|
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 ... |
38-347 |
2.99e-179 |
|
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: 499.00 E-value: 2.99e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 38 VASVLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGlgggDCRVKIATKANPWDGKSL 114
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG----ERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPT 194
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 195 VYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgKQPVGRFFGNS-WAETYRNRFWKEHHFEAI 273
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNNaLGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327764 274 ALVEKALQaaygASAPSVTSAALRWMYHHSQLQGAHGDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAW 347
Cdd:cd19075 235 EKVEEAAE----KEGISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
42-347 |
1.63e-61 |
|
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: 199.63 E-value: 1.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDD--VVIATKVgrrmgPGPNGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 114 LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsnGWILP 193
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 194 TVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKqpvgrffGNSWAETYRNRFWKEHHFEAI 273
Cdd:COG0667 174 VAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPE-------GDRAATNFVQGYLTERNLALV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327764 274 ALVeKALQAAYGASAPSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEgPLEPAVVDAFNQAW 347
Cdd:COG0667 247 DAL-RAIAAEHGVTPAQL---ALAWLLAQPGV-----TSVIPGARSPEQLEENLAAADL-ELSAEDLAALDAAL 310
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
41-328 |
1.36e-55 |
|
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: 181.56 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKA-----NPWDGKSLK 115
Cdd:cd06660 4 GLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRD-DVVIATKGghppgGDPSRSRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 116 PDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTV 195
Cdd:cd06660 83 PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 196 YQGMYN-ATTRQVETELFPCLRHFGLRFYAYNPLAGGLltgkykyedkdgkqpvgrffgnswaetyrnrfwkehhfeaia 274
Cdd:cd06660 163 VQPQYSlLDRSPMEEELLDWAEENGLPLLAYSPLARGP------------------------------------------ 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41327764 275 lvekalqaaygasapsvTSAALRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLA 328
Cdd:cd06660 201 -----------------AQLALAWLLSQP-----FVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
37-331 |
3.38e-53 |
|
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: 177.76 E-value: 3.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 37 RVASV-LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKA------N 107
Cdd:cd19087 12 KVSRLcLGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIA-----GRRddIVLATKVfgpmgdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 108 PWD-GKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCK 186
Cdd:cd19087 87 PNDrGLSRR--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 187 SNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNswaETYRNRFWK 266
Cdd:cd19087 165 RRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYG---KGKRPESGRLVER---ARYQARYGL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327764 267 EHHFEAIALVEkALQAAYGASAPSVtsaALRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAATE 331
Cdd:cd19087 239 EEYRDIAERFE-ALAAEAGLTPASL---ALAWVLSHPAVTSP-----IIGPRTLEQLEDSLAALE 294
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
41-344 |
6.64e-52 |
|
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: 174.32 E-value: 6.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD-------GQSETILGGLGLGLGGGDcRVKIATKANPW---D 110
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRGKRD-RVVIATKVGFPmgpN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 111 GKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGW 190
Cdd:cd19081 92 GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 191 ILPTVYQGMYNATTRQ-VETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgnsWAETYRNRFWKEHH 269
Cdd:cd19081 172 PRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGST--------RRGEAAKRYLNERG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41327764 270 FEAIALVEkALQAAYGASAPSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATeEGPLEPAVVDAFN 344
Cdd:cd19081 244 LRILDALD-EVAAEHGATPAQV---ALAWLLARPGV-----TAPIAGARTVEQLEDLLAAA-GLRLTDEEVARLD 308
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
64-331 |
3.14e-49 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 167.32 E-value: 3.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDG-----KSLKPDSVRSQLETSLKRLQCPQVDL 137
Cdd:cd19084 35 IDLGINFFDTAPVYGFGHSEEILGKALKGRRD---DVVIATKcGLRWDGgkgvtKDLSPESIRKEVEQSLRRLQTDYIDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 138 FYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwilPTVYQGMYNATTRQVETELFPCLRH 217
Cdd:cd19084 112 YQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVSLQPPYSMLEREIEEELLPYCRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 218 FGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNswaetYRNRFWkEHHFEAIALVeKALQAAYGASAPSVtsaALR 297
Cdd:cd19084 186 NGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPF-----FRGENF-EKNLEIVDKL-KEIAEKYGKSLAQL---AIA 255
|
250 260 270
....*....|....*....|....*....|....
