|
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 ... |
10-319 |
0e+00 |
|
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: 513.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMG---RRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLrlggSDCRVKIDTKAIPLFGNSL 86
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGL----GERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 87 KPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPT 166
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 167 VYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKngKQPVGRFFGNT-WAEMYRNRYWKEHHFEGI 245
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNNaLGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152114 246 ALVEKALQaaygASAPSMTSATLRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAAAEEGPLEPAVVDAFNQAW 319
Cdd:cd19075 235 EKVEEAAE----KEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
14-319 |
4.75e-64 |
|
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: 205.03 E-value: 4.75e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGR---RMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPLFGNS----- 85
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDD--VVIATKVGRRMGPGpngrg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 86 LKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsnGWILP 165
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 166 TVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKqpvgrffGNTWAEMYRNRYWKEHHFEGI 245
Cdd:COG0667 174 VAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPE-------GDRAATNFVQGYLTERNLALV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152114 246 ALVeKALQAAYGASAPSMtsAtLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAEEgPLEPAVVDAFNQAW 319
Cdd:COG0667 247 DAL-RAIAAEHGVTPAQL--A-LAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAAL 310
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
14-303 |
2.60e-57 |
|
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: 187.78 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGlrlggSDCR--VKIDTKA-------IPLFGN 84
Cdd:cd19087 18 LGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWI-----AGRRddIVLATKVfgpmgddPNDRGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 85 SLKpdSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIL 164
Cdd:cd19087 93 SRR--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 165 PTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKyedKNGKQPVGRFFGNtwaEMYRNRYWKEHHFEG 244
Cdd:cd19087 171 FVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYG---KGKRPESGRLVER---ARYQARYGLEEYRDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 41152114 245 IALVEkALQAAYGASAPSMTSAtlrWMYHHSQLQGAhgdavILGMSSLEQLEQNLAAAE 303
Cdd:cd19087 245 AERFE-ALAAEAGLTPASLALA---WVLSHPAVTSP-----IIGPRTLEQLEDSLAALE 294
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
10-300 |
1.20e-56 |
|
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: 183.49 E-value: 1.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcRVKIDTKAIPLFGNS---- 85
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRD-DVVIATKGGHPPGGDpsrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 86 -LKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIL 164
Cdd:cd06660 80 rLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 165 PTVYQGMYNAITRQV-ETELFPCLRHFGLRFYAFNPLAGGLltgkykyedkngkqpvgrffgntwaemyrnrywkehhfe 243
Cdd:cd06660 160 FAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARGP--------------------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 41152114 244 gialvekaLQAAygasapsmtsatLRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLA 300
Cdd:cd06660 201 --------AQLA------------LAWLLSQP-----FVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
13-316 |
2.85e-55 |
|
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: 182.41 E-value: 2.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 13 VLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYS-------EGQSETILGGLGLRLGGSDcRVKIDTK-AIPLFGN 84
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSawvpgnaGGESETIIGRWLKSRGKRD-RVVIATKvGFPMGPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 85 S--LKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGW 162
Cdd:cd19081 92 GpgLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 163 ILPTVYQGMYNAITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKqpvgrffgNTWAEMYRNRYWKEHH 241
Cdd:cd19081 172 PRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPG--------STRRGEAAKRYLNERG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152114 242 FEGIALVEkALQAAYGAsapSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAeEGPLEPAVVDAFN 316
Cdd:cd19081 244 LRILDALD-EVAAEHGA---TPAQVALAWLLARPGV-----TAPIAGARTVEQLEDLLAAA-GLRLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
13-319 |
1.11e-52 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 175.19 E-value: 1.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 13 VLGAMEMG---RRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGN---SL 86
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpsGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 87 KPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEIctlcKSNGWILPT 166
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA----LTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 167 VYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYrnrywkehhfEGIA 246
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----------EALE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 247 LVEKaLQAAYGAsapSMTSATLRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAAAeEGPLEPAVVDAFNQAW 319
Cdd:pfam00248 228 ALEE-IAKEHGV---SPAQVALRWALSKPG-----VTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
14-303 |
1.70e-52 |
|
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: 175.10 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAM----EMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGsdcRVKIDTKaiplFGNSLKPD 89
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRD---RIVLATK----YTMNRRPG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 90 ----------SLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKS 159
Cdd:cd19080 88 dpnaggnhrkNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 160 NGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyeDKNGKQPVGRFFGNTWAEMYRNrywkE 239
Cdd:cd19080 168 RGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKY---QRGEEGRAGEAKGVTVGFGKLT----E 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152114 240 HHFEgIALVEKALQAAYGAsapSMTSATLRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19080 241 RNWA-IVDVVAAVAEELGR---SAAQVALAWVRQKPG-----VVIPIIGARTLEQLKDNLGALD 295
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
14-303 |
4.71e-47 |
|
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: 160.77 E-value: 4.71e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRM-----DAPTSAAVTRAfLERGHTEIDTAFVYSEGQSETILGGLGlrlggSDCR--VKIDTK------AIP 80
Cdd:cd19084 9 LGTWAIGGTWwgevdDQESIEAIKAA-IDLGINFFDTAPVYGFGHSEEILGKAL-----KGRRddVVIATKcglrwdGGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 81 LFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsn 160
Cdd:cd19084 83 GVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 161 gwilPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKyedkngkqPVGRFFGNTWaeMYRNRYWKEH 240
Cdd:cd19084 161 ----IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYK--------KEPTFPPDDR--RSRFPFFRGE 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152114 241 HFE-GIALVE--KALQAAYGasaPSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19084 227 NFEkNLEIVDklKEIAEKYG---KSLAQLAIAWTLAQPGV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
10-303 |
3.58e-44 |
|
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: 153.92 E-value: 3.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMGRR---------MDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRlggSDCRVKIDTKAIP 80
Cdd:cd19091 14 SELALGTMTFGGGggffgawggVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---RRDDVLIATKVRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 81 LFGNSLKPDSL-RFQL----ETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICT 155
Cdd:cd19091 91 RMGEGPNDVGLsRHHIiravEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 156 LCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKyedKNGKQPVGRFFGNTWAEMYrnR 235
Cdd:cd19091 171 ISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYR---RGQPAPEGSRLRRTGFDFP--P 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 236 YWKEHhfeGIALVE--KALQAAYGASAPsmtSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19091 246 VDRER---GYDVVDalREIAKETGATPA---QVALAWL-----LSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
14-301 |
2.31e-42 |
|
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: 148.89 E-value: 2.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRR------MDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcRVKIDTKaiplFGNSLK 87
Cdd:cd19079 17 LGCMSFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRD-EVVIATK----VYFPMG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 88 PDS---------LRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK 158
Cdd:cd19079 92 DGPngrglsrkhIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 159 SNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPvgrffgnTWAEMYRNRYWK 238
Cdd:cd19079 172 KNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRST-------TDTAKLKYDYFT 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 239 EHHFEGIALVEKaLQAAYGAsapSMTSATLRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAA 301
Cdd:cd19079 245 EADKEIVDRVEE-VAKERGV---SMAQVALAWLLSKPG-----VTAPIVGATKLEHLEDAVAA 298
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
20-303 |
6.63e-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: 147.35 E-value: 6.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 20 GRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSD----CRVKIDTKAIPL-FGNSLKpdSLRFQ 94
Cdd:cd19074 16 GGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRESyvisTKVFWPTGPGPNdRGLSRK--HIFES 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNA 174
Cdd:cd19074 94 IHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 175 ITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedKNGKQPVGRFFGNTWaemyRNRYWKEHHF--EGIALVEKaL 252
