|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
22-314 |
7.56e-176 |
|
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: 489.37 E-value: 7.56e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIA 100
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGpVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRDSYYLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 101 TKVARYELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYP 180
Cdd:cd19163 81 TKVGRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQILNETLPALQKLKEEGKVRFIGITGYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 181 ISVLKEFLTRTAGRLDTVLTYARYTLTDETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQPWHPASDEQKAIARKASE 260
Cdd:cd19163 161 LDVLKEVLERSPVKIDTVLSYCHYTLNDTSLLELLPFFKEKGVGVINASPLSMGLLTERGPPDWHPASPEIKEACAKAAA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 66772279 261 VCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSDKEQE 314
Cdd:cd19163 241 YCKSRGVDISKLALQFALS-NPDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
24-321 |
8.29e-95 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 284.36 E-value: 8.29e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFGGGALCANYGFDLEE-GIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALK--DVPRESYYIA 100
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGASPLGSVFGPVSEEdAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKalGIPREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 101 TKVARYEldydKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAkDLDIVINETLPTLEQLVKEGKARFIGVSAYP 180
Cdd:PLN02587 81 TKCGRYG----EGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFG-SLDQIVNETIPALQKLKESGKVRFIGITGLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 181 ISVLKEFLTRTA-GRLDTVLTYARYTLTDETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQPWHPASDEQKAIARKAS 259
Cdd:PLN02587 156 LAIFTYVLDRVPpGTVDVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTENGPPEWHPAPPELKSACAAAA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66772279 260 EVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLD-ANEVGLSDKEQEVLRYLKE 321
Cdd:PLN02587 236 THCKEKGKNISKLALQYSLSN-KDISTTLVGMNSVQQVEENVAaATELETSGIDEELLSEVEA 297
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
25-305 |
6.80e-81 |
|
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: 248.22 E-value: 6.80e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 25 RNLGKTGLQVSKVSFGGGALCANYGFDLEEGI--KTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALK--DVPRESYYIA 100
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGDGLEQDEavAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAalQVPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 101 TKVARYEldyDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAkDLDIVINETLPTLEQLVKEGKARFIGVSAYP 180
Cdd:cd19153 83 TKVGRYR---DSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFV-DYDTLVDEALPALRTLKDEGVIKRIGIAGYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 181 ISVLKEFLTRTA-GRLDTVLTYARYTLTDETLLEYLDFFKSQNL-GVICAAAHALGLLTNAGPQPWHPASDEQKAIARKA 258
Cdd:cd19153 159 LDTLTRATRRCSpGSLDAVLSYCHLTLQDARLESDAPGLVRGAGpHVINASPLSMGLLTSQGPPPWHPASGELRHYAAAA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 66772279 259 SEVCKERGVELGKLAMYYTMSGLPEVSTFLTGMQTRQLLRINLDANE 305
Cdd:cd19153 239 DAVCASVEASLPDLALQYSLAAHAGVGTVLLGPSSLAQLRSMLAAVD 285
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
22-321 |
1.05e-72 |
|
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: 228.14 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIA 100
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWGgVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDDVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 101 TKVARYELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVSAYP 180
Cdd:COG0667 81 TKVGRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRP----DPDTPIEETLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 181 ISVLKEFLTRTAGRLDTVLTYARYTLTD-ETLLEYLDFFKSQNLGVICAAAHALGLLTNA-GPQPWHPASD--------- 249
Cdd:COG0667 157 AEQLRRALAIAEGLPPIVAVQNEYSLLDrSAEEELLPAARELGVGVLAYSPLAGGLLTGKyRRGATFPEGDraatnfvqg 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 250 ----EQKAIARKASEVCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSDkeqEVLRYLKE 321
Cdd:COG0667 237 ylteRNLALVDALRAIAAEHGVTPAQLALAWLLA-QPGVTSVIPGARSPEQLEENLAAADLELSA---EDLAALDA 308
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
35-303 |
1.09e-69 |
|
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: 218.96 E-value: 1.09e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGqgRSEEVLGLALKDVPRESYYIATKVARYELDYdkm 113
Cdd:cd19090 1 SALGLGTAGLGGVFGgVDDDEAVATIRAALDLGINYIDTAPAYG--DSEERLGLALAELPREPLVLSTKVGRLPEDT--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 114 FDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIV-INETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRta 192
Cdd:cd19090 76 ADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILaPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIET-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 193 GRLDTVLTYARYTLTDETLLEY-LDFFKSQNLGVICAAAHALGLLTNAGPQ----PWHPASDEQKAIARKASEVCKERGV 267
Cdd:cd19090 154 GDFDVVLTANRYTLLDQSAADElLPAAARHGVGVINASPLGMGLLAGRPPErvryTYRWLSPELLDRAKRLYELCDEHGV 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 66772279 268 ELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19090 234 PLPALALRFLLR-DPRISTVLVGASSPEELEQNVAA 268
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
32-303 |
7.49e-69 |
|
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: 217.53 E-value: 7.49e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 32 LQVSKVSFGGGALCANYGFDLEEgIKTVhEAVK----SGINYIDTAPWYGQgrSEEVLGLALK----DVPRESYYIATKV 103
Cdd:cd19164 11 AGLPPLIFGAATFSYQYTTDPES-IPPV-DIVRraleLGIRAFDTSPYYGP--SEIILGRALKalrdEFPRDTYFIITKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 104 ARYELDydkMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVinETLPTLEQLVKEGKARFIGVSAYPISV 183
Cdd:cd19164 87 GRYGPD---DFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVL--EALKELFKLKDEGKIRNVGISGYPLPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 184 L---KEFLTRTAGR-LDTVLTYARYTLTDETLLEYLD-FFKSQNLGVIC-AAAHALGLLTNAGPQPWHPASDEQKAIARK 257
Cdd:cd19164 162 LlrlAELARTTAGRpLDAVLSYCHYTLQNTTLLAYIPkFLAAAGVKVVLnASPLSMGLLRSQGPPEWHPASPELRAAAAK 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 66772279 258 ASEVCKERGVELGKLAMYYTMSGLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19164 242 AAEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDELEEAVEA 287
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-307 |
1.24e-54 |
|
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: 181.69 E-value: 1.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 23 EYRNLGKTGLQVSKVSFGGGALCANYGF-DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPrESYYIAT 101
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGLMGRtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLP-AGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 102 KVaryELDYDKMFDFSAkKTRESVEKSLKLLGLDYVDVIQIH-----------DIEFAKDLDIVINETLPTLEQLVKEGK 170
Cdd:cd19104 80 KV---RLDPDDLGDIGG-QIERSVEKSLKRLKRDSVDLLQLHnrigderdkpvGGTLSTTDVLGLGGVADAFERLRSEGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 171 ARFIGVSAY-PISVLKEFLtrTAGRLDTVLTYarYTLTDET----------LLEY---LDFFKSQNLGVICAAAHALGLL 236
Cdd:cd19104 156 IRFIGITGLgNPPAIRELL--DSGKFDAVQVY--YNLLNPSaaearprgwsAQDYggiIDAAAEHGVGVMGIRVLAAGAL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 237 T---NAGPQPwHPASDEQKAI----ARKASEVCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVG 307
Cdd:cd19104 232 TtslDRGREA-PPTSDSDVAIdfrrAAAFRALAREWGETLAQLAHRFALS-NPGVSTVLVGVKNREELEEAVAAEAAG 307
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-302 |
3.22e-53 |
|
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: 175.36 E-value: 3.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFGGGALcanYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQgrSEEVLGLALKDvPRESYYIATKV 103
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL---GRLSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKG-RRDKVFLATKT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 104 arYELDYDKMfdfsakktRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVI--NETLPTLEQLVKEGKARFIGVSAYPI 181
Cdd:cd19100 75 --GARDYEGA--------KRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFgpGGALEALLEAKEEGKIRFIGISGHSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 182 SVLKEFLTRtaGRLDTVL-----TYARYTLTDETLLEYLdffKSQNLGVICAAAHALGLLTNAGPQPWhpasdeqkaiar 256
Cdd:cd19100 145 EVLLRALET--GEFDVVLfpinpAGDHIDSFREELLPLA---REKGVGVIAMKVLAGGRLLSGDPLDP------------ 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 66772279 257 kasevckergvelgKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLD 302
Cdd:cd19100 208 --------------EQALRYALS-LPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
35-303 |
8.29e-53 |
|
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: 176.01 E-value: 8.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALCANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARY-------- 106
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLlepgaagr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEfaKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19162 81 PAGADRRFDFSADGIRRSIEASLERLGLDRLDLVFLHDPD--RHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 187 FLTRtaGRLDTVLTYARYTLTD-ETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQP----WHPASDEQKAIARKASEV 261
Cdd:cd19162 159 AARR--ADVDVVMVAGRYTLLDrRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGdrydYRPATPEVLARARRLAAV 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 66772279 262 CKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19162 237 CRRYGVPLPAAALQFPLRH-PAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
22-303 |
1.55e-52 |
|
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: 173.92 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALcanygfdLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIAT 101
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGL-------PRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVFLAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 102 KVaryeldYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDlDIVINETLPTLEQLVKEGKARFIGVSAYpi 181
Cdd:cd19105 74 KA------SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEE-RLLNEELLEALEKLKKEGKVRFIGFSTH-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 182 SVLKEFLTRTA--GRLDTVLTyaRYTLT--DETLLEYLDFFKSQNLGVICAAAhalglLTNAGPQPWHPASDEQKAIARK 257
Cdd:cd19105 145 DNMAEVLQAAIesGWFDVIMV--AYNFLnqPAELEEALAAAAEKGIGVVAMKT-----LAGGYLQPALLSVLKAKGFSLP 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 66772279 258 AsevckergvelgklAMYYTMSGLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19105 218 Q--------------AALKWVLSNPRVDTVVPGMRNFAELEENLAA 249
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
22-321 |
8.71e-52 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 175.39 E-value: 8.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANygfDLEEGIKTVHEAVKSGINYIDTAPWYGQgrSEEVLGLALKDvPRESYYIAT 101
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRLPRK---DEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKG-PRDKVILAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 102 KVARYELDYDKMfdfsakktRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVI--NETLPTLEQLVKEGKARFIGVSAY 179
Cdd:COG1453 75 KLPPWVRDPEDM--------RKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLkpGGALEALEKAKAEGKIRHIGFSTH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 180 -PISVLKEFLtrTAGRLDTV---LTYARYTLTDET-LLEYLdffKSQNLGVIC--AAAHalGLLTNagpqpwhPASDEQK 252
Cdd:COG1453 147 gSLEVIKEAI--DTGDFDFVqlqYNYLDQDNQAGEeALEAA---AEKGIGVIImkPLKG--GRLAN-------PPEKLVE 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 253 AIARKASEVckergvelgKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDA--NEVGLSDKEQEVLRYLKE 321
Cdd:COG1453 213 LLCPPLSPA---------EWALRFLLS-HPEVTTVLSGMSTPEQLDENLKTadNLEPLTEEELAILERLAE 273
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
31-317 |
4.21e-50 |
|
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: 168.86 E-value: 4.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGGGAL-CANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYIATKVA-RYE 107
Cdd:cd19084 1 DLKVSRIGLGTWAIgGTWWGeVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR-RDDVVIATKCGlRWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 108 LDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEF 187
Cdd:cd19084 80 GGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIH----WPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 188 ltRTAGRLDTVLTyaRYTLTD----ETLLEYLdffKSQNLGVICAAAHALGLLT---NAGPQPwhPASDEQ--------- 251
Cdd:cd19084 156 --RKYGPIVSLQP--PYSMLEreieEELLPYC---RENGIGVLPYGPLAQGLLTgkyKKEPTF--PPDDRRsrfpffrge 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 252 -----KAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDKEQEVLR 317
Cdd:cd19084 227 nfeknLEIVDKLKEIAEKYGKSLAQLAIAWTLAQ-PGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
37-312 |
5.42e-50 |
|
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: 168.64 E-value: 5.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 37 VSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKD--VPRESYYIATKVARYelDYDKM 113
Cdd:pfam00248 1 IGLGTWQLGGGWGpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDypVKRDKVVIATKVPDG--DGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 114 FDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDivinETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRTAG 193
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIE----ETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 194 RLDTVltYARYTL----TDETLLEYLdffKSQNLGVICAAAHALGLLT-----NAGPQPWHPASD------EQKAIARKA 258
Cdd:pfam00248 155 PIVAV--QVEYNLlrrrQEEELLEYC---KKNGIPLIAYSPLGGGLLTgkytrDPDKGPGERRRLlkkgtpLNLEALEAL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 66772279 259 SEVCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSDKE 312
Cdd:pfam00248 230 EEIAKEHGVSPAQVALRWALS-KPGVTIPIPGASNPEQLEDNLGALEFPLSDEE 282
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
24-312 |
1.93e-46 |
|
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: 160.13 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFG----GGALcANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYI 99
Cdd:cd19149 1 YRKLGKSGIEASVIGLGtwaiGGGP-WWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 100 ATKVA-RYEL----------DYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIH--DIEFAkdldivINETLPTLEQLV 166
Cdd:cd19149 79 ATKCGlRWDReggsfffvrdGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHwqDVETP------IEETMEALEELK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 167 KEGKARFIGVSAYPISVLKEFltRTAGRLDTVltYARYTLTDETL-LEYLDFFKSQNLGVICAAAHALGLLT-------- 237
Cdd:cd19149 153 RQGKIRAIGASNVSVEQIKEY--VKAGQLDII--QEKYSMLDRGIeKELLPYCKKNNIAFQAYSPLEQGLLTgkitpdre 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 238 -NAGPQ----PWHPASDEQKAIARKASE--VCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSD 310
Cdd:cd19149 229 fDAGDArsgiPWFSPENREKVLALLEKWkpLCEKYGCTLAQLVIAWTLA-QPGITSALCGARKPEQAEENAKAGDIRLSA 307
|
..
