Cdd:cd19088 150 QIEEARAIVRIV-SV-QNRYNLaNRDDEGVLDYCEAAGIAFIPWFPLGG---GDLAQPGGLLAEVAARLGATPAQVALAw 224
|
250 260 270
....*....|....*....|....*....|..
gi 17552492 233 -FAYCQGISVLPRTTNPEHVATNFKVTKLAIT 263
Cdd:cd19088 225 lLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-254 |
7.14e-24 |
|
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: 97.31 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV----------QKEEILRQVIDAGFkegyRFIDTAQVY-NNEAKIGRILEkllpanGLKREDIWITSKLAPSN 82
Cdd:cd19095 3 LGLGTSGIgrvwgvpseaEAARLLNTALDLGI----NLIDTAPAYgRSEERLGRALA------GLRRDDLFIATKVGTHG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 83 AGVKK--------ARESIEESLSNLKVEYLDLLLIHwpgsslkseNPANKKLRVESWNVMCEMMAEGKLRSVGVSnfeiC 154
Cdd:cd19095 73 EGGRDrkdfspaaIRASIERSLRRLGTDYIDLLQLH---------GPSDDELTGEVLETLEDLKAAGKVRYIGVS----G 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKK--DSNVVPAVnQVEYHPH-FHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEPLIKELAQKYNVEIPV--- 228
Cdd:cd19095 140 DGEELEAaiASGVFDVV-QLPYNVLdREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIgga 218
|
250 260 270
....*....|....*....|....*....|..
gi 17552492 229 ----LLLGFAYCQ-GI-SVLPRTTNPEHVATN 254
Cdd:cd19095 219 twaqAALRFVLSHpGVsSAIVGTTNPEHLEEN 250
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-273 |
7.17e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 98.13 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV-----------QKEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKLlpanglkREDIWITSKLA 79
Cdd:cd19102 4 IGLGTWAIggggwgggwgpQDDRDSIAAIRAALDLGINWIDTAAVYglgHSEEVVGRALKGL-------RDRPIVATKCG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 P-------SNAGVKKA--RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSN 150
Cdd:cd19102 77 LlwdeegrIRRSLKPAsiRAECEASLRRLGVDVIDLYQIHWPDPDEPIE---------EAWGALAELKEEGKVRAIGVSN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 151 FEIchlEELKKDSNVVP-AVNQVEY---HPHFHQdDLVKYCNENNIHFQAYSSLGS--------------------PTYR 206
Cdd:cd19102 148 FSV---DQMKRCQAIHPiASLQPPYsllRRGIEA-EILPFCAEHGIGVIVYSPMQSglltgkmtpervaslpaddwRRRS 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552492 207 KQLSEEPL---------IKELAQKYNVEIPVLLLGFAYCQ-GI-SVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19102 224 PFFQEPNLarnlalvdaLRPIAERHGRTVAQLAIAWVLRRpEVtSAIVGARRPDQIDETVGAADLRLTPEELAEIEAL 301
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-192 |
3.98e-23 |
|
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: 94.85 E-value: 3.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQ--------VQKEEILRqVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKllpanglKREDIWITSKLAPSN 82
Cdd:cd19086 6 IGFGTWGlggdwwgdVDDAEAIR-ALRAALDLGINFFDTADVYgdgHSERLLGKALKG-------RRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 83 AGVKKA---------RESIEESLSNLKVEYLDLLLIH-WPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSnfe 152
Cdd:cd19086 78 DGGPERpqdfspeyiREAVEASLKRLGTDYIDLYQLHnPPDEVLDND---------ELFEALEKLKQEGKIRAYGVS--- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 17552492 153 ICHLEELKK--DSNVVPAVnQVEYHPhFHQ---DDLVKYCNENNI 192
Cdd:cd19086 146 VGDPEEALAalRRGGIDVV-QVIYNL-LDQrpeEELFPLAEEHGV 188
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-273 |
1.10e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 95.09 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 10 NMPLIGIGTW----------QVQKEEI----LRQVIDAGFKEGYRFIDTAQVYNnEAKIGRILEKLLPAngLKREDIWIT 75
Cdd:cd19103 3 KLPKIALGTWswgsggaggdQVFGNHLdedtLKAVFDKAMAAGLNLWDTAAVYG-MGASEKILGEFLKR--YPREDYIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 76 SKLAPSNAGVK--KARESIEESLSNLKVEYLDLLLIHwpgsslkseNPANkklrVESWNV-MCEMMAEGKLRSVGVSNFe 152
Cdd:cd19103 80 TKFTPQIAGQSadPVADMLEGSLARLGTDYIDIYWIH---------NPAD----VERWTPeLIPLLKSGKVKHVGVSNH- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 153 icHLEELKKDSNV-------VPAVnQVEYHPHFH---QDDLVKYCNENNIHFQAYSSL-----------------GSP-- 203
Cdd:cd19103 146 --NLAEIKRANEIlakagvsLSAV-QNHYSLLYRsseEAGILDYCKENGITFFAYMVLeqgalsgkydtkhplpeGSGra 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552492 204 -TYRKQLSE----EPLIKELAQKYNVEIPVLLLGFAYCQGISVLPRTTNPEHVATNFKVTKLAITQEDIDRLLAL 273
Cdd:cd19103 223 eTYNPLLPQleelTAVMAEIGAKHGASIAQVAIAWAIAKGTTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
22-270 |
2.89e-22 |
|
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: 93.82 E-value: 2.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 22 QKEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKllpanglKREDIWITSKLAPS----------NAGVKKA 88
Cdd:cd19076 29 ADEEESIATLHRALELGVTFLDTADMYgpgTNEELLGKALKD-------RRDEVVIATKFGIVrdpgsgfrgvDGRPEYV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNfeiCHLEELKKDSNVVP- 167
Cdd:cd19076 102 RAACEASLKRLGTDVIDLYYQHRVDPNVPIE---------ETVGAMAELVEEGKVRYIGLSE---ASADTIRRAHAVHPi 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 168 -AVnQVEYHPhFHQD---DLVKYCNENNIHFQAYSSLG----------------------SPTYRK-------QLSEEpl 214
Cdd:cd19076 170 tAV-QSEYSL-WTRDiedEVLPTCRELGIGFVAYSPLGrgfltgaikspedlpeddfrrnNPRFQGenfdknlKLVEK-- 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 17552492 215 IKELAQKYNVEIPVLLLGFAYCQGISVL--PRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19076 246 LEAIAAEKGCTPAQLALAWVLAQGDDIVpiPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-192 |
3.75e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 92.16 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 12 PLIGIGTWQVQK------EEILRQVIDAGFkegyRFIDTAQVYNN-EAKIGRILEKllpanglKREDIWITSKLAPSNAg 84
Cdd:cd19100 12 SRLGFGGGPLGRlsqeeaAAIIRRALDLGI----NYFDTAPSYGDsEEKIGKALKG-------RRDKVFLATKTGARDY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 85 vKKARESIEESLSNLKVEYLDLLLIHwpgsSLKSENPANKKLRV-ESWNVMCEMMAEGKLRSVGVS--NFEIcHLEELKK 161
Cdd:cd19100 80 -EGAKRDLERSLKRLGTDYIDLYQLH----AVDTEEDLDQVFGPgGALEALLEAKEEGKIRFIGISghSPEV-LLRALET 153
|
170 180 190
....*....|....*....|....*....|....
