|
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 ... |
46-355 |
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: 506.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMG---RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGlgsgDCTVKIATKANPWEGKSL 122
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG----ERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPT 202
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 203 VYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgKQPVGRFFGNN-WAETYRNRFWKEHHFEAI 281
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNNaLGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23395756 282 ALVEKALQttygTNAPRMTSAALRWMYHHSQLQGTRGDAVILGMSSLEQLEQNLAATEEGPLEPAVVEAFDQAW 355
Cdd:cd19075 235 EKVEEAAE----KEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
50-360 |
9.44e-62 |
|
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: 200.40 E-value: 9.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGR---RMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKA-----NPWEGKS 121
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDD--VVIATKVgrrmgPGPNGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 122 LKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsnGWILP 201
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 202 TVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyeDKDGKQPVGRFFGNNWAETYRNrfwkEHHFEAI 281
Cdd:COG0667 174 VAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKY---RRGATFPEGDRAATNFVQGYLT----ERNLALV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23395756 282 ALVEKALQtTYGTNAPRMtsaALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATEEgPLEPAVVEAFDQAWNMVAH 360
Cdd:COG0667 247 DALRAIAA-EHGVTPAQL---ALAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAALAAVPA 315
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
46-336 |
6.29e-58 |
|
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: 187.73 E-value: 6.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDcTVKIATKA-----NPWEGK 120
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRD-DVVIATKGghppgGDPSRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 SLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWIL 200
Cdd:cd06660 80 RLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 201 PTVYQGMYN-ATTRQVEAELLPCLRHFGLRFYAYNPLAGGLltgkykyedkdgkqpvgrffgnnwaetyrnrfwkehhfe 279
Cdd:cd06660 160 FAAVQPQYSlLDRSPMEEELLDWAEENGLPLLAYSPLARGP--------------------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 280 aialvekalqttygtnaprmTSAALRWMYHHSqlqgtRGDAVILGMSSLEQLEQNLA 336
Cdd:cd06660 201 --------------------AQLALAWLLSQP-----FVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
49-355 |
4.24e-53 |
|
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: 177.50 E-value: 4.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 49 VLGTMEMG---RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANPWEGK---SL 122
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpsGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEIctlcKSNGWILPT 202
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA----LTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 203 VYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNNWAETYrnrfwkehhfEAIA 282
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----------EALE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23395756 283 LVEKaLQTTYGTNaprMTSAALRWMYHHSqlqgtRGDAVILGMSSLEQLEQNLAATeEGPLEPAVVEAFDQAW 355
Cdd:pfam00248 228 ALEE-IAKEHGVS---PAQVALRWALSKP-----GVTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
50-339 |
5.04e-52 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 175.07 E-value: 5.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGsgDCTVkIATKA------NPWE-GKSL 122
Cdd:cd19087 18 LGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRR--DDIV-LATKVfgpmgdDPNDrGLSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPT 202
Cdd:cd19087 95 R--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 203 VYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNnwaETYRNRFWKEHHFEAIA 282
Cdd:cd19087 173 SEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYG---KGKRPESGRLVER---ARYQARYGLEEYRDIAE 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 283 LVEkALQTTYGTNAprmTSAALRWMYHHSQLQgtrgdAVILGMSSLEQLEQNLAATE 339
Cdd:cd19087 247 RFE-ALAAEAGLTP---ASLALAWVLSHPAVT-----SPIIGPRTLEQLEDSLAALE 294
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
50-339 |
1.63e-50 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 170.78 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMG----RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATK-ANPWEG----- 119
Cdd:cd19084 9 LGTWAIGgtwwGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDD---VVIATKcGLRWDGgkgvt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwi 199
Cdd:cd19084 86 KDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 200 lPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYK----YEDKDGKQPVGRFFGNNWaetyrnrfwkE 275
Cdd:cd19084 161 -IVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKkeptFPPDDRRSRFPFFRGENF----------E 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23395756 276 HHFEAIALVEKALQTTYGTnaprMTSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATE 339
Cdd:cd19084 230 KNLEIVDKLKEIAEKYGKS----LAQLAIAWTLAQPGV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
49-352 |
9.37e-50 |
|
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: 169.32 E-value: 9.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 49 VLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCD-------GQSENILGGLGLGLGSGDCTVkIATKANPW---E 118
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRGKRDRVV-IATKVGFPmgpN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 119 GKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGW 198
Cdd:cd19081 92 GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 ILPTVYQGMYNATTRQ-VEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgnnWAETYRNRFWKEHH 277
Cdd:cd19081 172 PRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGST--------RRGEAAKRYLNERG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 278 FEAIALVEKALQTTYGTnaprMTSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATeEGPLEPAVVEAFD 352
Cdd:cd19081 244 LRILDALDEVAAEHGAT----PAQVALAWLLARPGV-----TAPIAGARTVEQLEDLLAAA-GLRLTDEEVARLD 308
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
50-339 |
4.52e-48 |
|
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: 164.70 E-value: 4.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTM----EMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGsgDCTVkIATK-------ANP-W 117
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNR--DRIV-LATKytmnrrpGDPnA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 118 EGKSLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNG 197
Cdd:cd19080 92 GGNHRK--NLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 198 WILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyeDKDGKQPVGRFFGNNWAETYRNrfwkEHH 277
Cdd:cd19080 170 WSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKY---QRGEEGRAGEAKGVTVGFGKLT----ERN 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23395756 278 FeaiALVEKALQTTYGTNAPrMTSAALRWMYHHSQlqgtrGDAVILGMSSLEQLEQNLAATE 339
Cdd:cd19080 243 W---AIVDVVAAVAEELGRS-AAQVALAWVRQKPG-----VVIPIIGARTLEQLKDNLGALD 295
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
68-354 |
8.92e-44 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 153.13 E-value: 8.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSgDCTvkIATKANPwegKSLKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19085 29 IHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRD-DVV--IATKVSP---DNLTPEDVRKSCERSLKRLGTDYIDLYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwilPTVYQGMYNATTRQVEAELLPCLRHFG 227
Cdd:cd19085 103 IHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCREHG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 228 LRFYAYNPLAGGLLTGKYkyeDKDGKQPVGR--------FFGNNWAETyrnrfwkehhFEAIALVeKALQTTYGTNaprM 299
Cdd:cd19085 177 IGVLAYSPLAQGLLTGKF---SSAEDFPPGDartrlfrhFEPGAEEET----------FEALEKL-KEIADELGVT---M 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 300 TSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATEEgPLEPAVVEAFDQA 354
Cdd:cd19085 240 AQLALAWVLQQPGV-----TSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
46-354 |
9.64e-43 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 151.23 E-value: 9.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGRR---------MDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATKANP 116
Cdd:cd19091 14 SELALGTMTFGGGggffgawggVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDD---VLIATKVRG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 117 WEGKSlkPDSV---RSQL----ETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEI 189
Cdd:cd19091 91 RMGEG--PNDVglsRHHIiravEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 190 CTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNNWAETYr 269
Cdd:cd19091 169 LGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYR---RGQPAPEGSRLRRTGFDFP- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 270 nRFWKEHHFEAI-ALVEKALQTtyGTNAPRmtsAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAATEEGpLEPAVV 348
Cdd:cd19091 245 -PVDRERGYDVVdALREIAKET--GATPAQ---VALAWL-----LSRPTVSSVIIGARNEEQLEDNLGAAGLS-LTPEEI 312
|
....*.
