|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
6-315 |
3.89e-177 |
|
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: 492.07 E-value: 3.89e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMG---RRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLglgrSGCKVKIATKAAPMFGKTL 82
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGL----GERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 83 KPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPT 162
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 163 VYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKdgKNPESRFFGN-PFSQLYMDRYWKEEHFNGI 241
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNnALGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4105406 242 ALVEKALKttygPTAPSMISAAVRWMYHHSQLKGTQGDAVILGMSSLEQLEQNLALVEEGPLEPAVVDAFDQAW 315
Cdd:cd19075 235 EKVEEAAE----KEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-320 |
4.58e-63 |
|
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: 202.72 E-value: 4.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGR---RMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMF-----GKT 81
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRD--DVVIATKVGRRMgpgpnGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 82 LKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKknGWIMP 161
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 162 TVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqDKDGKNPEsrffGNPFSQLYMDRYWKEEHFngi 241
Cdd:COG0667 174 VAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKY---RRGATFPE----GDRAATNFVQGYLTERNL--- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 242 ALVE--KALKTTYGPTAPSMisaAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVEEgPLEPAVVDAFDQAWNLVA 319
Cdd:COG0667 244 ALVDalRAIAAEHGVTPAQL---ALAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAALAAVP 314
|
.
gi 4105406 320 H 320
Cdd:COG0667 315 A 315
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
6-296 |
1.11e-57 |
|
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: 185.80 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSE-TILGDLGLGLGRSgcKVKIATKAAPMFGKT--- 81
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSErLLGRWLKGRGNRD--DVVIATKGGHPPGGDpsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 82 --LKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWI 159
Cdd:cd06660 79 srLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 160 MPTVYQGMYNAITRQV-ETELFPCLRHFGLRFYAFNPLAGGLltgrykyqdkdgknpesrffgnpfsqlymdrywkeehf 238
Cdd:cd06660 159 GFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARGP-------------------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 4105406 239 NGIALvekalkttygptapsmisaavRWMYHHSqlkgtQGDAVILGMSSLEQLEQNLA 296
Cdd:cd06660 201 AQLAL---------------------AWLLSQP-----FVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
10-315 |
6.24e-52 |
|
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: 173.53 E-value: 6.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGlglgrSGC--KVKIATKAapmFGKTLKPAD- 86
Cdd:cd19087 18 LGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWI-----AGRrdDIVLATKV---FGPMGDDPNd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 87 -------VRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWI 159
Cdd:cd19087 90 rglsrrhIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 160 MPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdkdGKNPESRFFGNPFSQLYMDRYWKEEHFN 239
Cdd:cd19087 170 RFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKY------GKGKRPESGRLVERARYQARYGLEEYRD 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4105406 240 GI-ALVEKALKTTYGPtapsmISAAVRWMYHHSQLKgtqgdAVILGMSSLEQLEQNLALVEEgPLEPAVVDAFDQAW 315
Cdd:cd19087 244 IAeRFEALAAEAGLTP-----ASLALAWVLSHPAVT-----SPIIGPRTLEQLEDSLAALEI-TLTPELLAEIDELF 309
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
9-312 |
2.23e-51 |
|
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: 172.01 E-value: 2.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 9 VLGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVY-------ANGQSETILGDLGLglgRSGC--KVKIATK-AAPMF 78
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLK---SRGKrdRVVIATKvGFPMG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 79 --GKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKN 156
Cdd:cd19081 90 pnGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 157 GWIMPTVYQGMYNAITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFGnpfsqlymDRYWKE 235
Cdd:cd19081 170 GLPRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEAA--------KRYLNE 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4105406 236 EHFNGIALVEkALKTTYGpTAPSMIsaAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLAlVEEGPLEPAVVDAFD 312
Cdd:cd19081 242 RGLRILDALD-EVAAEHG-ATPAQV--ALAWLLARPGV-----TAPIAGARTVEQLEDLLA-AAGLRLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
9-315 |
3.36e-51 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 170.96 E-value: 3.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 9 VLGAMEMG---RRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGCKVKIATKAAPMFGKT---L 82
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPWpsgG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 83 KPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYvSWEVAEIctlCKKNGWIMPT 162
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNF-DAEQIEK---ALTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 163 VYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkYQDKDGKNPESRFFGNPFSQLYMDRYwkeEHFNGIA 242
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKY-TRDPDKGPGERRRLLKKGTPLNLEAL---EALEEIA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 243 lvekalkTTYGptaPSMISAAVRWMYHHSqlkgtQGDAVILGMSSLEQLEQNLAlVEEGPLEPAVVDAFDQAW 315
Cdd:pfam00248 234 -------KEHG---VSPAQVALRWALSKP-----GVTIPIPGASNPEQLEDNLG-ALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-299 |
7.41e-49 |
|
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: 165.01 E-value: 7.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMG----RRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATK------AAPMFG 79
Cdd:cd19084 9 LGTWAIGgtwwGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR-RD--DVVIATKcglrwdGGKGVT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 80 KTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwi 159
Cdd:cd19084 86 KDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 160 mPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFgnpfsqlymdRYWKEEHF- 238
Cdd:cd19084 161 -IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRF----------PFFRGENFe 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 239 NGIALVE--KALKTTYGPTAPSMisaAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVE 299
Cdd:cd19084 230 KNLEIVDklKEIAEKYGKSLAQL---AIAWTLAQPGV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
10-296 |
1.17e-47 |
|
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: 162.39 E-value: 1.17e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAM----EMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATKaapmFGKTLKPA 85
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN-RD--RIVLATK----YTMNRRPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 86 DVRFQ----------LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKK 155
Cdd:cd19080 88 DPNAGgnhrknlrrsVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 156 NGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYK--YQDKDGKNPESRFFGNPFSqlymDRYW 233
Cdd:cd19080 168 RGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQrgEEGRAGEAKGVTVGFGKLT----ERNW 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 234 KeehfngIALVEKALKTTYGPTAPSMisaAVRWMYHHSqlkgtQGDAVILGMSSLEQLEQNLA 296
Cdd:cd19080 244 A------IVDVVAAVAEELGRSAAQV---ALAWVRQKP-----GVVIPIIGARTLEQLKDNLG 292
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
6-299 |
2.16e-43 |
|
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: 151.61 E-value: 2.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRR---------MDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATKAAP 76
Cdd:cd19091 14 SELALGTMTFGGGggffgawggVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR-RD--DVLIATKVRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 77 MFGKTlkPADV---RFQL----ETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEI 149
Cdd:cd19091 91 RMGEG--PNDVglsRHHIiravEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 150 CTLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKyqdKDGKNPE-SRFFGNPFSQLY 228
Cdd:cd19091 169 LGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYR---RGQPAPEgSRLRRTGFDFPP 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 229 MDRywkeEHFNGI--ALVEKALKTtyGPTAPsmiSAAVRWMYHHSQLKGtqgdaVILGMSSLEQLEQNLALVE 299
Cdd:cd19091 246 VDR----ERGYDVvdALREIAKET--GATPA---QVALAWLLSRPTVSS-----VIIGARNEEQLEDNLGAAG 304
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
20-314 |
4.34e-43 |
|
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: 150.04 E-value: 4.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 20 DVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRsgcKVKIATKAAPMfgkTLKPADVRFQLETSLKRLQ 99
Cdd:cd19085 21 DDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRD---DVVIATKVSPD---NLTPEDVRKSCERSLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 100 CPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwimPTVYQGMYNAITRQVETEL 179
Cdd:cd19085 95 TDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 180 FPCLRHFGLRFYAFNPLAGGLLTGRYkyqDKDGKNPE----SRFFgnpfsQLYMDRYWKEEhFNGIALVeKALKTTYGPT 255
Cdd:cd19085 169 LPFCREHGIGVLAYSPLAQGLLTGKF---SSAEDFPPgdarTRLF-----RHFEPGAEEET-FEALEKL-KEIADELGVT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 4105406 256 apsMISAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVEEgPLEPAVVDAFDQA 314
Cdd:cd19085 239 ---MAQLALAWVLQQPGV-----TSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
16-296 |
3.27e-42 |
|
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: 147.74 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 16 GRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGckVKIATKAapMFGKTLKPAD-------VR 88
Cdd:cd19074 16 GGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRES--YVISTKV--FWPTGPGPNDrglsrkhIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 89 FQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMY 168
Cdd:cd19074 92 ESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 169 NAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdKDGKNPESR-FFGNPFSQLYMDRYWKEEHfngIALVE-- 245
Cdd:cd19074 172 NMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKY----RDGIPPPSRsRATDEDNRDKKRRLLTDEN---LEKVKkl 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 4105406 246 KALKTTYGPTAPSMisaAVRWMYHHSQLKgtqgdAVILGMSSLEQLEQNLA 296
Cdd:cd19074 245 KPIADELGLTLAQL---ALAWCLRNPAVS-----SAIIGASRPEQLEENVK 287
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
28-295 |
1.57e-37 |
|
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: 136.01 E-value: 1.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 28 VRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMFG--KTL---KPADVRFQLETSLKRLQCPR 102
Cdd:cd19083 39 VREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRN--EVVIATKGAHKFGgdGSVlnnSPEFLRSAVEKSLKRLNTDY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 103 VDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEictlCKKNGWImpTVYQGMYNAITRQVETELFPC 182
Cdd:cd19083 117 IDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE----ANKDGYV--DVLQGEYNLLQREAEEDILPY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 183 LRHFGLRFYAFNPLAGGLLTGRY----KYQDKDGKNPESRFFGNPFSQLyMDRYWKeehfngialvEKALKTTYGPTAPS 258
Cdd:cd19083 191 CVENNISFIPYFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKGERFSEN-LDKVDK----------LKSIADEKGVTVAH 259
|
250 260 270
....*....|....*....|....*....|....*..