gi 17552492 162 ---DSnVVPAVNQVEYHPHFHQDDLVKYCNENNI 192
Cdd:cd19100 154 gefDV-VLFPINPAGDHIDSFREELLPLAREKGV 186
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
14-200 |
1.92e-21 |
|
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: 91.60 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQV-------QKEEILRQVIDAGFKEGYRFIDTAQVYN---NEAKIGRILEKLLpanglKREDIWITSKLA---- 79
Cdd:cd19148 7 IALGTWAIggwmwggTDEKEAIETIHKALDLGINLIDTAPVYGfglSEEIVGKALKEYG-----KRDRVVIATKVGlewd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 -----PSNAGVKKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNFEIC 154
Cdd:cd19148 82 eggevVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIE---------ETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELKKdsnVVP-AVNQVEYHpHFHQD---DLVKYCNENNIHFQAYSSL 200
Cdd:cd19148 153 QMETFRK---VAPlHTVQPPYN-LFEREiekDVLPYARKHNIVTLAYGAL 198
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
30-267 |
4.85e-21 |
|
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: 90.97 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 30 VIDAGFKEGYRFIDTAQVY-NNEAKIGRILEKllpaNGLKREDIWITSKLA----------PSNAGVKKARESIEESLSN 98
Cdd:cd19144 39 VLDAAFELGCTFWDTADIYgDSEELIGRWFKQ----NPGKREKIFLATKFGieknvetgeySVDGSPEYVKKACETSLKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 99 LKVEYLDLLLIHwpgsSLKSENPANKKLRveswnVMCEMMAEGKLRSVGVSNfeiCHLEELKKDSNVVP--AVnQVEYHP 176
Cdd:cd19144 115 LGVDYIDLYYQH----RVDGKTPIEKTVA-----AMAELVQEGKIKHIGLSE---CSAETLRRAHAVHPiaAV-QIEYSP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 177 hFHQD------DLVKYCNENNIHFQAYSSLG---------SPT------YRKQL---SEEPL---------IKELAQKYN 223
Cdd:cd19144 182 -FSLDierpeiGVLDTCRELGVAIVAYSPLGrgfltgairSPDdfeegdFRRMAprfQAENFpknlelvdkIKAIAKKKN 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 17552492 224 VEIPVLLLGFAYCQG--ISVLPRTTNPEHVATNFKVTKLAITQEDI 267
Cdd:cd19144 261 VTAGQLTLAWLLAQGddIIPIPGTTKLKRLEENLGALKVKLTEEEE 306
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-234 |
4.25e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 87.20 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQ-------------VQKEEIlRQVIDAGFKEGYRFIDTAQVYNN-EAKIGRILEKLLPANglkrediwITSKLA 79
Cdd:cd19097 3 LALGTAQfgldygianksgkPSEKEA-KKILEYALKAGINTLDTAPAYGDsEKVLGKFLKRLDKFK--------IITKLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 80 PSNAGVKKA----RESIEESLSNLKVEYLDLLLIHWPgSSLKSENPankklrvESWNVMCEMMAEGKLRSVGVSnfeICH 155
Cdd:cd19097 74 PLKEDKKEDeaaiEASVEASLKRLKVDSLDGLLLHNP-DDLLKHGG-------KLVEALLELKKEGLIRKIGVS---VYS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 156 LEELKK--DSNVVPAVnQVEYHP---HFHQDDLVKYCNENNIHFQAYSSL----------GSPTYRKQLSeePLIK---E 217
Cdd:cd19097 143 PEELEKalESFKIDII-QLPFNIldqRFLKSGLLAKLKKKGIEIHARSVFlqglllmepdKLPAKFAPAK--PLLKklhE 219
|
250
....*....|....*..