gi 41327764 298 WMYHHSQLqgahgDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19084 256 WTLAQPGV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
41-347 |
5.33e-49 |
|
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: 166.33 E-value: 5.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGK---SL 114
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpsGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEIctlcKSNGWILPT 194
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA----LTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 195 VYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYrnrfwkehhfEAIA 274
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----------EALE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327764 275 LVEKaLQAAYGASAPSVtsaALRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAATeEGPLEPAVVDAFNQAW 347
Cdd:pfam00248 228 ALEE-IAKEHGVSPAQV---ALRWALSKPG-----VTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-331 |
3.69e-46 |
|
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: 159.31 E-value: 3.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTM----EMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK----ANPWD--- 110
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRD---RIVLATKytmnRRPGDpna 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 111 -GKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNG 189
Cdd:cd19080 92 gGNHRK--NLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 190 WILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKY-KYEDKDGKQPVGRFFGNSwAETYRNrfwkeh 268
Cdd:cd19080 170 WSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYqRGEEGRAGEAKGVTVGFG-KLTERN------ 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327764 269 hfEAIALVEKALQAAYGASAPSVtsaALRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19080 243 --WAIVDVVAAVAEELGRSAAQV---ALAWVRQKPG-----VVIPIIGARTLEQLKDNLGALD 295
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
64-331 |
3.29e-45 |
|
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: 157.39 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANPWDGKSlkPDSV---RSQL----ETSLKRLQCPQVD 136
Cdd:cd19091 49 LDAGINFFDTADVYSEGESEEILGKALKGRRD---DVLIATKVRGRMGEG--PNDVglsRHHIiravEASLKRLGTDYID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 137 LFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLR 216
Cdd:cd19091 124 LYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLAL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 217 HFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYrnRFWKEHHFEAI-ALVEKAlqAAYGASAPSVtsaA 295
Cdd:cd19091 204 DQGVGLLVWSPLAGGLLSGKYR---RGQPAPEGSRLRRTGFDFP--PVDRERGYDVVdALREIA--KETGATPAQV---A 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 41327764 296 LRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19091 274 LAWL-----LSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
64-346 |
3.11e-42 |
|
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: 148.89 E-value: 3.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19085 33 LDAGINFFDTAEAYGDGHSEEVLGKALK-----GRRddVVIATKVSP---DNLTPEDVRKSCERSLKRLGTDYIDLYQIH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 APDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwilPTVYQGMYNATTRQVETELFPCLRHFGLR 221
Cdd:cd19085 105 WPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCREHGIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 222 FYAYNPLAGGLLTGKYkyeDKDGKQPVGR--------FFGNSWAETyrnrfwkehhFEAIALVeKALQAAYGAsapSVTS 293
Cdd:cd19085 179 VLAYSPLAQGLLTGKF---SSAEDFPPGDartrlfrhFEPGAEEET----------FEALEKL-KEIADELGV---TMAQ 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 41327764 294 AALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEgPLEPAVVDAFNQA 346
Cdd:cd19085 242 LALAWVLQQPGV-----TSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
64-331 |
1.03e-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: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKANP-----WDGKSLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19079 45 LDLGINFFDTANVYSGGASEEILGRALKEFAPRD-EVVIATKVYFpmgdgPNGRGLSRKHIMAEVDASLKRLGTDYIDLY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHF 218
Cdd:cd19079 124 QIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 219 GLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYRnrfwKEHHFEAIALVEKaLQAAYGASAPSVtsaALRW 298
Cdd:cd19079 204 GIGVIPWSPLARGRLARPWG---DTTERRRSTTDTAKLKYDYF----TEADKEIVDRVEE-VAKERGVSMAQV---ALAW 272
|
250 260 270
....*....|....*....|....*....|...
gi 41327764 299 MYHHSQlqgahGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19079 273 LLSKPG-----VTAPIVGATKLEHLEDAVAALD 300
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
102-338 |
1.57e-36 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 134.31 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKA--NPW-----DGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYA 174
Cdd:cd19089 80 ISTKAgyGMWpgpygDGGSRK--YLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 175 SWEVAEICTLCKSNGwILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGRFFGN 254
Cdd:cd19089 158 GAKARRAIALLRELG-VPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAAE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 255 SWaetyrnrFWKEHHF-EAIALVEKALQAAYGASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAATEEG 333
Cdd:cd19089 233 SK-------FLTEEALtPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVT-----SVLIGASSPSQLEDNVAALKNL 300
|
....*
gi 41327764 334 PLEPA 338
Cdd:cd19089 301 DFSEE 305
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-344 |
1.57e-36 |
|
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: 134.61 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATKA------NP 108
Cdd:cd19094 6 LGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKGNRD-KVVLATKVagpgegIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 109 W---DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPV------------------EETLHACQRLHQEGKFVE 167
Cdd:cd19094 85 WprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALGELVKAGKIRH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 168 LGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQp 247
Cdd:cd19094 165 IGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAARPEG- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 248 vGRFFGNSWaetYRNRFWKEHHFEAI-ALVEKALQAAYgasapSVTSAALRWMYHHSqlqgaHGDAVILGMSSLEQLEQN 326
Cdd:cd19094 244 -GRLNLFPG---YMARYRSPQALEAVaEYVKLARKHGL-----SPAQLALAWVRSRP-----FVTSTIIGATTLEQLKEN 309
|
330
....*....|....*...