Cdd:cd19074 174 LWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKY----RDGIPPPSRSRATDE----DNRDKKRRLLtdENLEKVKK-L 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 41152114 253 QAAYGASAPSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19074 245 KPIADELGLTLAQLALAWC-----LRNPAVSSAIIGASRPEQLEENVKASG 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
28-318 |
7.64e-39 |
|
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: 138.87 E-value: 7.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 28 SAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGlrlggSDCR--VKIDTKAiplFGNSLKPDSLRFQLETSLKRLQCP 105
Cdd:cd19085 25 SIATIHAALDAGINFFDTAEAYGDGHSEEVLGKAL-----KGRRddVVIATKV---SPDNLTPEDVRKSCERSLKRLGTD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 106 RVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwilPTVYQGMYNAITRQVETELFP 185
Cdd:cd19085 97 YIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 186 CLRHFGLRFYAFNPLAGGLLTGKYKYEDKNgkqPVGR--------FFGNTWAEMyrnrywkehhFEGIALVeKALQAAYG 257
Cdd:cd19085 171 FCREHGIGVLAYSPLAQGLLTGKFSSAEDF---PPGDartrlfrhFEPGAEEET----------FEALEKL-KEIADELG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152114 258 AsapSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAEEgPLEPAVVDAFNQA 318
Cdd:cd19085 237 V---TMAQLALAWVLQQPGV-----TSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
83-310 |
4.31e-37 |
|
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: 134.69 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 83 GNSLKpdSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGw 162
Cdd:cd19089 96 GGSRK--YLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 163 ILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedKNGKQPVGRFFGNTWaemyrnrYWKEHHF 242
Cdd:cd19089 173 VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAAESK-------FLTEEAL 241
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 243 EGiALVEKALQ-----AAYGASAPSMtsaTLRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAAAEEGPLEPA 310
Cdd:cd19089 242 TP-EKLEQLRKlnkiaAKRGQSLAQL---ALSWVLRDPRVT-----SVLIGASSPSQLEDNVAALKNLDFSEE 305
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
23-303 |
4.44e-35 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 129.46 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 23 MDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPLFG-------NSlkPDSLRFQL 95
Cdd:cd19083 30 LDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNE--VVIATKGAHKFGgdgsvlnNS--PEFLRSAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 96 ETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEictlckSNGWILPTVYQGMYNAI 175
Cdd:cd19083 106 EKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE------ANKDGYVDVLQGEYNLL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 176 TRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKY----KYEDKNGKQPVGRFFGNTWAEMYRNrywkehhfegialVEKA 251
Cdd:cd19083 180 QREAEEDILPYCVENNISFIPYFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKGERFSENLDK-------------VDKL 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 41152114 252 LQAAYGASApSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19083 247 KSIADEKGV-TVAHLALAWYLTRPAI-----DVVIPGAKRAEQVIDNLKALD 292
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-303 |
7.20e-33 |
|
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: 123.55 E-value: 7.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 28 SAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGsdcRVKIDTKAIPLF------GNSLKPDSLRFQLETSLKR 101
Cdd:cd19102 28 SIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRD---RPIVATKCGLLWdeegriRRSLKPASIRAECEASLRR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 102 LQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTlcksngwILP-TVYQGMYNAITRQVE 180
Cdd:cd19102 105 LGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPiASLQPPYSLLRRGIE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 181 TELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedknGKQPVGRFFGNTWAEmyRNRYWKEHHF-EGIALVE--KALQAAYG 257
Cdd:cd19102 178 AEILPFCAEHGIGVIVYSPMQSGLLTGKM------TPERVASLPADDWRR--RSPFFQEPNLaRNLALVDalRPIAERHG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41152114 258 ASAPSMTSAtlrWMYHHSQLQGAhgdavILGMSSLEQLEQNLAAAE 303
Cdd:cd19102 250 RTVAQLAIA---WVLRRPEVTSA-----IVGARRPDQIDETVGAAD 287
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
20-314 |
1.25e-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: 123.09 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 20 GRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAipLFGNSLKPDS--------L 91
Cdd:cd19143 25 GNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKI--FWGGGGPPPNdrglsrkhI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 92 RFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGM 171
Cdd:cd19143 103 VEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 172 YNAITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedkNGKQPVGRFFGNTWAEMYRNRYWKEHHfEGIALVEK 250
Cdd:cd19143 183 YNLFHRErVEVEYAPLYEKYGLGTTTWSPLASGLLTGKY-----NNGIPEGSRLALPGYEWLKDRKEELGQ-EKIEKVRK 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152114 251 ALQAA--YGASAPSMTSAtlrWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAEEGP-LEPAVVDA 314
Cdd:cd19143 257 LKPIAeeLGCSLAQLAIA---WC-----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEK 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
14-303 |
1.85e-32 |
|
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: 122.32 E-value: 1.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEM---GRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGsdcRVKIDTK-------AIPLFG 83
Cdd:cd19076 17 LGCMGMsafYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRD---EVVIATKfgivrdpGSGFRG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 84 NSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYA------AWEVAEIctlc 157
Cdd:cd19076 94 VDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASadtirrAHAVHPI---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 158 ksngwilpTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGntwaemyrnRYW 237
Cdd:cd19076 170 --------TAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNP---------RFQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152114 238 KEHHFEGIALVEK--ALQAAYGASAPSMtsaTLRWMYHhsqlQGAhgDAV-ILGMSSLEQLEQNLAAAE 303
Cdd:cd19076 233 GENFDKNLKLVEKleAIAAEKGCTPAQL---ALAWVLA----QGD--DIVpIPGTKRIKYLEENVGALD 292
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
95-316 |
5.10e-31 |
|
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: 119.21 E-value: 5.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDH------------------STPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTL 156
Cdd:cd19094 102 VEGSLKRLGTDYIDLYQLHWPDRytplfgggyytepseeedSVSFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLEL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 157 CKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKyeDKNGKQPVGRF---------FGNT 227
Cdd:cd19094 182 AEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYL--DGAARPEGGRLnlfpgymarYRSP 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 228 WAEMYRNRYWKEHHFEGIALVEKALqaAYGASAPSMTSAtlrwmyhhsqlqgahgdavILGMSSLEQLEQNLAAAeEGPL 307
Cdd:cd19094 260 QALEAVAEYVKLARKHGLSPAQLAL--AWVRSRPFVTST-------------------IIGATTLEQLKENIDAF-DVPL 317
|
....*....
gi 41152114 308 EPAVVDAFN 316
Cdd:cd19094 318 SDELLAEID 326
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
13-303 |
6.39e-30 |
|
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: 115.34 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 13 VLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYS----EGQSETILGGLGLRLGGSDcRVKIDTK-AIPLFGNS-- 85
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKSRGNRD-KVVIATKgGHPDLEDMsr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 86 --LKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNyaaWEVAEIC---TLCKSN 160
Cdd:cd19082 83 srLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERIAeanAYAKAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 161 GWILPTVYQGMYNAITRQVETELFPCL-------RHF----GLRFYAFNPLAGGLLTGKYKYEDkngkqpvgrffgnTWA 229
Cdd:cd19082 160 GLPGFAASSPQWSLARPNEPPWPGPTLvamdeemRAWheenQLPVFAYSSQARGFFSKRAAGGA-------------EDD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41152114 230 EMYRNRYWKEHHFEGIALVeKALQAAYGASApsmTSATLRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAAAE 303
Cdd:cd19082 227 SELRRVYYSEENFERLERA-KELAEEKGVSP---TQIALAYVLNQPFPTVP-----IIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
10-303 |
7.01e-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: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMG-----RRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGsdcRVKIDTK------- 77
Cdd:cd19149 12 SVIGLGTWAIGggpwwGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRD---KVVLATKcglrwdr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 78 ----------AIPLFGNsLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAA 147
Cdd:cd19149 89 eggsfffvrdGVTVYKN-LSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 148 WEVAEICtlckSNGWIlpTVYQGMYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGKYKyedkngkqPVGRFFGN 226
Cdd:cd19149 168 EQIKEYV----KAGQL--DIIQEKYSMLDRGIEKELLPyCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 227 TWaeMYRNRYWKEHHFEGI-ALVE--KALQAAYGAsapSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19149 233 DA--RSGIPWFSPENREKVlALLEkwKPLCEKYGC---TLAQLVIAWTLAQPGI-----TSALCGARKPEQAEENAKAGD 302
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-303 |
1.92e-28 |
|
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: 111.27 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSE-------GQSETILGGLGLRLGGSDcRVKIDTKA---- 78
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFwteggvgGESERLIGRWLKDRGNRD-DVVIATKVgagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 79 -IPLFGN----SLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEI 153
Cdd:cd19752 80 rDPDGGPespeGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 154 CTLCKSNGWILPTVYQ----------GMYNAITRQVETELFPCLR-HFGLRFYAFNPlaggLLTGKYKYEDKngkqPVgr 222
Cdd:cd19752 160 RQIARQQGWAEFSAIQqrhsylrprpGADFGVQRIVTDELLDYASsRPDLTLLAYSP----LLSGAYTRPDR----PL-- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 223 ffgntwAEMYRNrywkehhfEGIALVEKALQAAYGASAPSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAA 302
Cdd:cd19752 230 ------PEQYDG--------PDSDARLAVLEEVAGELGATPNQVVLAWL-----LHRTPAIIPLLGASTVEQLEENLAAL 290
|
.