gi 4105406 259 MISAavrWMYHHSQLkgtqgDAVILGMSSLEQLEQNL 295
Cdd:cd19083 260 LALA---WYLTRPAI-----DVVIPGAKRAEQVIDNL 288
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
10-299 |
3.02e-37 |
|
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: 135.40 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRR------MDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETIL-GDLGLGLGRSgcKVKIATKA-APM---- 77
Cdd:cd19079 17 LGCMSFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILgRALKEFAPRD--EVVIATKVyFPMgdgp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 78 FGKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNG 157
Cdd:cd19079 95 NGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 158 WIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKyqdKDGKNPESRFFGNPFSQLYMdrywKEEH 237
Cdd:cd19079 175 WTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWG---DTTERRRSTTDTAKLKYDYF----TEAD 247
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 238 FNGIALVEKALKTtygpTAPSMISAAVRWMYHHSqlkgtQGDAVILGMSSLEQLEQNLALVE 299
Cdd:cd19079 248 KEIVDRVEEVAKE----RGVSMAQVALAWLLSKP-----GVTAPIVGATKLEHLEDAVAALD 300
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
90-306 |
6.34e-36 |
|
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: 131.61 E-value: 6.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 90 QLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGwIMPTVYQGMYN 169
Cdd:cd19089 105 SLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 170 AITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdKDGKNPESRFFGNPFSQlymdrywKEEHFNGiALVEKALK 249
Cdd:cd19089 184 LLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAAESKFL-------TEEALTP-EKLEQLRK 251
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 250 TT-----YGPTAPSMisaAVRWmyhhsQLKGTQGDAVILGMSSLEQLEQNLALVEEGPLEPA 306
Cdd:cd19089 252 LNkiaakRGQSLAQL---ALSW-----VLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEE 305
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
67-312 |
8.31e-34 |
|
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: 126.53 E-value: 8.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 67 KVKIATKAA--------PMFGKT-LKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTP------------------IEE 119
Cdd:cd19094 69 KVVLATKVAgpgegitwPRGGGTrLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 120 TLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGG 199
Cdd:cd19094 149 QLEALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 200 LLTGryKYQDKDGKNPESRFfgNPFSQlYMDRYWKE---EHFNgiALVEKALKTTYGPTApsmisAAVRWMYHHSQLKGT 276
Cdd:cd19094 229 VLTG--KYLDGAARPEGGRL--NLFPG-YMARYRSPqalEAVA--EYVKLARKHGLSPAQ-----LALAWVRSRPFVTST 296
|
250 260 270
....*....|....*....|....*....|....*.
gi 4105406 277 qgdavILGMSSLEQLEQNLALVeEGPLEPAVVDAFD 312
Cdd:cd19094 297 -----IIGATTLEQLKENIDAF-DVPLSDELLAEID 326
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
40-314 |
1.67e-32 |
|
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: 122.70 E-value: 1.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 40 DTAFVYANGQSETI--LGDLGLGLGRSGckVKIATKAapMFGKTLKPADVRF--------QLETSLKRLQCPRVDLFYLH 109
Cdd:cd19143 49 DNAEVYANGQSEEImgQAIKELGWPRSD--YVVSTKI--FWGGGGPPPNDRGlsrkhiveGTKASLKRLQLDYVDLVFCH 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 110 FPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQ-VETELFPCLRHFGL 188
Cdd:cd19143 125 RPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 189 RFYAFNPLAGGLLTGRYkyqdKDGKNPESRFFGNPFSQLymdryWKEEHFNGIALVEKALKTTygPTAP----SMISAAV 264
Cdd:cd19143 205 GTTTWSPLASGLLTGKY----NNGIPEGSRLALPGYEWL-----KDRKEELGQEKIEKVRKLK--PIAEelgcSLAQLAI 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 4105406 265 RWMyhhsqLKGTQGDAVILGMSSLEQLEQNLALVEEGP-LEPAVVDAFDQA 314
Cdd:cd19143 274 AWC-----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEKIEAI 319
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-267 |
1.29e-31 |
|
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: 120.10 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRRM----DVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGcKVKIATKAA------PMFG 79
Cdd:cd19148 9 LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlewdegGEVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 80 KTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYvSWEVAE----ICTLckk 155
Cdd:cd19148 88 RNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNF-SPEQMEtfrkVAPL--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 156 ngwimpTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdkdgkNPESRFFGNPFSQLymDRYWKE 235
Cdd:cd19148 164 ------HTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKM--------TKDTKFEGDDLRRT--DPKFQE 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 4105406 236 EHFNG-IALVE--KAL-KTTYGptaPSMISAAVRWM 267
Cdd:cd19148 228 PRFSQyLAAVEelDKLaQERYG---KSVIHLAVRWL 260
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-296 |
2.70e-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: 119.24 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEM----GRRMDVTSSSASVRAfLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATKaapmFGKTLKPA 85
Cdd:cd19076 17 LGCMGMsafyGPADEEESIATLHRA-LELGVTFLDTADMYGPGTNEELLGKALKDR-RD--EVVIATK----FGIVRDPG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 86 D-----------VRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNyVSweVAEIctlcK 154
Cdd:cd19076 89 SgfrgvdgrpeyVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE-AS--ADTI----R 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 155 KNGWIMP-TVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDgknPESRFFG-NPFSQlymdry 232
Cdd:cd19076 162 RAHAVHPiTAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDL---PEDDFRRnNPRFQ------ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4105406 233 wkEEHF-NGIALVEK--ALKTTYGPTaPSMISAAvrWMYHhsqlkgtQGDAV--ILGMSSLEQLEQNLA 296
Cdd:cd19076 233 --GENFdKNLKLVEKleAIAAEKGCT-PAQLALA--WVLA-------QGDDIvpIPGTKRIKYLEENVG 289
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-295 |
3.62e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 118.93 E-value: 3.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 20 DVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLglgRSGCKVKIATKAAPMFGKT------LKPADVRFQLET 93
Cdd:cd19102 24 DDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK---GLRDRPIVATKCGLLWDEEgrirrsLKPASIRAECEA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 94 SLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTlckkngwIMP-TVYQGMYNAIT 172
Cdd:cd19102 101 SLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPiASLQPPYSLLR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 173 RQVETELFPCLRHFGLRFYAFNPLAGGLLTG-----RYKYQDKDGKNPESRFFGNPfsqlYMDRYwkeehfngIALVE-- 245
Cdd:cd19102 174 RGIEAEILPFCAEHGIGVIVYSPMQSGLLTGkmtpeRVASLPADDWRRRSPFFQEP----NLARN--------LALVDal 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 4105406 246 KALKTTYGPTAPSMisaAVRWMYHHSQLKGtqgdaVILGMSSLEQLEQNL 295
Cdd:cd19102 242 RPIAERHGRTVAQL---AIAWVLRRPEVTS-----AIVGARRPDQIDETV 283
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-299 |
2.63e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 113.58 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYA-------NGQSE-TILGDLGLGLGRSgcKVKIATKAAPM 77
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESErLIGRWLKDRGNRD--DVVIATKVGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 78 FGKT---------LKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAE 148
Cdd:cd19752 79 PRDPdggpespegLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 149 ICTLCKKNGWIMPTVYQ----------GMYNAITRQVETELFPCLR-HFGLRFYAFNPLAGGLLTgrykyqdkDGKNPES 217
Cdd:cd19752 159 ARQIARQQGWAEFSAIQqrhsylrprpGADFGVQRIVTDELLDYASsRPDLTLLAYSPLLSGAYT--------RPDRPLP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 218 RFFGNPFSQLYMdrywkeehfngiALVEKALKTTyGPTAPSMISAavrWMYHhsqlkGTQGDAVILGMSSLEQLEQNLAL 297
Cdd:cd19752 231 EQYDGPDSDARL------------AVLEEVAGEL-GATPNQVVLA---WLLH-----RTPAIIPLLGASTVEQLEENLAA 289
|
..