gi 41327764 327 LAATeEGPLEPAVVDAFN 344
Cdd:cd19094 310 IDAF-DVPLSDELLAEID 326
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
64-329 |
4.95e-36 |
|
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: 132.33 E-value: 4.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGD----CRVKIATKANPWD-GKSLKpdSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19074 32 YDLGINFFDTADVYAAGQAEEVLGKALKGWPRESyvisTKVFWPTGPGPNDrGLSRK--HIFESIHASLKRLQLDYVDIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHF 218
Cdd:cd19074 110 YCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 219 GLRFYAYNPLAGGLLTGKYkyedKDGK-QPVGRFFGNSWAETYRNRFWKEHHFEAIALVeKALQAAYGASAPsvtSAALR 297
Cdd:cd19074 190 GIGLVVWSPLAQGLLTGKY----RDGIpPPSRSRATDEDNRDKKRRLLTDENLEKVKKL-KPIADELGLTLA---QLALA 261
|
250 260 270
....*....|....*....|....*....|..
gi 41327764 298 WMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19074 262 WC-----LRNPAVSSAIIGASRPEQLEENVKA 288
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
64-331 |
8.12e-36 |
|
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: 131.95 E-value: 8.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDGKSL------KPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19076 42 LELGVTFLDTADMYGPGTNEELLGKALKDRRD---EVVIATKfGIVRDPGSGfrgvdgRPEYVRAACEASLKRLGTDVID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 137 LFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSnyaswEVAEiCTLCKSNGwILP-TVYQGMYNATTRQVETELFPCL 215
Cdd:cd19076 119 LYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS-----EASA-DTIRRAHA-VHPiTAVQSEYSLWTRDIEDEVLPTC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 216 RHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGnswaetyrnRFWKEhHFEA-IALVEK--ALQAAYGASAPSVt 292
Cdd:cd19076 192 RELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNP---------RFQGE-NFDKnLKLVEKleAIAAEKGCTPAQL- 260
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 41327764 293 saALRWMYHhsqlQGAhgDAV-ILGMSSLEQLEQNLAATE 331
Cdd:cd19076 261 --ALAWVLA----QGD--DIVpIPGTKRIKYLEENVGALD 292
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
64-332 |
2.20e-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: 131.00 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATK-ANPWDGKSLK----PDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19083 43 LDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNE--VVIATKgAHKFGGDGSVlnnsPEFLRSAVEKSLKRLNTDYIDLY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEictlckSNGWILPTVYQGMYNATTRQVETELFPCLRHF 218
Cdd:cd19083 121 YIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE------ANKDGYVDVLQGEYNLLQREAEEDILPYCVEN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 219 GLRFYAYNPLAGGLLTGKY----KYEDKDGKQPVGRFFGnswaETYRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsa 294
Cdd:cd19083 195 NISFIPYFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKG----ERFSENLDKVDKLKSIA-------DEKGVTVAHL--- 260
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41327764 295 ALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA-----TEE 332
Cdd:cd19083 261 ALAWYLTRPAI-----DVVIPGAKRAEQVIDNLKAldvtlTEE 298
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-331 |
1.67e-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: 125.52 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19752 4 CLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGNRD-DVVIATKvgagprdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 106 -ANPWDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTL 184
Cdd:cd19752 83 dGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 185 CKSNGWILPTVYQ----------GMYNATTRQVETELFPCLR-HFGLRFYAYNPLAGGLltgkykYEDKDGKQPvgrffg 253
Cdd:cd19752 163 ARQQGWAEFSAIQqrhsylrprpGADFGVQRIVTDELLDYASsRPDLTLLAYSPLLSGA------YTRPDRPLP------ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41327764 254 nswaETYRNRFwKEHHFEAIALVEKALqaayGASAPSVtsaALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19752 231 ----EQYDGPD-SDARLAVLEEVAGEL----GATPNQV---VLAWL-----LHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-331 |
8.63e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 118.54 E-value: 8.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANP-WDGK-----SLKPDSVRSQLETSLKRLQCPQVDL 137
Cdd:cd19102 36 LDLGINWIDTAAVYGLGHSEEVVGRALKGLRD---RPIVATKCGLlWDEEgrirrSLKPASIRAECEASLRRLGVDVIDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 138 FYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTlcksngwILP-TVYQGMYNATTRQVETELFPCLR 216
Cdd:cd19102 113 YQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPiASLQPPYSLLRRGIEAEILPFCA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 217 HFGLRFYAYNPLAGGLLTGKYkyedkdGKQPVGRFFGNSWAEtyRNRFWKEHHF-EAIALVE--KALQAAYGASAPSVts 293
Cdd:cd19102 186 EHGIGVIVYSPMQSGLLTGKM------TPERVASLPADDWRR--RSPFFQEPNLaRNLALVDalRPIAERHGRTVAQL-- 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 41327764 294 aALRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAATE 331
Cdd:cd19102 256 -AIAWVLRRPEVTSA-----IVGARRPDQIDETVGAAD 287
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
34-299 |
2.32e-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: 114.71 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 34 PPPRVAsvLGTMEMGRRM----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKAN-P 108