gi 41152114 303 E 303
Cdd:cd19752 291 D 291
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
14-303 |
1.46e-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: 109.24 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEM----GRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGsdcRVKIDTK---------AIP 80
Cdd:cd19078 9 LGCMGMshgyGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRD---QVVIATKfgfkidggkPGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 81 LFGNSlKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSnyaawEVAEiCTLCKSN 160
Cdd:cd19078 86 LGLDS-RPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGV-ETIRRAH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 161 GwILP-TVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyeDKNGKqpvgrFFGNTwaemYRN---RY 236
Cdd:cd19078 159 A-VCPvTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKI---DENTK-----FDEGD----DRAslpRF 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41152114 237 WKEHHFEGIALVE--KALQAAYGAsapsmTSA--TLRWMYHhsqlQGAHgdAV-ILGMSSLEQLEQNLAAAE 303
Cdd:cd19078 226 TPEALEANQALVDllKEFAEEKGA-----TPAqiALAWLLA----KKPW--IVpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
3-301 |
1.50e-27 |
|
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: 109.82 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 3 RQLS-----RARPaTVLGAMEMGRR-------MDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDC 70
Cdd:cd19146 1 RQLSptagvRVSP-LCLGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 71 RVkIDTKAIPLF-------------GNSLKpdSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKF 137
Cdd:cd19146 80 MV-LATKYTTGYrrggpikiksnyqGNHAK--SLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 138 VELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAggllTGKYKYEDknGK 217
Cdd:cd19146 157 LYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG----QGQFRTEE--EF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 218 QPVGRFFGNTWAEmyrnrywKEHHFEgialVEKALQAAYGASAPSMTSATLRWMYHHSQLqgahgdaV--ILGMSSLEQL 295
Cdd:cd19146 231 KRRGRSGRKGGPQ-------TEKERK----VSEKLEKVAEEKGTAITSVALAYVMHKAPY-------VfpIVGGRKVEHL 292
|
....*.
gi 41152114 296 EQNLAA 301
Cdd:cd19146 293 KGNIEA 298
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
13-227 |
2.23e-27 |
|
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: 109.14 E-value: 2.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 13 VLGAMEMG-------RRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcRVKIDTK-------- 77
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRD-QIVIATKfttdykay 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 78 ------AIPLFGNSLKpdSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVA 151
Cdd:cd19147 93 evgkgkAVNYCGNHKR--SLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 152 EICTLCKSNGWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYED--KNGkQPVGRFFGNT 227
Cdd:cd19147 171 AANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGKFQSKKAVEErkKNG-EGLRSFVGGT 247
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
14-214 |
5.45e-27 |
|
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: 107.78 E-value: 5.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRM----DAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcRVKIDTKAI-------PLF 82
Cdd:cd19148 9 LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlewdeggEVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 83 GNSlKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAaweVAEICTLCKsnGW 162
Cdd:cd19148 88 RNS-SPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS---PEQMETFRK--VA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41152114 163 ILPTVyQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDK 214
Cdd:cd19148 162 PLHTV-QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTK 212
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-220 |
7.46e-27 |
|
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: 106.54 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMGRRMDAPTS-----AAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPlfgN 84
Cdd:cd19072 5 PVLGLGTWGIGGGMSKDYSddkkaIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRED--LFITTKVSP---D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 85 SLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwil 164
Cdd:cd19072 80 HLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGP--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 165 PTVYQGMYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGKYKYE------DKNGKQPV 220
Cdd:cd19072 157 IVANQVEYNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKGSPlldeiaKKYGKTPA 218
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
14-303 |
1.00e-25 |
|
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: 103.07 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAM------EMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRlggSDCRVKIDTK--AIPLFGNS 85
Cdd:cd19088 6 YGAMrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKggLVRTGPGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 86 LKPD----SLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNY------AAWEVAEICT 155
Cdd:cd19088 83 WGPDgspeYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVtvaqieEARAIVRIVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 156 LcksngwilptvyQGMYNAITRQVETELFPCLRHfGLRFYAFNPLAGGLLTgkykyedkngkQPVGRFfgntwaemyrnr 235
Cdd:cd19088 163 V------------QNRYNLANRDDEGVLDYCEAA-GIAFIPWFPLGGGDLA-----------QPGGLL------------ 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 236 ywkehhfegialveKALQAAYGASAPsmtSATLRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19088 207 --------------AEVAARLGATPA---QVALAWLLARSP-----VMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-311 |
2.34e-25 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 102.63 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRMDAptSAAVTRAFLERGHTEIDTAFVYseGQSETILGGLGLRLGGSDCRV--KIDTKAIPLFGNSlkPDSL 91
Cdd:cd19090 10 LGGVFGGVDDDE--AVATIRAALDLGINYIDTAPAY--GDSEERLGLALAELPREPLVLstKVGRLPEDTADYS--ADRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 92 RFQLETSLKRLQCPRVDLFYLHMPDHSTPVEET-----LRACHQLHQEGKFVELGLsnyAAWEVAEICTLCKSNGW--IL 164
Cdd:cd19090 84 RRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGL---GGGPPDLLRRAIETGDFdvVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 165 ptVYQGmYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYRnryWKEHHfe 243
Cdd:cd19090 161 --TANR-YTLLDQSAADELLPaAARH-GVGVINASPLGMGLLAGRPPERVRYTYRWLSPELLDRAKRLYE---LCDEH-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 244 GIALVEKALQaaYGASAPSMtsatlrwmyhhsqlqgahgDAVILGMSSLEQLEQNLAAAeEGPLEPAV 311
Cdd:cd19090 232 GVPLPALALR--FLLRDPRI-------------------STVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
20-302 |
2.10e-23 |
|
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: 97.68 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 20 GRRMDAPTSAAVTRAfLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcRVKIDTKAIPLFgNSLKPDSLRFQLETSL 99
Cdd:cd19093 21 GEYGDEDLQAAFDAA-LEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKFAPLP-WRLTRRSVVKALKASL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 100 KRLQCPRVDLFYLHMPDH-STPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwILPTVYQGMYNAITRQ 178
Cdd:cd19093 98 ERLGLDSIDLYQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 179 VET-ELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFGNTWAEMYrnrywkehhfegiALVE--KALQAA 255
Cdd:cd19093 177 PEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQ-------------PLLDalEEIAEK 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41152114 256 YGAsapSMTSATLRWMYHHSQLqgahgdaVILGMSSLEQLEQNLAAA 302
Cdd:cd19093 244 YGK---TPAQVALNWLIAKGVV-------PIPGAKNAEQAEENAGAL 280
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
95-301 |
2.86e-23 |
|
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: 97.86 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwiLPT-VYQGMYN 173
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG--TPClIHQPKYS 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 174 AITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKY---EDKNGKQPvGRFFgntwaemyrnrywKEHHF--EGIALV 248
Cdd:cd19151 185 MFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNgipEDSRAAKG-SSFL-------------KPEQIteEKLAKV 250
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 41152114 249 eKALQAAYGASAPSMTSATLRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAA 301
Cdd:cd19151 251 -RRLNEIAQARGQKLAQMALAWVLRNKRVT-----SVLIGASKPSQIEDAVGA 297
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
95-301 |
6.58e-23 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 97.37 E-value: 6.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSngWILP-TVYQGMYN 173
Cdd:PRK09912 120 LDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLRE--WKIPlLIHQPSYN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 174 AITRQVE-TELFPCLRHFGLRFYAFNPLAGGLLTGKYKY---EDKNGKQPVGRFFGNTwaemyrNRYWKEHHFEGIALVE 249
Cdd:PRK09912 198 LLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNgipQDSRMHREGNKVRGLT------PKMLTEANLNSLRLLN 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 41152114 250 KALQaaygASAPSMTSATLRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAA 301
Cdd:PRK09912 272 EMAQ----QRGQSMAQMALSWLLKDERVT-----SVLIGASRAEQLEENVQA 314
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
2-301 |
2.80e-20 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 89.42 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 2 SRQLSRARPA-TVLGAMEMG-------RRMDAPTSAAVTRAFlERGHTEIDTAFVYseGQSETILGGLGLRLGGSDCRVK 73
Cdd:cd19144 3 TRTLGRNGPSvPALGFGAMGlsafygpPKPDEERFAVLDAAF-ELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 74 IDTKaiplFGNSL-----------KPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGL 142
Cdd:cd19144 80 LATK----FGIEKnvetgeysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 143 SNYAAWEVAEICTlcksngwILP-TVYQGMYNAITRQVET---ELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKngkq 218
Cdd:cd19144 156 SECSAETLRRAHA-------VHPiAAVQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDD---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 219 pvgrFFGNTWaEMYRNRYWKEHHFEGIALVE--KALQAAYGASApsmTSATLRWMYhhsqlqgAHGDAV--ILGMSSLEQ 294
Cdd:cd19144 225 ----FEEGDF-RRMAPRFQAENFPKNLELVDkiKAIAKKKNVTA---GQLTLAWLL-------AQGDDIipIPGTTKLKR 289
|
....*..