gi 4105406 298 VE 299
Cdd:cd19752 290 LD 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
6-294 |
5.65e-29 |
|
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: 113.14 E-value: 5.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMG-----RRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATKAAPMFG- 79
Cdd:cd19149 12 SVIGLGTWAIGggpwwGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR-RD--KVVLATKCGLRWDr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 80 ---------------KTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSW 144
Cdd:cd19149 89 eggsfffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 145 EVAEICtlckKNGWImpTVYQGMYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGRYKyqdkdgknPESRFFGNP 223
Cdd:cd19149 169 QIKEYV----KAGQL--DIIQEKYSMLDRGIEKELLPyCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAGD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4105406 224 fsQLYMDRYWKEEHFNGI-ALVE--KALKTTYGPTAPSMisaAVRWMYHhsqlkgtQGD--AVILGMSSLEQLEQN 294
Cdd:cd19149 234 --ARSGIPWFSPENREKVlALLEkwKPLCEKYGCTLAQL---VIAWTLA-------QPGitSALCGARKPEQAEEN 297
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
6-215 |
7.75e-28 |
|
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: 108.86 E-value: 7.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRRM--DVTSSSASVRAF---LQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMFgk 80
Cdd:cd19072 5 PVLGLGTWGIGGGMskDYSDDKKAIEALryaIELGINLIDTAEMYGGGHAEELVGKAIKGFDRE--DLFITTKVSPDH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 81 tLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGwim 160
Cdd:cd19072 81 -LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGP--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 161 PTVYQGMYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGRY------KYQDKDGKNP 215
Cdd:cd19072 157 IVANQVEYNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKgsplldEIAKKYGKTP 217
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-299 |
3.64e-27 |
|
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: 108.09 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEM----GRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRsgcKVKIATKAAPMFGKTLK-- 83
Cdd:cd19078 9 LGCMGMshgyGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRD---QVVIATKFGFKIDGGKPgp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 84 ------PADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSnyvswEVAE--------I 149
Cdd:cd19078 86 lgldsrPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGVetirrahaV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 150 CTLckkngwimpTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdkdgkNPESRFFGNPFSQLyM 229
Cdd:cd19078 161 CPV---------TAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKI--------DENTKFDEGDDRAS-L 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4105406 230 DRYWKEEHFNGIALVE--KALKTTYGPTaPSMISAAvrWMYHhsqlkgtQGDAV--ILGMSSLEQLEQNLALVE 299
Cdd:cd19078 223 PRFTPEALEANQALVDllKEFAEEKGAT-PAQIALA--WLLA-------KKPWIvpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
9-296 |
2.05e-26 |
|
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: 105.71 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 9 VLGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYAN----GQSE-TILGDLGLGLGRSgcKVKIATKAA-----PMF 78
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASErVIGEWLKSRGNRD--KVVIATKGGhpdleDMS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 79 GKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNyvsWEVAEIC---TLCKK 155
Cdd:cd19082 82 RSRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERIAeanAYAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 156 NGWIMPTVYQGMYNAITRQVETELFPCL-------RHF----GLRFYAFNPLAGGLLTGRYKYQDKDgknpesrffgnpf 224
Cdd:cd19082 159 HGLPGFAASSPQWSLARPNEPPWPGPTLvamdeemRAWheenQLPVFAYSSQARGFFSKRAAGGAED------------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 225 SQLYMDRYWKEEHFNGIALVeKALKTTYGpTAPSMISAAvrWMYHHSQlkgtQGDAVIlGMSSLEQLEQNLA 296
Cdd:cd19082 226 DSELRRVYYSEENFERLERA-KELAEEKG-VSPTQIALA--YVLNQPF----PTVPII-GPRTPEQLRDSLA 288
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-226 |
2.42e-26 |
|
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: 106.06 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 9 VLGAMEMG-------RRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSET-ILGDLGLGLGRSgcKVKIATKAAPMF-- 78
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETwIGEWMKSRKNRD--QIVIATKFTTDYka 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 79 GKTLKPADVRF----------QLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAE 148
Cdd:cd19147 92 YEVGKGKAVNYcgnhkrslhvSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4105406 149 ICTLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFGNPFSQ 226
Cdd:cd19147 172 ANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEERKKNGEGLRSFVGGTEQ 249
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
91-296 |
1.18e-22 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 96.60 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKngWIMP-TVYQGMYN 169
Cdd:PRK09912 120 LDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLRE--WKIPlLIHQPSYN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 170 AITRQVE-TELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRffGNPFSQLyMDRYWKEEHFNGIALVEKAL 248
Cdd:PRK09912 198 LLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRE--GNKVRGL-TPKMLTEANLNSLRLLNEMA 274
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 4105406 249 KTtygpTAPSMISAAVRWMyhhsqLKGTQGDAVILGMSSLEQLEQNLA 296
Cdd:PRK09912 275 QQ----RGQSMAQMALSWL-----LKDERVTSVLIGASRAEQLEENVQ 313
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
10-296 |
2.18e-22 |
|
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: 93.70 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRR----MDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgRSgcKVKIATKAAPMFGKTLK-- 83
Cdd:cd19086 8 FGTWGLGGDwwgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGR-RD--KVVIATKFGNRFDGGPErp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 84 ----PADVRFQLETSLKRLQCPRVDLFYLHFP-DHGTPIEETLQACHQLHQEGKFVELGlsnyVSWEVAEICTLCKKNGW 158
Cdd:cd19086 85 qdfsPEYIREAVEASLKRLGTDYIDLYQLHNPpDEVLDNDELFEALEKLKQEGKIRAYG----VSVGDPEEALAALRRGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 159 ImpTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRykyqdkdgknpesrffgnpfsqlymdrywkeehf 238
Cdd:cd19086 161 I--DVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK---------------------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 4105406 239 ngialvekalkttygptapsMISAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLA 296
Cdd:cd19086 205 --------------------LAQAALRFILSHPAV-----STVIPGARSPEQVEENAA 237
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
10-307 |
1.15e-21 |
|
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: 92.62 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRRMDvtSSSASVRAFLQRGHTEIDTAFVYanGQSETILGDLGLGLGRSGckVKIATKAAPMFGKTLK--PADV 87
Cdd:cd19090 10 LGGVFGGVDDD--EAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREP--LVLSTKVGRLPEDTADysADRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 88 RFQLETSLKRLQCPRVDLFYLHFPDHGTP-----IEETLQACHQLHQEGKFVELGLSnyvSWEVAEICTLCKKNGWIMPT 162
Cdd:cd19090 84 RRSVEESLERLGRDRIDLLMIHDPERVPWvdilaPGGALEALLELKEEGLIKHIGLG---GGPPDLLRRAIETGDFDVVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 163 VYQGmYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFGNPFSQLYMdryWKEEHfnGI 241
Cdd:cd19090 161 TANR-YTLLDQSAADELLPaAARH-GVGVINASPLGMGLLAGRPPERVRYTYRWLSPELLDRAKRLYE---LCDEH--GV 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4105406 242 ALVEkalkttygptapsmisAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVeEGPLEPAV 307
Cdd:cd19090 234 PLPA----------------LALRFLLRDPRI-----STVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
26-296 |
1.49e-21 |
|
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: 92.68 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGcKVKIATKAAPMFGkTLKPADVRFQLETSLKRLQCPRVDL 105
Cdd:cd19093 30 AAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKFAPLPW-RLTRRSVVKALKASLERLGLDSIDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 106 FYLHFPDH-GTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGwIMPTVYQGMYNAITRQVET-ELFPCL 183
Cdd:cd19093 108 YQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQnGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 184 RHFGLRFYAFNPLAGGLLTGRYkyqdkdgkNPESRfFGNPFSQLYMDRYWKEehfngIALVEKALK---TTYGPTapsMI 260
Cdd:cd19093 187 DELGITLIAYSPLAQGLLTGKY--------SPENP-PPGGRRRLFGRKNLEK-----VQPLLDALEeiaEKYGKT---PA 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 4105406 261 SAAVRWMYHhsqlkgtQGDAVILGMSSLEQLEQNLA 296
Cdd:cd19093 250 QVALNWLIA-------KGVVPIPGAKNAEQAEENAG 278
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
91-298 |
1.51e-21 |
|
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: 92.85 E-value: 1.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGwiMPT-VYQGMYN 169
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG--TPClIHQPKYS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 170 AITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRY-KYQDKDGKNPESRFFGNPfSQLYMDRYWKEEHFNGIAlvekal 248
Cdd:cd19151 185 MFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYlNGIPEDSRAAKGSSFLKP-EQITEEKLAKVRRLNEIA------ 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 4105406 249 kTTYGPTAPSMisaAVRWMyhhsqLKGTQGDAVILGMSSLEQLEQNLALV 298