Cdd:cd19148 3 PVSRIA--LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 109 WDGKSLK-----PDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYAsweVAEICT 183
Cdd:cd19148 80 WDEGGEVvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFS---PEQMET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 184 LCKsnGWILPTVyQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGK----YKYEDKDGKQPVGRFFGnswaet 259
Cdd:cd19148 157 FRK--VAPLHTV-QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKmtkdTKFEGDDLRRTDPKFQE------ 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 41327764 260 yrNRFwkEHHFEAIALVEKALQAAYGAsapSVTSAALRWM 299
Cdd:cd19148 228 --PRF--SQYLAAVEELDKLAQERYGK---SVIHLAVRWL 260
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
42-331 |
7.32e-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: 7.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGRRM-----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPWdgkSLKP 116
Cdd:cd19072 9 LGTWGIGGGMskdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRED--LFITTKVSPD---HLKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGwilPTVY 196
Cdd:cd19072 84 DDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKKGP---IVAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 197 QGMYNATTRQVETELFP-CLRHfGLRFYAYNPLAGGLLTGKYKYEDkdgkqpvgrffgnswaetyrnrfwkehhfeaiaL 275
Cdd:cd19072 161 QVEYNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKGSPL---------------------------------L 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 276 VEkaLQAAYGASAPSVtsaALRWMYHHSqlqgahGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19072 207 DE--IAKKYGKTPAQI---ALNWLISKP------NVIAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
64-329 |
1.66e-28 |
|
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: 112.75 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKAN-PWDG---------------KSLKPDSVRSQLETSL 127
Cdd:cd19149 43 LDLGINLIDTAPAYGFGHSEEIVGKAIKGRRD---KVVLATKCGlRWDReggsfffvrdgvtvyKNLSPESIREEVEQSL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 128 KRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICtlckSNGWIlpTVYQGMYNATTRQV 207
Cdd:cd19149 120 KRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYV----KAGQL--DIIQEKYSMLDRGI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 208 ETELFP-CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqPVGRFFGNSWaetyRNR---FWKEHHFEAIALVE--KALQ 281
Cdd:cd19149 194 EKELLPyCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAGDA----RSGipwFSPENREKVLALLEkwKPLC 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 41327764 282 AAYGASAPSVtsaALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 329
Cdd:cd19149 261 EKYGCTLAQL---VIAWTLAQPGI-----TSALCGARKPEQAEENAKA 300
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
72-342 |
2.13e-27 |
|
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: 109.61 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 72 DTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDS-------VRSQLETSLKRLQCPQVDLFYLHAPD 144
Cdd:cd19143 49 DNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIF-WGGGGPPPNDrglsrkhIVEGTKASLKRLQLDYVDLVFCHRPD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 145 HGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VETELFPCLRHFGLRFY 223
Cdd:cd19143 128 PATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 224 AYNPLAGGLLTGKYkyedKDGKQPVGRFFGNSWaetyrnrFWKEHHFEA-----IALVEKALQAA--YGASAPSVtsaAL 296
Cdd:cd19143 208 TWSPLASGLLTGKY----NNGIPEGSRLALPGY-------EWLKDRKEElgqekIEKVRKLKPIAeeLGCSLAQL---AI 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41327764 297 RWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP-LEPAVVDA 342
Cdd:cd19143 274 AWC-----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEK 315
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
41-331 |
6.25e-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: 108.02 E-value: 6.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD----GQSETILGGLGLGLGGGDcRVKIATKA-----NPWDG 111
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGNRD-KVVIATKGghpdlEDMSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 112 KSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNyasWEVAEIC---TLCKSN 188
Cdd:cd19082 83 SRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERIAeanAYAKAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 189 GWILPTVYQGMYNATTRQVETELFPCL-------RHF----GLRFYAYNPLAGGLLTGKYKYEDKDGKQpvgrffgnswa 257
Cdd:cd19082 160 GLPGFAASSPQWSLARPNEPPWPGPTLvamdeemRAWheenQLPVFAYSSQARGFFSKRAAGGAEDDSE----------- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327764 258 etYRNRFWKEHHFEAIALVeKALQAAYGAsapSVTSAALRWMYHHSQLQGAhgdavILGMSSLEQLEQNLAATE 331
Cdd:cd19082 229 --LRRVYYSEENFERLERA-KELAEEKGV---SPTQIALAYVLNQPFPTVP-----IIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
64-331 |
2.51e-26 |
|
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: 106.55 E-value: 2.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK--------ANPWDGKSLKPDSVRSQLETSLKRLQCPQV 135
Cdd:cd19078 35 VELGITFFDTAEVYGPYTNEELVGEALKPFRD---QVVIATKfgfkidggKPGPLGLDSRPEHIRKAVEGSLKRLQTDYI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 136 DLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSnyaswEVAEiCTLCKSNGwILP-TVYQGMYNATTRQVETELFPC 214