gi 41152114 295 LEQNLAA 301
Cdd:cd19144 290 LEENLGA 296
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-301 |
2.88e-19 |
|
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: 85.22 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRMDAPTS-----AAVTRAfLERGHTEIDTAFVYSEGQSETILGGLGlrlggSDCR--VKIDTKaiplFGNSL 86
Cdd:cd19086 8 FGTWGLGGDWWGDVDdaeaiRALRAA-LDLGINFFDTADVYGDGHSERLLGKAL-----KGRRdkVVIATK----FGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 87 K----------PDSLRFQLETSLKRLQCPRVDLFYLHMPDHS-TPVEETLRACHQLHQEGKFVELGLS---NYAAWEVAE 152
Cdd:cd19086 78 DggperpqdfsPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 153 ictlcksNGWIlpTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKykyedkngkqpvgrffgntwaemy 232
Cdd:cd19086 158 -------RGGI--DVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK------------------------ 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152114 233 rnrywkehhfegialvekalqaaygasapsMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 301
Cdd:cd19086 205 ------------------------------LAQAALRFILSHPAV-----STVIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
31-301 |
4.71e-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: 85.96 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 31 VTRAFlERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKaipLF--GNSLKPDSLRFQ-----LETSLKRLQ 103
Cdd:cd19141 36 VTLAY-ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK---IFwgGKAETERGLSRKhiiegLKASLERLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 104 CPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITR-QVETE 182
Cdd:cd19141 112 LEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 183 LfPCLRH-FGLRFYAFNPLAGGLLTGKYkyedKNGKQPVGR--FFGNTWaemYRNRYWKEHHFEGIALVEKALQAA--YG 257
Cdd:cd19141 192 L-PELFHkIGVGAMTWSPLACGILSGKY----DDGVPEYSRasLKGYQW---LKEKILSEEGRRQQAKLKELQIIAdrLG 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 41152114 258 ASAPSMTSAtlrWMYHHsqlQGAHGdaVILGMSSLEQLEQNLAA 301
Cdd:cd19141 264 CTLPQLAIA---WCLKN---EGVSS--VLLGASSTEQLYENLQA 299
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
95-301 |
5.50e-18 |
|
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: 82.89 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILpTVYQGMYNA 174
Cdd:cd19150 107 LDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELGTPL-LIHQPSYNM 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 175 ITRQVE-TELFPCLRHFGLRFYAFNPLAGGLLTGKYKyedknGKQPVGrffgntwaemyrNRYWKEHHFEGIALVE---- 249
Cdd:cd19150 186 LNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG------------SRASKERSLSPKMLTEanln 248
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 41152114 250 --KALQAAYGASAPSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 301
Cdd:cd19150 249 siRALNEIAQKRGQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENVGA 297
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
14-301 |
1.12e-16 |
|
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: 79.01 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRMDAPTSA----AVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSdcRVKIDTK-AIPLFGNSLK- 87
Cdd:cd19145 17 LGCMGLSGDYGAPKPEeegiALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDGPRE--KVQLATKfGIHEIGGSGVe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 88 ----PDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAwevaeiCTLCKSNGwI 163
Cdd:cd19145 95 vrgdPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASA------DTIRRAHA-V 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 164 LP-TVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFgntwaemyrNRYWKEHHF 242
Cdd:cd19145 168 HPiTAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSH---------PRFQGENLE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 243 EGIALVEK--ALQAAYGASaPSMTSatLRWMYHhsqlqgaHGDAV--ILGMSSLEQLEQNLAA 301
Cdd:cd19145 239 KNKVLYERveALAKKKGCT-PAQLA--LAWVLH-------QGEDVvpIPGTTKIKNLNQNIGA 291
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
10-205 |
5.49e-16 |
|
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: 76.52 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMG-RRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGlrlggSDCR--VKIDTKAIPlfGNSl 86
Cdd:cd19138 12 PALGQGTWYMGeDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAI-----RGRRdkVFLVSKVLP--SNA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 87 KPDSLRFQLETSLKRLQCPRVDLFYLHMPDhSTPVEETLRACHQLHQEGKFVELGLSNY------AAWEVAeictlcksn 160
Cdd:cd19138 84 SRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFdtddmeELWAVP--------- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 41152114 161 GWILPTVYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLA-GGLL 205
Cdd:cd19138 154 GGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAqGGLL 199
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
29-145 |
1.08e-15 |
|
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: 75.39 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 29 AAVTRAFLERGHTEIDTAFVYsEGQSETILGGLGLRLGGSDcrVKIDTKaipLFGNSLKPDSLRFQLETSLKRLQCPRVD 108
Cdd:cd19073 17 ANAVKEALELGYRHIDTAEIY-NNEAEVGEAIAESGVPRED--LFITTK---VWRDHLRPEDLKKSVDRSLEKLGTDYVD 90
|
90 100 110
....*....|....*....|....*....|....*..
gi 41152114 109 LFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNY 145
Cdd:cd19073 91 LLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNF 127
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
15-266 |
1.09e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 76.22 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 15 GAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPLfGNSLKPDSLRFQ 94
Cdd:cd19103 21 GDQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPRED--YIISTKFTPQ-IAGQSADPVADM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPdhsTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVyQGMYNA 174
Cdd:cd19103 98 LEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 175 ITRQVETE--LFPCLRHfGLRFYAFNPLAGGLLTGKYkyeDKNGKQPVGRFFGNTWaemyrNRYWKEhhFEGIALVEKAL 252
Cdd:cd19103 174 LYRSSEEAgiLDYCKEN-GITFFAYMVLEQGALSGKY---DTKHPLPEGSGRAETY-----NPLLPQ--LEELTAVMAEI 242
|
250
....*....|....
gi 41152114 253 QAAYGASAPSMTSA 266
Cdd:cd19103 243 GAKHGASIAQVAIA 256
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
20-306 |
1.79e-15 |
|
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: 75.89 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 20 GRRMDAPTSAAVTRAFlERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKaIPLFGNSLKPDSLRFQ----- 94
Cdd:cd19158 26 GQITDEMAEHLMTLAY-DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK-IFWGGKAETERGLSRKhiieg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNA 174
Cdd:cd19158 104 LKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHM 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 175 ITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedKNGKQPVGR--FFGNTWaemYRNRYWKEHHFEGIALVeKA 251
Cdd:cd19158 184 FQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKY----DSGIPPYSRasLKGYQW---LKDKILSEEGRRQQAKL-KE 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 41152114 252 LQAAYGASAPSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAEEGP 306
Cdd:cd19158 256 LQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVLP 305
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
37-306 |
2.23e-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: 75.46 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 37 ERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKaipLF--GNSLKPDSLRFQ-----LETSLKRLQCPRVDL 109
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYwgGKAETERGLSRKhiiegLKGSLQRLQLEYVDV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 110 FYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQ-VETELfPCLR 188
Cdd:cd19159 119 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQL-PELY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 189 H-FGLRFYAFNPLAGGLLTGKYkyedKNGKQPVGRFFGNTWaEMYRNRYWKEHHFEGIALVEKALQAA--YGASAPSMTS 265
Cdd:cd19159 198 HkIGVGAMTWSPLACGIISGKY----GNGVPESSRASLKCY-QWLKERIVSEEGRKQQNKLKDLSPIAerLGCTLPQLAV 272
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41152114 266 AtlrWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAEEGP 306
Cdd:cd19159 273 A---WC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
24-317 |
1.31e-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: 73.48 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAFlERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKaIPLFGNSLKPDSLRFQ-----LETS 98
Cdd:cd19160 32 DETAEDLLTVAY-EHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTK-IYWGGQAETERGLSRKhiiegLRGS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 99 LKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNAITRQ 178
Cdd:cd19160 110 LDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQRE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 179 -VETELfPCLRH-FGLRFYAFNPLAGGLLTGkyKYEDKNGKQPVGRFFGNTW-AEMYRNRYWKEHHfegiALVEKALQAA 255
Cdd:cd19160 190 kVEMQL-PELYHkIGVGSVTWSPLACGLITG--KYDGRVPDTCRAAVKGYQWlKEKVQSEEGKKQQ----AKVKELHPIA 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 256 YGASApSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAEE-GPLEPAVVDAFNQ 317