Cdd:cd19151 258 -QARGQKLAQM---ALAWV-----LRNKRVTSVLIGASKPSQIEDAVGAL 298
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-199 |
3.85e-21 |
|
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: 92.10 E-value: 3.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMG----RRMDVTSSSASVR---AFLQRGHTEIDTAFVYANGQSET-ILGDLGLGLGRSgcKVKIATKAAPMFGKT 81
Cdd:cd19146 16 LGAMSFGeawkSMMGECDKETAFKlldAFYEQGGNFIDTANNYQGEESERwVGEWMASRGNRD--EMVLATKYTTGYRRG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 82 LK-PADVRFQ----------LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEIC 150
Cdd:cd19146 94 GPiKIKSNYQgnhakslrlsVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKAN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 4105406 151 TLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGG 199
Cdd:cd19146 174 AYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG 222
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
10-296 |
3.36e-20 |
|
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: 88.04 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAM------EMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgckVKIATKA------APM 77
Cdd:cd19088 6 YGAMrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDD---VVIATKGglvrtgPGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 78 FGKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAE---ICTLCk 154
Cdd:cd19088 83 WGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEaraIVRIV- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 155 kngwimpTVyQGMYNAITRQVETELFPCLRHfGLRFYAFNPLAGGLLtgrykyqdkdgknpesrffgnpfsqlymdrywk 234
Cdd:cd19088 162 -------SV-QNRYNLANRDDEGVLDYCEAA-GIAFIPWFPLGGGDL--------------------------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 235 eeHFNGIALVEKALKttYGPTaPSMIsaAVRWMYHHSqlkgtQGDAVILGMSSLEQLEQNLA 296
Cdd:cd19088 200 --AQPGGLLAEVAAR--LGAT-PAQV--ALAWLLARS-----PVMLPIPGTSSVEHLEENLA 249
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
91-295 |
7.56e-19 |
|
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: 85.19 E-value: 7.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNA 170
Cdd:cd19141 103 LKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 171 ITR-QVETELfPCLRH-FGLRFYAFNPLAGGLLTGRYkyqdKDGKNPESRffgnpfSQLYMDRYWKEEHFNGIALVEKAL 248
Cdd:cd19141 183 FQReKVEMQL-PELFHkIGVGAMTWSPLACGILSGKY----DDGVPEYSR------ASLKGYQWLKEKILSEEGRRQQAK 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 4105406 249 KTTYGPTAP----SMISAAVRWMyhhsqLKGTQGDAVILGMSSLEQLEQNL 295
Cdd:cd19141 252 LKELQIIADrlgcTLPQLAIAWC-----LKNEGVSSVLLGASSTEQLYENL 297
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
35-296 |
9.77e-19 |
|
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: 85.19 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 35 GHTEIDTAFVYanGQSETILGDLGLGLGRSGCKVKIATKaapmFGKTLKPAD-----------VRFQLETSLKRLQCPRV 103
Cdd:cd19144 47 GCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATK----FGIEKNVETgeysvdgspeyVKKACETSLKRLGVDYI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 104 DLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTlckkngwIMP-TVYQGMYNAITRQVET---EL 179
Cdd:cd19144 121 DLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-------VHPiAAVQIEYSPFSLDIERpeiGV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 180 FPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKdgknpesrFFGNPFsQLYMDRYWKEEHFNGIALVE--KALKTTYGPTaP 257
Cdd:cd19144 194 LDTCRELGVAIVAYSPLGRGFLTGAIRSPDD--------FEEGDF-RRMAPRFQAENFPKNLELVDkiKAIAKKKNVT-A 263
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 4105406 258 SMISAAvrWMYhhsqlkgTQGDAV--ILGMSSLEQLEQNLA 296
Cdd:cd19144 264 GQLTLA--WLL-------AQGDDIipIPGTTKLKRLEENLG 295
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
35-296 |
1.65e-18 |
|
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: 84.41 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 35 GHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKaapmFGKTLK----------PADVRFQLETSLKRLQCPRVD 104
Cdd:cd19145 46 GVTFLDTSDIYGPNTNEVLLGKALKDGPRE--KVQLATK----FGIHEIggsgvevrgdPAYVRAACEASLKRLDVDYID 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 105 LFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNyvswevAEICTLCKKNGwIMP-TVYQGMYNAITRQVETELFPCL 183
Cdd:cd19145 120 LYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE------ASADTIRRAHA-VHPiTAVQLEWSLWTRDIEEEIIPTC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 184 RHFGLRFYAFNPLAGGLLTGRYKYQdkdgKNPESRFFGNPFSqlymdRYWKE--EHFNGIALVEKALKTTYGPTaPSMIs 261
Cdd:cd19145 193 RELGIGIVPYSPLGRGFFAGKAKLE----ELLENSDVRKSHP-----RFQGEnlEKNKVLYERVEALAKKKGCT-PAQL- 261
|
250 260 270
....*....|....*....|....*....|....*..
gi 4105406 262 aAVRWMYHhsqlkgtQGDAV--ILGMSSLEQLEQNLA 296
Cdd:cd19145 262 -ALAWVLH-------QGEDVvpIPGTTKIKNLNQNIG 290
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
26-201 |
5.38e-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: 82.30 E-value: 5.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQSETILGDLGlglgrSGC--KVKIATKAAPMfgkTLKPADVRFQLETSLKRLQCPRV 103
Cdd:cd19138 33 EALRAGIDLGMTLIDTAEMYGDGGSEELVGEAI-----RGRrdKVFLVSKVLPS---NASRQGTVRACERSLRRLGTDYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 104 DLFYLHFPDhGTPIEETLQACHQLHQEGKFVELGLSNYvswEVAEICTLCKKNGWIMPTVYQGMYNAITRQVETELFPCL 183
Cdd:cd19138 105 DLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNF---DTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWC 180
|
170
....*....|....*....
gi 4105406 184 RHFGLRFYAFNPLA-GGLL 201
Cdd:cd19138 181 REHGVPVMAYSPLAqGGLL 199
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
91-299 |
2.95e-17 |
|
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: 80.96 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKngWIMPT-VYQGMYN 169
Cdd:cd19150 107 LDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRE--LGTPLlIHQPSYN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 170 AITRQVE-TELFPCLRHFGLRFYAFNPLAGGLLTGRYKyqdkdGKNPESrffgnpfSQLYMDRYWKEEHFNGIALVE-KA 247
Cdd:cd19150 185 MLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG-------SRASKERSLSPKMLTEANLNSiRA 252
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 4105406 248 LKTTYGPTAPSMISAAVRWMyhhsqLKGTQGDAVILGMSSLEQLEQNLALVE 299
Cdd:cd19150 253 LNEIAQKRGQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-298 |
4.35e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 79.17 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRRmdvtsSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMFGKTlKPADVRF 89
Cdd:cd19105 18 FGGGGLPRE-----SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRD--KVFLATKASPRLDKK-DKAELLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 90 QLETSLKRLQCPRVDLFYLHFPDHGTPI---EETLQACHQLHQEGKFVELGLS-NYVSWEVAEicTLCKKNGW--IMPTv 163
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFStHDNMAEVLQ--AAIESGWFdvIMVA- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 164 yqgmYNAITRQVE-TELFP-CLRHfGLRFYAFNPLAGGlltgryKYQDKDGKNPESRFFGNPfsqlymdrywkeehfngi 241
Cdd:cd19105 167 ----YNFLNQPAElEEALAaAAEK-GIGVVAMKTLAGG------YLQPALLSVLKAKGFSLP------------------ 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 4105406 242 alvekalkttygptapsmiSAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALV 298
Cdd:cd19105 218 -------------------QAALKWVLSNPRV-----DTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
26-141 |
4.46e-17 |
|
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: 79.24 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANgQSETILGDLGLGLGRSgcKVKIATKAAPMFgktLKPADVRFQLETSLKRLQCPRVDL 105
Cdd:cd19073 18 NAVKEALELGYRHIDTAEIYNN-EAEVGEAIAESGVPRE--DLFITTKVWRDH---LRPEDLKKSVDRSLEKLGTDYVDL 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 4105406 106 FYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19073 92 LLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNF 127
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
40-312 |
6.75e-16 |
|
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: 77.05 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 40 DTAFVYANGQSETILGDLGLGLGRSGCKVKIATK----AAPMFGKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGT 115
Cdd:cd19158 49 DTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKifwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 116 PIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQ-VETELFPCLRHFGLRFYAFN 194
Cdd:cd19158 129 PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWS 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 195 PLAGGLLTGRYkyqdKDGKNPESRFFGNPFsQLYMDRYWKEEHFNGIALVE--KALKTTYGPTAPSMisaAVRWMyhhsq 272
Cdd:cd19158 209 PLACGIVSGKY----DSGIPPYSRASLKGY-QWLKDKILSEEGRRQQAKLKelQAIAERLGCTLPQL---AIAWC----- 275
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 4105406 273 LKGTQGDAVILGMSSLEQLEQNLALVEEGP-LEPAVVDAFD 312
Cdd:cd19158 276 LRNEGVSSVLLGASNAEQLMENIGAIQVLPkLSSSIVHEID 316
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
33-312 |
1.03e-15 |
|
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: 76.62 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 33 QRGHTEIDTAFVYANGQSETILGDLGLGLGRSGCKVKIATK----AAPMFGKTLKPADVRFQLETSLKRLQCPRVDLFYL 108
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKlywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 109 HFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQ-VETELfPCLRH-F 186