gi 17552492 218 LAQKYNVEIPVLLLGFA 234
Cdd:cd19097 220 LAKKLGLSPLELALGFV 236
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-257 |
1.50e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 82.63 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKN--NMPLIGIGT--WQVQKEEILRQVIDAGFkegyRFIDTAQVY---NNEAKIGRILEkllpanGLKREDIW 73
Cdd:cd19105 1 MPYRTLGKTglKVSRLGFGGggLPRESPELLRRALDLGI----NYFDTAEGYgngNSEEIIGEALK------GLRRDKVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 74 ITSKLAPSNAGVKKA--RESIEESLSNLKVEYLDLLLIH---WPGSSLKSENPAnkklrveswNVMCEMMAEGKLRSVGV 148
Cdd:cd19105 71 LATKASPRLDKKDKAelLKSVEESLKRLQTDYIDIYQLHgvdTPEERLLNEELL---------EALEKLKKEGKVRFIGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 149 SnfeiCHleelkkdSNVVPAVN-----------QVEY---HPHFHQDDLVKYCNENNIHFQAYSSLGSPTYRKQLSEEPL 214
Cdd:cd19105 142 S----TH-------DNMAEVLQaaiesgwfdviMVAYnflNQPAELEEALAAAAEKGIGVVAMKTLAGGYLQPALLSVLK 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17552492 215 IKELaqkynvEIPVLLLGFA-YCQGIS-VLPRTTNPEHVATNFKV 257
Cdd:cd19105 211 AKGF------SLPQAALKWVlSNPRVDtVVPGMRNFAELEENLAA 249
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-270 |
4.94e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 82.26 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 11 MPLIGIGTWQV--------QKEEILRQvIDAGFKEGYRFIDTAQVYNN-EAKIGRILeKLLPANGLKREDIWITSKLAPS 81
Cdd:cd19101 2 ISRVINGMWQLsgghggirDEDAAVRA-MAAYVDAGLTTFDCADIYGPaEELIGEFR-KRLRRERDAADDVQIHTKWVPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 82 NA--GVKKA--RESIEESLSNLKVEYLDLLLIHWpgsslksENPANKKLrVESWNVMCEMMAEGKLRSVGVSNFEICHLE 157
Cdd:cd19101 80 PGelTMTRAyvEAAIDRSLKRLGVDRLDLVQFHW-------WDYSDPGY-LDAAKHLAELQEEGKIRHLGLTNFDTERLR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 158 ELKkdSNVVPAV-NQVEY-----HPhfhQDDLVKYCNENNIHFQAYSSLG----------------------SPTYRKQL 209
Cdd:cd19101 152 EIL--DAGVPIVsNQVQYslldrRP---ENGMAALCEDHGIKLLAYGTLAggllsekylgvpeptgpaletrSLQKYKLM 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17552492 210 SEE-----------PLIKELAQKYNVEIPVLLLGFAYCQ-GI-SVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19101 227 IDEwggwdlfqellRTLKAIADKHGVSIANVAVRWVLDQpGVaGVIVGARNSEHIDDNVRAFSFRLDDEDRAAI 300
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
14-265 |
6.24e-18 |
|
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: 81.87 E-value: 6.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTW-----QVqKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILekllpaNGLKREDIWITSKL-APSNAG 84
Cdd:cd19074 7 LSLGTWltfggQV-DDEDAKACVRKAYDLGINFFDTADVYAAgqaEEVLGKAL------KGWPRESYVISTKVfWPTGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 85 V-------KKARESIEESLSNLKVEYLDLLLIHWPgsslKSENPANKKLRveswnVMCEMMAEGKLRSVGVSNFEICHLE 157
Cdd:cd19074 80 PndrglsrKHIFESIHASLKRLQLDYVDIYYCHRY----DPETPLEETVR-----AMDDLIRQGKILYWGTSEWSAEQIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 158 E---LKKDSNVV-PAVNQVEYHPHF--HQDDLVKYCNENNIHFQAYSSL-----------GSP----------------- 203
Cdd:cd19074 151 EahdLARQFGLIpPVVEQPQYNMLWreIEEEVIPLCEKNGIGLVVWSPLaqglltgkyrdGIPppsrsratdednrdkkr 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552492 204 --TYRKQLSEEPLIKELAQKYNVEIPVLLLgfAYC----QGISVLPRTTNPEHVATNFKVTKLAITQE 265
Cdd:cd19074 231 rlLTDENLEKVKKLKPIADELGLTLAQLAL--AWClrnpAVSSAIIGASRPEQLEENVKASGVKLSPE 296
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
24-192 |
1.55e-17 |
|
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: 79.91 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 24 EEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLlpanglKREDIWITSKLAPSNagVKKA---RESIEESLS 97
Cdd:cd19096 20 EEKAIEMIRYAIDAGINYFDTAYGYGGgksEEILGEALKEG------PREKFYLATKLPPWS--VKSAedfRRILEESLK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 98 NLKVEYLDLLLIHWPGSslkSENPAnKKLRVESWNVMCEMMAEGKLRSVGVSnFeicH--LEELKK--DSNVVPAVnQVE 173
Cdd:cd19096 92 RLGVDYIDFYLLHGLNS---PEWLE-KARKGGLLEFLEKAKKEGLIRHIGFS-F---HdsPELLKEilDSYDFDFV-QLQ 162
|
170 180
....*....|....*....|...
gi 17552492 174 YH----PHFHQDDLVKYCNENNI 192
Cdd:cd19096 163 YNyldqENQAGRPGIEYAAKKGM 185
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
25-267 |
2.95e-17 |
|
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: 79.97 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 25 EILRQVIDAGfkegYRFIDTAQVY---NNEAKIGrilEKLLPanglKREDIWITSKLAPSNAGVKKA-----------RE 90
Cdd:cd19078 29 ELIRKAVELG----ITFFDTAEVYgpyTNEELVG---EALKP----FRDQVVIATKFGFKIDGGKPGplgldsrpehiRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 SIEESLSNLKVEYLDLLLIHWPGSSLKSENPAnkklrveswNVMCEMMAEGKLRSVGVSNfeiCHLEELKKDSNVVP--A 168
Cdd:cd19078 98 AVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVA---------GTMKELIKEGKIRHWGLSE---AGVETIRRAHAVCPvtA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 169 VnQVEYHPHF--HQDDLVKYCNENNIHFQAYSSLG---------------SPTYRK---QLSEE---------PLIKELA 219
Cdd:cd19078 166 V-QSEYSMMWrePEKEVLPTLEELGIGFVPFSPLGkgfltgkidentkfdEGDDRAslpRFTPEaleanqalvDLLKEFA 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 17552492 220 QKYNVEIPVLLLGFAYCQG--ISVLPRTTNPEHVATNFKVTKLAITQEDI 267
Cdd:cd19078 245 EEKGATPAQIALAWLLAKKpwIVPIPGTTKLSRLEENIGAADIELTPEEL 294
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
14-202 |
8.86e-17 |
|
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: 78.75 E-value: 8.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQVQ----KEEILRQVIDAGFKEGYRFIDTAQVYNNEAKigrilEKLLPANGLKREDIWITSKLAPSNAGVKKA- 88