gi 23395756 349 EAFDQA 354
Cdd:cd19091 313 ARLDKV 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
50-339 |
1.31e-38 |
|
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: 140.03 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRR------MDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDcTVKIATKANP-----WE 118
Cdd:cd19079 17 LGCMSFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFAPRD-EVVIATKVYFpmgdgPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 119 GKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGW 198
Cdd:cd19079 96 GRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGW 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 ILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNNWAETYRnrfwKEHHF 278
Cdd:cd19079 176 TKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWG---DTTERRRSTTDTAKLKYDYF----TEADK 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23395756 279 EAIALVEKALQTtygTNAPrMTSAALRWMYHHSQlqgtrGDAVILGMSSLEQLEQNLAATE 339
Cdd:cd19079 249 EIVDRVEEVAKE---RGVS-MAQVALAWLLSKPG-----VTAPIVGATKLEHLEDAVAALD 300
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
50-337 |
2.58e-37 |
|
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: 136.18 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGT-MEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdcTVKIATKA------NPWE-GKS 121
Cdd:cd19074 9 LGTwLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWPRE--SYVISTKVfwptgpGPNDrGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 122 LKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILP 201
Cdd:cd19074 87 RK--HIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 202 TVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGRFFGNNWaetyRNRFWKEHHF--E 279
Cdd:cd19074 165 VVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKY----RDGIPPPSRSRATDE----DNRDKKRRLLtdE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 280 AIALVE--KALQTTYGTNAPRMtsaALRWMYHHSQLQgtrgdAVILGMSSLEQLEQNLAA 337
Cdd:cd19074 237 NLEKVKklKPIADELGLTLAQL---ALAWCLRNPAVS-----SAIIGASRPEQLEENVKA 288
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
110-346 |
3.92e-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: 135.85 E-value: 3.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKA--NPW-----EGKSLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 182
Cdd:cd19089 80 ISTKAgyGMWpgpygDGGSRK--YLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 183 SWEVAEICTLCKSNGwILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGRFFGN 262
Cdd:cd19089 158 GAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 263 NWaetyrnrFWKEHHF-EAIALVEKALQTTYGTNAPRMTSAALRWmyhhsQLQGTRGDAVILGMSSLEQLEQNLAATEEG 341
Cdd:cd19089 233 SK-------FLTEEALtPEKLEQLRKLNKIAAKRGQSLAQLALSW-----VLRDPRVTSVLIGASSPSQLEDNVAALKNL 300
|
....*
gi 23395756 342 PLEPA 346
Cdd:cd19089 301 DFSEE 305
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
110-352 |
7.19e-35 |
|
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: 130.38 E-value: 7.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKA------NPWEGK---SLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDH------------------STPVEETLR 162
Cdd:cd19094 72 LATKVagpgegITWPRGggtRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRytplfgggyytepseeedSVSFEEQLE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 163 ACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLT 242
Cdd:cd19094 152 ALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 243 GKYKYEDKDGKQpvGRFF-GNNWAETYRNRFWKEHHFEAIALVEKalqttYGTNaprMTSAALRWMYHHSQLQGTrgdav 321
Cdd:cd19094 232 GKYLDGAARPEG--GRLNlFPGYMARYRSPQALEAVAEYVKLARK-----HGLS---PAQLALAWVRSRPFVTST----- 296
|
250 260 270
....*....|....*....|....*....|.
gi 23395756 322 ILGMSSLEQLEQNLAATeEGPLEPAVVEAFD 352
Cdd:cd19094 297 IIGATTLEQLKENIDAF-DVPLSDELLAEID 326
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
68-340 |
9.78e-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: 9.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKANPWEGK-----SLKPDSVRSQLETSLKRLQCPR 142
Cdd:cd19083 39 VREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNE--VVIATKGAHKFGGdgsvlNNSPEFLRSAVEKSLKRLNTDY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 143 VDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEictlckSNGWILPTVYQGMYNATTRQVEAELLPC 222
Cdd:cd19083 117 IDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE------ANKDGYVDVLQGEYNLLQREAEEDILPY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 223 LRHFGLRFYAYNPLAGGLLTGKY----KYEDKDGKQPVGRFFGnnwaETYRNRFWKEHHFEAIAlvekalqTTYGTNAPR 298
Cdd:cd19083 191 CVENNISFIPYFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKG----ERFSENLDKVDKLKSIA-------DEKGVTVAH 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 23395756 299 MtsaALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAA-----TEE 340
Cdd:cd19083 260 L---ALAWYLTRPAI-----DVVIPGAKRAEQVIDNLKAldvtlTEE 298
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
50-339 |
2.86e-33 |
|
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: 125.41 E-value: 2.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEM----GRRMDASASAASVRAfLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATK-------ANPWE 118
Cdd:cd19076 17 LGCMGMsafyGPADEEESIATLHRA-LELGVTFLDTADMYGPGTNEELLGKALKDRRDE---VVIATKfgivrdpGSGFR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 119 GKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSnyaswEVAEiCTLCKSNGw 198
Cdd:cd19076 93 GVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS-----EASA-DTIRRAHA- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 ILP-TVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGnnwaetyrnRFWKEhH 277
Cdd:cd19076 166 VHPiTAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNP---------RFQGE-N 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 278 FEA-IALVEK--ALQTTYGTNAPRMtsaALRWMYHhsqlqgtRGDAV--ILGMSSLEQLEQNLAATE 339
Cdd:cd19076 236 FDKnLKLVEKleAIAAEKGCTPAQL---ALAWVLA-------QGDDIvpIPGTKRIKYLEENVGALD 292
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-339 |
6.97e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 123.98 E-value: 6.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYC-------DGQSENILGGLGLGLGSGDcTVKIATK----- 113
Cdd:cd19752 1 SELCLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGNRD-DVVIATKvgagp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 114 ----ANPWEGKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEI 189
Cdd:cd19752 80 rdpdGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 190 CTLCKSNGWILPTVYQ----------GMYNATTRQVEAELLPCLR-HFGLRFYAYNPLAGGLltgkykYEDKDGKQPvgr 258
Cdd:cd19752 160 RQIARQQGWAEFSAIQqrhsylrprpGADFGVQRIVTDELLDYASsRPDLTLLAYSPLLSGA------YTRPDRPLP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 259 ffgnnwaETYRNrfwkEHHFEAIALVEKALQTTYGTnaprMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAAT 338
Cdd:cd19752 231 -------EQYDG----PDSDARLAVLEEVAGELGAT----PNQVVLAWL-----LHRTPAIIPLLGASTVEQLEENLAAL 290
|
.
gi 23395756 339 E 339
Cdd:cd19752 291 D 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
68-354 |
9.56e-32 |
|
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: 121.24 E-value: 9.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATKANP-WEGK-----SLKPDSVRSQLETSLKRLQCP 141
Cdd:cd19102 32 IRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDR---PIVATKCGLlWDEEgrirrSLKPASIRAECEASLRRLGVD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 142 RVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTlcksngwILP-TVYQGMYNATTRQVEAELL 220
Cdd:cd19102 109 VIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPiASLQPPYSLLRRGIEAEIL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 221 PCLRHFGLRFYAYNPLAGGLLTGKYkyedkdGKQPVGRFFGNNWAEtyRNRFWKEHHF-EAIALVE--KALQTTYGTNAP 297
Cdd:cd19102 182 PFCAEHGIGVIVYSPMQSGLLTGKM------TPERVASLPADDWRR--RSPFFQEPNLaRNLALVDalRPIAERHGRTVA 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 298 RMtsaALRWMYHHSQLQGtrgdaVILGMSSLEQLEQNLAATEEgPLEPAVVEAFDQA 354
Cdd:cd19102 254 QL---AIAWVLRRPEVTS-----AIVGARRPDQIDETVGAADL-RLTPEELAEIEAL 301
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
80-354 |
1.32e-29 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 116.16 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 80 DTAFMYCDGQSENILGGLGLGLGSGDCTVKIATK------ANPWEGKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDH 153
Cdd:cd19143 49 DNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKifwgggGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 154 STPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VEAELLPCLRHFGLRFYA 232
Cdd:cd19143 129 ATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 233 YNPLAGGLLTGKYkyedKDGKQPVGRF----FGNNWAETYRNRFWKEHHFEAIALVEKALQTTygtnaprMTSAALRWMy 308
Cdd:cd19143 209 WSPLASGLLTGKY----NNGIPEGSRLalpgYEWLKDRKEELGQEKIEKVRKLKPIAEELGCS-------LAQLAIAWC- 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 23395756 309 hhsqLQGTRGDAVILGMSSLEQLEQNLAATEEGP-LEPAVVEAFDQA 354
Cdd:cd19143 277 ----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEKIEAI 319
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
46-337 |
6.72e-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: 113.91 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMG-----RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATK------- 113
Cdd:cd19149 12 SVIGLGTWAIGggpwwGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDK---VVLATKcglrwdr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 114 ---ANPWEG------KSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASW 184
Cdd:cd19149 89 eggSFFFVRdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 185 EVAEICtlckSNGWIlpTVYQGMYNATTRQVEAELLP-CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqPVGRFFGNN 263
Cdd:cd19149 169 QIKEYV----KAGQL--DIIQEKYSMLDRGIEKELLPyCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAGD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23395756 264 WaetyRNR---FWKEHHFEAIALVE--KALQTTYGTNaprMTSAALRWMYHhsqlQGTRgDAVILGMSSLEQLEQNLAA 337
Cdd:cd19149 234 A----RSGipwFSPENREKVLALLEkwKPLCEKYGCT---LAQLVIAWTLA----QPGI-TSALCGARKPEQAEENAKA 300
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
50-307 |
7.46e-29 |
|
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: 113.56 E-value: 7.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRRM----DASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDcTVKIATKAN-PWEGKSLK- 123
Cdd:cd19148 9 LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlEWDEGGEVv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 124 ----PDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAsweVAEICTLCKsnGWI 199
Cdd:cd19148 88 rnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS---PEQMETFRK--VAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 200 LPTVyQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGK----YKYEDKDGKQPVGRFFGNNWAetyrnrfwke 275
Cdd:cd19148 163 LHTV-QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKmtkdTKFEGDDLRRTDPKFQEPRFS---------- 231
|
250 260 270
....*....|....*....|....*....|..