gi 66772279 311 KE 312
Cdd:cd19149 308 ED 309
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
32-303 |
6.93e-46 |
|
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: 156.10 E-value: 6.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 32 LQVSKVSFGGGALCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDvPRESYYIATKV-ARYEL 108
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWWgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG-RRDKVVIATKFgNRFDG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 109 DYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAkdlDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19086 80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDE---VLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 189 TRtaGRLDTV-LTYARytLTDETLLEYLDFFKSQNLGVICAAAHALGLLTNagpqpwhpasdeqkaiarkasevckergv 267
Cdd:cd19086 157 RR--GGIDVVqVIYNL--LDQRPEEELFPLAEEHGVGVIARVPLASGLLTG----------------------------- 203
|
250 260 270
....*....|....*....|....*....|....*.
gi 66772279 268 ELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19086 204 KLAQAALRFILS-HPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
34-328 |
6.54e-44 |
|
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: 152.74 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 34 VSKVSFGGGALCANYGF---DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYIATKVARYELDY 110
Cdd:cd19085 1 VSRLGLGCWQFGGGYWWgdqDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGR-RDDVVIATKVSPDNLTP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 111 DKMfdfsakktRESVEKSLKLLGLDYVDVIQIHdieFAKDlDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFLtr 190
Cdd:cd19085 80 EDV--------RKSCERSLKRLGTDYIDLYQIH---WPSS-DVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEAL-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 191 TAGRLDTV-LTYarytltdeTLL------EYLDFFKSQNLGVICAAAHALGLLTNAGPQPWH-PASDEQKAIAR------ 256
Cdd:cd19085 146 DAGRIDSNqLPY--------NLLwraieyEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDfPPGDARTRLFRhfepga 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 257 ---------KASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDkeqEVLRYLKEnvLTKP 327
Cdd:cd19085 218 eeetfealeKLKEIADELGVTMAQLALAWVLQQ-PGVTSVIVGARNPEQLEENAAAVDLELSP---SVLERLDE--ISDP 291
|
.
gi 66772279 328 F 328
Cdd:cd19085 292 L 292
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
22-321 |
1.12e-43 |
|
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: 152.73 E-value: 1.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGggalCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYI 99
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLG----TMNFGgrTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR-RDDIVL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 100 ATKVaryeldYDKMFD------FSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARF 173
Cdd:cd19087 76 ATKV------FGPMGDdpndrgLSRRHIRRAVEASLRRLQTDYIDLYQMHHF----DRDTPLEETLRALDDLVRQGKIRY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 174 IGVSAYPISVLKEFLTRTA--GRLDTVLTYARYTLTDETL-LEYLDFFKSQNLGVICAAAHALGLLT-----NAGPQPWH 245
Cdd:cd19087 146 IGVSNFAAWQIAKAQGIAArrGLLRFVSEQPMYNLLKRQAeLEILPAARAYGLGVIPYSPLAGGLLTgkygkGKRPESGR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 246 PASDEQKA----------IARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDkeqEV 315
Cdd:cd19087 226 LVERARYQarygleeyrdIAERFEALAAEAGLTPASLALAWVLSH-PAVTSPIIGPRTLEQLEDSLAALEITLTP---EL 301
|
....*.
gi 66772279 316 LRYLKE 321
Cdd:cd19087 302 LAEIDE 307
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
35-311 |
1.70e-41 |
|
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: 146.99 E-value: 1.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALcANyGF---DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARY----- 106
Cdd:cd19152 1 PKLGFGTAPL-GN-LYeavSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGREDYVISTKVGRLlvplq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ------------ELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIE-------FAKDLDIVINETLPTLEQLVK 167
Cdd:cd19152 79 eveptfepgfwnPLPFDAVFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDedlagaeSDEHFAQAIKGAFRALEELRE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 168 EGKARFIGVSAYPISVLKEFLTRtaGRLDTVLTYARYTLTDETllEYLDFFKS---QNLGVICAAAHALGLLtnAGPQPW 244
Cdd:cd19152 159 EGVIKAIGLGVNDWEVILRILEE--ADLDWVMLAGRYTLLDHS--AARELLPEcekRGVKVVNAGPFNSGFL--AGGDNF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66772279 245 H-----PASDEQKAIARKASEVCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSDK 311
Cdd:cd19152 233 DyyeygPAPPELIARRDRIEALCEQHGVSLAAAALQFALA-PPAVASVAPGASSPERVEENVALLATEIPAA 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
49-303 |
8.98e-41 |
|
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: 143.53 E-value: 8.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 49 GFDLEEGIKTVHEAVKSGINYIDTAPWYGqgRSEEVLGLALKDVPRESYYIATKVARYELDYDKMFDFSAKKTRESVEKS 128
Cdd:cd19095 16 VPSEAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAGLRRDDLFIATKVGTHGEGGRDRKDFSPAAIRASIERS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 129 LKLLGLDYVDVIQIHdiefaKDLDIVIN-ETLPTLEQLVKEGKARFIGVSAYPiSVLKEFLtrTAGRLDTV-LTYARYTL 206
Cdd:cd19095 94 LRRLGTDYIDLLQLH-----GPSDDELTgEVLETLEDLKAAGKVRYIGVSGDG-EELEAAI--ASGVFDVVqLPYNVLDR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 207 TDETLLEYLdffKSQNLGVICAAAHALGLLTNAGPQPWHPASDEQKAIARKASEvckerGVELGKLAMYYTMSGlPEVST 286
Cdd:cd19095 166 EEEELLPLA---AEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIG-----GATWAQAALRFVLSH-PGVSS 236
|
250
....*....|....*....
gi 66772279 287 FLTGmqTRQL--LRINLDA 303
Cdd:cd19095 237 AIVG--TTNPehLEENLAA 253
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
23-179 |
7.79e-40 |
|
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: 142.72 E-value: 7.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 23 EYRNLGKTGLQVSKVSFGggalCANYG--------FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKD-VP 93
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLG----CMSFGdpkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEfAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 94 RESYYIATKVaryeldYDKMFD------FSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVK 167
Cdd:cd19079 77 RDEVVIATKV------YFPMGDgpngrgLSRKHIMAEVDASLKRLGTDYIDLYQIHRW----DYETPIEETLEALHDVVK 146
|
170
....*....|..
gi 66772279 168 EGKARFIGVSAY 179
Cdd:cd19079 147 SGKVRYIGASSM 158
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
35-238 |
1.35e-38 |
|
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: 136.88 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGggalCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVP-RESYYIATKVARYELDYD 111
Cdd:cd06660 1 SRLGLG----TMTFGgdGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGnRDDVVIATKGGHPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 112 KMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDivinETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRT 191
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVE----ETLEALNELVREGKIRYIGVSNWSAERLAEALAYA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 192 AGRLDTVLTY--ARYTL--TDETLLEYLDFFKSQNLGVIC-------AAAHALGLLTN 238
Cdd:cd06660 153 KAHGLPGFAAvqPQYSLldRSPMEEELLDWAEENGLPLLAysplargPAQLALAWLLS 210
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
25-312 |
2.99e-38 |
|
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: 138.32 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 25 RNLGKTGLQVSKVSFGGGALCANY---GFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIAT 101
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNEVVIAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 102 KVARYELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIH--DIEFAKDldivinETLPTLEQLVKEGKARFIGVSAY 179
Cdd:cd19083 82 KGAHKFGGDGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHfpDGETPKA------EAVGALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 180 PISVLKEFltRTAGRLDTVltYARYTLTD-ETLLEYLDFFKSQNLGVICAAAHALGLLTNA-GPQPWHPASDEQKAIAR- 256
Cdd:cd19083 156 SLEQLKEA--NKDGYVDVL--QGEYNLLQrEAEEDILPYCVENNISFIPYFPLASGLLAGKyTKDTKFPDNDLRNDKPLf 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 257 -------------KASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDKE 312
Cdd:cd19083 232 kgerfsenldkvdKLKSIADEKGVTVAHLALAWYLTR-PAIDVVIPGAKRAEQVIDNLKALDVTLTEEE 299
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
31-237 |
1.12e-37 |
|
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: 136.67 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFG----GGALCAnyGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDV-PRESYYIATKVAr 105
Cdd:cd19148 1 DLPVSRIALGtwaiGGWMWG--GTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgKRDRVVIATKVG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 106 yeLDYD----KMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPI 181
Cdd:cd19148 78 --LEWDeggeVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVH----WPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 182 SVLKEFltRTAGRLDTVltYARYTL----TDETLLEYLdffKSQNLGVICAAAHALGLLT 237
Cdd:cd19148 152 EQMETF--RKVAPLHTV--QPPYNLfereIEKDVLPYA---RKHNIVTLAYGALCRGLLS 204
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
31-310 |
2.00e-35 |
|
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: 130.40 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGGgALCANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVarY---- 106
Cdd:cd19074 1 GLKVSELSLGT-WLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESYVISTKV--Fwptg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ELDYDKmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19074 78 PGPNDR--GLSRKHIFESIHASLKRLQLDYVDIYYCH----RYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 187 F--LTRTAGRLDTVLTYARY-TLTDETLLEYLDFFKSQNLGVICAAAHALGLLTN--------------AGPQPWHPA-- 247
Cdd:cd19074 152 AhdLARQFGLIPPVVEQPQYnMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGkyrdgipppsrsraTDEDNRDKKrr 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66772279 248 --SDEQKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSD 310
Cdd:cd19074 232 llTDENLEKVKKLKPIADELGLTLAQLALAWCLRN-PAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
22-316 |
3.27e-35 |
|
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: 130.43 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANYGF-------DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpR 94
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFfgawggvDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 95 ESYYIATKVaryeldYDKMFD------FSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKE 168
Cdd:cd19091 80 DDVLIATKV------RGRMGEgpndvgLSRHHIIRAVEASLKRLGTDYIDLYQLHGF----DALTPLEETLRALDDLVRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 169 GKARFIGVSAYP---------ISVLKEFltrtaGRLDTVLTYarYTLTDETL-LEYLDFFKSQNLGVICAAAHALGLLT- 237
Cdd:cd19091 150 GKVRYIGVSNFSawqimkalgISERRGL-----ARFVALQAY--YSLLGRDLeHELMPLALDQGVGLLVWSPLAGGLLSg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 238 ---NAGPQP-----------WHPASDEQ-KAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLD 302
Cdd:cd19091 223 kyrRGQPAPegsrlrrtgfdFPPVDRERgYDVVDALREIAKETGATPAQVALAWLLSR-PTVSSVIIGARNEEQLEDNLG 301
|
330
....*....|....