Cdd:cd19160 263 DRLGC-TVAQLAIAWC-----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
20-303 |
1.32e-14 |
|
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: 73.01 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 20 GRRMDAPTSAAVT--RAFLERGHTEIDTAFVYseGQSETIL---GGLGLRLGGSDCRVKIDTKAIPlFGNSLKPDS--LR 92
Cdd:cd19101 15 GHGGIRDEDAAVRamAAYVDAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVP-DPGELTMTRayVE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 93 FQLETSLKRLQCPRVDLFYLHMPDHSTP-VEETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGwiLPTVY-QG 170
Cdd:cd19101 92 AAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----DAG--VPIVSnQV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 171 MYNAITRQVETELFP-CLRHfGLRFYAFNPLAGGLLTGKYKyedknGKQPVGRFFGNTWA-EMYRnRYWKEhhFEGIALV 248
Cdd:cd19101 166 QYSLLDRRPENGMAAlCEDH-GIKLLAYGTLAGGLLSEKYL-----GVPEPTGPALETRSlQKYK-LMIDE--WGGWDLF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41152114 249 EKALQA------AYGAsapSMTSATLRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19101 237 QELLRTlkaiadKHGV---SIANVAVRWV-----LDQPGVAGVIVGARNSEHIDDNVRAFS 289
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-302 |
3.41e-14 |
|
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: 71.08 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRmdaptSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPLfGNSLKPDSLRF 93
Cdd:cd19105 18 FGGGGLPRE-----SPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDK--VFLATKASPR-LDKKDKAELLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 94 QLETSLKRLQCPRVDLFYLHMPDHSTP---VEETLRACHQLHQEGKFVELGLS-NYAAWEVAEicTLCKSnGWIlpTVYQ 169
Cdd:cd19105 90 SVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFStHDNMAEVLQ--AAIES-GWF--DVIM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 170 GMYNAITRQVetELFPCLrhfglrfyafnPLAG----GLLTGKykyedkngkqpvgrffgnTWAEMYRNRyWKEHHFEGi 245
Cdd:cd19105 165 VAYNFLNQPA--ELEEAL-----------AAAAekgiGVVAMK------------------TLAGGYLQP-ALLSVLKA- 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 41152114 246 alvekalqaaygaSAPSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAA 302
Cdd:cd19105 212 -------------KGFSLPQAALKWVLSNPRV-----DTVVPGMRNFAELEENLAAA 250
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-299 |
4.59e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 71.81 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRRMDAPTSAAVTRAFLERGHTEIDTAFVY-------SEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGN-- 84
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSREKLIIASKVSGPSRNNdk 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 85 SLKPD------SLRFQLETSLKRLQCPRVDLFYLHMPDH--------------STPVE---ETLRACHQLHQEGKFVELG 141
Cdd:PRK10625 98 GIRPNqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdSAPAVsllETLDALAEQQRAGKIRYIG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 142 LSNYAAWEVAEICTLCKSNGwiLPTVY--QGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYkyedKNGKQP 219
Cdd:PRK10625 178 VSNETAFGVMRYLHLAEKHD--LPRIVtiQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAKP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 220 VGRffGNTWAEMYrNRYWKEHHFEGIAlVEKALQAAYGASAPSMTSATLRwmyhhsqlQGAHGDAVILGMSSLEQLEQNL 299
Cdd:PRK10625 252 AGA--RNTLFSRF-TRYSGEQTQKAVA-AYVDIAKRHGLDPAQMALAFVR--------RQPFVASTLLGATTMEQLKTNI 319
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
14-320 |
7.32e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 71.39 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMemgR--RMDAPTSAAVTRAFLERGHTEIDTAFVYseGQSETILGGLGlrlggSDCR--VKIDTKaIPLFGNSlkPD 89
Cdd:COG1453 18 FGGM---RlpRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKAL-----KGPRdkVILATK-LPPWVRD--PE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 90 SLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLR------ACHQLHQEGKFVELGLSNYAAWEVAEicTLCKSNGWi 163
Cdd:COG1453 85 DMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHIGFSTHGSLEVIK--EAIDTGDF- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 164 lpTVYQGMYNAI--TRQVETELFPCLRHFGLRFYAFNPLAGGLLTgkykyedkNGKQPVGrffgntwaemyrnrywkehh 241
Cdd:COG1453 162 --DFVQLQYNYLdqDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA--------NPPEKLV-------------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 242 fegiALVEKALQAAYGAsapsmtsatLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAEEG-PL---EPAVVDAFNQ 317
Cdd:COG1453 212 ----ELLCPPLSPAEWA---------LRFLLSHPEV-----TTVLSGMSTPEQLDENLKTADNLePLteeELAILERLAE 273
|
...
gi 41152114 318 AWH 320
Cdd:COG1453 274 ELG 276
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-305 |
9.46e-14 |
|
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: 69.90 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEM----GRRMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSdcRVKIDTKaIPLFGNSlKPD 89
Cdd:cd19096 5 FGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPRE--KFYLATK-LPPWSVK-SAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 90 SLRFQLETSLKRLQCPRVDLFYLHMPDHSTpVEETLRACH------QLHQEGKFVELGLSNYAAWEVaeICTLCKSNGW- 162
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLNSPE-WLEKARKGGllefleKAKKEGLIRHIGFSFHDSPEL--LKEILDSYDFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 163 --ILPtvyqgmYNAItRQVETELFPCLRH---FGLRFYAFNPLAGGLLTgkykyedkngkqpvgrffgntwaemyrnryw 237
Cdd:cd19096 158 fvQLQ------YNYL-DQENQAGRPGIEYaakKGMGVIIMEPLKGGGLA------------------------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 238 kehhfegiALVEKALQAAYGASAPSMTSAtLRWMYHHsqlQGAHgdAVILGMSSLEQLEQNLAAAEEG 305
Cdd:cd19096 200 --------NNPPEALAILCGAPLSPAEWA-LRFLLSH---PEVT--TVLSGMSTPEQLDENIAAADEF 253
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
33-205 |
1.10e-13 |
|
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: 69.91 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 33 RAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDcrVKIDTKAIPlfgNSLKPDSLRFQLETSLKRLQCPRVDLFYL 112
Cdd:cd19137 33 KTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFPRED--LFIVTKVWP---TNLRYDDLLRSLQNSLRRLDTDYIDLYLI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 113 HMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSngwilPTVY-QGMYNAITRQVETE-LFPCLRHF 190
Cdd:cd19137 108 HWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-----PIVCnQVKYNLEDRDPERDgLLEYCQKN 182
|
170
....*....|....*
gi 41152114 191 GLRFYAFNPLAGGLL 205
Cdd:cd19137 183 GITVVAYSPLRRGLE 197
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
28-158 |
2.64e-13 |
|
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: 69.06 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 28 SAAVTRAfLERGHTEIDTAFVY-SEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFgnsLKPDSLRFQLETSLKRLQCPR 106
Cdd:cd19111 20 RAAVDYA-LFVGYRHIDTALSYqNEKAIGEALKWWLKNGKLKREEVFITTKLPPVY---LEFKDTEKSLEKSLENLKLPY 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152114 107 VDLFYLHMP-------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK 158
Cdd:cd19111 96 VDLYLIHHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-301 |
1.34e-12 |
|
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: 66.49 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGR---RMDAPTSAAVTRAFLERGHTEIDTAFVYseGQSETILGGLGLRLGGSDcrVKIDTKAIPLFGNSLK--- 87
Cdd:cd19095 5 LGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDD--LFIATKVGTHGEGGRDrkd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 88 --PDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAawevAEICTLCKSNgwiLP 165
Cdd:cd19095 81 fsPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASG---VF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 166 TVYQGMYNAITRQVEtELFPCLRHFGLRFYAFNPLAGGLLtgkykyedkngkqpVGRFFGNTWAEMYRNRYWKEHHFEGI 245
Cdd:cd19095 154 DVVQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRL--------------RRRVRRRPLYADYARRPEFAAEIGGA 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41152114 246 ALVEKAlqaaygasapsmtsatLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 301
Cdd:cd19095 219 TWAQAA----------------LRFVLSHPGV-----SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
13-303 |
1.72e-12 |
|
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: 66.81 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 13 VLGAMemgRRMDAPTSAAVTRAF----LERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKA-I----PLFG 83
Cdd:cd19092 10 VLGCM---RLADWGESAEELLSLieaaLELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCgIrlgdDPRP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 84 NSLK-----PDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVA------- 151
Cdd:cd19092 87 GRIKhydtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEllqsyld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 152 --------EICTLCksngwiLPTVYQGMynaitrqveteLFPCLRHfGLRFYAFNPLAGglltgkykyedkngkqpvGRF 223
Cdd:cd19092 167 qplvtnqiELSLLH------TEAIDDGT-----------LDYCQLL-DITPMAWSPLGG------------------GRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 224 FGNTWAEMYRNRywkehhfegiALVEKaLQAAYGASApsmTSATLRW-MYHHSQLQgahgdaVILGMSSLEQLEQNLAAA 302
Cdd:cd19092 211 FGGFDERFQRLR----------AALEE-LAEEYGVTI---EAIALAWlLRHPARIQ------PILGTTNPERIRSAVKAL 270
|
.