Cdd:cd19078 112 DLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGV-ETIRRAHA-VCPvTAVQSEYSMMWREPEKEVLPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 215 LRHFGLRFYAYNPLAGGLLTGKYkyeDKDGKqpvgrfFGnswAETYRN---RFWKEHHFEAIALVE--KALQAAYGAsap 289
Cdd:cd19078 185 LEELGIGFVPFSPLGKGFLTGKI---DENTK------FD---EGDDRAslpRFTPEALEANQALVDllKEFAEEKGA--- 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41327764 290 svTSA--ALRWMYHhsqlQGAHgdAV-ILGMSSLEQLEQNLAATE 331
Cdd:cd19078 250 --TPAqiALAWLLA----KKPW--IVpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
64-329 |
1.06e-23 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 99.22 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK--ANPWdgkSLKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19093 36 LEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKfaPLPW---RLTRRSVVKALKASLERLGLDSIDLYQLH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 APDH-GTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGwILPTVYQGMYNATTRQVET-ELFPCLRHFG 219
Cdd:cd19093 112 WPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQnGLLPACDELG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 220 LRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYrnrfwkehhfeaiALVE--KALQAAYGASAPSVtsaALR 297
Cdd:cd19093 191 ITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKVQ-------------PLLDalEEIAEKYGKTPAQV---ALN 254
|
250 260 270
....*....|....*....|....*....|..
gi 41327764 298 WMYHHSQLqgahgdaVILGMSSLEQLEQNLAA 329
Cdd:cd19093 255 WLIAKGVV-------PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
64-339 |
1.54e-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: 98.40 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSLK--PDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19090 30 LDLGINYIDTAPAY--GDSEERLGLALAELPRE--PLVLSTKVGRLPEDTADysADRVRRSVEESLERLGRDRIDLLMIH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 APDHGTPVEET-----LHACQRLHQEGKFVELGLsnyASWEVAEICTLCKSNGW--ILptVYQGmYNATTRQVETELFP- 213
Cdd:cd19090 106 DPERVPWVDILapggaLEALLELKEEGLIKHIGL---GGGPPDLLRRAIETGDFdvVL--TANR-YTLLDQSAADELLPa 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 214 CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqpvgrffgnSWAETYRNRFWKEHHFEAIALveKALQAAYGASAPsvtS 293
Cdd:cd19090 180 AARH-GVGVINASPLGMGLLAGRPP----------------ERVRYTYRWLSPELLDRAKRL--YELCDEHGVPLP---A 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 41327764 294 AALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATeEGPLEPAV 339
Cdd:cd19090 238 LALRFLLRDPRI-----STVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
41-329 |
1.82e-23 |
|
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: 99.13 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 41 VLGTMEMG-------RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRD-QIVIATKfttdykay 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 106 ------ANPWDGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVA 179
Cdd:cd19147 93 evgkgkAVNYCGNHKR--SLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 180 EICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGG-LLTGKYKYEDKDGKQPVGRFFGNSwae 258
Cdd:cd19147 171 AANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGLRSFVGGT--- 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41327764 259 tyrnrfwkEHHFEAIALVEKALQAAYGASAPSVTSAALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19147 248 --------EQTPEEVKISEALEKVAEEHGTESVTAIALAYV-----RSKAPNVFPLVGGRKIEHLKDNIEA 305
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
42-329 |
5.58e-23 |
|
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: 97.88 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGRR-------MDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVkIATK--------- 105
Cdd:cd19146 16 LGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMV-LATKyttgyrrgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 106 ----ANPWDGKSLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEI 181
Cdd:cd19146 95 pikiKSNYQGNHAK--SLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 182 CTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGlltgkyKYEDKDGKQPVGRFFGNSWAETyr 261
Cdd:cd19146 173 NAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG------QFRTEEEFKRRGRSGRKGGPQT-- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 262 nrfwkEHHFEAIALVEKaLQAAYGASApsvTSAALRWMYHHSQLqgahgdaV--ILGMSSLEQLEQNLAA 329
Cdd:cd19146 245 -----EKERKVSEKLEK-VAEEKGTAI---TSVALAYVMHKAPY-------VfpIVGGRKVEHLKGNIEA 298
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
64-331 |
3.14e-22 |
|
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: 94.21 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLgggDCRVKIATKA-------NPW--DGKslkPDSVRSQLETSLKRLQCPQ 134
Cdd:cd19088 34 LELGVNFIDTADSYGPDVNERLIAEALHPY---PDDVVIATKGglvrtgpGWWgpDGS---PEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 135 VDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwiLPTVyQGMYNATTRQVETELFPC 214
Cdd:cd19088 108 IDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR-----IVSV-QNRYNLANRDDEGVLDYC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 215 LRHfGLRFYAYNPLAGGLLTgkykyedkdgkQPVGRFfgnswaetyrnrfwkehhfeaialveKALQAAYGASAPSVtsa 294
Cdd:cd19088 182 EAA-GIAFIPWFPLGGGDLA-----------QPGGLL--------------------------AEVAARLGATPAQV--- 220
|
250 260 270
....*....|....*....|....*....|....*..