Cdd:cd19075 5 LGTMTFGSQgrftTAEAAAELLDAFLERGHTEIDTARVYPDGTS-----EELLGELGLGERGFKIDTKANPGVGGGLSPe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 89 --RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNF------EICHLeeLK 160
Cdd:cd19075 80 nvRKQLETSLKRLKVDKVDVFYLHAPDRSTPLE---------ETLAAIDELYKEGKFKEFGLSNYsawevaEIVEI--CK 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 17552492 161 KDSNVVPAVNQVEYHP--HFHQDDLVKYCNENNIHFQAYSSLGS 202
Cdd:cd19075 149 ENGWVLPTVYQGMYNAitRQVETELFPCLRKLGIRFYAYSPLAG 192
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
14-270 |
1.38e-16 |
|
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: 78.02 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGT----WQVQKE---EILRQVIDAGFkegyRFIDTAQVYNN----------EAKIGRILEKLLpanglKREDIWITS 76
Cdd:cd19081 12 LCLGTmvfgWTADEEtsfALLDAFVDAGG----NFIDTADVYSAwvpgnaggesETIIGRWLKSRG-----KRDRVVIAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 77 KLA----PSNAGVKKA--RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSN 150
Cdd:cd19081 83 KVGfpmgPNGPGLSRKhiRRAVEASLRRLQTDYIDLYQAHWDDPATPLE---------ETLGALNDLIRQGKVRYIGASN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 151 FEICHLEE---LKKDSNVVPAVN-QVEY---HPHFHQDDLVKYCNENNIHFQAYSSLGS--------------------P 203
Cdd:cd19081 154 YSAWRLQEaleLSRQHGLPRYVSlQPEYnlvDRESFEGELLPLCREEGIGVIPYSPLAGgfltgkyrseadlpgstrrgE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17552492 204 TYRKQLSEEPL-----IKELAQKYNVEIP-VLLLGFAYCQGI-SVLPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19081 234 AAKRYLNERGLrildaLDEVAAEHGATPAqVALAWLLARPGVtAPIAGARTVEQLEDLLAAAGLRLTDEEVARL 307
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
14-235 |
2.21e-16 |
|
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: 77.61 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGT--W--QVQKEEILRQvIDAGFKEGYRFIDTAQVY------NNEAKIGRILEKLLPANGlKREDIWITSKLAPSNA 83
Cdd:cd19094 4 ICLGTmtWgeQNTEAEAHEQ-LDYAFDEGVNFIDTAEMYpvppspETQGRTEEIIGSWLKKKG-NRDKVVLATKVAGPGE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 84 GVKKAR------------ESIEESLSNLKVEYLDLLLIHWP----------GSSLKSENPANKKLRvESWNVMCEMMAEG 141
Cdd:cd19094 82 GITWPRgggtrldrenirEAVEGSLKRLGTDYIDLYQLHWPdrytplfgggYYTEPSEEEDSVSFE-EQLEALGELVKAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 142 KLRSVGVSN---FEICHLEELKKDSNVVPAVN-QVEY---HPHFhQDDLVKYCNENNIHFQAYSSLG------------- 201
Cdd:cd19094 161 KIRHIGLSNetpWGVMKFLELAEQLGLPRIVSiQNPYsllNRNF-EEGLAEACHRENVGLLAYSPLAggvltgkyldgaa 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 17552492 202 -------------SPTYRKQLSEEPLIK--ELAQKYNVEIPVLLLGFAY 235
Cdd:cd19094 240 rpeggrlnlfpgyMARYRSPQALEAVAEyvKLARKHGLSPAQLALAWVR 288
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-256 |
4.12e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 76.97 E-value: 4.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTWQVQKEEILRQV----IDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLLPANGLKREDIWITSK--------- 77
Cdd:cd19099 6 LGLGTYRGDSDDETDEEyreaLKAALDSGINVIDTAINYRGgrsERLIGKALRELIEKGGIKRDEVVIVTKagyipgdgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 78 -----LAPSNAGVKKA-------------------RESIEESLSNLKVEYLDLLLIHWPGSSL--KSENPANKKLRvESW 131
Cdd:cd19099 86 eplrpLKYLEEKLGRGlidvadsaglrhcispaylEDQIERSLKRLGLDTIDLYLLHNPEEQLleLGEEEFYDRLE-EAF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 132 NVMCEMMAEGKLRSVGVSNFEI-----CHLEELKKDSNVVPAVNQVEYHPHFH-----------------------QDDL 183
Cdd:cd19099 165 EALEEAVAEGKIRYYGISTWDGfrappALPGHLSLEKLVAAAEEVGGDNHHFKviqlplnllepealtekntvkgeALSL 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552492 184 VKYCNENNIHFQAYSSLGSPtyrKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQ--GISVLPRTTNPEHVATNFK 256
Cdd:cd19099 245 LEAAKELGLGVIASRPLNQG---QLLGELRLADLLALPGGATLAQRALQFARSTpgVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-256 |
4.99e-15 |
|
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: 73.36 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGT----WQVQKEE---ILRQVIDAGFkegyRFIDTAQVYNNEAKIG---RILEKLLPANGlKREDIWITSKLAPSNA 83
Cdd:cd19082 3 IVLGTadfgTRIDEEEafaLLDAFVELGG----NFIDTARVYGDWVERGaseRVIGEWLKSRG-NRDKVVIATKGGHPDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 84 GVKKA--------RESIEESLSNLKVEYLDLLLIHwpgsslkSENPAnkkLRVESW-NVMCEMMAEGKLRSVGVSNFEIC 154
Cdd:cd19082 78 EDMSRsrlspediRADLEESLERLGTDYIDLYFLH-------RDDPS---VPVGEIvDTLNELVRAGKIRAFGASNWSTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 155 HLEELK---KDSNVVP-AVNQVEY------HPH-------FHQDDLVKYCNENNIHFQAYSSLG---------------S 202
Cdd:cd19082 148 RIAEANayaKAHGLPGfAASSPQWslarpnEPPwpgptlvAMDEEMRAWHEENQLPVFAYSSQArgffskraaggaeddS 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552492 203 PTYRKQLSEEPL-----IKELAQKYNVEIPVLLLGFAYCQGISVLP--RTTNPEHVATNFK 256
Cdd:cd19082 228 ELRRVYYSEENFerlerAKELAEEKGVSPTQIALAYVLNQPFPTVPiiGPRTPEQLRDSLA 288
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
29-265 |
3.63e-14 |
|
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: 70.66 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 29 QVIDAGFKEGYRFIDTAQVYNN-EAKIGRILekllpaNGLKREDIWITSKLAPSNAG-----VKKARESIEESLSNLKVE 102
Cdd:cd19090 24 ATIRAALDLGINYIDTAPAYGDsEERLGLAL------AELPREPLVLSTKVGRLPEDtadysADRVRRSVEESLERLGRD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 103 YLDLLLIHWPGsslksenpankklRVESWNVMC---------EMMAEGKLRSVGVSNFEIchlEELKK--DSNVVPAVnq 171