gi 66772279 303 ANEVGLSDKEQEVL 316
Cdd:cd19091 302 AAGLSLTPEEIARL 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
35-303 |
5.48e-35 |
|
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: 128.06 E-value: 5.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGAL--CANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARYEL---- 108
Cdd:cd19096 1 SVLGFGTMRLpeSDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREKFYLATKLPPWSVksae 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 109 DYDKMFdfsakktresvEKSLKLLGLDYVDVIQIHDI------EFAKDLDIvinetLPTLEQLVKEGKARFIGVSAY-PI 181
Cdd:cd19096 81 DFRRIL-----------EESLKRLGVDYIDFYLLHGLnspewlEKARKGGL-----LEFLEKAKKEGLIRHIGFSFHdSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 182 SVLKEFLtrTAGRLDTVLTYarytltdetlLEYLDFFKSQNLGVIcAAAHALGLLTNA------GPQPWHPASDEQKAIA 255
Cdd:cd19096 145 ELLKEIL--DSYDFDFVQLQ----------YNYLDQENQAGRPGI-EYAAKKGMGVIImeplkgGGLANNPPEALAILCG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 66772279 256 RKASEVckergvelgKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19096 212 APLSPA---------EWALRFLLS-HPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
51-316 |
4.97e-34 |
|
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: 127.02 E-value: 4.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYIATKVARYELDYDKMF-DFSAKKTRESVEKSL 129
Cdd:cd19102 24 DDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL-RDRPIVATKCGLLWDEEGRIRrSLKPASIRAECEASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 130 KLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEflTRTAGRLDTVltYARYTLTD- 208
Cdd:cd19102 103 RRLGVDVIDLYQIH----WPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR--CQAIHPIASL--QPPYSLLRr 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 209 ETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQPW---HPASDEQK--------------AIARKASEVCKERGVELGK 271
Cdd:cd19102 175 GIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvasLPADDWRRrspffqepnlarnlALVDALRPIAERHGRTVAQ 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 66772279 272 LAMYYTMSgLPEVSTFLTGMQTRQLLRINLDANEVGLSDKEQEVL 316
Cdd:cd19102 255 LAIAWVLR-RPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEI 298
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
31-312 |
3.18e-33 |
|
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: 123.88 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFG----GGALCANYGFDlEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARY 106
Cdd:cd19072 1 GEEVPVLGLGtwgiGGGMSKDYSDD-KKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDREDLFITTKVSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ELDYDKMfdfsakktRESVEKSLKLLGLDYVDVIQIHDIEFAkdldIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19072 80 HLKYDDV--------IKAAKESLKRLGTDYIDLYLIHWPNPS----IPIEETLRAMEELVEEGKIRYIGVSNFSLEELEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 187 FLtRTAGRLDTVLTYARYTLTD-ETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQPwhpasdeqkaiarKASEVCKER 265
Cdd:cd19072 148 AQ-SYLKKGPIVANQVEYNLFDrEEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSP-------------LLDEIAKKY 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 66772279 266 GVELGKLAMYYTMSglPEVSTFLTGMQTRQLLRINLDANEVGLSDKE 312
Cdd:cd19072 214 GKTPAQIALNWLIS--KPNVIAIPKASNIEHLEENAGALGWELSEED 258
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
35-303 |
7.01e-33 |
|
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: 123.98 E-value: 7.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALCANY-GFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARY------- 106
Cdd:cd19161 1 SELGLGTAGLGNLYtAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKPRDEFVLSTKVGRLlkpareg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ----------ELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDI-------EFAKDLD-IVINETLPTLEQLVKE 168
Cdd:cd19161 81 svpdpngfvdPLPFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIgvythgdRKERHHFaQLMSGGFKALEELKKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 169 G--KARFIGVSAYPI--SVLKEFltrtagRLDTVLTYARYTLTDETLL-EYLDFFKSQNLGVICAAAHALGLL-TNAGPQ 242
Cdd:cd19161 161 GviKAFGLGVNEVQIclEALDEA------DLDCFLLAGRYSLLDQSAEeEFLPRCEQRGTSLVIGGVFNSGILaTGTKSG 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66772279 243 PWHPASDEQKAIARKASE---VCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19161 235 AKFNYGDAPAEIISRVMEiekICDAYNVPLAAAALQFPLRH-PAVASVLTGARNPAQLRQNVEA 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
23-177 |
3.00e-31 |
|
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: 119.63 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 23 EYRNLGKTGLQVSKVSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDvPRESYYIAT 101
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGpADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD-RRDEVVIAT 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 102 K--VARYELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19076 80 KfgIVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV----DPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
27-312 |
3.84e-31 |
|
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: 119.24 E-value: 3.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 27 LGKTGLQVSKVSFGGgalcANYGFDLEEgiKTVHEA----VKSGINYIDTAPWYGQ-------GRSEEVLGLALKD-VPR 94
Cdd:cd19081 2 LGRTGLSVSPLCLGT----MVFGWTADE--ETSFALldafVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSrGKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 95 ESYYIATKVARYELDYDKmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFI 174
Cdd:cd19081 76 DRVVIATKVGFPMGPNGP--GLSRKHIRRAVEASLRRLQTDYIDLYQAH----WDDPATPLEETLGALNDLIRQGKVRYI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 175 GVSAYPISVLKEFL--TRTAGRLDTVLTYARYTLTDETLLEY--LDFFKSQNLGVICAAAHALGLLT---NAGPQPwhPA 247
Cdd:cd19081 150 GASNYSAWRLQEALelSRQHGLPRYVSLQPEYNLVDRESFEGelLPLCREEGIGVIPYSPLAGGFLTgkyRSEADL--PG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66772279 248 SDEQKAIARK------------ASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDKE 312
Cdd:cd19081 228 STRRGEAAKRylnerglrildaLDEVAAEHGATPAQVALAWLLAR-PGVTAPIAGARTVEQLEDLLAAAGLRLTDEE 303
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
24-313 |
8.96e-31 |
|
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: 118.51 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFGggaLCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYG--QGRSEEVLGLALKDV---PRES 96
Cdd:cd19089 1 YRRCGRSGLHLPAISLG---LWHNFGdyTSPEEARELLRTAFDLGITHFDLANNYGppPGSAEENFGRILKRDlrpYRDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 97 YYIATKvARYELDYDKMFDFSAKK-TRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIG 175
Cdd:cd19089 78 LVISTK-AGYGMWPGPYGDGGSRKyLLASLDQSLKRMGLDYVDIFYHHRY----DPDTPLEETMTALADAVRSGKALYVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 176 VSAYPISVLKE---FLTRTAGRLdtVLTYARYTLTDETLLEYL-DFFKSQNLGVICAAAHALGLLTNA---GPQPWHPAS 248
Cdd:cd19089 153 ISNYPGAKARRaiaLLRELGVPL--IIHQPRYSLLDRWAEDGLlEVLEEAGIGFIAFSPLAQGLLTDKylnGIPPDSRRA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 249 DEQKAIA------------RKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGM-QTRQLLRINLDANEVGLSDKEQ 313
Cdd:cd19089 231 AESKFLTeealtpekleqlRKLNKIAAKRGQSLAQLALSWVLRD-PRVTSVLIGAsSPSQLEDNVAALKNLDFSEEEL 307
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
31-316 |
3.47e-30 |
|
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: 115.75 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFG----GGALCANYGFDlEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVARY 106
Cdd:cd19137 1 GEKIPALGLGtwgiGGFLTPDYSRD-EEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPREDLFIVTKVWPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 ELDYDKMFDfsakktreSVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19137 80 NLRYDDLLR--------SLQNSLRRLDTDYIDLYLIH----WPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 187 flTRTAGRLDTVLTYARYTLTDETLLE--YLDFFKSQNLGVICAAAHALGLLtnagpqpwhPASDEQKAIArkasevcKE 264
Cdd:cd19137 148 --AISKSQTPIVCNQVKYNLEDRDPERdgLLEYCQKNGITVVAYSPLRRGLE---------KTNRTLEEIA-------KN 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 66772279 265 RGVELGKLAMYYTMSGlPEVSTFLTGMQTRQlLRINLDANEVGLSDKEQEVL 316
Cdd:cd19137 210 YGKTIAQIALAWLIQK-PNVVAIPKAGRVEH-LKENLKATEIKLSEEEMKLL 259
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
22-306 |
5.41e-30 |
|
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: 116.54 E-value: 5.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGgalCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALK--DVPRESY 97
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGS---WVTFGnqVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKelGWPRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 98 YIATKV---ARYELDYDKmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFI 174
Cdd:cd19143 78 VVSTKIfwgGGGPPPNDR--GLSRKHIVEGTKASLKRLQLDYVDLVFCH----RPDPATPIEETVRAMNDLIDQGKAFYW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 175 GVSAYPISVLKEFLtRTAGRLDT---VLTYARYTLTDETLLE--YLDFFKSQNLGVICAAAHALGLLT---NAG------ 240
Cdd:cd19143 152 GTSEWSAQQIEEAH-EIADRLGLippVMEQPQYNLFHRERVEveYAPLYEKYGLGTTTWSPLASGLLTgkyNNGipegsr 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66772279 241 ----PQPW-----HPASDEQKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEV 306
Cdd:cd19143 231 lalpGYEWlkdrkEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKN-PNVSTVITGATKVEQLEENLKALEV 304
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
25-177 |
1.32e-28 |
|
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: 112.53 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 25 RNLGKTGLQVSKVSFGGGALCANYGFDL--EEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATK 102
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMGLSGDYGAPKpeEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPREKVQLATK 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 103 VARYELDYDKM-FDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19145 83 FGIHEIGGSGVeVRGDPAYVRAACEASLKRLDVDYIDLYYQHRI----DTTVPIEITMGELKKLVEEGKIKYIGLS 154
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
48-191 |
4.27e-28 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 109.76 E-value: 4.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 48 YGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESV 125
Cdd:COG0656 13 WQLPGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAAsgVPREELFVTTKVWNDNHGYDD--------TLAAF 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 126 EKSLKLLGLDYVDVIQIH---DIEFAkdldivinETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRT 191
Cdd:COG0656 82 EESLERLGLDYLDLYLIHwpgPGPYV--------ETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
34-273 |
8.05e-28 |
|
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: 109.23 E-value: 8.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 34 VSKVSFGGGALCANYGF----DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPrESYYIATKV--ARYE 107
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWgppaDREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYP-DDVVIATKGglVRTG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 108 LDYDKMfDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEf 187
Cdd:cd19088 80 PGWWGP-DGSPEYLRQAVEASLRRLGLDRIDLYQLHRI----DPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEE- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 188 lTRTAGRLDTVLTyaRYTLT---DETLLEYLdffksqnlgvicaAAHALGLLtnagpqPWHP-ASDEQKAIARKASEVCK 263
Cdd:cd19088 154 -ARAIVRIVSVQN--RYNLAnrdDEGVLDYC-------------EAAGIAFI------PWFPlGGGDLAQPGGLLAEVAA 211
|
250
....*....|
gi 66772279 264 ERGVELGKLA 273
Cdd:cd19088 212 RLGATPAQVA 221
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
29-273 |
1.77e-26 |
|
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: 106.10 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 29 KTGLQVSKVSFGGGALcANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVP--RESYYIATK---- 102
Cdd:cd19092 1 PEGLEVSRLVLGCMRL-ADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPglREKIEIQTKcgir 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 103 -VARYELDYDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDivinETLPTLEQLVKEGKARFIGVSAYPI 181
Cdd:cd19092 80 lGDDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPE----EVAEAFDELVKSGKVRYFGVSNFTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 182 SVLkEFLTRtagRLDTVLT--------YARYTLTDETlLEYLdffksQNLGVicaaahalglltnaGPQPWHP------- 246
Cdd:cd19092 156 SQI-ELLQS---YLDQPLVtnqielslLHTEAIDDGT-LDYC-----QLLDI--------------TPMAWSPlgggrlf 211
|
250 260
....*....|....*....|....*....