gi 23395756 276 HHFEAIALVEKALQTTYGTnapRMTSAALRWM 307
Cdd:cd19148 232 QYLAAVEELDKLAQERYGK---SVIHLAVRWL 260
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
46-248 |
9.17e-29 |
|
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: 112.32 E-value: 9.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGRRM-----DASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKANPWEgk 120
Cdd:cd19072 5 PVLGLGTWGIGGGMskdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRED--LFITTKVSPDH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 sLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGwil 200
Cdd:cd19072 81 -LKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGP--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 23395756 201 PTVYQGMYNATTRQVEAELLP-CLRHfGLRFYAYNPLAGGLLTGKYKYE 248
Cdd:cd19072 157 IVANQVEYNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKGSP 204
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
49-339 |
2.11e-27 |
|
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: 109.18 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 49 VLGTMEMGRRMDASASAASVRAFLERGHSELDTAFMYCD----GQSENILGGLGLGLGSGDCTVkIATKA-----NPWEG 119
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGNRDKVV-IATKGghpdlEDMSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNyasWEVAEIC---TLCKSN 196
Cdd:cd19082 83 SRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERIAeanAYAKAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 197 GWILPTVYQGMYNATTRQVEAELLPCL-------RHF----GLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGN-NW 264
Cdd:cd19082 160 GLPGFAASSPQWSLARPNEPPWPGPTLvamdeemRAWheenQLPVFAYSSQARGFFSKRAAGGAEDDSELRRVYYSEeNF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 265 AETYRnrfwkehhfeAIALVEKalqttYGTNAprmTSAALRWMYHhsqlQGTRGDAVIlGMSSLEQLEQNLAATE 339
Cdd:cd19082 240 ERLER----------AKELAEE-----KGVSP---TQIALAYVLN----QPFPTVPII-GPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
50-339 |
1.25e-25 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 104.62 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEM----GRRMDASASAASVRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGDcTVKIATK--------ANPW 117
Cdd:cd19078 9 LGCMGMshgyGPPPDKEEMIELIRKAVELGITFFDTAEVY--GPYTNEELVGEALKPFRD-QVVIATKfgfkidggKPGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 118 EGKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSnyaswEVAEiCTLCKSNG 197
Cdd:cd19078 86 LGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGV-ETIRRAHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 198 wILP-TVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyeDKDGKqpvgrFFGNNwaetYRN---RFW 273
Cdd:cd19078 160 -VCPvTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKI---DENTK-----FDEGD----DRAslpRFT 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23395756 274 KEHHFEAIALVE--KALQTTYGtnaprMTSA--ALRWMYHhsqlqgTRGDAV-ILGMSSLEQLEQNLAATE 339
Cdd:cd19078 227 PEALEANQALVDllKEFAEEKG-----ATPAqiALAWLLA------KKPWIVpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
49-261 |
8.43e-25 |
|
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: 102.98 E-value: 8.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 49 VLGTMEMG-------RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVkIATK-------- 113
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRDQIV-IATKfttdykay 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 114 ------ANPWEGKSLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVA 187
Cdd:cd19147 93 evgkgkAVNYCGNHKR--SLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 188 EICTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGG-LLTGKYKYEDKDGKQPVGRFFG 261
Cdd:cd19147 171 AANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGLRSFVG 245
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
50-337 |
9.29e-25 |
|
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: 102.89 E-value: 9.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRR-------MDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVkIATK--------- 113
Cdd:cd19146 16 LGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMV-LATKyttgyrrgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 114 ----ANPWEGKSLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEI 189
Cdd:cd19146 95 pikiKSNYQGNHAK--SLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 190 CTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGlltgkyKYEDKDGKQPVGRFFGNNWAETyr 269
Cdd:cd19146 173 NAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG------QFRTEEEFKRRGRSGRKGGPQT-- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 270 nrfwkEHHFEAIALVEKaLQTTYGTNAprmTSAALRWMYHHSQLqgtrgdaV--ILGMSSLEQLEQNLAA 337
Cdd:cd19146 245 -----EKERKVSEKLEK-VAEEKGTAI---TSVALAYVMHKAPY-------VfpIVGGRKVEHLKGNIEA 298
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
50-347 |
1.01e-23 |
|
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: 98.78 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRRMDASASAasVRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGDctVKIATKANPWEGKSLK--PDSV 127
Cdd:cd19090 10 LGGVFGGVDDDEAVAT--IRAALDLGINYIDTAPAY--GDSEERLGLALAELPREP--LVLSTKVGRLPEDTADysADRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 128 RSQLETSLKRLQCPRVDLFYLHAPDHSTPVEET-----LRACHQLHQEGKFVELGLsnyASWEVAEICTLCKSNGW--IL 200
Cdd:cd19090 84 RRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGL---GGGPPDLLRRAIETGDFdvVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 201 ptVYQGmYNATTRQVEAELLP-CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqpvgrffgnNWAETYRNRFWKEHHFE 279
Cdd:cd19090 161 --TANR-YTLLDQSAADELLPaAARH-GVGVINASPLGMGLLAGRPP----------------ERVRYTYRWLSPELLDR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 280 AIALveKALQTTYGTNaprMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAATeEGPLEPAV 347
Cdd:cd19090 221 AKRL--YELCDEHGVP---LPALALRFL-----LRDPRISTVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
50-339 |
1.08e-23 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 98.44 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTM------EMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLgsgDCTVKIATKA-------NP 116
Cdd:cd19088 6 YGAMrltgpgIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPY---PDDVVIATKGglvrtgpGW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 117 WeGKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsn 196
Cdd:cd19088 83 W-GPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 197 gwiLPTVyQGMYNATTRQVEAELLPCLRHfGLRFYAYNPLAGGLLTgkykyedkdgkQPVGRFfgnnwaetyrnrfwkeh 276
Cdd:cd19088 160 ---IVSV-QNRYNLANRDDEGVLDYCEAA-GIAFIPWFPLGGGDLA-----------QPGGLL----------------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23395756 277 hfeaialveKALQTTYGTNAPRmtsAALRWMYHHSQlqgtrGDAVILGMSSLEQLEQNLAATE 339
Cdd:cd19088 207 ---------AEVAARLGATPAQ---VALAWLLARSP-----VMLPIPGTSSVEHLEENLAAAG 252
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
110-337 |
1.27e-23 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 100.06 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKA--NPWEGKSLKPDSVR---SQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASW 184
Cdd:PRK09912 94 ISTKAgyDMWPGPYGSGGSRKyllASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 185 EVAEICTLCKSngWILP-TVYQGMYNATTRQVE-AELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGK--QPVGrff 260
Cdd:PRK09912 174 RTQKMVELLRE--WKIPlLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSrmHREG--- 248
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 261 gnNWAETYRNRFWKEHHFEAIALVEKALQttygTNAPRMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAA 337
Cdd:PRK09912 249 --NKVRGLTPKMLTEANLNSLRLLNEMAQ----QRGQSMAQMALSWL-----LKDERVTSVLIGASRAEQLEENVQA 314
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
110-338 |
5.54e-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: 97.47 E-value: 5.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKAN--PWEGK-----SLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 182
Cdd:cd19151 81 ISTKAGytMWPGPygdwgSKK--YLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 183 SWEVAEICTLCKSNGwiLPT-VYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKY---EDKDGKQPvgr 258
Cdd:cd19151 159 PEEAREAAAILKDLG--TPClIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNgipEDSRAAKG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 259 ffgnnwaetyrNRFWKEHHF--EAIALVeKALQTTYGTNAPRMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLA 336
Cdd:cd19151 234 -----------SSFLKPEQIteEKLAKV-RRLNEIAQARGQKLAQMALAWV-----LRNKRVTSVLIGASKPSQIEDAVG 296
|
..