Cdd:cd19159 122 NRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQL-PELYHkI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 187 GLRFYAFNPLAGGLLTGRYkyqdkDGKNPESRFFGNPFSQLYMDRYWKEEHFNGIALVEK--ALKTTYGPTAPSMisaAV 264
Cdd:cd19159 201 GVGAMTWSPLACGIISGKY-----GNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDlsPIAERLGCTLPQL---AV 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 4105406 265 RWMyhhsqLKGTQGDAVILGMSSLEQLEQNLALVEEGP-LEPAVVDAFD 312
Cdd:cd19159 273 AWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEID 316
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
10-301 |
1.24e-15 |
|
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: 75.29 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEM----GRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMFGKTlkPA 85
Cdd:cd19096 5 FGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPRE--KFYLATKLPPWSVKS--AE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 86 DVRFQLETSLKRLQCPRVDLFYLHFPDHGT---------PIEETLQAchqlHQEGKFVELGLSNYVSWEVaeICTLCKKN 156
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLNSPEwlekarkggLLEFLEKA----KKEGLIRHIGFSFHDSPEL--LKEILDSY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 157 GWIMPTVYqgmYNAItRQVETELFPCLRH---FGLRFYAFNPLAGGLLtgrykyqdkdGKNPESRffgnpfsqlyMDRYW 233
Cdd:cd19096 155 DFDFVQLQ---YNYL-DQENQAGRPGIEYaakKGMGVIIMEPLKGGGL----------ANNPPEA----------LAILC 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4105406 234 KEEHfngialvekalkttygptapSMISAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVEEG 301
Cdd:cd19096 211 GAPL--------------------SPAEWALRFLLSHPEV-----TTVLSGMSTPEQLDENIAAADEF 253
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-297 |
2.39e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 75.32 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 21 VTSSSASVRAFLQ---RGHTEIDTAFVYanGQSETIL---GDLGLGLGRSGCKVKIATKAAPMFGK-TLKPADVRFQLET 93
Cdd:cd19101 19 IRDEDAAVRAMAAyvdAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVPDPGElTMTRAYVEAAIDR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 94 SLKRLQCPRVDLFYLHFPDHGTP-IEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTlckkNGwiMPTVY-QGMYNAI 171
Cdd:cd19101 97 SLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILD----AG--VPIVSnQVQYSLL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 172 TRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGRYKyqdkdGKNPESRFFGNPFSqLYMDRYWKEEhFNGIALVEKALKT 250
Cdd:cd19101 171 DRRPENGMAAlCEDH-GIKLLAYGTLAGGLLSEKYL-----GVPEPTGPALETRS-LQKYKLMIDE-WGGWDLFQELLRT 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 4105406 251 T------YGptaPSMISAAVRWMyhhsqLKGTQGDAVILGMSSLEQLEQNLAL 297
Cdd:cd19101 243 LkaiadkHG---VSIANVAVRWV-----LDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
10-296 |
1.78e-14 |
|
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: 71.88 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRrMDVTSSSASVRAFLQR----GHTEIDTAFVYanGQSETILGDLGLGLGRSgcKVKIATKA-----APMFGK 80
Cdd:cd19095 5 LGTSGIGR-VWGVPSEAEAARLLNTaldlGINLIDTAPAY--GRSEERLGRALAGLRRD--DLFIATKVgthgeGGRDRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 81 TLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYvsweVAEICTLCKKN--GW 158
Cdd:cd19095 80 DFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGD----GEELEAAIASGvfDV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 159 IMPTvyqgmYNAITRQVEtELFPCLRHFGLRFYAFNPLAGGLLTgrykyqdkdgknpeSRFFGNPFSQLYMDRYWKEEHF 238
Cdd:cd19095 156 VQLP-----YNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLR--------------RRVRRRPLYADYARRPEFAAEI 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 4105406 239 NGIALVEKALkttygptapsmisaavRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLA 296
Cdd:cd19095 216 GGATWAQAAL----------------RFVLSHPGV-----SSAIVGTTNPEHLEENLA 252
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
40-313 |
1.82e-14 |
|
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: 73.10 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 40 DTAFVYANGQSE-TILGDLGLGLGRSGCKV---KIATKAAPMFGKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGT 115
Cdd:cd19160 51 DTAEVYAAGKAErTLGNILKSKGWRRSSYVvttKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 116 PIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQ-VETELfPCLRH-FGLRFYAF 193
Cdd:cd19160 131 PMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQL-PELYHkIGVGSVTW 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 194 NPLAGGLLTGRYkyqdkDGKNPESrffgnpfSQLYMDRY-W-KEEHFNGIALVEKALKTTYGPTAPSM----ISAAVRWM 267
Cdd:cd19160 210 SPLACGLITGKY-----DGRVPDT-------CRAAVKGYqWlKEKVQSEEGKKQQAKVKELHPIADRLgctvAQLAIAWC 277
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 4105406 268 yhhsqLKGTQGDAVILGMSSLEQLEQNLALVEE-GPLEPAVVDAFDQ 313
Cdd:cd19160 278 -----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
39-314 |
2.06e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 72.93 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 39 IDTAFVYanGQSETILGDLGLGLgRSgcKVKIATKAAPmfgKTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIE 118
Cdd:COG1453 46 IDTARGY--GDSEEFLGKALKGP-RD--KVILATKLPP---WVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 119 ET------LQACHQLHQEGKFVELGLSNYVSWEVAEicTLCKKNGW--IMptvYQgmYNAI--TRQVETELFPCLRHFGL 188
Cdd:COG1453 118 KVlkpggaLEALEKAKAEGKIRHIGFSTHGSLEVIK--EAIDTGDFdfVQ---LQ--YNYLdqDNQAGEEALEAAAEKGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 189 RFYAFNPLAGGLLTgrykyqdkdgkNPESRFfgnpfsqlymdrywkeehfngIALVEKALkttygptapSMISAAVRWMY 268
Cdd:COG1453 191 GVIIMKPLKGGRLA-----------NPPEKL---------------------VELLCPPL---------SPAEWALRFLL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 4105406 269 HHSQLkgtqgDAVILGMSSLEQLEQNLALVEEG-PLEPAVVDAFDQA 314
Cdd:COG1453 230 SHPEV-----TTVLSGMSTPEQLDENLKTADNLePLTEEELAILERL 271
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
28-199 |
3.44e-14 |
|
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: 70.97 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 28 VRAFLQRGHTEIDTAFVYANGQS--ETILgdlglglgRSGCK---VKIATKAAPmfgKTLKPADVRFQLETSLKRLQCPR 102
Cdd:cd19071 20 VLAALEAGYRHIDTAAAYGNEAEvgEAIR--------ESGVPreeLFITTKLWP---TDHGYERVREALEESLKDLGLDY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 103 VDLFYLHFP------DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAITRQVE 176
Cdd:cd19071 89 LDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELHPYLQQKE 164
|
170 180
....*....|....*....|...
gi 4105406 177 TELFpCLRHfGLRFYAFNPLAGG 199
Cdd:cd19071 165 LVEF-CKEH-GIVVQAYSPLGRG 185
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
27-201 |
6.96e-14 |
|
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: 70.29 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPmfgKTLKPADVRFQLETSLKRLQCPRVDLF 106
Cdd:cd19137 31 LLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPRE--DLFIVTKVWP---TNLRYDDLLRSLQNSLRRLDTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 107 YLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKngwimPTVY-QGMYNAITRQVETE-LFPCLR 184
Cdd:cd19137 106 LIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-----PIVCnQVKYNLEDRDPERDgLLEYCQ 180
|
170
....*....|....*..
gi 4105406 185 HFGLRFYAFNPLAGGLL 201
Cdd:cd19137 181 KNGITVVAYSPLRRGLE 197
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
26-202 |
1.63e-13 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 69.31 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYAN----GqsETILgdlglglgRSGCK---VKIATKAAPMFgktLKPADVRFQLETSLKRL 98
Cdd:COG0656 22 AAVRTALEAGYRHIDTAAMYGNeegvG--EAIA--------ASGVPreeLFVTTKVWNDN---HGYDDTLAAFEESLERL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 99 QCPRVDLFYLHFPDHGtPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAITRQveTE 178
Cdd:COG0656 89 GLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ--RE 161
|
170 180
....*....|....*....|....*
gi 4105406 179 LFPCLRHFGLRFYAFNPLA-GGLLT 202
Cdd:COG0656 162 LLAFCREHGIVVEAYSPLGrGKLLD 186
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-141 |
3.44e-13 |
|
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: 68.74 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 9 VLGAMemgRRMDVTSSSASVRAF----LQRGHTEIDTAFVYANGQSETI--LGDLGLGLGRSgcKVKIATKAAPMFGKTL 82
Cdd:cd19092 10 VLGCM---RLADWGESAEELLSLieaaLELGITTFDHADIYGGGKCEELfgEALALNPGLRE--KIEIQTKCGIRLGDDP 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4105406 83 KPADVRF----------QLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19092 85 RPGRIKHydtskehilaSVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNF 153
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
10-295 |
4.23e-13 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 69.11 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYA-------NGQSET-ILGDLGLGLGRSgcKVKIATK-AAPMFG- 79
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetQGLTETyIGNWLAKRGSRE--KLIIASKvSGPSRNn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 80 -------KTLKPADVRFQLETSLKRLQCPRVDLFYLHFPDHGT-----------------PIEETLQACHQLHQEGKFVE 135
Cdd:PRK10625 96 dkgirpnQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsapavSLLETLDALAEQQRAGKIRY 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 136 LGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGRYkyqdKDGKNP 215
Cdd:PRK10625 176 IGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 216 E-------SRF--FGNPFSQLYMDRYwkeehfngIALVEKalkttYGPTAPSMISAAVRWMYHHSqlkgtqgdAVILGMS 286
Cdd:PRK10625 252 AgarntlfSRFtrYSGEQTQKAVAAY--------VDIAKR-----HGLDPAQMALAFVRRQPFVA--------STLLGAT 310
|
....*....