gi 66772279 247 --ASDEQKAIARKASEVCKERGVELGKLA 273
Cdd:cd19092 212 ggFDERFQRLRAALEELAEEYGVTIEAIA 240
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-303 |
1.23e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 103.38 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALCANYGF-------DLEEGIKTVHEAVKSGINYIDTAPWYGQgrSEEVLGLALKDvpRESYYIATKVARYE 107
Cdd:cd19097 1 SKLALGTAQFGLDYGIanksgkpSEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKR--LDKFKIITKLPPLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 108 LDYDKmfdfSAKKTRESVEKSLKLLGLDYVDVIQIHDiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEF 187
Cdd:cd19097 77 EDKKE----DEAAIEASVEASLKRLKVDSLDGLLLHN---PDDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 188 LTRtaGRLDTVltYARYTLTDETLLE--YLDFFKSQNLGVicaaaHA----L-GLLTnAGPQPWHPASDEQKAIARKASE 260
Cdd:cd19097 150 LES--FKIDII--QLPFNILDQRFLKsgLLAKLKKKGIEI-----HArsvfLqGLLL-MEPDKLPAKFAPAKPLLKKLHE 219
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 66772279 261 VCKERGVELGKLAMYYTMSgLPEVSTFLTGMQTRQLLRINLDA 303
Cdd:cd19097 220 LAKKLGLSPLELALGFVLS-LPEIDKIVVGVDSLEQLKEIIAA 261
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
38-237 |
4.62e-25 |
|
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: 102.69 E-value: 4.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 38 SFGGGALCANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVP-RESYYIATKVARYELdydkmfDF 116
Cdd:cd19093 11 QWGDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGdRDEVVIATKFAPLPW------RL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 117 SAKKTRESVEKSLKLLGLDYVDVIQIHdieFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRTAGRLD 196
Cdd:cd19093 85 TRRSVVKALKASLERLGLDSIDLYQLH---WPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 66772279 197 TV--------LTYaRYTLTDEtLLEYLDffksqNLGVICAAAH--ALGLLT 237
Cdd:cd19093 162 PLasnqveysLLY-RDPEQNG-LLPACD-----ELGITLIAYSplAQGLLT 205
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
48-188 |
1.81e-24 |
|
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: 99.86 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 48 YGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESV 125
Cdd:cd19071 9 YKLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIREsgVPREELFITTKLWPTDHGYER--------VREAL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66772279 126 EKSLKLLGLDYVDVIQIH----DIEFAKDLDIVinETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19071 78 EESLKDLGLDYLDLYLIHwpvpGKEGGSKEARL--ETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
31-188 |
2.17e-24 |
|
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: 100.00 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFG-GGALCANYGFDLEEG-IKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARy 106
Cdd:cd19120 1 GSKIPAIAFGtGTAWYKSGDDDIQRDlVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKEsgVPREDLFITTKVSP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 107 eldydkmfdfSAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19120 77 ----------GIKDPREALRKSLAKLGVDYVDLYLIHSPFFAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEE 146
|
..
gi 66772279 187 FL 188
Cdd:cd19120 147 LL 148
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
32-177 |
3.06e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 100.86 E-value: 3.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 32 LQVSKVSFGGgALCANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALK------DVPRESYYIATKV-- 103
Cdd:cd19099 1 LTLSSLGLGT-YRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekgGIKRDEVVIVTKAgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 104 -----------ARYELDYDK------------MFDFSAKKTRESVEKSLKLLGLDYVDVIQIHD--IEFAKDLDIVINET 158
Cdd:cd19099 80 ipgdgdeplrpLKYLEEKLGrglidvadsaglRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNpeEQLLELGEEEFYDR 159
|
170 180
....*....|....*....|...
gi 66772279 159 LPT----LEQLVKEGKARFIGVS 177
Cdd:cd19099 160 LEEafeaLEEAVAEGKIRYYGIS 182
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
23-290 |
2.47e-22 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 95.55 E-value: 2.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 23 EYRNLGKTGLQVSKVSFGggaLCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYG--QGRSEEVLGLALKD---VPRE 95
Cdd:cd19151 1 KYNRCGRSGLKLPAISLG---LWHNFGdvDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlkPYRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 96 SYYIATKVARYELD--YDkmfDFSAKKTR-ESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKAR 172
Cdd:cd19151 78 ELIISTKAGYTMWPgpYG---DWGSKKYLiASLDQSLKRMGLDYVDIFYHH----RPDPETPLEETMGALDQIVRQGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 173 FIGVSAYP-------ISVLKEFLTRtagrldTVLTYARYTLTDETLLE-YLDFFKSQNLGVICAAAHALGLLTN------ 238
Cdd:cd19151 151 YVGISNYPpeeareaAAILKDLGTP------CLIHQPKYSMFNRWVEEgLLDVLEEEGIGCIAFSPLAQGLLTDrylngi 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66772279 239 -----AGpQPWHP-----ASDEQKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTG 290
Cdd:cd19151 225 pedsrAA-KGSSFlkpeqITEEKLAKVRRLNEIAQARGQKLAQMALAWVLRN-KRVTSVLIG 284
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
51-188 |
4.38e-22 |
|
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: 93.85 E-value: 4.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD------VPRESYYIATKVARYELDYDKmfdfsakkTRES 124
Cdd:cd19136 13 GEEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDllpkygLSREDIFITSKLAPKDQGYEK--------ARAA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66772279 125 VEKSLKLLGLDYVDVIQIH---------DIEFAKDLDIvinETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19136 82 CLGSLERLGTDYLDLYLIHwpgvqglkpSDPRNAELRR---ESWRALEDLYKEGKLRAIGVSNYTVRHLEELL 151
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
53-177 |
6.89e-22 |
|
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: 94.55 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWY-------GQGRSEEVLGLALKD-VPRESYYIATKVARYELDY----DKMFDFSAKK 120
Cdd:cd19094 18 AEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKKkGNRDKVVLATKVAGPGEGItwprGGGTRLDREN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 121 TRESVEKSLKLLGLDYVDVIQIH-------------DIEFAKDLDIV-INETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19094 98 IREAVEGSLKRLGTDYIDLYQLHwpdrytplfgggyYTEPSEEEDSVsFEEQLEALGELVKAGKIRHIGLS 168
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
27-316 |
2.41e-21 |
|
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: 92.67 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 27 LGKTGLQVSKVSFGGGALCANYGF--DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVpRESYYIATKVA 104
Cdd:cd19080 3 LGRSGLRVSPLALGTMTFGTEWGWgaDREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN-RDRIVLATKYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 105 RYeldyDKMFDFSA-----KKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAY 179
Cdd:cd19080 82 MN----RRPGDPNAggnhrKNLRRSVEASLRRLQTDYIDLLYVH----AWDFTTPVEEVMRALDDLVRAGKVLYVGISDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 180 PisvlkefltrtAGRLDTVLTYA-------------RYTLTDETL-LEYLDFFKSQNLGVICAAAHALGLLT-------- 237
Cdd:cd19080 154 P-----------AWVVARANTLAelrgwspfvalqiEYSLLERTPeRELLPMARALGLGVTPWSPLGGGLLTgkyqrgee 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 238 ------NAGPQPWHPASDEQKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEVGLSDK 311
Cdd:cd19080 223 grageaKGVTVGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQK-PGVVIPIIGARTLEQLKDNLGALDLTLSPE 301
|
....*
gi 66772279 312 EQEVL 316
Cdd:cd19080 302 QLARL 306
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
31-177 |
4.19e-21 |
|
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: 91.91 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGGGALCANYG--FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDvPRESYYIATKVA-RYE 107
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGppPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP-FRDQVVIATKFGfKID 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66772279 108 LDYDKM--FDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19078 80 GGKPGPlgLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRV----DPNVPIEEVAGTMKELIKEGKIRHWGLS 147
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
53-192 |
1.80e-20 |
|
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: 88.97 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLK 130
Cdd:cd19131 23 DEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRAsgVPREELFITTKLWNSDQGYDS--------TLRAFDESLR 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66772279 131 LLGLDYVDVIQIHDIEFAKDLDIvinETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRTA 192
Cdd:cd19131 92 KLGLDYVDLYLIHWPVPAQDKYV---ETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG 150
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
53-186 |
2.49e-20 |
|
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: 88.48 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALK--DVPRESYYIATKVARYELDYDKMfdfsakktRESVEKSLK 130
Cdd:cd19073 14 DDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAesGVPREDLFITTKVWRDHLRPEDL--------KKSVDRSLE 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 131 LLGLDYVDVIQIHDIEFAKDldivINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19073 83 KLGTDYVDLLLIHWPNPTVP----LEETLGALKELKEAGKVKSIGVSNFTIELLEE 134
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
22-322 |
4.88e-20 |
|
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: 89.04 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANYGFDL--EEGIKTVHEAVKSGINYIDTAPWYGQgrSEEVLGLALKDVP--RESY 97
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYGPPKpdEERFAVLDAAFELGCTFWDTADIYGD--SEELIGRWFKQNPgkREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 98 YIATKVARYELDYDKMF--DFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIG 175
Cdd:cd19144 79 FLATKFGIEKNVETGEYsvDGSPEYVKKACETSLKRLGVDYIDLYYQHRV----DGKTPIEKTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 176 VS------------AYPISVLKefltrtagrldtvLTYARYTLTDET-LLEYLDFFKSQNLGVICAAAHALGLLTNAGPQ 242
Cdd:cd19144 155 LSecsaetlrrahaVHPIAAVQ-------------IEYSPFSLDIERpEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 243 PWH-PASDEQKAIARKASE--------------VCKERGVELGKLAMYYTMSglpEVSTFLTGMQTRQLLRI--NLDANE 305
Cdd:cd19144 222 PDDfEEGDFRRMAPRFQAEnfpknlelvdkikaIAKKKNVTAGQLTLAWLLA---QGDDIIPIPGTTKLKRLeeNLGALK 298
|
330
....*....|....*..