gi 41152114 303 E 303
Cdd:cd19092 271 D 271
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
27-203 |
1.73e-12 |
|
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: 66.35 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 27 TSAAVTRAfLERGHTEIDTAFVYS--EGQSETIlgglglrlggSDCRVK-----IDTKaipLFGNSLKPDSLRFQLETSL 99
Cdd:cd19071 16 TAEAVLAA-LEAGYRHIDTAAAYGneAEVGEAI----------RESGVPreelfITTK---LWPTDHGYERVREALEESL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 100 KRLQCPRVDLFYLHMP------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYN 173
Cdd:cd19071 82 KDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELH 157
|
170 180 190
....*....|....*....|....*....|
gi 41152114 174 AITRQVETELFpCLRHfGLRFYAFNPLAGG 203
Cdd:cd19071 158 PYLQQKELVEF-CKEH-GIVVQAYSPLGRG 185
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
24-303 |
3.90e-12 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 65.46 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAfLERGHTEIDTAFVYS--EGQSETILGglglrlggSDCR---VKIDTKaipLFGNSLKPDSLRFQLETS 98
Cdd:COG0656 17 GEEAAAAVRTA-LEAGYRHIDTAAMYGneEGVGEAIAA--------SGVPreeLFVTTK---VWNDNHGYDDTLAAFEES 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 99 LKRLQCPRVDLFYLHMPDHsTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYNAITRQ 178
Cdd:COG0656 85 LERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 179 veTELFPCLRHFGLRFYAFNPLA-GGLLtgkykyedkngKQPVgrffgntwaemyrnrywkehhFEGIAlvekalqAAYG 257
Cdd:COG0656 160 --RELLAFCREHGIVVEAYSPLGrGKLL-----------DDPV---------------------LAEIA-------EKHG 198
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41152114 258 ASAPsmtSATLRWmyhHSQlqgaHGDAVILGMSSLEQLEQNLAAAE 303
Cdd:COG0656 199 KTPA---QVVLRW---HLQ----RGVVVIPKSVTPERIRENLDAFD 234
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-307 |
1.16e-10 |
|
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: 61.00 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 33 RAFLERGHTEIDTAFVYseGQSETILGGLGLrlggSDCRVKIDTKaIPLFGNSLK--PDSLRFQLETSLKRLQCPRVDLF 110
Cdd:cd19097 33 EYALKAGINTLDTAPAY--GDSEKVLGKFLK----RLDKFKIITK-LPPLKEDKKedEAAIEASVEASLKRLKVDSLDGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 111 YLHMPD----HSTPVEETLRachQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwilPTVYQGMYNAIT-RQVETELFP 185
Cdd:cd19097 106 LLHNPDdllkHGGKLVEALL---ELKKEGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNILDqRFLKSGLLA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 186 CLRHFGLRFYA---FnpLAgGLLTgkykyedKNGKQPVGRFFGntwaemyrnryWKEHH--FEGIAlvekalqAAYGASA 260
Cdd:cd19097 177 KLKKKGIEIHArsvF--LQ-GLLL-------MEPDKLPAKFAP-----------AKPLLkkLHELA-------KKLGLSP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41152114 261 PSMtsaTLRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLAAAEEGPL 307
Cdd:cd19097 229 LEL---ALGFVLSLP-----EIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
95-301 |
2.35e-10 |
|
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: 60.56 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWILPTVYQGMYNA 174
Cdd:cd19142 103 VRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 175 ITRQ-VETELFPCLRHFGLRFYAFNPLAGGLLTGK--------YKYEDKNGKQPVGRFFGNTWAEMYRNrywKEHHFEGI 245
Cdd:cd19142 183 FCREkMELYMPELYNKVGVGLITWSPLSLGLDPGIseetrrlvTKLSFKSSKYKVGSDGNGIHEETRRA---SHKLRELS 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 41152114 246 ALVEKalqaaYGAsapSMTSATLRWmyhhsQLQGAHGDAVILGMSSLEQLEQNLAA 301
Cdd:cd19142 260 LIAER-----LGC---DLTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQLNS 302
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-300 |
7.53e-10 |
|
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: 59.25 E-value: 7.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 33 RAFLERGHTEIDTAFVYSEGQSETI----------------------------------LGGLGLRLGGSDCRVKIDTKA 78
Cdd:cd19099 28 KAALDSGINVIDTAINYRGGRSERLigkalreliekggikrdevvivtkagyipgdgdePLRPLKYLEEKLGRGLIDVAD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 79 IPLFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPV----------EETLRACHQLHQEGK------------ 136
Cdd:cd19099 108 SAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLElgeeefydrlEEAFEALEEAVAEGKiryygistwdgf 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 137 --------FVELGLSNYAAWEVAE----------ICTLCKSNGWILPTVYQGMYnaitrqveTELFPCLRHFGLRFYAFN 198
Cdd:cd19099 188 rappalpgHLSLEKLVAAAEEVGGdnhhfkviqlPLNLLEPEALTEKNTVKGEA--------LSLLEAAKELGLGVIASR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 199 PLAGGLLTGKykyedkngkqpvgrffgntwaemyRNRYWKEHHFEGIALVEKALQAAygASAPSMTSatlrwmyhhsqlq 278
Cdd:cd19099 260 PLNQGQLLGE------------------------LRLADLLALPGGATLAQRALQFA--RSTPGVDS------------- 300
|
330 340
....*....|....*....|..
gi 41152114 279 gahgdaVILGMSSLEQLEQNLA 300
Cdd:cd19099 301 ------ALVGMRRPEHVDENLA 316
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
21-145 |
4.58e-09 |
|
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: 56.11 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 21 RRMDAPTSAAVTRAFLERGHTEIDTAFVY-SEGQ-SETIlgglglrlggSDCRVKID-----TKAIPlfgNSLKPDSLRF 93
Cdd:cd19140 16 YPLTGEECTRAVEHALELGYRHIDTAQMYgNEAQvGEAI----------AASGVPRDelfltTKVWP---DNYSPDDFLA 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 41152114 94 QLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSNY 145
Cdd:cd19140 83 SVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNF 134
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-319 |
1.40e-08 |
|
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: 55.35 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 19 MGRRMDAPTSAAVTRAfLERGHTEIDTAFVYSEGQSETilGGLGLRLGGSDcRVKIDTK-AIPLFGNSLKPDSLRFQLET 97
Cdd:cd19104 26 MGRTTREEQIAAVRRA-LDLGINFFDTAPSYGDGKSEE--NLGRALKGLPA-GPYITTKvRLDPDDLGDIGGQIERSVEK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 98 SLKRLQCPRVDLFYLH---MPDHSTPVEETLRACH------------QLHQEGKFVELGLSnyaAWEVAE-ICTLCKSNg 161
Cdd:cd19104 102 SLKRLKRDSVDLLQLHnriGDERDKPVGGTLSTTDvlglggvadafeRLRSEGKIRFIGIT---GLGNPPaIRELLDSG- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 162 wiLPTVYQGMYN------AITRQVETELFP-------CLRH----FGLRfyafnPLAGGLLTGKykyEDKNGKQPVgrFF 224
Cdd:cd19104 178 --KFDAVQVYYNllnpsaAEARPRGWSAQDyggiidaAAEHgvgvMGIR-----VLAAGALTTS---LDRGREAPP--TS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 225 GNTWAEMYRNRywkehhfegialveKALQAAYGASAPSMTSATLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAEE 304
Cdd:cd19104 246 DSDVAIDFRRA--------------AAFRALAREWGETLAQLAHRFALSNPGV-----STVLVGVKNREELEEAVAAEAA 306
|
330
....*....|....*
gi 41152114 305 GPLEPAVVDAFNQAW 319
Cdd:cd19104 307 GPLPAENLARLEALW 321
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
24-219 |
1.91e-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: 54.30 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAfLERGHTEIDTAFVY--SEGQSETILGGLGLRLggsdcRVKIDTKaipLFGNSLKPDSLRFQLETSLKR 101
Cdd:cd19131 22 NDEAASAVREA-LEVGYRSIDTAAIYgnEEGVGKAIRASGVPRE-----ELFITTK---LWNSDQGYDSTLRAFDESLRK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 102 LQCPRVDLFYLHMPdhsTPVE----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYNAITR 177
Cdd:cd19131 93 LGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG----VVPVVNQIELHPRFQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 41152114 178 QVETELFpCLRHfGLRFYAFNPLA-GGLLTGKY--KYEDKNGKQP 219
Cdd:cd19131 166 QRELRAF-HAKH-GIQTESWSPLGqGGLLSDPVigEIAEKHGKTP 208
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
87-303 |
2.00e-08 |
|
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: 54.55 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 87 KPDSLRFQLETSLKRLQCP-RVDLFYLHMPDHSTPVEETLRACHQLHQEGKFVELGLSnyaawEV-AEicTLCKSNGWIL 164
Cdd:cd19077 92 SPEAVRKSIENILRALGGTkKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLS-----EVsAE--TIRRAHAVHP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 165 PTVYQGMYNAITRQVET-ELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRFFgntwaemyrNRYWKEHHFE 243
Cdd:cd19077 165 IAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL---------DRFNGENFEK 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152114 244 GIALVE--KALQAAYGASAPSMTSATLRwmyhhsqlqgAHGDAVIL---GMSSLEQLEQNLAAAE 303
Cdd:cd19077 236 NLKLVDalQELAEKKGCTPAQLALAWIL----------AQSGPKIIpipGSTTLERVEENLKAAN 290
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-300 |
3.68e-08 |
|
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: 53.25 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 14 LGAMEMGRrMDAPTSAAVTRAFLERGHTEIDTAFVYseGQSEtilgglglrlggsdcrvkidtkaiPLFGNSLKP----- 88
Cdd:cd19100 16 FGGGPLGR-LSQEEAAAIIRRALDLGINYFDTAPSY--GDSE------------------------EKIGKALKGrrdkv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 89 -----------DSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPVEET------LRACHQLHQEGKFVELGLS---NYAAW 148
Cdd:cd19100 69 flatktgardyEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISghsPEVLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 149 EVAEictlcksNGWIlPTVyQGMYNAITRQV---ETELFP-CLRHfGLRFYAFNPLAGGLLTGKykyedkngkqpvgrff 224
Cdd:cd19100 149 RALE-------TGEF-DVV-LFPINPAGDHIdsfREELLPlAREK-GVGVIAMKVLAGGRLLSG---------------- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152114 225 gntwaemyrnrywkehhfeGIALVEKALQaaygasapsmtsatlrwmYHHSQlqgAHGDAVILGMSSLEQLEQNLA 300
Cdd:cd19100 203 -------------------DPLDPEQALR------------------YALSL---PPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
30-158 |
1.26e-07 |
|