gi 4105406 287 SLEQLEQNL 295
Cdd:PRK10625 311 TMEQLKTNI 319
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
25-154 |
2.33e-12 |
|
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: 66.37 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 25 SASVRAFLQRGHTEIDTAFVYANGQS--ETILGDLGLGLGRSGcKVKIATKAAPMFgktLKPADVRFQLETSLKRLQCPR 102
Cdd:cd19111 20 RAAVDYALFVGYRHIDTALSYQNEKAigEALKWWLKNGKLKRE-EVFITTKLPPVY---LEFKDTEKSLEKSLENLKLPY 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4105406 103 VDLFYLHFP-------------DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCK 154
Cdd:cd19111 96 VDLYLIHHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-303 |
5.72e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 64.86 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 28 VRAFLQRGHTEIDTAFVYanGQSETILGDLGlglgRSGCKVKIATKAAPMFGKTLKPAD-VRFQLETSLKRLQCPRVDLF 106
Cdd:cd19097 32 LEYALKAGINTLDTAPAY--GDSEKVLGKFL----KRLDKFKIITKLPPLKEDKKEDEAaIEASVEASLKRLKVDSLDGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 107 YLHFPD----HGTPIEETLQachQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwimPTVYQGMYNAIT-RQVETELFP 181
Cdd:cd19097 106 LLHNPDdllkHGGKLVEALL---ELKKEGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNILDqRFLKSGLLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 182 CLRHFGLRFYA---FnpLAgGLLTgrykyQDKDGKNPESRFFGNPFSQLymDRYWKEehfNGIalvekalkttygptapS 258
Cdd:cd19097 177 KLKKKGIEIHArsvF--LQ-GLLL-----MEPDKLPAKFAPAKPLLKKL--HELAKK---LGL----------------S 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 4105406 259 MISAAVRWMYHHSQLkgtqgDAVILGMSSLEQLEQNLALVEEGPL 303
Cdd:cd19097 228 PLELALGFVLSLPEI-----DKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-215 |
2.05e-11 |
|
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: 63.51 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 11 GAMEMGRRMDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAAPMfGKTLKPADVRFQ 90
Cdd:cd19103 21 GDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPRE--DYIISTKFTPQ-IAGQSADPVADM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPdhgTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVyQGMYNA 170
Cdd:cd19103 98 LEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 4105406 171 ITRQVETE--LFPCLRHfGLRFYAFNPLAGGLLTGRYkyqdkDGKNP 215
Cdd:cd19103 174 LYRSSEEAgiLDYCKEN-GITFFAYMVLEQGALSGKY-----DTKHP 214
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
67-296 |
4.34e-11 |
|
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: 62.64 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 67 KVKIATKAAPMFGK---TLKPADVRFQLETSLKRLQCP-RVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNyV 142
Cdd:cd19077 73 KVVLSVKGGLDPDTlrpDGSPEAVRKSIENILRALGGTkKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSE-V 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 143 SWE-------VAEICTLckkngwimptvyQGMYNAITRQVET-ELFPCLRHFGLRFYAFNPLAGGLLTGRYKyQDKDGKN 214
Cdd:cd19077 152 SAEtirrahaVHPIAAV------------EVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIK-SLADIPE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 215 PESRffgnpfsqLYMDRYwKEEHFNG-IALVE--KALKTTYGPTAPSMISAAVRwmyhhsqlkgTQGDAVIL---GMSSL 288
Cdd:cd19077 219 GDFR--------RHLDRF-NGENFEKnLKLVDalQELAEKKGCTPAQLALAWIL----------AQSGPKIIpipGSTTL 279
|
....*...
gi 4105406 289 EQLEQNLA 296
Cdd:cd19077 280 ERVEENLK 287
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
26-141 |
1.93e-10 |
|
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: 60.35 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQS--ETILgdlglglgRSGCK---VKIATKAAPmfgKTLKPADVRFQLETSLKRLQC 100
Cdd:cd19140 25 RAVEHALELGYRHIDTAQMYGNEAQvgEAIA--------ASGVPrdeLFLTTKVWP---DNYSPDDFLASVEESLRKLRT 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 4105406 101 PRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19140 94 DYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNF 134
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
20-141 |
3.25e-10 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 59.87 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 20 DVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAA-------PMFgkTLKPADVRFQLE 92
Cdd:cd19163 31 DEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIPRD--SYYLATKVGrygldpdKMF--DFSAERITKSVE 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 4105406 93 TSLKRLQCPRVDLFYLHFPDHGTP----IEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19163 107 ESLKRLGLDYIDIIQVHDIEFAPSldqiLNETLPALQKLKEEGKVRFIGITGY 159
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
26-154 |
5.00e-10 |
|
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: 59.73 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANgqsETILGDLGLGLGRSGcKVK-----IATKAAPMFgktLKPADVRFQLETSLKRLQC 100
Cdd:cd19154 29 TAVRTALKAGYRLIDTAFLYQN---EEAIGEALAELLEEG-VVKredlfITTKLWTHE---HAPEDVEEALRESLKKLQL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 101 PRVDLFYLHFP-----------------DHGTPI--EETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCK 154
Cdd:cd19154 102 EYVDLYLIHAPaafkddegesgtmengmSIHDAVdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR 174
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
25-202 |
6.48e-10 |
|
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: 58.80 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 25 SASVRAFLQRGHTEIDTAFVYANgqSETILGDLGLGLGRSGCK---VKIATKAAPmfgKTLKPADVRFQLETSLKRLQCP 101
Cdd:cd19136 18 RQAVDAALKAGYRLIDTASVYRN--EADIGKALRDLLPKYGLSredIFITSKLAP---KDQGYEKARAACLGSLERLGTD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 102 RVDLFYLHFP-----DHGTPIE-----ETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAi 171
Cdd:cd19136 93 YLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE----VPPAVNQVEFHP- 167
|
170 180 190
....*....|....*....|....*....|.
gi 4105406 172 tRQVETELFPCLRHFGLRFYAFNPLAGGLLT 202
Cdd:cd19136 168 -HLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
26-299 |
2.56e-09 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 57.62 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSgcKVKIATKAapmfGKTLKP-----------------ADVR 88
Cdd:cd19152 24 ATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELGRE--DYVISTKV----GRLLVPlqeveptfepgfwnplpFDAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 89 F---------QLETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGkFVEL------GLSNYVS-----WEVAE 148
Cdd:cd19152 98 FdysydgilrSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKGA-FRALeelreeGVIKAIGlgvndWEVIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 149 -ICTLCKKNgWIMptvYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTG-----RYKYQDKDGKNPESRffgn 222
Cdd:cd19152 177 rILEEADLD-WVM---LAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGgdnfdYYEYGPAPPELIARR---- 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4105406 223 pfsqlymDRYWK--EEHfnGIALVEKALKTTYGPtapsmisAAVRwmyhhsqlkgtqgdAVILGMSSLEQLEQNLALVE 299
Cdd:cd19152 249 -------DRIEAlcEQH--GVSLAAAALQFALAP-------PAVA--------------SVAPGASSPERVEENVALLA 297
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
24-165 |
3.75e-09 |
|
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: 56.47 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 24 SSASVRAFLQRGHTEIDTAFVYANgQSETILGDLGLGLGRSgcKVKIATKAAPmfgktlKPADVRFQLETSLKRLQCPRV 103
Cdd:cd19120 27 LVDSVKLALKAGFRHIDTAEMYGN-EKEVGEALKESGVPRE--DLFITTKVSP------GIKDPREALRKSLAKLGVDYV 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4105406 104 DLFYLHFP----DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQ 165
Cdd:cd19120 98 DLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQ 159
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-132 |
5.35e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 56.56 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 15 MGRRMDVTSSSA--SVRAFLQRGHTEIDTAFVYANGQSETI------LGDLGLGLGRSgcKVKIATKAAPMFGKTLKPAD 86
Cdd:cd19099 12 RGDSDDETDEEYreALKAALDSGINVIDTAINYRGGRSERLigkalrELIEKGGIKRD--EVVIVTKAGYIPGDGDEPLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 87 ------------------------------VRFQLETSLKRLQCPRVDLFYLHFPDHGTP----------IEETLQACHQ 126
Cdd:cd19099 90 plkyleeklgrglidvadsaglrhcispayLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefydrLEEAFEALEE 169
|
....*.
gi 4105406 127 LHQEGK 132
Cdd:cd19099 170 AVAEGK 175
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
27-196 |
6.46e-09 |
|
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: 56.20 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYANgqsETILGDLGLGLGRSGCkVK-----IATKaapMFGKTLKPADVRFQLETSLKRLQCP 101
Cdd:cd19125 29 AVKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLFEDGV-VKredlfITSK---LWCTDHAPEDVPPALEKTLKDLQLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 102 RVDLFYLHFP------DHG--------TPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGM 167
Cdd:cd19125 102 YLDLYLIHWPvrlkkgAHMpepeevlpPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVE 177
|
170 180
....*....|....*....|....*....