gi 41327764 295 ALRWMYHHSQlqgahGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19088 221 ALAWLLARSP-----VMLPIPGTSSVEHLEENLAAAG 252
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
64-329 |
7.05e-22 |
|
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: 94.43 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDgqSETILGGLGLGLGGGDCRVKIATK----ANPWDGK---SLKPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19144 44 FELGCTFWDTADIYGD--SEELIGRWFKQNPGKREKIFLATKfgieKNVETGEysvDGSPEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 137 LFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTlcksngwILP-TVYQGMYNATTRQVET---ELF 212
Cdd:cd19144 122 LYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-------VHPiAAVQIEYSPFSLDIERpeiGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 213 PCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgkqpvgrFFGNSWaETYRNRFWKEHHFEAIALVEKaLQAAygASAPSVT 292
Cdd:cd19144 195 DTCRELGVAIVAYSPLGRGFLTGAIRSPDD--------FEEGDF-RRMAPRFQAENFPKNLELVDK-IKAI--AKKKNVT 262
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41327764 293 SA--ALRWMYhhsqlqgAHGDAV--ILGMSSLEQLEQNLAA 329
Cdd:cd19144 263 AGqlTLAWLL-------AQGDDIipIPGTTKLKRLEENLGA 296
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
102-329 |
7.54e-22 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 95.06 E-value: 7.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKA--NPWDGKSLKPDSVR---SQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASW 176
Cdd:PRK09912 94 ISTKAgyDMWPGPYGSGGSRKyllASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 177 EVAEICTLCKSngWILP-TVYQGMYNATTRQVE-TELFPCLRHFGLRFYAYNPLAGGLLTGKY-------KYEDKDGKQP 247
Cdd:PRK09912 174 RTQKMVELLRE--WKIPlLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYlngipqdSRMHREGNKV 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 248 VGrffgnswaetYRNRFWKEHHFEAIALVEKALQaaygASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNL 327
Cdd:PRK09912 252 RG----------LTPKMLTEANLNSLRLLNEMAQ----QRGQSMAQMALSWLLKDERVT-----SVLIGASRAEQLEENV 312
|
..
gi 41327764 328 AA 329
Cdd:PRK09912 313 QA 314
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
102-330 |
8.44e-22 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 94.01 E-value: 8.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKAN--PWDGK-----SLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYA 174
Cdd:cd19151 81 ISTKAGytMWPGPygdwgSKK--YLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 175 SWEVAEICTLCKSNGwiLPT-VYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKY---EDKDGKQPvgr 250
Cdd:cd19151 159 PEEAREAAAILKDLG--TPClIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNgipEDSRAAKG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 251 ffgnswaetyrNRFWKEHHF--EAIALVeKALQAAYGASAPSVTSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLA 328
Cdd:cd19151 234 -----------SSFLKPEQIteEKLAKV-RRLNEIAQARGQKLAQMALAWVLRNKRVT-----SVLIGASKPSQIEDAVG 296
|
..
gi 41327764 329 AT 330
Cdd:cd19151 297 AL 298
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
65-329 |
6.76e-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: 88.66 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDIVF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 140 LHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTR-QVETELfPCLRH- 217
Cdd:cd19141 120 ANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQL-PELFHk 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 218 FGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSWaetYRNRFWKEHHFEAIALVeKALQAAYGASAPSVTSAA 295
Cdd:cd19141 199 IGVGAMTWSPLACGILSGKY----DDGVPEYSRasLKGYQW---LKEKILSEEGRRQQAKL-KELQIIADRLGCTLPQLA 270
|
250 260 270
....*....|....*....|....*....|....