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: 52.41 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 30 AVTRAFLERGHTEIDTAFVYsegQSETILGGLGLRLGGSDcRVK-----IDTKAIPLFgnsLKPDSLRFQLETSLKRLQC 104
Cdd:cd19154 29 TAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELLEEG-VVKredlfITTKLWTHE---HAPEDVEEALRESLKKLQL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152114 105 PRVDLFYLHMP-----------------DHSTPV--EETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK 158
Cdd:cd19154 102 EYVDLYLIHAPaafkddegesgtmengmSIHDAVdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR 174
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
89-205 |
1.37e-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: 51.94 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 89 DSLRFQLETSLKRLQCPRVDLFYLHMPDHSTPV-------EETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsng 161
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS--- 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41152114 162 wILPTVYQGMYNAITRQVetELFPCLRHFGLRFYAFNPLAGGLL 205
Cdd:cd19135 160 -VVPHVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA 200
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
24-169 |
2.38e-07 |
|
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: 51.08 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAfLERGHTEIDTAFVYSEgQSETILGGLGLRLGGSDcrVKIDTKAIPlfgnslKPDSLRFQLETSLKRLQ 103
Cdd:cd19120 24 QRDLVDSVKLA-LKAGFRHIDTAEMYGN-EKEVGEALKESGVPRED--LFITTKVSP------GIKDPREALRKSLAKLG 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 104 CPRVDLFYLHMP----DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQ 169
Cdd:cd19120 94 VDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQ 159
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
94-203 |
3.19e-07 |
|
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: 50.65 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 94 QLETSLKRLQCPRVDLFYLHMPDHStpVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYN 173
Cdd:cd19133 85 AFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE----VKPAVNQIETH 158
|
90 100 110
....*....|....*....|....*....|
gi 41152114 174 AITRQVETELFpcLRHFGLRFYAFNPLAGG 203
Cdd:cd19133 159 PFNQQIEAVEF--LKKYGVQIEAWGPFAEG 186
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
10-145 |
3.64e-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: 50.43 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAmemGRRMDAPTSAAVTRAfLERGHTEIDTAFVY-SEGQ-SETIlgglglrlggSDCRVK-----IDTKaipLF 82
Cdd:cd19139 2 PAFGLGT---FRLKDDVVIDSVRTA-LELGYRHIDTAQIYdNEAAvGQAI----------AESGVPrdelfITTK---IW 64
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152114 83 GNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMP--DHSTPVEETLRACHQLHQEGKFVELGLSNY 145
Cdd:cd19139 65 IDNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPspNDEVPVEEYIGALAEAKEQGLTRHIGVSNF 129
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
30-206 |
4.52e-07 |
|
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: 50.32 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 30 AVTRAFLERGHTEIDTAFVY-SEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSlkpDSLRFQLETSLKRLQCPRVD 108
Cdd:cd19136 19 QAVDAALKAGYRLIDTASVYrNEADIGKALRDLLPKYGLSREDIFITSKLAPKDQGY---EKARAACLGSLERLGTDYLD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 109 LFYLHMP-----DHSTPVE-----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYNAitRQ 178
Cdd:cd19136 96 LYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE----VPPAVNQVEFHP--HL 169
|
170 180
....*....|....*....|....*...
gi 41152114 179 VETELFPCLRHFGLRFYAFNPLAGGLLT 206
Cdd:cd19136 170 VQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
24-169 |
1.11e-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: 49.20 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAfLERGHTEIDTAFVY------SEGQSETILGGLglrlggsdcrVK-----IDTKaipLFGNSLKPDSLR 92
Cdd:cd19116 24 DEGVRQAVKHA-IEAGYRHIDTAYLYgneaevGEAIREKIAEGV----------VKredlfITTK---LWNSYHEREQVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 93 FQLETSLKRLQCPRVDLFYLHMP------------DHSTPVE----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTL 156
Cdd:cd19116 90 PALRESLKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSN 169
|
170
....*....|...
gi 41152114 157 CKsngwILPTVYQ 169
Cdd:cd19116 170 CN----IKPAVNQ 178
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
81-200 |
2.67e-06 |
|
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: 48.11 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 81 LFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMPDH--------------STPVEETLRACHQLHQEGKFVELGLSNYA 146
Cdd:cd19125 77 LWCTDHAPEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFS 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 41152114 147 AWEVAEICTLCKsngwILPTVYQGMYNAITRQveTELFPCLRHFGLRFYAFNPL 200
Cdd:cd19125 157 VKKLEDLLAVAR----VPPAVNQVECHPGWQQ--DKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
10-308 |
2.70e-06 |
|
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: 48.12 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 10 PATVLGAMEMGR--RMDAPTSAAVTRAFLERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKAIPLFGNSLK 87
Cdd:cd19162 1 PRLGLGAASLGNlaRAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVVSTKVGRLLEPGAAGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 88 PDSLRFQ-----------LETSLKRLQCPRVDLFYLHMPDH--STPVEETLRACHQLHQEGKFVELGL---SNYAAWEVA 151
Cdd:cd19162 81 PAGADRRfdfsadgirrsIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVgvtDWAALLRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 152 EICTLcksnGWILPTvyqGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGKQPVGRffgNTWAEM 231
Cdd:cd19162 161 RRADV----DVVMVA---GRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYDYRPATP---EVLARA 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 41152114 232 YRNRYWKEHHfeGIALVEKALQaaYGASAPSMTSatlrwmyhhsqlqgahgdaVILGMSSLEQLEQNLAAAEEGPLE 308
Cdd:cd19162 231 RRLAAVCRRY--GVPLPAAALQ--FPLRHPAVAS-------------------VVVGAASPAELRDNLALLRTPIPA 284
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
81-202 |
7.41e-06 |
|
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: 46.75 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 81 LFGNSLKPDSLRFQLETSLKRLQCPRVDLFYLHMP-------------------DHSTPVEETLRACHQLHQEGKFVELG 141
Cdd:cd19128 67 LWPTMHQPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIG 146
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152114 142 LSNYAAWEVAEICTLCKsngwILPtvyqgmynaITRQVETEL-FP-------CLRHfGLRFYAFNPLAG 202
Cdd:cd19128 147 VSNYSTKLLTDLLNYCK----IKP---------FMNQIECHPyFQndklikfCIEN-NIHVTAYRPLGG 201
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
94-303 |
8.16e-06 |
|
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: 46.83 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 94 QLETSLKRLQCPRVDLFYLHMPDHSTPVEETL-----------RACHQLHQEGKFVELGL-SNyaAWEVAE-ICTLCKSN 160
Cdd:cd19152 108 SIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEELREEGVIKAIGLgVN--DWEVILrILEEADLD 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 161 gWILptvYQGMYNAITRQVETELFPCLRHFGLRFYAFNPLAGGLLTGKYKYEDKNGkQPVGrffgntwAEMY--RNRYW- 237
Cdd:cd19152 186 -WVM---LAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEY-GPAP-------PELIarRDRIEa 253
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 238 --KEHhfeGIALVEKALQAAYGASAPSmtsatlrwmyhhsqlqgahgdAVILGMSSLEQLEQNLAAAE 303
Cdd:cd19152 254 lcEQH---GVSLAAAALQFALAPPAVA---------------------SVAPGASSPERVEENVALLA 297
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
29-200 |
1.00e-05 |
|
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: 46.61 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 29 AAVTRAfLERGHTEIDTAFVYSEGQS--ETILGGLGLRLGGSDCRVKIDTKaipLFGNSLKPDSLRFQLETSLKRLQCPR 106
Cdd:cd19106 24 AAVKYA-LDAGYRHIDCAAVYGNEQEvgEALKEKVGPGKAVPREDLFVTSK---LWNTKHHPEDVEPALRKTLKDLQLDY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 107 VDLFYLHMP------DH-------------STPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGWILPTV 167
Cdd:cd19106 100 LDLYLIHWPyafergDNpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDIL----SVARIKPAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 41152114 168 YqgmynaitrQVE-------TELFPCLRHFGLRFYAFNPL 200
Cdd:cd19106 176 L---------QVEchpylaqNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
29-200 |
1.54e-05 |
|
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: 45.98 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 29 AAVTRAfLERGHTEIDTAFVYsegQSETILGGLGLRLGGSDcRVK-----IDTKaIPLFGNslKPDSLRFQLETSLKRLQ 103
Cdd:cd19155 29 TAVDTA-LEAGYRHIDTAYVY---RNEAAIGNVLKKWIDSG-KVKreelfIVTK-LPPGGN--RREKVEKFLLKSLEKLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 104 CPRVDLFYLHMP---------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngw 162
Cdd:cd19155 101 LDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR---- 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 41152114 163 ILPTVYQGMYNAITRQVETELFpCLRHfGLRFYAFNPL 200
Cdd:cd19155 177 IKPANLQVELHVYLQQKDLVDF-CSTH-SITVTAYAPL 212
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
96-203 |
1.78e-05 |
|
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: 45.46 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 96 ETSLKRLQCPRVDLFYLHMPDhSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYNAi 175
Cdd:cd19157 88 EASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHP- 161
|
90 100
....*....|....*....|....*...