gi 23395756 337 AT 338
Cdd:cd19151 297 AL 298
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
41-337 |
3.79e-21 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 92.51 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 41 GAPLRPATVLGTMEM----GRRMDASASAASVRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGDCTVKIATK--- 113
Cdd:cd19144 9 NGPSVPALGFGAMGLsafyGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATKfgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 114 -ANPWEGK---SLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEI 189
Cdd:cd19144 87 eKNVETGEysvDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 190 CTlcksngwILP-TVYQGMYNATTRQVE---AELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgkqpvgrFFGNNWa 265
Cdd:cd19144 167 HA-------VHPiAAVQIEYSPFSLDIErpeIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDD--------FEEGDF- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23395756 266 ETYRNRFWKEHHFEAIALVE--KALQTTYGTNAPRMTsaaLRWMYhhsqlqgTRGDAV--ILGMSSLEQLEQNLAA 337
Cdd:cd19144 231 RRMAPRFQAENFPKNLELVDkiKAIAKKKNVTAGQLT---LAWLL-------AQGDDIipIPGTTKLKRLEENLGA 296
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
73-337 |
1.93e-20 |
|
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: 90.58 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 73 ERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANpWEGKS-----LKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDIVF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTR-QVEAElLPCLRH- 225
Cdd:cd19141 120 ANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQ-LPELFHk 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 226 FGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNNW------AETYRNRFWKEHHFEAIAlvekalqTTYGTNAP 297
Cdd:cd19141 199 IGVGAMTWSPLACGILSGKY----DDGVPEYSRasLKGYQWlkekilSEEGRRQQAKLKELQIIA-------DRLGCTLP 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 23395756 298 RMTSAalrWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAA 337
Cdd:cd19141 268 QLAIA---WC-----LKNEGVSSVLLGASSTEQLYENLQA 299
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
108-337 |
8.68e-20 |
|
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: 88.64 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 108 VKIATKANPWEGKSLK------PDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNy 181
Cdd:cd19145 77 VQLATKFGIHEIGGSGvevrgdPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSE- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 182 ASWEvaeicTLCKSNGwILP-TVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYKYE----DKDGKQPV 256
Cdd:cd19145 156 ASAD-----TIRRAHA-VHPiTAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEelleNSDVRKSH 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 257 GRFFGNNWaetyrnrfwkEHH---FEAI-ALVEKALQTTygtnaprmTSAALRWMYHhsqlqgtRGDAV--ILGMSSLEQ 330
Cdd:cd19145 230 PRFQGENL----------EKNkvlYERVeALAKKKGCTP--------AQLALAWVLH-------QGEDVvpIPGTTKIKN 284
|
....*..
gi 23395756 331 LEQNLAA 337
Cdd:cd19145 285 LNQNIGA 291
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
110-337 |
1.07e-19 |
|
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: 88.28 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKA--NPW-----EGKSLKpdSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 182
Cdd:cd19150 81 ISTKAgyDMWpgpygEWGSRK--YLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 183 SWEVAEICTLCKSNGWILpTVYQGMYNATTRQVE-AELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGrffg 261
Cdd:cd19150 159 PERTREAAAILRELGTPL-LIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 262 nnwaetyrNRFWKEHHFEAIALVEKALQTTYGTNA------PRMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNL 335
Cdd:cd19150 229 --------SRASKERSLSPKMLTEANLNSIRALNEiaqkrgQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENV 295
|
..
gi 23395756 336 AA 337
Cdd:cd19150 296 GA 297
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
68-337 |
2.06e-19 |
|
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: 87.28 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDcTVKIATK--ANPWegkSLKPDSVRSQLETSLKRLQCPRVDL 145
Cdd:cd19093 32 FDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKfaPLPW---RLTRRSVVKALKASLERLGLDSIDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 146 FYLHAPDH-STPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGwILPTVYQGMYNATTRQVEA-ELLPCL 223
Cdd:cd19093 108 YQLHWPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQnGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 224 RHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNNWAETYRNRfwkehhfEAIALVEKALQTTygtnaprMTSAA 303
Cdd:cd19093 187 DELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQPLL-------DALEEIAEKYGKT-------PAQVA 252
|
250 260 270
....*....|....*....|....*....|....
gi 23395756 304 LRWMYHHSQLqgtrgdaVILGMSSLEQLEQNLAA 337
Cdd:cd19093 253 LNWLIAKGVV-------PIPGAKNAEQAEENAGA 279
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
46-241 |
4.18e-19 |
|
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: 85.76 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMG-RRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSgdcTVKIATKANPWEGKslkP 124
Cdd:cd19138 12 PALGQGTWYMGeDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRD---KVFLVSKVLPSNAS---R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDhSTPVEETLRACHQLHQEGKFVELGLSNYaswEVAEICTLCKSNGWILPTVY 204
Cdd:cd19138 86 QGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNF---DTDDMEELWAVPGGGNCAAN 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 23395756 205 QGMYNATTRQVEAELLPCLRHFGLRFYAYNPLA-GGLL 241
Cdd:cd19138 162 QVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAqGGLL 199
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
68-239 |
5.28e-18 |
|
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: 82.32 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYcDGQSENILGGLGLGLGSGDctVKIATKANPwegKSLKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19073 20 VKEALELGYRHIDTAEIY-NNEAEVGEAIAESGVPRED--LFITTKVWR---DHLRPEDLKKSVDRSLEKLGTDYVDLLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEictlCKSNGWILPTVYQGMYNATTRQveAELLPCLRHFG 227
Cdd:cd19073 94 IHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE----ALDISPLPIAVNQVEFHPFLYQ--AELLEYCREND 167
|
170
....*....|..
gi 23395756 228 LRFYAYNPLAGG 239
Cdd:cd19073 168 IVITAYSPLARG 179
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
50-337 |
9.05e-18 |
|
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: 81.37 E-value: 9.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRR----MDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGdctVKIATKANPWEGKSLK-- 123
Cdd:cd19086 8 FGTWGLGGDwwgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDK---VVIATKFGNRFDGGPErp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 124 ----PDSVRSQLETSLKRLQCPRVDLFYLH-APDHSTPVEETLRACHQLHQEGKFVELGLSnyaSWEVAEICTLCKSNGw 198
Cdd:cd19086 85 qdfsPEYIREAVEASLKRLGTDYIDLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVS---VGDPEEALAALRRGG- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 ilPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKykyedkdgkqpvgrffgnnwaetyrnrfwkehhf 278
Cdd:cd19086 161 --IDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK---------------------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 23395756 279 eaialvekalqttygtnaprMTSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAA 337
Cdd:cd19086 205 --------------------LAQAALRFILSHPAV-----STVIPGARSPEQVEENAAA 238
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
73-352 |
1.64e-17 |
|
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: 82.44 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 73 ERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANpWEGKS-----LKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VEAELLPCLRHF 226
Cdd:cd19158 121 ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 227 GLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNNW------AETYRNRFWKEHHFEAIAlvekalqTTYGTNAPR 298
Cdd:cd19158 201 GVGAMTWSPLACGIVSGKY----DSGIPPYSRasLKGYQWlkdkilSEEGRRQQAKLKELQAIA-------ERLGCTLPQ 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 299 MtsaALRWMYHHSQLQgtrgdAVILGMSSLEQLEQNLAATEEGP-LEPAVVEAFD 352
Cdd:cd19158 270 L---AIAWCLRNEGVS-----SVLLGASNAEQLMENIGAIQVLPkLSSSIVHEID 316
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
73-342 |
1.98e-17 |
|
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: 82.01 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 73 ERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANpWEGKS-----LKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLY-WGGKAetergLSRKHIIEGLKGSLQRLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VEAElLPCLRH- 225
Cdd:cd19159 121 ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQ-LPELYHk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 226 FGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFgnNW------AETYRNRFWKEHHFEAIAlvEKalqttYGTNAPRM 299
Cdd:cd19159 200 IGVGAMTWSPLACGIISGKYGNGVPESSRASLKCY--QWlkerivSEEGRKQQNKLKDLSPIA--ER-----LGCTLPQL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 23395756 300 tsaALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAATEEGP 342
Cdd:cd19159 271 ---AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
50-341 |
6.53e-17 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 79.53 E-value: 6.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEM----GRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKANPWEGKSlkPD 125
Cdd:cd19096 5 FGTMRLpesdDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGPREK--FYLATKLPPWSVKS--AE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 126 SVRSQLETSLKRLQCPRVDLFYLHAPDHSTpVEETLRACH------QLHQEGKFVELGLSNYASWEVaeICTLCKSNGW- 198
Cdd:cd19096 81 DFRRILEESLKRLGVDYIDFYLLHGLNSPE-WLEKARKGGllefleKAKKEGLIRHIGFSFHDSPEL--LKEILDSYDFd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 --ILPtvyqgmYNATTRQVEAElLPCLRH---FGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrffgnnwaetyrnrfw 273
Cdd:cd19096 158 fvQLQ------YNYLDQENQAG-RPGIEYaakKGMGVIIMEPLKGGGLA------------------------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 274 kehhfeaiALVEKALQTTYGTNAPRMtSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATEEG 341
Cdd:cd19096 200 --------NNPPEALAILCGAPLSPA-EWALRFLLSHPEV-----TTVLSGMSTPEQLDENIAAADEF 253
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
73-353 |
9.96e-17 |
|
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: 80.03 E-value: 9.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 73 ERGHSELDTAFMYCDGQSE----NILGGLGLGLGSGDCTVKIATKANPWEGKSLKPDSVRSQLETSLKRLQCPRVDLFYL 148
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAErtlgNILKSKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 149 HAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVEAELLPCLRH-FG 227
Cdd:cd19160 124 NRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHkIG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 228 LRFYAYNPLAGGLLTGKYkyEDKDGKQPVGRFFGNNW-AETYRNRFWKEHHFEAIAL--VEKALQTTygtnaprMTSAAL 304
Cdd:cd19160 204 VGSVTWSPLACGLITGKY--DGRVPDTCRAAVKGYQWlKEKVQSEEGKKQQAKVKELhpIADRLGCT-------VAQLAI 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 23395756 305 RWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAATEE-GPLEPAVVEAFDQ 353
Cdd:cd19160 275 AWC-----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
68-337 |
3.22e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 74.54 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTvkIATKANpWEGKSLKPDSVRSQLETSLKRLQCPRVDLFY 147
Cdd:cd19105 31 LRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLRRDKVF--LATKAS-PRLDKKDKAELLKSVEESLKRLQTDYIDIYQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 148 LHAPDHSTP---VEETLRACHQLHQEGKFVELGLS-NYASWEVAEicTLCKSnGWIlpTVYQGMYNATTRQVEA-ELLP- 221
Cdd:cd19105 108 LHGVDTPEErllNEELLEALEKLKKEGKVRFIGFStHDNMAEVLQ--AAIES-GWF--DVIMVAYNFLNQPAELeEALAa 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 222 CLRHfGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVgrffgnnwaetyrnrfwkehhfeaialvekalqttygtnaprmTS 301
Cdd:cd19105 183 AAEK-GIGVVAMKTLAGGYLQPALLSVLKAKGFSL-------------------------------------------PQ 218
|
250 260 270
....*....|....*....|....*....|....*.