gi 41327764 296 LRWMYHHsqlQGAHGdaVILGMSSLEQLEQNLAA 329
Cdd:cd19141 271 IAWCLKN---EGVSS--VLLGASSTEQLYENLQA 299
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
64-329 |
9.00e-20 |
|
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: 87.15 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPWDGKSLK------PDSVRSQLETSLKRLQCPQV 135
Cdd:cd19086 34 LDLGINFFDTADVYGDGHSERLLGKALK-----GRRdkVVIATKFGNRFDGGPErpqdfsPEYIREAVEASLKRLGTDYI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 136 DLFYLH-APDHGTPVEETLHACQRLHQEGKFVELGLSnyaSWEVAEICTLCKSNGwilPTVYQGMYNATTRQVETELFPC 214
Cdd:cd19086 109 DLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVS---VGDPEEALAALRRGG---IDVVQVIYNLLDQRPEEELFPL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 215 LRHFGLRFYAYNPLAGGLLTGKykyedkdgkqpvgrffgnswaetyrnrfwkehhfeaiaLVEKALQaaYGASAPSVTSa 294
Cdd:cd19086 183 AEEHGVGVIARVPLASGLLTGK--------------------------------------LAQAALR--FILSHPAVST- 221
|
250 260 270
....*....|....*....|....*....|....*
gi 41327764 295 alrwmyhhsqlqgahgdaVILGMSSLEQLEQNLAA 329
Cdd:cd19086 222 ------------------VIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
67-329 |
7.37e-19 |
|
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: 85.56 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 67 GHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATK---ANPWDGKSL---KPDSVRSQLETSLKRLQCPQVDLFYL 140
Cdd:cd19145 46 GVTFLDTSDIYGPNTNEVLLGKALKDGPRE--KVQLATKfgiHEIGGSGVEvrgDPAYVRAACEASLKRLDVDYIDLYYQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 141 HAPDHGTPVEETLHACQRLHQEGKFVELGLSNyASWEvaeicTLCKSNGwILP-TVYQGMYNATTRQVETELFPCLRHFG 219
Cdd:cd19145 124 HRIDTTVPIEITMGELKKLVEEGKIKYIGLSE-ASAD-----TIRRAHA-VHPiTAVQLEWSLWTRDIEEEIIPTCRELG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 220 LRFYAYNPLAGGLLTGKYKYE----DKDGKQPVGRFFGNSWaetyrnrfwkEHH---FEAIAlvekALQAAYGASaPSvt 292
Cdd:cd19145 197 IGIVPYSPLGRGFFAGKAKLEelleNSDVRKSHPRFQGENL----------EKNkvlYERVE----ALAKKKGCT-PA-- 259
|
250 260 270
....*....|....*....|....*....|....*....
gi 41327764 293 SAALRWMYHhsqlqgaHGDAV--ILGMSSLEQLEQNLAA 329
Cdd:cd19145 260 QLALAWVLH-------QGEDVvpIPGTTKIKNLNQNIGA 291
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
64-331 |
1.50e-18 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 84.22 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETIlgglgLGLGGGDCR--VKIATKANPWDGkslKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19138 39 IDLGMTLIDTAEMYGDGGSEEL-----VGEAIRGRRdkVFLVSKVLPSNA---SRQGTVRACERSLRRLGTDYLDLYLLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 APDhGTPVEETLHACQRLHQEGKFVELGLSNYaswEVAEICTLCKSNGWILPTVYQGMYNATTRQVETELFPCLRHFGLR 221
Cdd:cd19138 111 WRG-GVPLAETVAAMEELKKEGKIRAWGVSNF---DTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 222 FYAYNPLAGGLLTGKYKYEDKDGKqpvgrffgnswaetyrnrfwkehhfeAIAlvekalqAAYGASAPSVtsaALRWMYH 301
Cdd:cd19138 187 VMAYSPLAQGGLLRRGLLENPTLK--------------------------EIA-------ARHGATPAQV---ALAWVLR 230
|
250 260 270
....*....|....*....|....*....|
gi 41327764 302 HSqlqgahGDAVILGMSSLEQLEQNLAATE 331
Cdd:cd19138 231 DG------NVIAIPKSGSPEHARENAAAAD 254
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
102-329 |
1.82e-18 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 84.81 E-value: 1.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKA--NPWDGK-----SLKpdSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYA 174
Cdd:cd19150 81 ISTKAgyDMWPGPygewgSRK--YLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 175 SWEVAEICTLCKSNGWILpTVYQGMYNATTRQVE-TELFPCLRHFGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGrffg 253
Cdd:cd19150 159 PERTREAAAILRELGTPL-LIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG---- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 254 nswaetyrNRFWKEHHFEAIALVE------KALQAAYGASAPSVTSAALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNL 327
Cdd:cd19150 229 --------SRASKERSLSPKMLTEanlnsiRALNEIAQKRGQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEENV 295
|
..