gi 66772279 306 VGLSDKEQEVLRYLKEN 322
Cdd:cd19144 299 VKLTEEEEKEIREIAEE 315
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
31-186 |
6.31e-20 |
|
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: 87.70 E-value: 6.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGggalcaNYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYel 108
Cdd:cd19140 5 GVRIPALGLG------TYPLTGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAAsgVPRDELFLTTKVWPD-- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 109 dydkmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19140 74 ------NYSPDDFLASVEESLRKLRTDYVDLLLLH----WPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE 141
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
22-189 |
1.01e-18 |
|
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: 85.59 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGggaLCANYGFDLEEGI--KTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDV--PRESY 97
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLG---TWSTFSTAISEEQaeEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKgwKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 98 YIATKVARYELDYDKmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19142 78 IVSTKIYWSYGSEER--GLSRKHIIESVRASLRRLQLDYIDIVIIHKA----DPMCPMEEVVRAMSYLIDNGLIMYWGTS 151
|
170
....*....|...
gi 66772279 178 AY-PISVLKEFLT 189
Cdd:cd19142 152 RWsPVEIMEAFSI 164
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
53-177 |
1.92e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 84.31 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTV-HEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPRESYYIATKVAryeldyDKMFDFSAKKTRESVEKSLKL 131
Cdd:cd19103 31 EDTLKAVfDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPREDYIISTKFT------PQIAGQSADPVADMLEGSLAR 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 66772279 132 LGLDYVDVIQIH---DIEfakdldivinETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19103 105 LGTDYIDIYWIHnpaDVE----------RWTPELIPLLKSGKVKHVGVS 143
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
36-189 |
2.87e-18 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 83.76 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 36 KVSFGGGALCANYGFDLEEGIKTVHEAVKS-GINYIDTAPWYGQGRSEEVLGLAlkDVPRESYYIATKVAryeldYDKMF 114
Cdd:cd19075 2 KIILGTMTFGSQGRFTTAEAAAELLDAFLErGHTEIDTARVYPDGTSEELLGEL--GLGERGFKIDTKAN-----PGVGG 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66772279 115 DFSAKKTRESVEKSLKLLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFLT 189
Cdd:cd19075 75 GLSPENVRKQLETSLKRLKVDKVDVFYLH----APDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVE 145
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
53-177 |
4.77e-18 |
|
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: 82.68 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDvPRESYYIATKV----ARYELdydkmfdfsakkTRESVEKS 128
Cdd:cd19138 29 AQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG-RRDKVFLVSKVlpsnASRQG------------TVRACERS 95
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 66772279 129 LKLLGLDYVDVIQIH---DIEFAkdldivinETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19138 96 LRRLGTDYLDLYLLHwrgGVPLA--------ETVAAMEELKKEGKIRAWGVS 139
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
53-189 |
8.98e-18 |
|
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: 81.67 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLK 130
Cdd:cd19157 24 SEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKEsgIPREELFITSKVWNADQGYDS--------TLKAFEASLE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 131 LLGLDYVDVIQIHDIEFAKDldiviNETLPTLEQLVKEGKARFIGVSAYPISVLKEFLT 189
Cdd:cd19157 93 RLGLDYLDLYLIHWPVKGKY-----KETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLA 146
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
63-303 |
2.22e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 81.22 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 63 VKSGINYIDTAPWYGQ-------GRSEEVLGLALKDVP-RESYYIATKV-ARYELDYDKMFDF---SAKKTRESVEKSLK 130
Cdd:cd19752 27 VAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRGnRDDVVIATKVgAGPRDPDGGPESPeglSAETIEQEIDKSLR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 131 LLGLDYVDVIQIHdiefAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEF--LTRTAGRLDTVLTYARYT--- 205
Cdd:cd19752 107 RLGTDYIDLYYAH----VDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERArqIARQQGWAEFSAIQQRHSylr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 206 -----------LTDETLLEYLDFFKsqNLGVICAAAHALGLLTNAG---PQPW-HPASDeqkAIARKASEVCKERGVELG 270
Cdd:cd19752 183 prpgadfgvqrIVTDELLDYASSRP--DLTLLAYSPLLSGAYTRPDrplPEQYdGPDSD---ARLAVLEEVAGELGATPN 257
|
250 260 270
....*....|....*....|....*....|...
gi 66772279 271 KLAMYYTMSGLPEVSTfLTGMQTRQLLRINLDA 303
Cdd:cd19752 258 QVVLAWLLHRTPAIIP-LLGASTVEQLEENLAA 289
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
51-177 |
2.99e-17 |
|
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: 79.93 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVAryeldydkMFDFSAKKTRESVEKS 128
Cdd:cd19133 21 DPEECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKsgIPREELFITTKLW--------IQDAGYEKAKKAFERS 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 66772279 129 LKLLGLDYVDVIQIH----DIEFAKDLdivinetlptLEQLVKEGKARFIGVS 177
Cdd:cd19133 90 LKRLGLDYLDLYLIHqpfgDVYGAWRA----------MEELYKEGKIRAIGVS 132
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
35-279 |
5.11e-17 |
|
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: 79.90 E-value: 5.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 35 SKVSFGGGALCANYgfDLEEGIKTVHEAVKSGINYIDTAP----WYGQGRSEEVLGLALKD-VPRESYYIATKVARYELD 109
Cdd:cd19082 1 SRIVLGTADFGTRI--DEEEAFALLDAFVELGGNFIDTARvygdWVERGASERVIGEWLKSrGNRDKVVIATKGGHPDLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 110 YDKMFDFSAKKTRESVEKSLKLLGLDYVDVIQIH-DiefakDLDIVINETLPTLEQLVKEGKARFIGVSAYpisvlkefl 188
Cdd:cd19082 79 DMSRSRLSPEDIRADLEESLERLGTDYIDLYFLHrD-----DPSVPVGEIVDTLNELVRAGKIRAFGASNW--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 189 trTAGRLDTVLTYAR-------------YTL--------TDETLL----EYLDFFKSQNLGVICAAAHALGLLTNAGPQP 243
Cdd:cd19082 145 --STERIAEANAYAKahglpgfaasspqWSLarpneppwPGPTLVamdeEMRAWHEENQLPVFAYSSQARGFFSKRAAGG 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 66772279 244 WHPASDEQK--------AIARKASEVCKERGVELGKLAMYYTMS 279
Cdd:cd19082 223 AEDDSELRRvyyseenfERLERAKELAEEKGVSPTQIALAYVLN 266
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
15-312 |
6.85e-17 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 80.42 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 15 DEAKVRRMEYRNLGKTGLQVSKVSFGggaLCANYGFD--LEEGIKTVHEAVKSGINYIDTAPWYG--QGRSEEVLGLALK 90
Cdd:PRK09912 6 NPERYGQMQYRYCGKSGLRLPALSLG---LWHNFGHVnaLESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 91 D---VPRESYYIATKvARYEL---DYDKmfDFSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQ 164
Cdd:PRK09912 83 EdfaAYRDELIISTK-AGYDMwpgPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRV----DENTPMEETASALAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 165 LVKEGKARFIGVSAYP-------ISVLKEFltrtagRLDTVLTYARYTL----TDETLLeyLDFFKSQNLGVICAAAHAL 233
Cdd:PRK09912 156 AVQSGKALYVGISSYSpertqkmVELLREW------KIPLLIHQPSYNLlnrwVDKSGL--LDTLQNNGVGCIAFTPLAQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 234 GLLT----NAGPQPWHPASDEQKAIA--------------RKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQ 295
Cdd:PRK09912 228 GLLTgkylNGIPQDSRMHREGNKVRGltpkmlteanlnslRLLNEMAQQRGQSMAQMALSWLLKD-ERVTSVLIGASRAE 306
|
330
....*....|....*...
gi 66772279 296 LLRINLDA-NEVGLSDKE 312
Cdd:PRK09912 307 QLEENVQAlNNLTFSTEE 324
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
51-225 |
1.20e-16 |
|
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: 78.71 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESVEKS 128
Cdd:cd19156 21 DGAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIREsgVPREEVFVTTKLWNSDQGYES--------TLAAFEES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 129 LKLLGLDYVDVIQIHDIEFAKDLDivineTLPTLEQLVKEGKARFIGVSAYPISVLKEFLT--RTAGRLDTVLTYAryTL 206
Cdd:cd19156 90 LEKLGLDYVDLYLIHWPVKGKFKD-----TWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKscKVAPMVNQIELHP--LL 162
|
170
....*....|....*....
gi 66772279 207 TDETLLEYLdffKSQNLGV 225
Cdd:cd19156 163 TQEPLRKFC---KEKNIAV 178
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
60-188 |
2.94e-16 |
|
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: 77.36 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 60 HEAV-----KSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLKLL 132
Cdd:cd19135 28 HEAVvyalkECGYRHIDTAKRYG---CEELLGKAIKEsgVPREDLFLTTKLWPSDYGYES--------TKQAFEASLKRL 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 133 GLDYVDVIQIH---DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19135 97 GVDYLDLYLLHwpdCPSSGKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLL 155
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
53-323 |
6.25e-16 |
|
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: 76.77 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVARYELdydkmfdfSAKKTRESVE 126
Cdd:cd19111 17 EEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWwlkngkLKREEVFITTKLPPVYL--------EFKDTEKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 127 KSLKLLGLDYVDVIQIH---------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISvlkefltrtagRLDT 197
Cdd:cd19111 86 KSLENLKLPYVDLYLIHhpcgfvnkkDKGERELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPR-----------QINK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 198 VLTYARyTLTDETLLEYLDFFKSQNLGVICAA------AHA-LGLLTNAGPQPWHPASD--EQKAIARKASEVCKERGVE 268
Cdd:cd19111 155 ILAYAK-VKPSNLQLECHAYLQQRELRKFCNKknivvtAYApLGSPGRANQSLWPDQPDllEDPTVLAIAKELDKTPAQV 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 66772279 269 LGKLAMYYTMSGLPEvstfltgMQTRQLLRINLDANEVGLSDKEQEVLRYLKENV 323
Cdd:cd19111 234 LLRFVLQRGTGVLPK-------STNKERIEENFEVFDFELTEEHFKKLKTLDRNM 281
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
24-177 |
4.05e-15 |
|
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: 74.79 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFG-----GGALCAnygfDLEEGIKTVheAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVPRES 96
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGtwvtfGSQISD----EVAEELVTL--AYENGINLFDTAEVYAAGKAEIVLGkiLKKKGWRRSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 97 YYIATKV---ARYELDYdkmfDFSAKKTRESVEKSLKLLGLDYVDVIqihdieFAK--DLDIVINETLPTLEQLVKEGKA 171
Cdd:cd19141 76 YVITTKIfwgGKAETER----GLSRKHIIEGLKASLERLQLEYVDIV------FANrpDPNTPMEEIVRAFTHVINQGMA 145
|
....*.