gi 23395756 302 AALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAA 337
Cdd:cd19105 219 AALKWVLSNPRV-----DTVVPGMRNFAELEENLAA 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
50-337 |
4.65e-15 |
|
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: 74.19 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGR---RMDASASAASVRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGDCTvkIATKAnpWEG------- 119
Cdd:cd19095 5 LGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDDLF--IATKV--GTHgeggrdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAswevAEICTLCKSNgwi 199
Cdd:cd19095 79 KDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASG--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 200 LPTVYQGMYNATTRQvEAELLPCLRHFGLRFYAYNPLAGGLLtgkykyedkdgkqpVGRFFGNNWAETYRNRFWKEHHFE 279
Cdd:cd19095 152 VFDVVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRL--------------RRRVRRRPLYADYARRPEFAAEIG 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 280 AIALVEkalqttygtnaprmtsAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAA 337
Cdd:cd19095 217 GATWAQ----------------AALRFVLSHPGV-----SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
46-241 |
5.47e-15 |
|
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: 74.14 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGRRM--DASASAASVRAF---LERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKANPwegK 120
Cdd:cd19137 5 PALGLGTWGIGGFLtpDYSRDEEMVELLktaIELGYTHIDTAEMYGGGHTEELVGKAIKDFPRED--LFIVTKVWP---T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 SLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSngwil 200
Cdd:cd19137 80 NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT----- 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 23395756 201 PTVY-QGMYNATTRQVEAE-LLPCLRHFGLRFYAYNPLAGGLL 241
Cdd:cd19137 155 PIVCnQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLE 197
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
108-354 |
1.12e-14 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 74.47 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 108 VKIATKANPWegkSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLR------ACHQLHQEGKFVELGLSNY 181
Cdd:COG1453 70 VILATKLPPW---VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHIGFSTH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 182 ASWEVAEicTLCKSNGWilpTVYQGMYNA--TTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrf 259
Cdd:COG1453 147 GSLEVIK--EAIDTGDF---DFVQLQYNYldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA----------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 260 fgnnwaetyrnrfwkEHHFEAIALVEKalqttygtnaPRMT-SAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAAT 338
Cdd:COG1453 205 ---------------NPPEKLVELLCP----------PLSPaEWALRFLLSHPEV-----TTVLSGMSTPEQLDENLKTA 254
|
250
....*....|....*..
gi 23395756 339 EEG-PLEPAVVEAFDQA 354
Cdd:COG1453 255 DNLePLTEEELAILERL 271
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
49-339 |
1.54e-14 |
|
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: 72.97 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 49 VLGTMEMGR-RMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKA--------NPWEG 119
Cdd:cd19092 10 VLGCMRLADwGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCgirlgddpRPGRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KS--LKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVA---------- 187
Cdd:cd19092 90 KHydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEllqsyldqpl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 188 -----EICTLCksngwiLPTVYQGMYNAttrqveaellpCLRHfGLRFYAYNPLAGglltgkykyedkdgkqpvGRFFGN 262
Cdd:cd19092 170 vtnqiELSLLH------TEAIDDGTLDY-----------CQLL-DITPMAWSPLGG------------------GRLFGG 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 263 NWAETYRNRfwkehhfeaiALVEKaLQTTYGTNAprmTSAALRW-MYHHSQLQgtrgdaVILGMSSLEQLEQNLAATE 339
Cdd:cd19092 214 FDERFQRLR----------AALEE-LAEEYGVTI---EAIALAWlLRHPARIQ------PILGTTNPERIRSAVKALD 271
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
50-335 |
1.77e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 73.73 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMEMGRRMDASASAASVRAFLERGHSELDTAFMY-------CDGQSENILGGLGLGLGSGDCTVkIATK-ANPWEG-- 119
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSREKLI-IASKvSGPSRNnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KSLKPD------SVRSQLETSLKRLQCPRVDLFYLHAPDH--------------STPVE---ETLRACHQLHQEGKFVEL 176
Cdd:PRK10625 97 KGIRPNqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdSAPAVsllETLDALAEQQRAGKIRYI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 177 GLSNYASWEVAEICTLCKSNGwiLPTVY--QGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQ 254
Cdd:PRK10625 177 GVSNETAFGVMRYLHLAEKHD--LPRIVtiQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 255 PVGrffGNNWAETYRNRFWKEHHFEAIAlVEKALQTTYGTNAPRMTSAALRwmyhhsqlQGTRGDAVILGMSSLEQLEQN 334
Cdd:PRK10625 251 PAG---ARNTLFSRFTRYSGEQTQKAVA-AYVDIAKRHGLDPAQMALAFVR--------RQPFVASTLLGATTMEQLKTN 318
|
.
gi 23395756 335 L 335
Cdd:PRK10625 319 I 319
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
50-337 |
8.00e-14 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 70.47 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 50 LGTMemgrRMDASASAASVRAFLERGHSELDTAFMYcdgqsEN-------ILgglglglgsgDCTVK-----IATKANPW 117
Cdd:COG0656 10 LGTW----QLPGEEAAAAVRTALEAGYRHIDTAAMY-----GNeegvgeaIA----------ASGVPreelfVTTKVWND 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 118 EgksLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHsTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsng 197
Cdd:COG0656 71 N---HGYDDTLAAFEESLERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 198 wILPTVYQGMYNATTRQveAELLPCLRHFGLRFYAYNPLA-GGLLtgkykyedkdgKQPVgrffgnnwaetyrnrfwkeh 276
Cdd:COG0656 144 -VKPAVNQVELHPYLQQ--RELLAFCREHGIVVEAYSPLGrGKLL-----------DDPV-------------------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23395756 277 hFEAIAlvEKalqttYGtnaprMTSA--ALRWmyhHSQlqgtRGDAVILGMSSLEQLEQNLAA 337
Cdd:COG0656 190 -LAEIA--EK-----HG-----KTPAqvVLRW---HLQ----RGVVVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
110-239 |
4.91e-13 |
|
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: 68.28 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKANPwegKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAP------DHSTPVEETLRACHQLHQEGKFVELGLSNYAS 183
Cdd:cd19071 59 ITTKLWP---TDHGYERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 184 WEVAEICTLCKsngwILPTVYQGMYNATTRQveAELLP-CLRHfGLRFYAYNPLAGG 239
Cdd:cd19071 136 EHLEELLAAAR----IKPAVNQIELHPYLQQ--KELVEfCKEH-GIVVQAYSPLGRG 185
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
46-344 |
7.09e-13 |
|
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: 68.51 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGT-----------MEMGRRMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDctVKIATKA 114
Cdd:cd19103 5 PKIALGTwswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYPRED--YIISTKF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 115 NPwEGKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPdhsTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCK 194
Cdd:cd19103 83 TP-QIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 195 SNGWILPTVyQGMYNATTRQVE-AELLP-CLRHfGLRFYAYNPLAGGLLTGKYkyedkDGKQPVGRffGNNWAETYrNRF 272
Cdd:cd19103 159 KAGVSLSAV-QNHYSLLYRSSEeAGILDyCKEN-GITFFAYMVLEQGALSGKY-----DTKHPLPE--GSGRAETY-NPL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23395756 273 WKEhhFEAIALVEKALQTTYGTNAPRMTSAALRwmyhhsqlqgTRGDAVILGMSSLEQLEQ-------NLAATEEGPLE 344
Cdd:cd19103 229 LPQ--LEELTAVMAEIGAKHGASIAQVAIAWAI----------AKGTTPIIGVTKPHHVEDaaraasiTLTDDEIKELE 295
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
68-343 |
2.13e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 66.40 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGsgdcTVKIATK--ANPWEGKSLKpDSVRSQLETSLKRLQCPRVDL 145