gi 4105406 168 YNAITRQveTELFPCLRHFGLRFYAFNPL 196
Cdd:cd19125 178 CHPGWQQ--DKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-296 |
7.40e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 55.18 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 10 LGAMEMGRrMDVTSSSASVRAFLQRGHTEIDTAFVYanGQSET-----ILGDlglglgRSgcKVKIATKaapmFGKTlKP 84
Cdd:cd19100 16 FGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEkigkaLKGR------RD--KVFLATK----TGAR-DY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 85 ADVRFQLETSLKRLQCPRVDLFYLHFPDHGTPIEET------LQACHQLHQEGKFVELGLSNYvSWEVAeicTLCKKNGW 158
Cdd:cd19100 80 EGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISGH-SPEVL---LRALETGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 159 I----MPTVYQGMYNaitRQVETELFP-CLRHfGLRFYAFNPLAGGLLTgrykyqdkdGKNPESrffgnpfsqlymdryw 233
Cdd:cd19100 156 FdvvlFPINPAGDHI---DSFREELLPlAREK-GVGVIAMKVLAGGRLL---------SGDPLD---------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4105406 234 keehfngialvekalkttygptapsmISAAVRWMYhhsQLKGTqgDAVILGMSSLEQLEQNLA 296
Cdd:cd19100 207 --------------------------PEQALRYAL---SLPPV--DVVIVGMDSPEELDENLA 238
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
6-304 |
7.49e-09 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 55.83 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRRMDVTSSSA--SVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGckVKIATKAA--PMFGKT 81
Cdd:cd19162 1 PRLGLGAASLGNLARAGEDEAaaTLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAE--YVVSTKVGrlLEPGAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 82 LKPADVRFQ-----------LETSLKRLQCPRVDLFYLHFPDHG--TPIEETLQACHQLHQEGKFVELGlsnyVSWEVAE 148
Cdd:cd19162 79 GRPAGADRRfdfsadgirrsIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIG----VGVTDWA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 149 ICT-LCKKNGW--IMPTvyqGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGrykyqdkdGKNPESRFFGNPFS 225
Cdd:cd19162 155 ALLrAARRADVdvVMVA---GRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT--------DDPAGDRYDYRPAT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4105406 226 QLYMDRywkeehfngiALVEKALKTTYGPTAPsmiSAAVRWMYHHSQLKgtqgdAVILGMSSLEQLEQNLALVEEGPLE 304
Cdd:cd19162 224 PEVLAR----------ARRLAAVCRRYGVPLP---AAALQFPLRHPAVA-----SVVVGAASPAELRDNLALLRTPIPA 284
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
27-198 |
9.76e-09 |
|
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: 55.61 E-value: 9.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYANgqSETILGDLGLGLGRSGCKVK---IATKAAPMFgktLKPADVRFQLETSLKRLQCPRV 103
Cdd:cd19128 19 AVKNAIKAGYRHIDCAYYYGN--EAFIGIAFSEIFKDGGVKREdlfITSKLWPTM---HQPENVKEQLLITLQDLQLEYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 104 DLFYLHFP-------------------DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPtvy 164
Cdd:cd19128 94 DLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCK----IKP--- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4105406 165 qgmynaITRQVETEL-FP-------CLRHfGLRFYAFNPLAG 198
Cdd:cd19128 167 ------FMNQIECHPyFQndklikfCIEN-NIHVTAYRPLGG 201
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
28-215 |
4.36e-08 |
|
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: 53.14 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 28 VRAFLQRGHTEIDTAFVYAN--GQSETILgdlglglgRSGCK---VKIATK---AAPMFGKTLKPadvrfqLETSLKRLQ 99
Cdd:cd19131 29 VREALEVGYRSIDTAAIYGNeeGVGKAIR--------ASGVPreeLFITTKlwnSDQGYDSTLRA------FDESLRKLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 100 CPRVDLFYLHFPdhgTPIE----ETLQACHQLHQEGKFVELGLSNYvswEVAEICTLCKKNGwIMPTVYQGMYNAITRQV 175
Cdd:cd19131 95 LDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNF---TIEHLQRLIDETG-VVPVVNQIELHPRFQQR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 4105406 176 ETELFpCLRHfGLRFYAFNPLA-GGLLTGRY--KYQDKDGKNP 215
Cdd:cd19131 168 ELRAF-HAKH-GIQTESWSPLGqGGLLSDPVigEIAEKHGKTP 208
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
26-141 |
1.12e-07 |
|
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: 51.97 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQS--ETILGdlglglgrSGCK---VKIATKAAPmfgKTLKPADVRFQLETSLKRLQC 100
Cdd:cd19139 18 DSVRTALELGYRHIDTAQIYDNEAAvgQAIAE--------SGVPrdeLFITTKIWI---DNLSKDKLLPSLEESLEKLRT 86
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 4105406 101 PRVDLFYLHFP--DHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19139 87 DYVDLTLIHWPspNDEVPVEEYIGALAEAKEQGLTRHIGVSNF 129
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
26-196 |
1.90e-07 |
|
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: 51.62 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQS--ETILGDLGLGLGRSGCKVKIATKaapMFGKTLKPADVRFQLETSLKRLQCPRV 103
Cdd:cd19106 24 AAVKYALDAGYRHIDCAAVYGNEQEvgEALKEKVGPGKAVPREDLFVTSK---LWNTKHHPEDVEPALRKTLKDLQLDYL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 104 DLFYLHFP---DHG----------------TPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVY 164
Cdd:cd19106 101 DLYLIHWPyafERGdnpfpknpdgtirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPAVL 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 4105406 165 qgmynaitrQVE-------TELFPCLRHFGLRFYAFNPL 196
Cdd:cd19106 177 ---------QVEchpylaqNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
27-199 |
2.39e-07 |
|
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: 51.24 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYANgqsETILGDLGLGLGRSGCKVKIATK---AAPMFGKTLKPadvrfqLETSLKRLQCPRV 103
Cdd:cd19157 29 AVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKvwnADQGYDSTLKA------FEASLERLGLDYL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 104 DLFYLHFPDHGTpIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAitRQVETELFPCL 183
Cdd:cd19157 100 DLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHP--RLTQKELRDYC 172
|
170
....*....|....*.
gi 4105406 184 RHFGLRFYAFNPLAGG 199
Cdd:cd19157 173 KKQGIQLEAWSPLMQG 188
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
23-201 |
2.93e-07 |
|
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: 50.79 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 23 SSSASVRAFLQRGHTEIDTAfvyangqsetilgdlglglGRSGC--KVKIATKAA-----PMFGKT-LKPAD-----VRF 89
Cdd:cd19135 27 SHEAVVYALKECGYRHIDTA-------------------KRYGCeeLLGKAIKESgvpreDLFLTTkLWPSDygyesTKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 90 QLETSLKRLQCPRVDLFYLHFPDHGTP-------IEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPT 162
Cdd:cd19135 88 AFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS----VVPH 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 4105406 163 VYQGMYNAITRQVetELFPCLRHFGLRFYAFNPLAGGLL 201
Cdd:cd19135 164 VNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA 200
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
7-141 |
3.14e-07 |
|
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: 51.00 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 7 ATVLGAMEMGRR----MDVTSSSASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLGRSGCKVKIATKAAPMFGKTL 82
Cdd:cd19153 14 PVGLGTAALGGVygdgLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRDSEF 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4105406 83 K-PAD-VRFQLETSLKRLQCPRVDLFYLH---FPDHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19153 94 DySAErVRASVATSLERLHTTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
26-196 |
4.08e-07 |
|
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: 50.60 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANgqsETILGDLGLGLGRSGcKVK-----IATKAaPMFGKtlKPADVRFQLETSLKRLQC 100
Cdd:cd19155 29 TAVDTALEAGYRHIDTAYVYRN---EAAIGNVLKKWIDSG-KVKreelfIVTKL-PPGGN--RREKVEKFLLKSLEKLQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 101 PRVDLFYLHFP---------------------DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwI 159
Cdd:cd19155 102 DYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR----I 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 4105406 160 MPTVYQGMYNAITRQVETELFpCLRHfGLRFYAFNPL 196
Cdd:cd19155 178 KPANLQVELHVYLQQKDLVDF-CSTH-SITVTAYAPL 212
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
91-295 |
6.84e-07 |
|
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: 50.16 E-value: 6.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 91 LETSLKRLQCPRVDLFYLHFPDHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKKNGWIMPTVYQGMYNA 170
Cdd:cd19142 103 VRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 171 ITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGRYKYQDKDGKNPESRFFGNPFSQLYMDRYWKEEHFNGIALVEKALK 249
Cdd:cd19142 183 FCREkMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSKYKVGSDGNGIHEETRRASHKLRELSLIA 262
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 4105406 250 TTYGPTapsMISAAVRWmyhhsQLKGTQGDAVILGMSSLEQLEQNL 295
Cdd:cd19142 263 ERLGCD---LTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQL 300
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
27-201 |
1.39e-06 |
|
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: 49.05 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYANGQSetilgdLGLGLGRSGCK---VKIATK---AAPMFGKTLKpadvrfQLETSLKRLQC 100
Cdd:cd19156 28 AVKWAIEAGYRHIDTAAIYKNEEG------VGQGIRESGVPreeVFVTTKlwnSDQGYESTLA------AFEESLEKLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 101 PRVDLFYLHFPDHGTPIeETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQgmynaitrqveTELF 180
Cdd:cd19156 96 DYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQ-----------IELH 159
|
170 180 190
....*....|....*....|....*....|
gi 4105406 181 PCLRHFGLRFY---------AFNPLAGGLL 201
Cdd:cd19156 160 PLLTQEPLRKFckekniaveAWSPLGQGKL 189
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
27-201 |
2.49e-06 |
|
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: 48.20 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYAN--GQSETILgdlglglgRSGC---KVKIATKaapMFGKTLKPADVRFQLETSLKRLQCP 101
Cdd:cd19126 28 AVQTALENGYRSIDTAAIYKNeeGVGEAIR--------ESGVpreELFVTTK---LWNDDQRARRTEDAFQESLDRLGLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 102 RVDLFYLHFPDHGTpIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAitRQVETELFP 181
Cdd:cd19126 97 YVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHP--YLTQKELRG 169
|
170 180
....*....|....*....|
gi 4105406 182 CLRHFGLRFYAFNPLAGGLL 201
Cdd:cd19126 170 YCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
27-199 |
7.16e-06 |
|
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: 46.80 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYAN----GQSetilgdlglgLGRSGCKVK---IATKaapmfgktLKPADVRFQ-----LETS 94
Cdd:cd19133 28 AVLEAIKAGYRLIDTAAAYGNeeavGRA----------IKKSGIPREelfITTK--------LWIQDAGYEkakkaFERS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 95 LKRLQCPRVDLFYLHFP---DHGtpieeTLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngwIMPTVYQGMYNAI 171
Cdd:cd19133 90 LKRLGLDYLDLYLIHQPfgdVYG-----AWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE----VKPAVNQIETHPF 160
|
170 180
....*....|....*....|....*...