gi 66772279 172 RFIGVS 177
Cdd:cd19141 146 MYWGTS 151
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
49-177 |
5.02e-15 |
|
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: 74.24 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 49 GFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKvaryeLDYDKmfdFSAKKTR 122
Cdd:cd19116 21 LKDDEGVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREkiaegvVKREDLFITTK-----LWNSY---HEREQVE 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66772279 123 ESVEKSLKLLGLDYVDVIQIH---------DIEFAKDLDIVINETLPT---LEQLVKEGKARFIGVS 177
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHwpvafkennDSESNGDGSLSDIDYLETwrgMEDLVKLGLTRSIGVS 156
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
31-329 |
7.50e-15 |
|
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: 74.38 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFG----GGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVpRESYYIATKv 103
Cdd:cd19146 8 GVRVSPLCLGamsfGEAWKSMMGeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGewMASRGN-RDEMVLATK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 104 arYELDYDKMFDF---------SAKKTRESVEKSLKLLGLDYVDVIQIHDIEFAKDldivINETLPTLEQLVKEGKARFI 174
Cdd:cd19146 86 --YTTGYRRGGPIkiksnyqgnHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTS----IPELMQSLNHLVAAGKVLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 175 GVS---AYPISVLKEFlTRTAGRLDTVLTYARYTLTdetlleYLDFFKS-----QNLGVICAAAHALG---LLTNAGPQP 243
Cdd:cd19146 160 GVSdtpAWVVSKANAY-ARAHGLTQFVVYQGHWSAA------FRDFERDilpmcEAEGMALAPWGVLGqgqFRTEEEFKR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 244 --------WhPASDEQKAIARKASEVCKERGVELGKLAMYYTMSGLPEVSTFLTGMQTRQlLRINLDANEVGLSDKEQEV 315
Cdd:cd19146 233 rgrsgrkgG-PQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEH-LKGNIEALGISLSDEEIQE 310
|
330
....*....|....
gi 66772279 316 LrylkENVLtkPFD 329
Cdd:cd19146 311 I----EDAY--PFD 318
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
54-188 |
1.04e-14 |
|
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: 73.30 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 54 EGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYEldydkmfdfsAKKTRESVEKSLKL 131
Cdd:cd19117 28 EVAKAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDsgVPREEIFITTKLWCTW----------HRRVEEALDQSLKK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66772279 132 LGLDYVDVIQIH----------DIEFAKD--LDIVINE-----TLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19117 95 LGLDYVDLYLMHwpvpldpdgnDFLFKKDdgTKDHEPDwdfikTWELMQKLPATGKVKAIGVSNFSIKNLEKLL 168
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
53-225 |
1.46e-14 |
|
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: 72.47 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD--VPRESYYIATKVARYeldydkmfDFSAKKTRESVEKSLK 130
Cdd:cd19126 23 DETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIREsgVPREELFVTTKLWND--------DQRARRTEDAFQESLD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 131 LLGLDYVDVIQIHDIEFAKdldivINETLPTLEQLVKEGKARFIGVSAYPISVLKEFLT--RTAGRLDTVLTYARytLTD 208
Cdd:cd19126 92 RLGLDYVDLYLIHWPGKDK-----FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAhaDVVPAVNQVEFHPY--LTQ 164
|
170
....*....|....*..
gi 66772279 209 ETLLEYLdffKSQNLGV 225
Cdd:cd19126 165 KELRGYC---KSKGIVV 178
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
53-191 |
2.10e-14 |
|
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: 72.05 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLK 130
Cdd:cd19127 22 EETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRsgVDRSDIFVTTKLWISDYGYDK--------ALRGFDASLR 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 131 LLGLDYVDVIQIHdIEFAKDLDIVInETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRT 191
Cdd:cd19127 91 RLGLDYVDLYLLH-WPVPNDFDRTI-QAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDAT 149
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
24-312 |
2.42e-14 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 72.49 E-value: 2.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 24 YRNLGKTGLQVSKVSFGggaLCANYGFD--LEEGIKTVHEAVKSGINYIDTAPWYG--QGRSEEVLGLALK-DVP--RES 96
Cdd:cd19150 2 YRRCGKSGLKLPALSLG---LWHNFGDDtpLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILReDFAgyRDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 97 YYIATKvARYEL---DYDKMFdfSAKKTRESVEKSLKLLGLDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARF 173
Cdd:cd19150 79 LIISTK-AGYDMwpgPYGEWG--SRKYLLASLDQSLKRMGLDYVDIFYSHRF----DPDTPLEETMGALDHAVRSGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 174 IGVSAY-------PISVLKEFLTRTAGRLDTVLTYARYtLTDETLLEYLdffksQNLGV--ICAAAHALGLLTN------ 238
Cdd:cd19150 152 VGISSYspertreAAAILRELGTPLLIHQPSYNMLNRW-VEESGLLDTL-----QELGVgcIAFTPLAQGLLTDkylngi 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 239 -AGPQPWHPASDEQKAIA-------RKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDA-NEVGLS 309
Cdd:cd19150 226 pEGSRASKERSLSPKMLTeanlnsiRALNEIAQKRGQSLAQMALAWVLRD-GRVTSALIGASRPEQLEENVGAlDNLTFS 304
|
...
gi 66772279 310 DKE 312
Cdd:cd19150 305 ADE 307
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
57-188 |
4.68e-14 |
|
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: 71.41 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 57 KTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD-----VPRESYYIATKV-ARYEldydkmfdfsaKKTRESVEKSLK 130
Cdd:cd19121 29 AAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKEaiaggVKREDLFVTTKLwSTYH-----------RRVELCLDRSLK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 131 LLGLDYVDVIQIH----------DIEFAK------DLDIVIN--ETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19121 95 SLGLDYVDLYLVHwpvllnpngnHDLFPTlpdgsrDLDWDWNhvDTWKQMEKVLKTGKTKAIGVSNYSIPYLEELL 170
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
51-188 |
6.85e-14 |
|
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: 70.99 E-value: 6.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVarYELDYDKMfdfsakktRES 124
Cdd:cd19119 25 DRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRaiddgsIKREELFITTKV--WPTFYDEV--------ERS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 125 VEKSLKLLGLDYVDVIQIH-----------------------DIEFAKDLDIVinETLPTLEQLVKEGKARFIGVSAYPI 181
Cdd:cd19119 92 LDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgKTRYAASGDHI--TTYKQLEKIYLDGRAKAIGVSNYSI 169
|
....*..
gi 66772279 182 SVLKEFL 188
Cdd:cd19119 170 VYLERLI 176
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
59-188 |
6.88e-14 |
|
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: 70.84 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 59 VHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVARYELDydkmfdfsAKKTRESVEKSLKLL 132
Cdd:cd19125 30 VKTAIKEGYRHIDCAAIYG---NEKEIGKALKKlfedgvVKREDLFITSKLWCTDHA--------PEDVPPALEKTLKDL 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 133 GLDYVDVIQIH----------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFL 188
Cdd:cd19125 99 QLDYLDLYLIHwpvrlkkgahMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLL 164
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
31-177 |
9.93e-14 |
|
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: 69.99 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGggalcaNYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVARYEL 108
Cdd:cd19132 4 GTQIPAIGFG------TYPLKGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRsgVPREELFVTTKLPGRHH 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 109 DYDKmfdfsakkTRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIvinETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19132 75 GYEE--------ALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYV---EAWQALIEAREEGLVRSIGVS 132
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
22-321 |
1.21e-13 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 71.04 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGggalcaNYGFDLEEGIKTVHE----AVKSGINYIDTAPWY-------GQGRSEEVLGLALK 90
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLG------TMTFGEQNSEADAHAqldyAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 91 DV-PRESYYIATKVARYELDYDKMFD----FSAKKTRESVEKSLKLLGLDYVDVIQIH------------DIEFAKDLDI 153
Cdd:PRK10625 75 KRgSREKLIIASKVSGPSRNNDKGIRpnqaLDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklGYSWTDSAPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 154 V-INETLPTLEQLVKEGKARFIGVS-AYPISVLKEFLTRTAGRLDTVLTYAR-YTLTDET----LLEYldffkSQNLGV- 225
Cdd:PRK10625 155 VsLLETLDALAEQQRAGKIRYIGVSnETAFGVMRYLHLAEKHDLPRIVTIQNpYSLLNRSfevgLAEV-----SQYEGVe 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 226 -ICAAAHALGLLTNA---GPQPW------------HPASDEQKAIARKAsEVCKERGVELGKLAMYYTMSGlPEVSTFLT 289
Cdd:PRK10625 230 lLAYSCLAFGTLTGKylnGAKPAgarntlfsrftrYSGEQTQKAVAAYV-DIAKRHGLDPAQMALAFVRRQ-PFVASTLL 307
|
330 340 350
....*....|....*....|....*....|..