Cdd:cd19090 98 RIDLLMIHDPE-------------RVPWVDILApggaleallELKEEGLIKHIGLGGGPP---DLLRRaiETGDFDVV-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 172 veyHPHFH--------QDDLVKYCNENNIHFQAYSSLGS------------PTYRkQLSEEPL-----IKELAQKYNVEI 226
Cdd:cd19090 160 ---LTANRytlldqsaADELLPAAARHGVGVINASPLGMgllagrppervrYTYR-WLSPELLdrakrLYELCDEHGVPL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 17552492 227 PVLLLGFayCQGI----SVLPRTTNPEHVATNFKVTKLAITQE 265
Cdd:cd19090 236 PALALRF--LLRDprisTVLVGASSPEELEQNVAAAEGPLPEE 276
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
17-270 |
7.26e-14 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 70.31 E-value: 7.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 17 GTWQVQKEEIlRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLLPanglkREDIWITSKL------APSNAGVKK 87
Cdd:cd19079 28 RPWVLDEEES-RPIIKRALDLGINFFDTANVYSGgasEEILGRALKEFAP-----RDEVVIATKVyfpmgdGPNGRGLSR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 A--RESIEESLSNLKVEYLDLLLIHWpgssLKSENPankklrveswnvMCEMMA-------EGKLRSVGVSNF------E 152
Cdd:cd19079 102 KhiMAEVDASLKRLGTDYIDLYQIHR----WDYETP------------IEETLEalhdvvkSGKVRYIGASSMyawqfaK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 153 ICHLEELKKDSNVVPAVNQveYHPHFHQD--DLVKYCNENNIHFQAYSSLGS-------------------PTYRKQLSE 211
Cdd:cd19079 166 ALHLAEKNGWTKFVSMQNH--YNLLYREEerEMIPLCEEEGIGVIPWSPLARgrlarpwgdtterrrsttdTAKLKYDYF 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552492 212 EPL-------IKELAQKYNVEIPVLLLGFAYCQGISVLP--RTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19079 244 TEAdkeivdrVEEVAKERGVSMAQVALAWLLSKPGVTAPivGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
24-151 |
1.22e-13 |
|
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: 69.52 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 24 EEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpanglKREDIWITSKL-APSNAGV-------KKARESI 92
Cdd:cd19087 29 EETSFAIMDRALDAGINFFDTADVYGGgrsEEIIGRWIAG-------RRDDIVLATKVfGPMGDDPndrglsrRHIRRAV 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17552492 93 EESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNF 151
Cdd:cd19087 102 EASLRRLQTDYIDLYQMHHFDRDTPLE---------ETLRALDDLVRQGKIRYIGVSNF 151
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
14-270 |
2.44e-12 |
|
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: 65.72 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIG----TW---QVQKEEILrQVIDAGFKEGYRFIDTAQVY------NNEAKIGRILEKLlPANglkREDI-------W 73
Cdd:cd19077 8 IGLGlmglTWrpnPTPDEEAF-ETMKAALDAGSNLWNGGEFYgppdphANLKLLARFFRKY-PEY---ADKVvlsvkggL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 74 ITSKLAP--SNAGVKKareSIEESLSNLK-VEYLDLLlihwpgsslkseNPAnkklRV-------ESWNVMCEMMAEGKL 143
Cdd:cd19077 83 DPDTLRPdgSPEAVRK---SIENILRALGgTKKIDIF------------EPA----RVdpnvpieETIKALKELVKEGKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 144 RSVGVSNfeiCHLEELKKDSNVVP-AVNQVEYHP---HFHQDDLVKYCNENNIHFQAYSSLG---------SP------- 203
Cdd:cd19077 144 RGIGLSE---VSAETIRRAHAVHPiAAVEVEYSLfsrEIEENGVLETCAELGIPIIAYSPLGrglltgrikSLadipegd 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 204 -----------TYRKQLSEEPLIKELAQKYNVEIPVLLLGFAYCQG---ISVLPRTTNPEHVATNFKVTKLAITQEDIDR 269
Cdd:cd19077 221 frrhldrfngeNFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSgpkIIPIPGSTTLERVEENLKAANVELTDEELKE 300
|
.
gi 17552492 270 L 270
Cdd:cd19077 301 I 301
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-181 |
4.24e-12 |
|
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: 65.56 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNNM--PLIGIGTWQV----QKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpaNGLKRED 71
Cdd:cd19142 1 LKYRNLGKSGLrvSNVGLGTWSTfstaISEEQAEEIVTLAYENGINYFDTSDAFTSgqaETELGRILKK----KGWKRSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 72 IWITSKL----APSNAGV--KKARESIEESLSNLKVEYLDLLLIHwpgsSLKSENPANKKLRveswnVMCEMMAEGKLRS 145
Cdd:cd19142 77 YIVSTKIywsyGSEERGLsrKHIIESVRASLRRLQLDYIDIVIIH----KADPMCPMEEVVR-----AMSYLIDNGLIMY 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 17552492 146 VGVSNFEICHLEEL----KKDSNVVPAVNQVEYHPhFHQD 181
Cdd:cd19142 148 WGTSRWSPVEIMEAfsiaRQFNCPTPICEQSEYHM-FCRE 186
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-271 |
5.53e-10 |
|
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: 59.29 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNNMPL--IGIGTW-----QVQkEEILRQVIDAGFKEGYRFIDTAQVYnNEAKIGRILEKLLPANGLKREDIW 73
Cdd:cd19159 1 MKYRNLGKSGLRVscLGLGTWvtfggQIS-DEVAERLMTIAYESGVNLFDTAEVY-AAGKAEVILGSIIKKKGWRRSSLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 74 ITSKL-----APSNAGVKKAR--ESIEESLSNLKVEYLDLLLIHWPGSSlkseNPANKKLRVESWNVMCEM-MAEGKLRS 145
Cdd:cd19159 79 ITTKLywggkAETERGLSRKHiiEGLKGSLQRLQLEYVDVVFANRPDSN----TPMEEIVRAMTHVINQGMaMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 146 vgvSNFEICHLEELKKDSNVVPAV-NQVEYH-----------PHFHQDDLV---------------KYcnENNIHFQAYS 198
Cdd:cd19159 155 ---SAMEIMEAYSVARQFNMIPPVcEQAEYHlfqrekvevqlPELYHKIGVgamtwsplacgiisgKY--GNGVPESSRA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 199 SLGSPTYRKQ--LSEE-----PLIKEL---AQKYNVEIPvlLLGFAYC---QGI-SVLPRTTNPEHVATNFKVTKL---- 260
Cdd:cd19159 230 SLKCYQWLKEriVSEEgrkqqNKLKDLspiAERLGCTLP--QLAVAWClrnEGVsSVLLGSSTPEQLIENLGAIQVlpkm 307
|
330
....*....|..