Cdd:cd19097 32 LEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKlpPLKEDKKEDE-AAIEASVEASLKRLKVDSLDG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 146 FYLHAPD----HSTPVEETLRachQLHQEGKFVELGLSNYASWEVAEICTLCKsngwilPTVYQGMYNA-TTRQVEAELL 220
Cdd:cd19097 105 LLLHNPDdllkHGGKLVEALL---ELKKEGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNIlDQRFLKSGLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 221 PCLRHFGLRFYAYNPLAGGLLTgkykyedKDGKQPVGRFfgnnwaetyrnRFWKEHH--FEAIAlvekalqTTYGTNAPr 298
Cdd:cd19097 176 AKLKKKGIEIHARSVFLQGLLL-------MEPDKLPAKF-----------APAKPLLkkLHELA-------KKLGLSPL- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 23395756 299 mtSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATEEGPL 343
Cdd:cd19097 230 --ELALGFVLSLPEI-----DKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
68-352 |
4.22e-12 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 66.33 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSE----NILGGLGLGLGSGDCTVKIATKANPwEGKSLKPDSVRSQLETSLKRLQCPRV 143
Cdd:cd19142 37 VTLAYENGINYFDTSDAFTSGQAEtelgRILKKKGWKRSSYIVSTKIYWSYGS-EERGLSRKHIIESVRASLRRLQLDYI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 144 DLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VEAELLPC 222
Cdd:cd19142 116 DIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 223 LRHFGLRFYAYNPLAGGLLTGK--------YKYEDKDGKQPVGRfFGNNWAETYRNRfwKEHHFEAIALVEKaLQTTygt 294
Cdd:cd19142 196 YNKVGVGLITWSPLSLGLDPGIseetrrlvTKLSFKSSKYKVGS-DGNGIHEETRRA--SHKLRELSLIAER-LGCD--- 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 23395756 295 naprMTSAALRWMYHHSQLQgtrgdAVILGMSSLEQLEQNLAATEEGP-LEPAVVEAFD 352
Cdd:cd19142 269 ----LTQLLIAWSLKNENVQ-----CVLIGASSLEQLYSQLNSLQLLPkLNSAVMEELE 318
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
69-337 |
5.34e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 65.69 E-value: 5.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 69 RAFLERGHSELDTAFMYcdGQSENIL---GGLGLGLGSGDCTVKIATKANPWEGK-SLKPDSVRSQLETSLKRLQCPRVD 144
Cdd:cd19101 30 AAYVDAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVPDPGElTMTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 145 LFYLHAPDHSTP-VEETLRACHQLHQEGKFVELGLSNYASWEVAEICtlckSNGwiLPTVY-QGMYNATTRQVEAELLP- 221
Cdd:cd19101 108 LVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----DAG--VPIVSnQVQYSLLDRRPENGMAAl 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 222 CLRHfGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGRFFGNNWAETYRNRFWKEH----HFEAIALVEKALQTTYGTNap 297
Cdd:cd19101 182 CEDH-GIKLLAYGTLAGGLLSEKYL-----GVPEPTGPALETRSLQKYKLMIDEWggwdLFQELLRTLKAIADKHGVS-- 253
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 23395756 298 rMTSAALRWMyhhsqLQGTRGDAVILGMSSLEQLEQNLAA 337
Cdd:cd19101 254 -IANVAVRWV-----LDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
46-194 |
1.98e-11 |
|
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: 64.06 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMgrrmDASASAASVRAFLERGHSELDTAFMYcdgQSE----NILGGLGLGLGSGDCTVKIATKANPWEgks 121
Cdd:cd19111 5 PVIGLGTYQS----PPEEVRAAVDYALFVGYRHIDTALSY---QNEkaigEALKWWLKNGKLKREEVFITTKLPPVY--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 122 LKPDSVRSQLETSLKRLQCPRVDLFYLHAP-------------DHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAE 188
Cdd:cd19111 75 LEFKDTEKSLEKSLENLKLPYVDLYLIHHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINK 154
|
....*.
gi 23395756 189 ICTLCK 194
Cdd:cd19111 155 ILAYAK 160
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
123-337 |
9.05e-11 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 62.26 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCP-RVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSnyaswEV-AEicTLCKSNGWIL 200
Cdd:cd19077 92 SPEAVRKSIENILRALGGTkKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLS-----EVsAE--TIRRAHAVHP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 201 PTVYQGMYNATTRQVE-AELLPCLRHFGLRFYAYNPLAGGLLTGKYKYED----KDGKQPVGRFFGNNWAETyrnrfwke 275
Cdd:cd19077 165 IAAVEVEYSLFSREIEeNGVLETCAELGIPIIAYSPLGRGLLTGRIKSLAdipeGDFRRHLDRFNGENFEKN-------- 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23395756 276 hhfeaIALVEkALQTTYGTNAPRMTSAALRWMYHhsqlQGTRGDAVILGMSSLEQLEQNLAA 337
Cdd:cd19077 237 -----LKLVD-ALQELAEKKGCTPAQLALAWILA----QSGPKIIPIPGSTTLERVEENLKA 288
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
46-336 |
6.72e-10 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 58.81 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMemgrRMDASASAASVRAFLERGHSELDTAFMYcdgQSENilgglGLGLGSGDCTVK-----IATKAnpWEGK 120
Cdd:cd19140 9 PALGLGTY----PLTGEECTRAVEHALELGYRHIDTAQMY---GNEA-----QVGEAIAASGVPrdelfLTTKV--WPDN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 SLKPDSVRSqLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSngwil 200
Cdd:cd19140 75 YSPDDFLAS-VEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA----- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 201 PTVyqgmynatTRQVE-------AELLPCLRHFGLRFYAYNPLAgglltgkykyedkdgkqpvgrffgnnwaetyRNRFW 273
Cdd:cd19140 149 PLF--------TNQVEyhpyldqRKLLDAAREHGIALTAYSPLA-------------------------------RGEVL 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23395756 274 KEHHFEAIALvekalqttygtnAPRMTSA--ALRWMyhhsqLQGTrGDAVILGMSSLEQLEQNLA 336
Cdd:cd19140 190 KDPVLQEIGR------------KHGKTPAqvALRWL-----LQQE-GVAAIPKATNPERLEENLD 236
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
110-344 |
1.95e-08 |
|
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: 54.86 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKA-----NPWEGKSLKPDSVRSQLETSLKRLQCPRVDLFYLH----APDHSTPVEETLRACHQLHQEGKFVELGLSN 180
Cdd:cd19163 79 LATKVgryglDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGITG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 181 Y---ASWEVAE--------ICTLCKSNgwilptvyqgMYNATTRqveaELLPCLRHFGLRFYAYNPLAGGLLTgkykyed 249
Cdd:cd19163 159 YpldVLKEVLErspvkidtVLSYCHYT----------LNDTSLL----ELLPFFKEKGVGVINASPLSMGLLT------- 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 250 KDGKQPvgrffgnnwaetyrnrfWKEHHFEAIALVEKALQ--TTYGTNAPRMtsaALRWMYHHSQLQGTrgdavILGMSS 327
Cdd:cd19163 218 ERGPPD-----------------WHPASPEIKEACAKAAAycKSRGVDISKL---ALQFALSNPDIATT-----LVGTAS 272
|
250
....*....|....*..
gi 23395756 328 LEQLEQNLAATEEGPLE 344
Cdd:cd19163 273 PENLRKNLEAAEEPLDA 289
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
125-242 |
2.51e-08 |
|
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: 54.17 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAP-----DHSTPVE-----ETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCK 194
Cdd:cd19136 76 EKARAACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 23395756 195 sngwILPTVYQGMYNAttRQVEAELLPCLRHFGLRFYAYNPLAGGLLT 242
Cdd:cd19136 156 ----VPPAVNQVEFHP--HLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
125-239 |
7.11e-08 |
|
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: 52.96 E-value: 7.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDHStpVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 204
Cdd:cd19133 80 EKAKKAFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE----VKPAVN 153
|
90 100 110
....*....|....*....|....*....|....*
gi 23395756 205 QGMYNATTRQVEAelLPCLRHFGLRFYAYNPLAGG 239
Cdd:cd19133 154 QIETHPFNQQIEA--VEFLKKYGVQIEAWGPFAEG 186
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
46-194 |
9.36e-08 |
|
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: 52.80 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMgrrmDASASAASVRAFLERGHSELDTAFMYcdgQSENILGGLGLGLGSGDcTVK-----IATKANPWEgk 120
Cdd:cd19154 13 PLIGLGTWQS----KGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELLEEG-VVKredlfITTKLWTHE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 sLKPDSVRSQLETSLKRLQCPRVDLFYLHAP-----------------DHSTPV--EETLRACHQLHQEGKFVELGLSNY 181
Cdd:cd19154 83 -HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmSIHDAVdvEDVWRGMEKVYDEGLTKAIGVSNF 161
|
170
....*....|...