gi 66772279 290 GMQTRQLLRINLDANEVGLSdkeQEVLRYLKE 321
Cdd:PRK10625 308 GATTMEQLKTNIESLHLTLS---EEVLAEIEA 336
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
38-186 |
1.02e-12 |
|
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: 66.99 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 38 SFGGGAlcanYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVaryeldydKMFD 115
Cdd:cd19139 3 AFGLGT----FRLKDDVVIDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAEsgVPRDELFITTKI--------WIDN 67
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 116 FSAKKTRESVEKSLKLLGLDYVDVIQIHdiEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19139 68 LSKDKLLPSLEESLEKLRTDYVDLTLIH--WPSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDE 136
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
22-237 |
1.05e-12 |
|
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: 68.09 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFGGGALCANYGFD-LEEGIKTVheAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVPRESYY 98
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDeTAEDLLTV--AYEHGVNLFDTAEVYAAGKAERTLGniLKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 99 IATKV---ARYELDYdkmfDFSAKKTRESVEKSLKLLGLDYVDVIqihdieFAKDLD--IVINETLPTLEQLVKEGKARF 173
Cdd:cd19160 81 VTTKIywgGQAETER----GLSRKHIIEGLRGSLDRLQLEYVDIV------FANRSDpnSPMEEIVRAMTYVINQGMAMY 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 174 IGVSAYPISVLKEF--LTRTAGRLDTVLTYARYTL--TDETLLEYLDFFKSQNLGVICAAAHALGLLT 237
Cdd:cd19160 151 WGTSRWSAMEIMEAysVARQFNLIPPVCEQAEYHLfqREKVEMQLPELYHKIGVGSVTWSPLACGLIT 218
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
53-177 |
1.07e-12 |
|
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: 67.82 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD------VPRESYYIATKVARYELdydkmfdfSAKKTRESVE 126
Cdd:cd19154 25 AEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAElleegvVKREDLFITTKLWTHEH--------APEDVEEALR 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 66772279 127 KSLKLLGLDYVDVIQIH-------------DIEFAKDLDIVIN--ETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19154 94 ESLKKLQLEYVDLYLIHapaafkddegesgTMENGMSIHDAVDveDVWRGMEKVYDEGLTKAIGVS 159
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
22-306 |
2.29e-12 |
|
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: 67.03 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVSKVSFG-----GGALCAnygfDLEEGIKTVheAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVPR 94
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGtwvtfGGQITD----EMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGniIKKKGWRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 95 ESYYIATKV---ARYELDYdkmfDFSAKKTRESVEKSLKLLGLDYVDVIqihdieFAK--DLDIVINETLPTLEQLVKEG 169
Cdd:cd19158 75 SSLVITTKIfwgGKAETER----GLSRKHIIEGLKASLERLQLEYVDVV------FANrpDPNTPMEETVRAMTHVINQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 170 KARFIGVSAY-PISVLKEF-LTRTAGRLDTVLTYARYTL--TDETLLEYLDFFKSQNLGVICAAAHALGLLT---NAGPQ 242
Cdd:cd19158 145 MAMYWGTSRWsSMEIMEAYsVARQFNLIPPICEQAEYHMfqREKVEVQLPELFHKIGVGAMTWSPLACGIVSgkyDSGIP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 243 PWHPAS----------------DEQKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANEV 306
Cdd:cd19158 225 PYSRASlkgyqwlkdkilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRN-EGVSSVLLGASNAEQLMENIGAIQV 303
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
53-191 |
3.38e-12 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 65.86 E-value: 3.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALK--DVPRESYYIATKvaryeldydkMFDFSAKKTRESVEKSLK 130
Cdd:PRK11565 28 EEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKeaSVAREELFITTK----------LWNDDHKRPREALEESLK 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 66772279 131 LLGLDYVDVIQIHDIEFAKDLDIvinETLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRT 191
Cdd:PRK11565 95 KLQLDYVDLYLMHWPVPAIDHYV---EAWKGMIELQKEGLIKSIGVCNFQIHHLQRLIDET 152
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
22-306 |
4.21e-12 |
|
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo sapiens, Mus musculus, Mustela putorius, Rattus norvegicus, and Kvb1.1, Kvb1.2 from Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A3 (AKR6A3), A8 (AKR6A8), A10a (AKR6A10a), A13 (AKR6A13), A7 (AKR6A7) and A10b (AKR6A10b), respectively. KCAB1B, also called Shaker channel b-subunit 1(Kvb1), K(+) channel subunit beta-1, or Kv-beta-1, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It modulates action potentials via its effect on the pore-forming alpha subunits.
Pssm-ID: 381385 [Multi-domain] Cd Length: 323 Bit Score: 66.22 E-value: 4.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 22 MEYRNLGKTGLQVS------KVSFGGgalcaNYGFDLEEGIKTVheAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVP 93
Cdd:cd19159 1 MKYRNLGKSGLRVSclglgtWVTFGG-----QISDEVAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGsiIKKKGWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 94 RESYYIATKV---ARYELDYdkmfDFSAKKTRESVEKSLKLLGLDYVDVIqihdieFAK--DLDIVINETLPTLEQLVKE 168
Cdd:cd19159 74 RSSLVITTKLywgGKAETER----GLSRKHIIEGLKGSLQRLQLEYVDVV------FANrpDSNTPMEEIVRAMTHVINQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 169 GKARFIGVSAY-PISVLKEF-LTRTAGRLDTVLTYARYTLTDETLLEYL--DFFKSQNLGVICAAAHALGLLT----NAG 240
Cdd:cd19159 144 GMAMYWGTSRWsAMEIMEAYsVARQFNMIPPVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLACGIISgkygNGV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 241 PQPWHPA------------SDE---QKAIARKASEVCKERGVELGKLAMYYTMSGlPEVSTFLTGMQTRQLLRINLDANE 305
Cdd:cd19159 224 PESSRASlkcyqwlkerivSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRN-EGVSSVLLGSSTPEQLIENLGAIQ 302
|
.
gi 66772279 306 V 306
Cdd:cd19159 303 V 303
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
53-189 |
5.59e-12 |
|
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: 65.24 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVARYELDYDKMfdfsakktRESVE 126
Cdd:cd19128 14 SESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEifkdggVKREDLFITSKLWPTMHQPENV--------KEQLL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 127 KSLKLLGLDYVDVIQIH---------------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEFLT 189
Cdd:cd19128 83 ITLQDLQLEYLDLFLIHwplafdmdtdgdprdDNQIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLN 160
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
62-340 |
6.60e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 65.44 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 62 AVKSGINYIDTAPWYGqgRSEEVLG--LALKDVPRESYYIATK-----VARYELDYD--KMFDFSAKKTRESVEKSLKLL 132
Cdd:cd19098 44 AWAAGVRYFDAARSYG--RAEEFLGswLRSRNIAPDAVFVGSKwgytyTADWQVDAAvhEVKDHSLARLLKQWEETRSLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 133 GlDYVDVIQIHDIEFA----KDLDiVINEtlptLEQLVKEGKArfIGVSAYPIS---VLKEFLT--RTAGRL-DTVltYA 202
Cdd:cd19098 122 G-KHLDLYQIHSATLEsgvlEDAD-VLAA----LAELKAEGVK--IGLSLSGPQqaeTLRRALEieIDGARLfDSV--QA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 203 RYTLTDETLLEYLDFFKSQNLGVICAAAHALGLLTNAGPQPwhpasdEQKAIARKASEVCKERGVELGKLAMYYTMSgLP 282
Cdd:cd19098 192 TWNLLEQSAGEALEEAHEAGMGVIVKEALANGRLTDRNPSP------ELAPLMAVLKAVADRLGVTPDALALAAVLA-QP 264
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 283 EVSTFLTGMQTRQLLRINLDANEVGLSDKEQEVLRYLKEnvltkpfdwegnELEIYWA 340
Cdd:cd19098 265 FVDVVLSGAATPEQLRSNLRALDVSLDLELLAALADLAE------------PPEDYWA 310
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
57-198 |
1.32e-11 |
|
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: 63.78 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 57 KTVHEAVKSGINYIDTAPWYGqgrSEEVLG--LALKDVPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLKLLGL 134
Cdd:cd19130 27 RAVATALEVGYRHIDTAAIYG---NEEGVGaaIAASGIPRDELFVTTKLWNDRHDGDE--------PAAAFAESLAKLGL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66772279 135 DYVDVIQIHDIEFAKDLDIvinETLPTLEQLVKEGKARFIGVSAYpisvLKEFLTRTAGRLDTV 198
Cdd:cd19130 96 DQVDLYLVHWPTPAAGNYV---HTWEAMIELRAAGRTRSIGVSNF----LPPHLERIVAATGVV 152
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
46-188 |
5.95e-11 |
|
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: 62.29 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 46 ANYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD-------VPRESYYIATKVARYELDYDKMFdfsa 118
Cdd:cd19124 13 ASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlglvKSRDELFVTSKLWCSDAHPDLVL---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 119 kktrESVEKSLKLLGLDYVDVIQIH----------DIEFAKD--LDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:cd19124 86 ----PALKKSLRNLQLEYVDLYLIHwpvslkpgkfSFPIEEEdfLPFDIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQE 161
|
..
gi 66772279 187 FL 188
Cdd:cd19124 162 LL 163
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
30-189 |
6.55e-11 |
|
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: 62.25 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 30 TGLQVSKVSFGGGALCANYGfdleEGIKTVHEAVKSGINYIDTApWYGQGRSEevLGLALKD-------VPRESYYIATK 102
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKG----ETYAAVTKALDVGYRHLDCA-WFYLNEDE--VGDAVRDflkenpsVKREDLFICTK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 103 VARYELDYDKMfdfsakktRESVEKSLKLLGLDYVDVIQIH-----------DIEFAKDLDIVINETL-----PT---LE 163
Cdd:cd19122 78 VWNHLHEPEDV--------KWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrSPKLGPDGKYVILKDLtenpePTwraME 149
|
170 180
....*....|....*....|....*.
gi 66772279 164 QLVKEGKARFIGVSAYPISVLKEFLT 189
Cdd:cd19122 150 EIYESGKAKAIGVSNWTIPGLKKLLS 175
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
27-180 |
2.43e-10 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 60.61 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 27 LGKT-GLQVSKVSFG----GGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLG--LALKDVpRESYY 98
Cdd:cd19147 2 LSKTaGIRVSPLILGamsiGDAWSGFMGsMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGewMKSRKN-RDQIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 99 IATKVA----RYELDYDKMFDFSAKKTRE---SVEKSLKLLGLDYVDVIQIHDIEFAKDldivINETLPTLEQLVKEGKA 171
Cdd:cd19147 81 IATKFTtdykAYEVGKGKAVNYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYTTS----IEEVMDSLHILVQQGKV 156
|
....*....