gi 4105406 172 TRQVETELFpcLRHFGLRFYAFNPLAGG 199
Cdd:cd19133 161 NQQIEAVEF--LKKYGVQIEAWGPFAEG 186
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
26-165 |
8.81e-06 |
|
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: 46.51 E-value: 8.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYAN----GQ--SETIlgdlglglgRSGcKVK-----IATKaapMFGKTLKPADVRFQLETS 94
Cdd:cd19116 29 QAVKHAIEAGYRHIDTAYLYGNeaevGEaiREKI---------AEG-VVKredlfITTK---LWNSYHEREQVEPALRES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 95 LKRLQCPRVDLFYLHFP------------DHGTPIE----ETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkngw 158
Cdd:cd19116 96 LKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN---- 171
|
....*..
gi 4105406 159 IMPTVYQ 165
Cdd:cd19116 172 IKPAVNQ 178
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
26-315 |
8.93e-06 |
|
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: 46.87 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANGQSETILGDLGLGLgrsGCKVKIATKAApmfgktLKPAD-------VRFQLETSLKRL 98
Cdd:cd19104 36 AAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYITTKVR------LDPDDlgdiggqIERSVEKSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 99 QCPRVDLFYLH----------FPDHGTPI-----EETLQACHQLHQEGKFVELGLS------------------------ 139
Cdd:cd19104 107 KRDSVDLLQLHnrigderdkpVGGTLSTTdvlglGGVADAFERLRSEGKIRFIGITglgnppairelldsgkfdavqvyy 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 140 -------------NYVSWEVAEICTLCKKNGW-IMptvyqgmynaitrqvetelfpclrhfGLRfyafnPLAGGLLTGry 205
Cdd:cd19104 187 nllnpsaaearprGWSAQDYGGIIDAAAEHGVgVM--------------------------GIR-----VLAAGALTT-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 206 kyqDKDGKNPESRFFGNPFSQLYmDRywkeehfngiALVEKALKTTYGPTapsMISAAVRWMYHHSQLkgtqgDAVILGM 285
Cdd:cd19104 234 ---SLDRGREAPPTSDSDVAIDF-RR----------AAAFRALAREWGET---LAQLAHRFALSNPGV-----STVLVGV 291
|
330 340 350
....*....|....*....|....*....|
gi 4105406 286 SSLEQLEQNLALVEEGPLEPAVVDAFDQAW 315
Cdd:cd19104 292 KNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
26-141 |
1.60e-05 |
|
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: 45.86 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYANgQSEtILGDLGLGLGRSGCK---VKIATKaapMFGKTLKPADVRFQLETSLKRLQCPR 102
Cdd:cd19123 29 QAVKQALEAGYRHIDCAAIYGN-EAE-IGAALAEVFKEGKVKredLWITSK---LWNNSHAPEDVLPALEKTLADLQLDY 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 4105406 103 VDLFYLHFP---DHGT---------------PIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19123 104 LDLYLMHWPvalKKGVgfpesgedllslspiPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
20-200 |
2.10e-05 |
|
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: 45.53 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 20 DVTSSSASVRAFLQRGHTEIDTAFVYANGQS--ETILGDLGLGLGRSGcKVKIATKaapMFGKTLKPADVRFQLETSLKR 97
Cdd:cd19129 17 DPSATRNAVKAALEAGFRHFDCAERYRNEAEvgEAMQEVFKAGKIRRE-DLFVTTK---LWNTNHRPERVKPAFEASLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 98 LQCPRVDLFYLHFP--------------------DHGTPIEETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkng 157
Cdd:cd19129 93 LQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR--- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 4105406 158 wIMPTVYQgmYNAITRQVETELFPCLRHFGLRFYAFNPLAGGL 200
Cdd:cd19129 170 -IKPAVVQ--VESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
26-141 |
3.80e-05 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 44.63 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYAN----GQSetilgdlglgLGRSG---------CKVKIATKAApmfGKtLKPAdvrfqLE 92
Cdd:PRK11172 20 DSVKTALELGYRAIDTAQIYDNeaavGQA----------IAESGvprdelfitTKIWIDNLAK---DK-LIPS-----LK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 4105406 93 TSLKRLQCPRVDLFYLHF--PDHGTPIEETLQACHQLHQEGKFVELGLSNY 141
Cdd:PRK11172 81 ESLQKLRTDYVDLTLIHWpsPNDEVSVEEFMQALLEAKKQGLTREIGISNF 131
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
26-141 |
6.34e-05 |
|
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: 43.80 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 26 ASVRAFLQRGHTEIDTAFVYAN--GQSETILgdlglglgRSGC---KVKIATKAApmfGKTLKPADVRFQLETSLKRLQC 100
Cdd:cd19132 24 EAVVAALQAGYRLLDTAFNYENegAVGEAVR--------RSGVpreELFVTTKLP---GRHHGYEEALRTIEESLYRLGL 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 4105406 101 PRVDLFYLHFPDhgtPIE----ETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19132 93 DYVDLYLIHWPN---PSRdlyvEAWQALIEAREEGLVRSIGVSNF 134
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
6-201 |
6.64e-05 |
|
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: 43.69 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 6 PATVLGAMEMGRrmDVTSSSASvrAFLQRGHTEIDTAFVYANGQSetilgdLGLGLGRSGC---KVKIATK-AAPMFGKT 81
Cdd:cd19134 12 PVIGLGVGELSD--DEAERSVS--AALEAGYRLIDTAAAYGNEAA------VGRAIAASGIprgELFVTTKlATPDQGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 82 LKPADVRfqleTSLKRLQCPRVDLFYLHFP--DHGTPIeETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCkkngWI 159
Cdd:cd19134 82 ASQAACR----ASLERLGLDYVDLYLIHWPagREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 4105406 160 MPTVYQgmynaitrqveTELFPCLRHFGLRFY---------AFNPLAGGLL 201
Cdd:cd19134 153 TPAVNQ-----------IELHPLLNQAELRKVnaqhgivtqAYSPLGVGRL 192
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
35-150 |
1.54e-04 |
|
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: 42.99 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 35 GHTEIDTAFVYAN----GQSetilgdlglglGRSgckvKIA---TKAAPMFGKT------LKPADVRFQLETSLKRLQCP 101
Cdd:cd19108 40 GFRHIDSAYLYQNeeevGQA-----------IRS----KIAdgtVKREDIFYTSklwctfHRPELVRPALEKSLKKLQLD 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4105406 102 RVDLFYLHFP-------------DHGTPIEETLQACHqlhqegkfvelglsnyvSWEVAEIC 150
Cdd:cd19108 105 YVDLYLIHFPvalkpgeelfpkdENGKLIFDTVDLCA-----------------TWEAMEKC 149
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
28-199 |
2.75e-04 |
|
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: 42.10 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 28 VRAFLQRGHTEIDTAFVYangQSETILGDLGLGLGRSGcKVK-----IATKAAPMFGKtlkpaDVRFQLETSLKRLQCPR 102
Cdd:cd19119 33 VEAAIKEGYRHIDTAYAY---ETEDFVGEAIKRAIDDG-SIKreelfITTKVWPTFYD-----EVERSLDESLKALGLDY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 103 VDLFYLHFP--------DHGTPIE-----------------ETLQACHQLHQEGKFVELGLSNYVSWEVAEICTLCKkng 157
Cdd:cd19119 104 VDLLLVHWPvcfekdsdDSGKPFTpvnddgktryaasgdhiTTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECK--- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 4105406 158 wIMPTVYQGMYNAITRQVETELFpCLRHfGLRFYAFNPLAGG 199
Cdd:cd19119 181 -VVPAVNQVELHPHLPQMDLRDF-CFKH-GILVTAYSPLGSH 219
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
83-165 |
5.75e-04 |
|
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: 41.07 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 83 KPADVRFQLETSLKRLQCPRVDLFYLHFP------DHGTPI-----------------EETLQACHQLHQEGKFVELGLS 139
Cdd:cd19122 84 EPEDVKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYESGKAKAIGVS 163
|
90 100
....*....|....*....|....*.
gi 4105406 140 NYVSWEVAEICTLCKkngwIMPTVYQ 165
Cdd:cd19122 164 NWTIPGLKKLLSFAK----VKPHVNQ 185
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
27-111 |
1.89e-03 |
|
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: 39.40 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 27 SVRAFLQRGHTEIDTAFVYAN----GQSetilgdlglgLGRSGC---KVKIATKAAPMFGKtlkpaDVRFQLETSLKRLQ 99
Cdd:cd19117 32 AVEAALKAGYRHIDTAAIYGNeeevGQG----------IKDSGVpreEIFITTKLWCTWHR-----RVEEALDQSLKKLG 96
|
90
....*....|..
gi 4105406 100 CPRVDLFYLHFP 111
Cdd:cd19117 97 LDYVDLYLMHWP 108
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
32-141 |
2.78e-03 |
|
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: 38.74 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4105406 32 LQRGHTEIDTAFVYAN--GQSETILGDLGLglgRSgcKVKIATKaapMFGKTLKPADVRFQLETSLKRLQCPRVDLFYLH 109
Cdd:cd19130 33 LEVGYRHIDTAAIYGNeeGVGAAIAASGIP---RD--ELFVTTK---LWNDRHDGDEPAAAFAESLAKLGLDQVDLYLVH 104
|
90 100 110
....*....|....*....|....*....|....*.
gi 4105406 110 FPdhgTPIE----ETLQACHQLHQEGKFVELGLSNY 141
Cdd:cd19130 105 WP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNF 137
|
|
| |