gi 23395756 182 ASWEVAEICTLCK 194
Cdd:cd19154 162 NNDQIQRILDNAR 174
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
68-336 |
9.44e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 53.09 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSEN-----ILGGLGLGLGSGDcTVKIATKA-----------NPWE------------- 118
Cdd:cd19099 27 LKAALDSGINVIDTAINYRGGRSERligkaLRELIEKGGIKRD-EVVIVTKAgyipgdgdeplRPLKyleeklgrglidv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 119 ------GKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPV----------EETLRACHQLHQEGKfvelgLSNY- 181
Cdd:cd19099 106 adsaglRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLElgeeefydrlEEAFEALEEAVAEGK-----IRYYg 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 182 -ASWEVAEI---------------------------------CTLCKSNGWILPTVYQGMYnattrqveAELLPCLRHFG 227
Cdd:cd19099 181 iSTWDGFRAppalpghlsleklvaaaeevggdnhhfkviqlpLNLLEPEALTEKNTVKGEA--------LSLLEAAKELG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 228 LRFYAYNPLAGGLLTGKykyedkdgkqpvgrffgnnwaetyRNRFWKEHHFEAIALVEKALQttYGTNAPRMTSaalrwm 307
Cdd:cd19099 253 LGVIASRPLNQGQLLGE------------------------LRLADLLALPGGATLAQRALQ--FARSTPGVDS------ 300
|
330 340
....*....|....*....|....*....
gi 23395756 308 yhhsqlqgtrgdaVILGMSSLEQLEQNLA 336
Cdd:cd19099 301 -------------ALVGMRRPEHVDENLA 316
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
125-241 |
1.12e-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: 52.33 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPV-------EETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsng 197
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS--- 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 23395756 198 wILPTVYQGMYNATTRQVeaELLPCLRHFGLRFYAYNPLAGGLL 241
Cdd:cd19135 160 -VVPHVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA 200
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
117-236 |
1.40e-07 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 52.39 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 117 WEGKSlKPDSVRSQLETSLKRLQCPRVDLFYLHAP------DH-------------STPVEETLRACHQLHQEGKFVELG 177
Cdd:cd19106 75 WNTKH-HPEDVEPALRKTLKDLQLDYLDLYLIHWPyafergDNpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIG 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23395756 178 LSNYASWEVAEICtlckSNGWILPTVYqgmynattrQVEA-------ELLPCLRHFGLRFYAYNPL 236
Cdd:cd19106 154 LSNFNSRQIDDIL----SVARIKPAVL---------QVEChpylaqnELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
110-237 |
1.42e-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: 52.23 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKANPwegkslKPDSVRSQLETSLKRLQCPRVDLFYLHAP----DHSTPVEETLRACHQLHQEGKFVELGLSNYASWE 185
Cdd:cd19120 70 ITTKVSP------GIKDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIED 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 23395756 186 VAEICTLCKsngwILPTVYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLA 237
Cdd:cd19120 144 LEELLDTAK----IKPAVNQIEFHPYLYPQQPALLEYCREHGIVVSAYSPLS 191
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
110-336 |
2.22e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 51.33 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 110 IATKANPWegkslKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEET------LRACHQLHQEGKFVELGLSNYaS 183
Cdd:cd19100 70 LATKTGAR-----DYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISGH-S 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 184 WEVAEicTLCKSNGW--ILPTV-YQGMYNattRQVEAELLP-CLRHfGLRFYAYNPLAGGLLTGKykyedkdgkqpvgrf 259
Cdd:cd19100 144 PEVLL--RALETGEFdvVLFPInPAGDHI---DSFREELLPlAREK-GVGVIAMKVLAGGRLLSG--------------- 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23395756 260 fgnnWAETYRnrfwkehhfeaialvekalqttygtnaprmtsAALRWMYhhsQLQGTrgDAVILGMSSLEQLEQNLA 336
Cdd:cd19100 203 ----DPLDPE--------------------------------QALRYAL---SLPPV--DVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
46-181 |
2.90e-07 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 51.20 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMemgrRMDASASAASVRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGD---CTVKIatkanpWEgKSL 122
Cdd:cd19139 2 PAFGLGTF----RLKDDVVIDSVRTALELGYRHIDTAQIY--DNEAAVGQAIAESGVPRDelfITTKI------WI-DNL 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLH--APDHSTPVEETLRACHQLHQEGKFVELGLSNY 181
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNF 129
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
68-355 |
4.55e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 51.11 E-value: 4.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSE-NILGGLGLGLGsgdcTVKIATKAnpwegkSLKPDS-------VRSQLETSLKRLQ 139
Cdd:cd19104 38 VRRALDLGINFFDTAPSYGDGKSEeNLGRALKGLPA----GPYITTKV------RLDPDDlgdiggqIERSVEKSLKRLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 140 CPRVDLFYLH---------------APDHSTPVEETLRACHQLHQEGKFVELGLSnyASWEVAEICTLCKSNGW------ 198
Cdd:cd19104 108 RDSVDLLQLHnrigderdkpvggtlSTTDVLGLGGVADAFERLRSEGKIRFIGIT--GLGNPPAIRELLDSGKFdavqvy 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 199 ---ILPTVYQGMYNATTRQVEAELLP-CLRHfGLRFYAYNPLAGGLLTGKykyEDKDGKQPVgrffgnnwaeTYRNRFWK 274
Cdd:cd19104 186 ynlLNPSAAEARPRGWSAQDYGGIIDaAAEH-GVGVMGIRVLAAGALTTS---LDRGREAPP----------TSDSDVAI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 275 EHHFEA--IALVEKALQTtygtnaprMTSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAATEEGPLEPAVVEAFD 352
Cdd:cd19104 252 DFRRAAafRALAREWGET--------LAQLAHRFALSNPGV-----STVLVGVKNREELEEAVAAEAAGPLPAENLARLE 318
|
...
gi 23395756 353 QAW 355
Cdd:cd19104 319 ALW 321
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
124-236 |
6.64e-07 |
|
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: 50.42 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 124 PDSVRSQLETSLKRLQCPRVDLFYLHAPDH--------------STPVEETLRACHQLHQEGKFVELGLSNYASWEVAEI 189
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 23395756 190 CTLCKsngwILPTVYQGMYNATTRQveAELLPCLRHFGLRFYAYNPL 236
Cdd:cd19125 164 LAVAR----VPPAVNQVECHPGWQQ--DKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
123-238 |
2.68e-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: 48.29 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLHAP-------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAS 183
Cdd:cd19128 73 QPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYST 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 184 WEVAEICTLCKsngwILPTVYQ---GMYNATTRQVEAellpCLRHfGLRFYAYNPLAG 238
Cdd:cd19128 153 KLLTDLLNYCK----IKPFMNQiecHPYFQNDKLIKF----CIEN-NIHVTAYRPLGG 201
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
68-255 |
3.71e-06 |
|
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: 47.75 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGDcTVKIATKA-NPWEGKslkpDSVRSQLETSLKRLQCPRVDLF 146
Cdd:cd19131 29 VREALEVGYRSIDTAAIY--GNEEGVGKAIRASGVPRE-ELFITTKLwNSDQGY----DSTLRAFDESLRKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 147 YLHAPdhsTPVE----ETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQGMYNATTRQVEAELLpC 222
Cdd:cd19131 102 LIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG----VVPVVNQIELHPRFQQRELRAF-H 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 23395756 223 LRHfGLRFYAYNPLA-GGLLTGKY--KYEDKDGKQP 255
Cdd:cd19131 174 AKH-GIQTESWSPLGqGGLLSDPVigEIAEKHGKTP 208
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
46-337 |
8.56e-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: 46.97 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMEMGR--RMDASASAASVRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVkiATKA----NPWEG 119
Cdd:cd19162 1 PRLGLGAASLGNlaRAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARHPRAEYVV--STKVgrllEPGAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 120 KSLKP---------DSVRSQLETSLKRLQCPRVDLFYLHAPDH--STPVEETLRACHQLHQEGKFVELGLsnyASWEVAE 188
Cdd:cd19162 79 GRPAGadrrfdfsaDGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGV---GVTDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 189 ICTLCKSNGW--ILPTvyqGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGkykyedkdGKQPVGRFFGNNWAE 266
Cdd:cd19162 156 LLRAARRADVdvVMVA---GRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT--------DDPAGDRYDYRPATP 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23395756 267 TYRNRfwkehhfeAIALVEKAlqTTYGTNAPrmtSAALRWMYHHSQLQgtrgdAVILGMSSLEQLEQNLAA 337
Cdd:cd19162 225 EVLAR--------ARRLAAVC--RRYGVPLP---AAALQFPLRHPAVA-----SVVVGAASPAELRDNLAL 277
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
68-340 |
1.51e-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: 45.99 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYCDGQSENILGGLGLGLGSGDCTVKIATKANPW--EGKSLKPDSVRSQLETSLKRLQCPRVDL 145
Cdd:cd19153 39 VAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYrdSEFDYSAERVRASVATSLERLHTTYLDV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 146 FYLHA---PDHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKSNGwilPTVYQGMYNATTRQVEAE-LLP 221
Cdd:cd19153 119 VYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS---LDAVLSYCHLTLQDARLEsDAP 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 222 CLRH-FGLRFYAYNPLAGGLLTGKykyedkdGKQPvgrffgnnwaetyrnrfWKEHHFEAIALVEKALQTTYGTNApRMT 300
Cdd:cd19153 196 GLVRgAGPHVINASPLSMGLLTSQ-------GPPP-----------------WHPASGELRHYAAAADAVCASVEA-SLP 250
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 23395756 301 SAALRWMYHHSQLQGTrgdaVILGMSSLEQLEQNLAATEE 340
Cdd:cd19153 251 DLALQYSLAAHAGVGT----VLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
125-239 |
3.10e-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: 45.07 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDhSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 204
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVN 155
|
90 100 110
....*....|....*....|....*....|....*
gi 23395756 205 QGMYNAttRQVEAELLPCLRHFGLRFYAYNPLAGG 239
Cdd:cd19157 156 QVEFHP--RLTQKELRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
40-239 |
3.43e-05 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 45.09 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 40 SGAPLRPATVLGTMemgrRMDASASAASVRAFLERGHSELDTAFMYcDGQSEnILGGLGLGLGSGdcTVK-----IATKA 114
Cdd:cd19123 7 SNGDLIPALGLGTW----KSKPGEVGQAVKQALEAGYRHIDCAAIY-GNEAE-IGAALAEVFKEG--KVKredlwITSKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 115 npWEgKSLKPDSVRSQLETSLKRLQCPRVDLFYLHAP---------DHST---------PVEETLRACHQLHQEGKFVEL 176
Cdd:cd19123 79 --WN-NSHAPEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfPESGedllslspiPLEDTWRAMEELVDKGLCRHI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 177 GLSNYASWEVAEICTLCKsngwILPTVyqgmynattRQVE-------AELLPCLRHFGLRFYAYNPLAGG 239
Cdd:cd19123 156 GVSNFSVKKLEDLLATAR----IKPAV---------NQVElhpylqqPELLAFCRDNGIHLTAYSPLGSG 212
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
125-241 |
6.35e-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: 43.97 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLH--APDHstpVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPT 202
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHwpGKDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPA 152
|
90 100 110
....*....|....*....|....*....|....*....