gi 17552492 261 -AITQEDIDRLL 271
Cdd:cd19159 308 tSHVVNEIDNIL 319
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
19-151 |
6.90e-10 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 58.78 E-value: 6.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 19 WQVQKEEILRQV---IDAGFKegyrFIDTAQVYNN-EAKIgrILEKLLPAnglKREDIWITSKL------APSNAGVKKA 88
Cdd:cd19091 34 GGVDQEEADRLVdiaLDAGIN----FFDTADVYSEgESEE--ILGKALKG---RRDDVLIATKVrgrmgeGPNDVGLSRH 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552492 89 R--ESIEESLSNLKVEYLDLLLIHWPgsslKSENPANKKLRveswnVMCEMMAEGKLRSVGVSNF 151
Cdd:cd19091 105 HiiRAVEASLKRLGTDYIDLYQLHGF----DALTPLEETLR-----ALDDLVRQGKVRYIGVSNF 160
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-265 |
7.42e-10 |
|
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: 58.33 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNNM--PLIGIGT-------WQVQKEEILRqVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEkllpanGLK 68
Cdd:cd19163 1 MKYRKLGKTGLkvSKLGFGAsplggvfGPVDEEEAIR-TVHEALDSGINYIDTAPWYGQgrsETVLGKALK------GIP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 69 REDIWITSKLAPSNAGV--------KKARESIEESLSNLKVEYLDLLLIHWP--GSSLK---SEN-PANKKLRveswnvm 134
Cdd:cd19163 74 RDSYYLATKVGRYGLDPdkmfdfsaERITKSVEESLKRLGLDYIDIIQVHDIefAPSLDqilNETlPALQKLK------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 135 cemmAEGKLRSVGVSNFEICHLEELKKDSNVvpAVNQVEYHPHFH-QD----DLVKYCNENNIHFQAYS--SLGSPTYRK 207
Cdd:cd19163 147 ----EEGKVRFIGITGYPLDVLKEVLERSPV--KIDTVLSYCHYTlNDtsllELLPFFKEKGVGVINASplSMGLLTERG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 208 QLSEEPL---IKELA-------QKYNVEIPVLLLGFAYCQ--GISVLPRTTNPEHVATNFKVTKLAITQE 265
Cdd:cd19163 221 PPDWHPAspeIKEACakaaaycKSRGVDISKLALQFALSNpdIATTLVGTASPENLRKNLEAAEEPLDAH 290
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
12-149 |
1.24e-09 |
|
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: 57.75 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 12 PLIGIGTWQV-----QKEEILRQVIDAGFKEGYRFIDTAQVYN---NEAKIGRILEkllpanGLKREDIWITSKL----- 78
Cdd:cd19162 1 PRLGLGAASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYGlglSERRLGAALA------RHPRAEYVVSTKVgrlle 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 79 ---APSNAGVKKA--------RESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklRVESWNVMCEMMAEGKLRSVG 147
Cdd:cd19162 75 pgaAGRPAGADRRfdfsadgiRRSIEASLERLGLDRLDLVFLHDPDRHLLQA-------LTDAFPALEELRAEGVVGAIG 147
|
..
gi 17552492 148 VS 149
Cdd:cd19162 148 VG 149
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-110 |
4.65e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 56.12 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 17 GTWQVQKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLlpanglkREDIWITSK--LAPSNAG--VKKAR 89
Cdd:cd19104 24 GLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDgksEENLGRALKGL-------PAGPYITTKvrLDPDDLGdiGGQIE 96
|
90 100
....*....|....*....|.