gi 41152114 176 tRQVETELFPCLRHFGLRFYAFNPLAGG 203
Cdd:cd19157 162 -RLTQKELRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
19-205 |
2.26e-05 |
|
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: 45.20 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 19 MGRRMDAPTSAAVTRAFLERGHTEIDTAFVYS--EGQSETILGGLGLRLggsdcRVKIDTKaipLFGNSLKPDSLRFQLE 96
Cdd:cd19156 16 VWRVQDGAEAENAVKWAIEAGYRHIDTAAIYKneEGVGQGIRESGVPRE-----EVFVTTK---LWNSDQGYESTLAAFE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 97 TSLKRLQCPRVDLFYLHMPDHSTPVeETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQgmynait 176
Cdd:cd19156 88 ESLEKLGLDYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQ------- 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 41152114 177 rqveTELFPCLRHFGLRFY---------AFNPLAGGLL 205
Cdd:cd19156 156 ----IELHPLLTQEPLRKFckekniaveAWSPLGQGKL 189
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
95-308 |
2.82e-05 |
|
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: 45.23 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 95 LETSLKRLQCPRVDLFYLH----MPDHSTPVEETLRACHQLHQEGKFVELGLSNY--AAW-EVAE--------ICTLCKS 159
Cdd:cd19163 105 VEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGITGYplDVLkEVLErspvkidtVLSYCHY 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 160 NgwilptvyqgMYNaitrQVETELFPCLRHFGLRFYAFNPLAGGLLTgkykyedKNGKQPvgrffgntwaemyrnryWKE 239
Cdd:cd19163 185 T----------LND----TSLLELLPFFKEKGVGVINASPLSMGLLT-------ERGPPD-----------------WHP 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 240 HHFEGIALVEKAlqAAYGASAPSMTSA-TLRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAAAEEGPLE 308
Cdd:cd19163 227 ASPEIKEACAKA--AAYCKSRGVDISKlALQFALSNPDI-----ATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
24-204 |
2.96e-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: 45.14 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAFLERGHTEIDTAFVY-SEGQSETILGGLGLRLGGSDCRVKIDTKaipLFGNSLKPDSLRFQLETSLKRL 102
Cdd:cd19129 17 DPSATRNAVKAALEAGFRHFDCAERYrNEAEVGEAMQEVFKAGKIRREDLFVTTK---LWNTNHRPERVKPAFEASLKRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 103 QCPRVDLFYLHMP--------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngw 162
Cdd:cd19129 94 QLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR---- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 41152114 163 ILPTVYQgmYNAITRQVETELFPCLRHFGLRFYAFNPLAGGL 204
Cdd:cd19129 170 IKPAVVQ--VESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
31-205 |
4.44e-05 |
|
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: 44.35 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 31 VTRAFLERGHTEIDTAFVYsegQSETILGGLGLRLGGSDCRVKIDTKaipLFGNSLKPDSLRFQLETSLKRLQCPRVDLF 110
Cdd:cd19126 28 AVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTK---LWNDDQRARRTEDAFQESLDRLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 111 YLHMP--DHstpVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwILPTVYQGMYNAitRQVETELFPCLR 188
Cdd:cd19126 102 LIHWPgkDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHP--YLTQKELRGYCK 172
|
170
....*....|....*..
gi 41152114 189 HFGLRFYAFNPLAGGLL 205
Cdd:cd19126 173 SKGIVVEAWSPLGQGGL 189
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
26-304 |
6.41e-05 |
|
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: 44.06 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 26 PTSAAVTRAFlERGHTEIDTAFVYSEGQSETILGGLGLRLGGSDCRVKIDTKA--IPLFGNSLKPDSLRFQLETSLKRLQ 103
Cdd:cd19153 34 EAVAIVAEAF-AAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVgrYRDSEFDYSAERVRASVATSLERLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 104 CPRVDLFYLH---MPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwilPTVYQGmYNAITRQVE 180
Cdd:cd19153 113 TTYLDVVYLHdieFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS---LDAVLS-YCHLTLQDA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 181 TELF--PCLRH-FGLRFYAFNPLAGGLLTGKykyedknGKQPvgrffgntwaemyrnryWKEHHFEgiaLVEKALQAAYG 257
Cdd:cd19153 189 RLESdaPGLVRgAGPHVINASPLSMGLLTSQ-------GPPP-----------------WHPASGE---LRHYAAAADAV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41152114 258 ASAPSMTSATLRWMYHHSQLQGAhgDAVILGMSSLEQLEQNLAAAEE 304
Cdd:cd19153 242 CASVEASLPDLALQYSLAAHAGV--GTVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
29-145 |
1.48e-04 |
|
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: 42.78 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 29 AAVTRAfLERGHTEIDTAFVYseGQSETILGGLGLRLGGSDCR---VKIDTKaipLFGNSLKPDSLRFQLETSLKRLQCP 105
Cdd:cd19123 29 QAVKQA-LEAGYRHIDCAAIY--GNEAEIGAALAEVFKEGKVKredLWITSK---LWNNSHAPEDVLPALEKTLADLQLD 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 41152114 106 RVDLFYLHMP---------DHST---------PVEETLRACHQLHQEGKFVELGLSNY 145
Cdd:cd19123 103 YLDLYLMHWPvalkkgvgfPESGedllslspiPLEDTWRAMEELVDKGLCRHIGVSNF 160
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
24-145 |
9.17e-04 |
|
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: 40.28 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 24 DAPTSAAVTRAfLERGHTEIDTAFVY--SEGQSETILGGLGLRLggsdcRVKIDTKaipLFGNSLKPDSLRFQLETSLKR 101
Cdd:cd19130 22 PADTQRAVATA-LEVGYRHIDTAAIYgnEEGVGAAIAASGIPRD-----ELFVTTK---LWNDRHDGDEPAAAFAESLAK 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 41152114 102 LQCPRVDLFYLHMPdhsTPVE----ETLRACHQLHQEGKFVELGLSNY 145
Cdd:cd19130 93 LGLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNF 137
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
7-205 |
1.03e-03 |
|
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: 40.22 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 7 RARPATVLGAMEMGrrmDAPTSAAVTRAfLERGHTEIDTAFVYSegqSETILGGLGLRLGGSDCRVKIDTK-AIPLFGNS 85
Cdd:cd19134 9 NTMPVIGLGVGELS---DDEAERSVSAA-LEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKlATPDQGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 86 LKPDSLRfqleTSLKRLQCPRVDLFYLHMP--DHSTPVeETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGWI 163
Cdd:cd19134 82 ASQAACR----ASLERLGLDYVDLYLIHWPagREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLI----DLTFF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 41152114 164 LPTVYQgmynaitrqveTELFPCLRHFGLRFY---------AFNPLAGGLL 205
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) ... |
26-161 |
2.23e-03 |
|
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: 39.14 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152114 26 PTSAAV--TRAFLERGHTEIDTAFVYSE----GQS--ETIlgglglrlggSDCRVK-----IDTKaipLFGNSLKPDSLR 92
Cdd:cd19108 25 PKSKALeaTKLAIDAGFRHIDSAYLYQNeeevGQAirSKI----------ADGTVKredifYTSK---LWCTFHRPELVR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41152114 93 FQLETSLKRLQCPRVDLFYLHMPDHSTPVEETLRAchqlHQEGKF----VELglsnYAAWEVAEICT---LCKSNG 161
Cdd:cd19108 92 PALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPK----DENGKLifdtVDL----CATWEAMEKCKdagLAKSIG 159
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|
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