gi 23395756 203 VYQGMYNAttRQVEAELLPCLRHFGLRFYAYNPLAGGLL 241
Cdd:cd19126 153 VNQVEFHP--YLTQKELRGYCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
125-337 |
7.40e-05 |
|
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: 44.14 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETL-----------RACHQLHQEGKFVELGL-SNyaSWEVAE-ICT 191
Cdd:cd19152 103 DGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEELREEGVIKAIGLgVN--DWEVILrILE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 192 LCKSNgWILptvYQGMYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGLLTGkykyedkdgkqpvGRFFGnnwaeTYRNR 271
Cdd:cd19152 181 EADLD-WVM---LAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAG-------------GDNFD-----YYEYG 238
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 272 fwkEHHFEAIALVEK--ALQTTYGTNAPrmtSAALRWMYHHSQLqgtrgDAVILGMSSLEQLEQNLAA 337
Cdd:cd19152 239 ---PAPPELIARRDRieALCEQHGVSLA---AAALQFALAPPAV-----ASVAPGASSPERVEENVAL 295
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
68-236 |
1.05e-04 |
|
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: 43.67 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYC-DGQSENILGGLGLGLGSGDCTVKIATKANPwegKSLKPDSVRSQLETSLKRLQCPRVDLF 146
Cdd:cd19155 31 VDTALEAGYRHIDTAYVYRnEAAIGNVLKKWIDSGKVKREELFIVTKLPP---GGNRREKVEKFLLKSLEKLQLDYVDLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 147 YLHAP---------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQ 205
Cdd:cd19155 108 LIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR----IKPANLQ 183
|
170 180 190
....*....|....*....|....*....|.
gi 23395756 206 GMYNATTRQveAELLPCLRHFGLRFYAYNPL 236
Cdd:cd19155 184 VELHVYLQQ--KDLVDFCSTHSITVTAYAPL 212
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
123-240 |
2.46e-04 |
|
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: 42.44 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLHAP--------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYA 182
Cdd:cd19129 78 RPERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVS 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 23395756 183 SWEVAEICTLCKsngwILPTVYQgmYNATTRQVEAELLPCLRHFGLRFYAYNPLAGGL 240
Cdd:cd19129 158 LEKLREIFEAAR----IKPAVVQ--VESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
125-241 |
2.94e-04 |
|
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: 42.12 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 125 DSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVeETLRACHQLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 204
Cdd:cd19156 80 ESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVN 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 23395756 205 QgmynattrqveAELLPCLRHFGLRFY---------AYNPLAGGLL 241
Cdd:cd19156 155 Q-----------IELHPLLTQEPLRKFckekniaveAWSPLGQGKL 189
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
121-197 |
4.34e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 41.83 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 121 SLKPDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRAchqlHQEGKF----VELglsnYASWEVAEICT---LC 193
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPK----DENGKLifdtVDL----CATWEAMEKCKdagLA 155
|
....
gi 23395756 194 KSNG 197
Cdd:cd19108 156 KSIG 159
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
68-241 |
6.46e-04 |
|
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: 40.99 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 68 VRAFLERGHSELDTAFMYcdGQSENILGGLGLGLGSGD---CTVKIATKANPWegkslkpDSVRSQLETSLKRLQCPRVD 144
Cdd:cd19134 30 VSAALEAGYRLIDTAAAY--GNEAAVGRAIAASGIPRGelfVTTKLATPDQGF-------TASQAACRASLERLGLDYVD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 145 LFYLH--APDHSTPVeETLRACHQLHQEGKFVELGLSNYASWEVAEICtlckSNGWILPTVYQ-----GMYNATTRQVEA 217
Cdd:cd19134 101 LYLIHwpAGREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLI----DLTFFTPAVNQielhpLLNQAELRKVNA 175
|
170 180
....*....|....*....|....
gi 23395756 218 EllpclrhFGLRFYAYNPLAGGLL 241
Cdd:cd19134 176 Q-------HGIVTQAYSPLGVGRL 192
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
46-181 |
3.25e-03 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 38.85 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 46 PATVLGTMemgrRMDASASAASVRAFLERGHSELDTAFMYcDGQSENILGGLGLGLGSGD--CTVKIATkANpwegksLK 123
Cdd:PRK11172 4 PAFGLGTF----RLKDQVVIDSVKTALELGYRAIDTAQIY-DNEAAVGQAIAESGVPRDElfITTKIWI-DN------LA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 124 PDSVRSQLETSLKRLQCPRVDLFYLH--APDHSTPVEETLRACHQLHQEGKFVELGLSNY 181
Cdd:PRK11172 72 KDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNF 131
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
123-205 |
3.95e-03 |
|
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: 38.80 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 123 KPDSVRSQLETSLKRLQCPRVDLFYLHAP------------DHSTPVE----ETLRACHQLHQEGKFVELGLSNYASWEV 186
Cdd:cd19116 84 EREQVEPALRESLKRLGLDYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSEQI 163
|
90
....*....|....*....
gi 23395756 187 AEICTLCKsngwILPTVYQ 205
Cdd:cd19116 164 NRLLSNCN----IKPAVNQ 178
|
|
| AKR_AKR1D1-3 |
cd19109 |
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes ... |
124-225 |
5.96e-03 |
|
AKR1D family of aldo-keto reductase (AKR); The AKR1D family of aldo-keto reductase includes 3-oxo-5-beta-steroid 4-dehydrogenase (EC 1.3.1.3) from Homo sapiens (AKR1D1), Rattus norvegicus (liver, AKR1D2), and Oryctolagus cuniculus (AKR1D3). 3-oxo-5-beta-steroid 4-dehydrogenase, also called delta(4)-3-ketosteroid 5-beta-reductase (EC 1.3.99.6), or delta(4)-3-oxosteroid 5-beta-reductase, or 5-beta-reductase, efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites.
Pssm-ID: 381335 [Multi-domain] Cd Length: 308 Bit Score: 38.24 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23395756 124 PDSVRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETlracHQLHQEGKFVELGLSNYASWEVAEICT---LCKSngwil 200
Cdd:cd19109 81 PELVRPTLERTLKVLQLDYVDLYIIEMPMAFKPGDEI----YPRDENGKWLYHKTNLCATWEALEACKdagLVKS----- 151
|
90 100
....*....|....*....|....*.
gi 23395756 201 ptvyQGMYNATTRQVEAEL-LPCLRH 225
Cdd:cd19109 152 ----IGVSNFNRRQLELILnKPGLKH 173
|
|
| |