gi 17552492 90 ESIEESLSNLKVEYLDLLLIH 110
Cdd:cd19104 97 RSVEKSLKRLKRDSVDLLQLH 117
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
31-150 |
1.69e-08 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 54.86 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 31 IDAGFKEGYRFIDTAQVYN----------NEAKIGRILEKllpaNGlKREDIWITSKLA-PS---NAGV--------KKA 88
Cdd:PRK10625 36 LDYAVAQGINLIDVAEMYPvpprpetqglTETYIGNWLAK----RG-SREKLIIASKVSgPSrnnDKGIrpnqaldrKNI 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552492 89 RESIEESLSNLKVEYLDLLLIHWP----------GSSLKSENPANKKLrvESWNVMCEMMAEGKLRSVGVSN 150
Cdd:PRK10625 111 REALHDSLKRLQTDYLDLYQVHWPqrptncfgklGYSWTDSAPAVSLL--ETLDALAEQQRAGKIRYIGVSN 180
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
22-256 |
8.98e-08 |
|
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: 52.23 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 22 QKEEILRQVIDAGFkegyRFIDTAQVYNN--------EA-------------KIGRILEKLLPANGLKREDIWITSKLAP 80
Cdd:cd19152 21 EAKATLVAAWDLGI----RYFDTAPWYGAglseerlgAAlrelgredyvistKVGRLLVPLQEVEPTFEPGFWNPLPFDA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 81 ----SNAGVkkaRESIEESLSNLKVEYLDLLLIHWPGSSLKSENPANKK--LRVESWNVMCEMMAEGKLRSVGV-SNF-E 152
Cdd:cd19152 97 vfdySYDGI---LRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFaqAIKGAFRALEELREEGVIKAIGLgVNDwE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 153 ICH--LEELKKDSnVVPAVNqveYHP--HFHQDDLVKYCNENNIHFQ---AYSS---LGSPTYR----KQLSEEPL---- 214
Cdd:cd19152 174 VILriLEEADLDW-VMLAGR---YTLldHSAARELLPECEKRGVKVVnagPFNSgflAGGDNFDyyeyGPAPPELIarrd 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 17552492 215 -IKELAQKYNVEIPVLLLGFAYC--QGISVLPRTTNPEHVATNFK 256
Cdd:cd19152 250 rIEALCEQHGVSLAAAALQFALAppAVASVAPGASSPERVEENVA 294
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
15-151 |
9.31e-08 |
|
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: 52.22 E-value: 9.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 15 GIGTWQVQKEEILRQVIDAGfkeGYrFIDTAQVYNN---EAKIGRILEKllpanglKREDIWITSKLAPS------NAG- 84
Cdd:cd19080 25 GWGADREEARAMFDAYVEAG---GN-FIDTANNYTNgtsERLLGEFIAG-------NRDRIVLATKYTMNrrpgdpNAGg 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 85 --VKKARESIEESLSNLKVEYLDLLLIH-WPGSSlksenPANKKLRveswnVMCEMMAEGKLRSVGVSNF 151
Cdd:cd19080 94 nhRKNLRRSVEASLRRLQTDYIDLLYVHaWDFTT-----PVEEVMR-----ALDDLVRAGKVLYVGISDT 153
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
14-175 |
1.15e-07 |
|
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: 52.06 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTW-----QVQkEEILRQVIDAGFKEGYRFIDTAQVYNNEaKIGRILEKLLPANGLKREDIWITSKL-----APSNA 83
Cdd:cd19141 15 LGLGTWvtfgsQIS-DEVAEELVTLAYENGINLFDTAEVYAAG-KAEIVLGKILKKKGWRRSSYVITTKIfwggkAETER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 84 GV--KKARESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNF---EICHLEE 158
Cdd:cd19141 93 GLsrKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME---------EIVRAFTHVINQGMAMYWGTSRWsamEIMEAYS 163
|
170
....*....|....*...
gi 17552492 159 LKKDSNVV-PAVNQVEYH 175
Cdd:cd19141 164 VARQFNLIpPIVEQAEYH 181
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-158 |
1.26e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 51.95 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 24 EEILRQVIDAGFKEGYRFIDTAQVYN----------NEAKIGRILEkllpANGlKREDIWITSKLA------------PS 81
Cdd:cd19752 16 EETSFAILDRYVAAGGNFLDTANNYAfwteggvggeSERLIGRWLK----DRG-NRDDVVIATKVGagprdpdggpesPE 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17552492 82 NAGVKKARESIEESLSNLKVEYLDLLLIHW--PGSSLKsenpankklrvESWNVMCEMMAEGKLRSVGVSNFEICHLEE 158
Cdd:cd19752 91 GLSAETIEQEIDKSLRRLGTDYIDLYYAHVddRDTPLE-----------ETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-175 |
2.17e-07 |
|
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: 51.14 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 1 MEHREYVKNNMPL--IGIGTW-----QVQkEEILRQVIDAGFKEGYRFIDTAQVYNNeAKIGRILEKLLPANGLKREDIW 73
Cdd:cd19160 3 MKYRNLGKSGLRVscLGLGTWvtfgsQIS-DETAEDLLTVAYEHGVNLFDTAEVYAA-GKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 74 ITSKL-----APSNAGVKKAR--ESIEESLSNLKVEYLDLLLihwpGSSLKSENPANKKLRveswnVMCEMMAEGKLRSV 146
Cdd:cd19160 81 VTTKIywggqAETERGLSRKHiiEGLRGSLDRLQLEYVDIVF----ANRSDPNSPMEEIVR-----AMTYVINQGMAMYW 151
|
170 180 190
....*....|....*....|....*....|...
gi 17552492 147 GVSNF---EICHLEELKKDSNVVPAV-NQVEYH 175
Cdd:cd19160 152 GTSRWsamEIMEAYSVARQFNLIPPVcEQAEYH 184
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
14-175 |
2.82e-07 |
|
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: 50.85 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 14 IGIGTW-----QVQkEEILRQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEKllpaNGLKREDIWITSKL-----AP 80
Cdd:cd19158 16 LGLGTWvtfggQIT-DEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKK----KGWRRSSLVITTKIfwggkAE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 81 SNAGVKKAR--ESIEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSNF---EICH 155
Cdd:cd19158 91 TERGLSRKHiiEGLKASLERLQLEYVDVVFANRPDPNTPME---------ETVRAMTHVINQGMAMYWGTSRWssmEIME 161
|
170 180
....*....|....*....|.
gi 17552492 156 LEELKKDSNVVPAV-NQVEYH 175
Cdd:cd19158 162 AYSVARQFNLIPPIcEQAEYH 182
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
15-270 |
4.21e-07 |
|
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: 50.51 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 15 GIGTWQVQKEEIlrQVIDAGFKEGYRFIDTAQVY---NNEAKIGRILEkllpanGLKREDIWITSKLAPSNAGVKK---- 87
Cdd:cd19145 25 DYGAPKPEEEGI--ALIHHAFNSGVTFLDTSDIYgpnTNEVLLGKALK------DGPREKVQLATKFGIHEIGGSGvevr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 88 -----ARESIEESLSNLKVEYLDLLLIHWPGSSLKSENP--ANKKLrVEswnvmcemmaEGKLRSVGVSnfEICHlEELK 160
Cdd:cd19145 97 gdpayVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITmgELKKL-VE----------EGKIKYIGLS--EASA-DTIR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 161 KDSNVVP--AVnQVEYH--PHFHQDDLVKYCNENNIHFQAYSSLG---------------SPTYRKQL---SEEPL---- 214
Cdd:cd19145 163 RAHAVHPitAV-QLEWSlwTRDIEEEIIPTCRELGIGIVPYSPLGrgffagkakleelleNSDVRKSHprfQGENLeknk 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17552492 215 -----IKELAQKYNVEIPVLLLGFAYCQGISV--LPRTTNPEHVATNFKVTKLAITQEDIDRL 270
Cdd:cd19145 242 vlyerVEALAKKKGCTPAQLALAWVLHQGEDVvpIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
17-112 |
4.90e-07 |
|
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: 50.29 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 17 GTW-----QVqKEEILRQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKLlpanGLKREDIWITSKL-------APS 81
Cdd:cd19143 19 GSWvtfgnQV-DVDEAKECMKAAYDAGVNFFDNAEVYANgqsEEIMGQAIKEL----GWPRSDYVVSTKIfwggggpPPN 93
|
90 100 110
....*....|....*....|....*....|...