gi 66772279 172 RFIGVSAYP 180
Cdd:cd19147 157 LYLGVSDTP 165
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
53-191 |
2.68e-10 |
|
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: 60.25 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALK--DVPRESYYIATKVARYELDYDKmfdfsakkTRESVEKSLK 130
Cdd:cd19134 24 DEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAasGIPRGELFVTTKLATPDQGFTA--------SQAACRASLE 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66772279 131 LLGLDYVDVIQIH--DIEFAKDLDivineTLPTLEQLVKEGKARFIGVSAYPISVLKEFLTRT 191
Cdd:cd19134 93 RLGLDYVDLYLIHwpAGREGKYVD-----SWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT 150
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
30-177 |
7.38e-10 |
|
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: 59.17 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 30 TGLQVSKVSFGGGALCANYG-FDLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLaLKDV----P--RESYYIATK 102
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNpTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLKL-LARFfrkyPeyADKVVLSVK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 66772279 103 VAryeLDYDKMF-DFSAKKTRESVEKSLKLLG-LDYVDVIQIHDIefakDLDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19077 80 GG---LDPDTLRpDGSPEAVRKSIENILRALGgTKKIDIFEPARV----DPNVPIEETIKALKELVKEGKIRGIGLS 149
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
59-257 |
7.87e-10 |
|
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: 58.96 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 59 VHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD-------VPRESYYIATKVaryeldydkmfdFSAKKTRESVEK---- 127
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQ---NQHEVGQALKEllkeepgVKREDLFITSKL------------WNNSHRPEYVEPaldd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 128 SLKLLGLDYVDVIQIH--------------------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKEf 187
Cdd:cd19118 91 TLKELGLDYLDLYLIHwpvafkptgdlnpltavptnGGEVDLDLSVSLVDTWKAMVELKKTGKVKSIGVSNFSIDHLQA- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 188 LTRTAGRLDTVLTYARYTLTDETllEYLDFFKSQNlgVICAAAHALGllTNAGPQPWHPASDEQKAIARK 257
Cdd:cd19118 170 IIEETGVVPAVNQIEAHPLLLQD--ELVDYCKSKN--IHITAYSPLG--NNLAGLPLLVQHPEVKAIAAK 233
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-238 |
1.26e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 58.37 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 47 NYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgRSEEVLGLALKDVPRESYY-----IATKVA--RYELDYDKMFdfsak 119
Cdd:cd19101 17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYG--PAEELIGEFRKRLRRERDAaddvqIHTKWVpdPGELTMTRAY----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 120 kTRESVEKSLKLLGLDYVDVIQIH--DIEFAKDLDivineTLPTLEQLVKEGKARFIGVSAYPISVLKEFLtrTAGrLDT 197
Cdd:cd19101 90 -VEAAIDRSLKRLGVDRLDLVQFHwwDYSDPGYLD-----AAKHLAELQEEGKIRHLGLTNFDTERLREIL--DAG-VPI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 66772279 198 VLTYARYTLTDETLLEYL-DFFKSQNLGVICAAAHALGLLTN 238
Cdd:cd19101 161 VSNQVQYSLLDRRPENGMaALCEDHGIKLLAYGTLAGGLLSE 202
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
51-177 |
2.10e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 57.67 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 51 DLEEGIKTVHEAVKSGINYIDTAPWYGQGRSEEVLGLALKDVPrESYYIATKV-ARYELDYDKMFDFSAKKTRESVEKSL 129
Cdd:PRK10376 38 DRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYP-DDLTIVTKVgARRGEDGSWLPAFSPAELRRAVHDNL 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 66772279 130 KLLGLDYVDVIQI---HDIEFAKDLDivINETLPTLEQLVKEGKARFIGVS 177
Cdd:PRK10376 117 RNLGLDVLDVVNLrlmGDGHGPAEGS--IEEPLTVLAELQRQGLVRHIGLS 165
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
57-204 |
3.20e-09 |
|
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: 57.42 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 57 KTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKDVPRESyyiatKVARYEL-DYDKMFDFSAKK--TRESVEKSLKLLG 133
Cdd:cd19123 29 QAVKQALEAGYRHIDCAAIYG---NEAEIGAALAEVFKEG-----KVKREDLwITSKLWNNSHAPedVLPALEKTLADLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 134 LDYVDVIQIH-------DIEFAKD-------LDIVINETLPTLEQLVKEGKARFIGVSAYpiSVLKefltrtagrLDTVL 199
Cdd:cd19123 101 LDYLDLYLMHwpvalkkGVGFPESgedllslSPIPLEDTWRAMEELVDKGLCRHIGVSNF--SVKK---------LEDLL 169
|
....*
gi 66772279 200 TYARY 204
Cdd:cd19123 170 ATARI 174
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
56-186 |
5.09e-09 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 56.19 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 56 IKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD--VPRESYYIATKVAryeldydkMFDFSAKKTRESVEKSLKLLG 133
Cdd:PRK11172 19 IDSVKTALELGYRAIDTAQIYD---NEAAVGQAIAEsgVPRDELFITTKIW--------IDNLAKDKLIPSLKESLQKLR 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 66772279 134 LDYVDVIQIHdiEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPISVLKE 186
Cdd:PRK11172 88 TDYVDLTLIH--WPSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQ 138
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
40-234 |
5.66e-09 |
|
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: 56.31 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 40 GGGALCAnYGF-----DLEEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD------VPRESYYIATKV----A 104
Cdd:cd19129 2 GSGAIPA-LGFgtlipDPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEvfkagkIRREDLFVTTKLwntnH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 105 RYEldydkmfdfsakKTRESVEKSLKLLGLDYVDVIQIHdIEFA-----------------KDLDIVINETLPTLEQLVK 167
Cdd:cd19129 78 RPE------------RVKPAFEASLKRLQLDYLDLYLIH-TPFAfqpgdeqdprdangnviYDDGVTLLDTWRAMERLVD 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 66772279 168 EGKARFIGVSAYPISVLKEFLtrTAGRLD-TVLTYARYTLTDETllEYLDFFKSQnlGVICAAAHALG 234
Cdd:cd19129 145 EGRCKAIGLSDVSLEKLREIF--EAARIKpAVVQVESHPYLPEW--ELLDFCKNH--GIVLQAFAPLG 206
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
59-177 |
3.38e-08 |
|
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: 54.31 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 59 VHEAVK----SGINYIDTAPWYGqgrSEEVLGLALKD-------VPRESYYIATKVaryeldydkmfdFSAKKTRESVE- 126
Cdd:cd19106 22 VKAAVKyaldAGYRHIDCAAVYG---NEQEVGEALKEkvgpgkaVPREDLFVTSKL------------WNTKHHPEDVEp 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 127 ---KSLKLLGLDYVDVIQIH--------DIEFAKDLDIVIN-------ETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19106 87 alrKTLKDLQLDYLDLYLIHwpyafergDNPFPKNPDGTIRydsthykETWKAMEKLVDKGLVKAIGLS 155
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
53-179 |
5.44e-08 |
|
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: 53.68 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 53 EEGIKTVHEAVKSGINYIDTAPWYgqgRSEEVLGLALKD------VPRESYYIATKVARyeldydkmfdfsAKKTRESVE 126
Cdd:cd19155 25 EEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKwidsgkVKREELFIVTKLPP------------GGNRREKVE 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66772279 127 K----SLKLLGLDYVDVIQIH-----------------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAY 179
Cdd:cd19155 90 KfllkSLEKLQLDYVDLYLIHfpvgslskeddsgkldpTGEHKQDYTTDLLDIWKAMEAQVDQGLTRSIGLSNF 163
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
30-214 |
1.39e-07 |
|
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: 52.45 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 30 TGLQVSKVSFGggalCanYGFDLEEGIKTVHEAVKSGINYIDTAPWYGQgrSEEV---LGLALKD--VPRESYYIATKVA 104
Cdd:cd19113 7 SGYKMPSVGFG----C--WKLDNATAADQIYQAIKAGYRLFDGAEDYGN--EKEVgegVNRAIDEglVKREELFLTSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 105 RyeldydkmfDFSAKKTRE-SVEKSLKLLGLDYVDVIQIH--------DIE-------FAKDLDIVINETLP------TL 162
Cdd:cd19113 79 N---------NFHDPKNVEtALNKTLSDLKLDYVDLFLIHfpiafkfvPIEekyppgfYCGDGDNFVYEDVPildtwkAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 66772279 163 EQLVKEGKARFIGVSAYPISVLKEFLtRTAGRLDTVLTYARYT-LTDETLLEY 214
Cdd:cd19113 150 EKLVDAGKIKSIGVSNFPGALILDLL-RGATIKPAVLQIEHHPyLQQPKLIEY 201
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
30-214 |
1.52e-07 |
|
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: 52.42 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 30 TGLQVSKVSFG----GGALCANygfdleegikTVHEAVKSGINYIDTAPWY------GQGrseevLGLALKD--VPRESY 97
Cdd:cd19115 9 SGYDMPLVGFGlwkvNNDTCAD----------QVYNAIKAGYRLFDGACDYgneveaGQG-----VARAIKEgiVKREDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 98 YIATKVARYELDYDKMfdfsakktRESVEKSLKLLGLDYVDVIQIH-----------------------DIEFAKDldiV 154
Cdd:cd19115 74 FIVSKLWNTFHDGERV--------EPICRKQLADWGIDYFDLFLIHfpialkyvdpavryppgwfydgkKVEFSNA---P 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66772279 155 INETLPTLEQLVKEGKARFIGVSAYpisvlkefltrTAGRLDTVLTYAR------------YtLTDETLLEY 214
Cdd:cd19115 143 IQETWTAMEKLVDKGLARSIGVSNF-----------SAQLLMDLLRYARirpatlqiehhpY-LTQPRLVKY 202
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
54-177 |
1.55e-07 |
|
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: 52.23 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 54 EGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVA----RYELdydkmfdfsakkTRE 123
Cdd:cd19108 28 KALEATKLAIDAGFRHIDSAYLYQ---NEEEVGQAIRSkiadgtVKREDIFYTSKLWctfhRPEL------------VRP 92
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 66772279 124 SVEKSLKLLGLDYVDVIQIH--------DIEFAKD------LDIV-INETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19108 93 ALEKSLKKLQLDYVDLYLIHfpvalkpgEELFPKDengkliFDTVdLCATWEAMEKCKDAGLAKSIGVS 161
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
61-190 |
2.46e-07 |
|
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: 51.72 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 61 EAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVarYELDYDKMfdfsakktRESVEKSLKLLGL 134
Cdd:cd19112 32 NAIKIGYRHFDCAADYK---NEKEVGEALAEafktglVKREDLFITTKL--WNSDHGHV--------IEACKDSLKKLQL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66772279 135 DYVDVIQIH-------------------DIEFAKDLDIVINETLPTLEQLVKEGKARFIGVSAYPIsvlkeFLTR 190
Cdd:cd19112 99 DYLDLYLVHfpvatkhtgvgttgsalgeDGVLDIDVTISLETTWHAMEKLVSAGLVRSIGISNYDI-----FLTR 168
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
31-189 |
9.21e-07 |
|
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: 49.86 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 31 GLQVSKVSFGggalcaNYGFDLEEGIKTVHEAVKSGINYIDTAPWYGqgrSEEVLGLALKD------VPRESYYIATKVA 104
Cdd:cd19114 1 GDKMPLVGFG------TAKIKANETEEVIYNAIKVGYRLIDGALLYG---NEAEVGRGIRKaiqeglVKREDLFIVTKLW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 105 RyeldydkmfDFSAKK-TRESVEKSLKLLGLDYVDVIQIHDIEFAKDLDIVIN---------------------ETLPTL 162
Cdd:cd19114 72 N---------NFHGKDhVREAFDRQLKDYGLDYIDLYLIHFPIPAAYVDPAENypflwkdkelkkfpleqspmqECWREM 142
|
170 180
....*....|....*....|....*..
gi 66772279 163 EQLVKEGKARFIGVSAYPISVLKEFLT 189
Cdd:cd19114 143 EKLVDAGLVRNIGIANFNVQLILDLLT 169
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
59-177 |
4.01e-06 |
|
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: 47.80 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 59 VHEAVKSGIN----YIDTAPWYgqgRSEEVLGLALKD------VPRESYYIATKVarYELDYDKmfdfsaKKTRESVEKS 128
Cdd:cd19107 19 VTEAVKVAIDagyrHIDCAYVY---QNENEVGEAIQEkikeqvVKREDLFIVSKL--WCTFHEK------GLVKGACQKT 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66772279 129 LKLLGLDYVDVIQIH--------DIEFAKD-------LDIVINETLPTLEQLVKEGKARFIGVS 177
Cdd:cd19107 88 LSDLKLDYLDLYLIHwptgfkpgKELFPLDesgnvipSDTTFLDTWEAMEELVDEGLVKAIGVS 151
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
59-225 |
9.83e-04 |
|
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: 40.33 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 59 VHEAVKSGINYIDTAPWYgQGRSEEVLGLALK----DVPRESYYIATKvaryeldydkMFDFSAKKT--RESVEKSLKLL 132
Cdd:cd19110 23 VKVAIDAGYRHFDCAYLY-HNESEVGAGIREKikegVVRREDLFIVSK----------LWCTCHKKSlvKTACTRSLKAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66772279 133 GLDYVDVIQIH----------DIEFAKDLDIVINET--LPT---LEQLVKEGKARFIGVSAYPISVLKEFLTRTAGRLDT 197
Cdd:cd19110 92 KLNYLDLYLIHwpmgfkpgepDLPLDRSGMVIPSDTdfLDTweaMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLRVKP 171
|
170 180 190
....*....|....*....|....*....|
gi 66772279 198 VLTY--ARYTLTDETLleyLDFFKSQNLGV 225
Cdd:cd19110 172 VTNQieCHPYLTQKKL---ISFCQSRNVSV 198
|
|
| |