gi 17552492 82 NAGV--KKARESIEESLSNLKVEYLDLLLIHWP 112
Cdd:cd19143 94 DRGLsrKHIVEGTKASLKRLQLDYVDLVFCHRP 126
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
12-200 |
2.10e-06 |
|
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: 48.02 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 12 PLIGIGTWQ----VQKEEILRQVIDAGFKEGYRFIDTAqvyNN--------EAKIGRILEKLLPAnglKREDIWITSK-- 77
Cdd:cd19089 12 PAISLGLWHnfgdYTSPEEARELLRTAFDLGITHFDLA---NNygpppgsaEENFGRILKRDLRP---YRDELVISTKag 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 78 --LAPS---NAGVKK-ARESIEESLSNLKVEYLDLLLIHWPGSS--LKsENPANKKLRVESwnvmcemmaeGKLRSVGVS 149
Cdd:cd19089 86 ygMWPGpygDGGSRKyLLASLDQSLKRMGLDYVDIFYHHRYDPDtpLE-ETMTALADAVRS----------GKALYVGIS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 17552492 150 NFEICHLEELKK---DSNVVPAVNQVEYHpHFHQ---DDLVKYCNENNIHFQAYSSL 200
Cdd:cd19089 155 NYPGAKARRAIAllrELGVPLIIHQPRYS-LLDRwaeDGLLEVLEEAGIGFIAFSPL 210
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
24-186 |
2.63e-06 |
|
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: 48.04 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 24 EEILRQVIDAGFkegyRFIDTAQVY-NNEAKIGRILEKLlpANGLKREDIWITSK---LAP-----SNAGVkkaRESIEE 94
Cdd:cd19164 37 VDIVRRALELGI----RAFDTSPYYgPSEIILGRALKAL--RDEFPRDTYFIITKvgrYGPddfdySPEWI---RASVER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 95 SLSNLKVEYLDLLLIHwpgsslksenpankklRVE------SWNVMCEMM---AEGKLRSVGVSNF------EICHL--E 157
Cdd:cd19164 108 SLRRLHTDYLDLVYLH----------------DVEfvadeeVLEALKELFklkDEGKIRNVGISGYplpvllRLAELarT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 17552492 158 ELKK--DS----------NVVPAvnqvEYHPHFHQDDLVKY 186
Cdd:cd19164 172 TAGRplDAvlsychytlqNTTLL----AYIPKFLAAAGVKV 208
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
24-167 |
4.30e-06 |
|
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: 47.14 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 24 EEILRQVIDAGFKEGYRFIDTAQVYNNEAKiGRILEKLLPANGLKREDIWITSKLAPSNAG-----VKKARESIEESLSN 98
Cdd:cd19153 32 QDEAVAIVAEAFAAGINHFDTSPYYGAESS-EAVLGKALAALQVPRSSYTVATKVGRYRDSefdysAERVRASVATSLER 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17552492 99 LKVEYLDLLLIHwpgsslKSENPANKKLRVESWNVMCEMMAEGKLRSVGVSNFEICHLEELKKDSNVVP 167
Cdd:cd19153 111 LHTTYLDVVYLH------DIEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS 173
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
28-154 |
2.32e-05 |
|
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: 45.01 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 28 RQVIDAGFKEGYRFIDTAQVYNN---EAKIGRILEKllpangLKREDIWITSK----LAPSNAGVKKARE---------- 90
Cdd:cd19161 23 DATLDAAWDSGIRYFDTAPMYGHglaEHRLGDFLRE------KPRDEFVLSTKvgrlLKPAREGSVPDPNgfvdplpfei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 91 -----------SIEESLSNLKVEYLDLLLIH-----WPGSslKSENPANKKLRVESWNVMCEMMAEGKLRSV--GVSNFE 152
Cdd:cd19161 97 vydysydgimrSFEDSLQRLGLNRIDILYVHdigvyTHGD--RKERHHFAQLMSGGFKALEELKKAGVIKAFglGVNEVQ 174
|
..
gi 17552492 153 IC 154
Cdd:cd19161 175 IC 176
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
23-110 |
4.54e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 40.92 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 23 KEEILRQVIDAGFKEGYRFIDTAQVYNNEAKiGRILEKLLPANGLKREDIWITSKLAPSNAG----VKKARESIEESLSN 98
Cdd:PLN02587 29 SEEDAIASVREAFRLGINFFDTSPYYGGTLS-EKVLGKALKALGIPREKYVVSTKCGRYGEGfdfsAERVTKSVDESLAR 107
|
90
....*....|..
gi 17552492 99 LKVEYLDLLLIH 110
Cdd:PLN02587 108 LQLDYVDILHCH 119
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
30-150 |
5.36e-04 |
|
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: 40.87 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552492 30 VIDAGFKEGYRFIDTAQVYNNEAK---IGRILEKllPANglkREDIWITSKLA---------------PSNaGVKKARES 91
Cdd:cd19146 40 LLDAFYEQGGNFIDTANNYQGEESerwVGEWMAS--RGN---RDEMVLATKYTtgyrrggpikiksnyQGN-HAKSLRLS 113
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 17552492 92 IEESLSNLKVEYLDLLLIHWPGSSLKSEnpankklrvESWNVMCEMMAEGKLRSVGVSN 150
Cdd:cd19146 114 VEASLKKLQTSYIDILYVHWWDYTTSIP---------ELMQSLNHLVAAGKVLYLGVSD 163
|
|
| |