gi 41327764 328 AA 329
Cdd:cd19150 296 GA 297
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
102-329 |
2.95e-17 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 80.48 E-value: 2.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGtPVEETLHACQRLHQEGKFVELGLSNYASWEVAEI 181
Cdd:COG0656 63 VTTKVWNDN---HGYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 182 CTLCKsngwILPTVYQGMYNATTRQveTELFPCLRHFGLRFYAYNPLA-GGLLtgkykyedkdgKQPVgrffgnswaety 260
Cdd:COG0656 139 LAETG----VKPAVNQVELHPYLQQ--RELLAFCREHGIVVEAYSPLGrGKLL-----------DDPV------------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327764 261 rnrfwkehhFEAIAlvekalqAAYGASAPSVtsaALRWmyhHSQlqgaHGDAVILGMSSLEQLEQNLAA 329
Cdd:COG0656 190 ---------LAEIA-------EKHGKTPAQV---VLRW---HLQ----RGVVVIPKSVTPERIRENLDA 232
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
65-334 |
8.57e-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: 80.13 E-value: 8.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIF-WGGKAetergLSRKHIIEGLKASLERLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 140 LHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VETELFPCLRHF 218
Cdd:cd19158 121 ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 219 GLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSWaetYRNRFWKEHHFEAIALVeKALQAAYGASAPSVTSAAL 296
Cdd:cd19158 201 GVGAMTWSPLACGIVSGKY----DSGIPPYSRasLKGYQW---LKDKILSEEGRRQQAKL-KELQAIAERLGCTLPQLAI 272
|
250 260 270
....*....|....*....|....*....|....*...
gi 41327764 297 RWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP 334
Cdd:cd19158 273 AWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVLP 305
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
64-329 |
1.65e-16 |
|
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: 78.08 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19073 24 LELGYRHIDTAEIY-NNEAEVGEAIAESGVPRED--LFITTKVWR---DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEictlCKSNGWILPTVYQGMYNATTRQVETELFpCLRHfGLRFY 223
Cdd:cd19073 98 NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE----ALDISPLPIAVNQVEFHPFLYQAELLEY-CREN-DIVIT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 224 AYNPLAGGLLtgkykyedkdgkqpvgrffgnswaetyrnrfwkEHHFEAIALVEKalqaaYGASAPSVtsaALRWMYhhs 303
Cdd:cd19073 172 AYSPLARGEV---------------------------------LRDPVIQEIAEK-----YDKTPAQV---ALRWLV--- 207
|
250 260
....*....|....*....|....*.
gi 41327764 304 qlqgAHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19073 208 ----QKGIVVIPKASSEDHLKENLAI 229
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
65-334 |
1.66e-16 |
|
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: 79.32 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLY-WGGKAetergLSRKHIIEGLKGSLQRLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 140 LHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VETELfPCLRH- 217
Cdd:cd19159 121 ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQL-PELYHk 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 218 FGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFgnSW------AETYRNRFWKEHHFEAIAlvEKalqaaYGASAPSV 291
Cdd:cd19159 200 IGVGAMTWSPLACGIISGKYGNGVPESSRASLKCY--QWlkerivSEEGRKQQNKLKDLSPIA--ER-----LGCTLPQL 270
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 41327764 292 tsaALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEEGP 334
Cdd:cd19159 271 ---AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
65-345 |
1.71e-15 |
|
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: 76.18 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKS-----LKPDSVRSQLETSLKRLQCPQVDLFY 139
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIY-WGGQAetergLSRKHIIEGLRGSLDRLQLEYVDIVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 140 LHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVYQGMYNATTRQ-VETELfPCLRH- 217
Cdd:cd19160 123 ANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQL-PELYHk 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 218 FGLRFYAYNPLAGGLLTGkyKYEDKDGKQPVGRFFGNSW-AETYRNRFWKEHHFEAIALVEKALQAAYgasapSVTSAAL 296
Cdd:cd19160 202 IGVGSVTWSPLACGLITG--KYDGRVPDTCRAAVKGYQWlKEKVQSEEGKKQQAKVKELHPIADRLGC-----TVAQLAI 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 41327764 297 RWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAATEE-GPLEPAVVDAFNQ 345
Cdd:cd19160 275 AWC-----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-329 |
4.11e-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: 74.16 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdCRVKIATKANPWDGKSlKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19105 35 LDLGINYFDTAEGYGNGNSEEIIGEALKGLRR--DKVFLATKASPRLDKK-DKAELLKSVEESLKRLQTDYIDIYQLHGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 DHGTP---VEETLHACQRLHQEGKFVELGLS-NYASWEVAEicTLCKSnGWIlpTVYQGMYNATTRQVetELFPCLrhfg 219
Cdd:cd19105 112 DTPEErllNEELLEALEKLKKEGKVRFIGFStHDNMAEVLQ--AAIES-GWF--DVIMVAYNFLNQPA--ELEEAL---- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 220 lrfyaynPLAG----GLLTGKykyedkdgKQPVGRFFGNSWAETYrnrfwkehhfeaialvekalqaaygASAPSVTSAA 295
Cdd:cd19105 181 -------AAAAekgiGVVAMK--------TLAGGYLQPALLSVLK-------------------------AKGFSLPQAA 220
|
250 260 270
....*....|....*....|....*....|....
gi 41327764 296 LRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 329
Cdd:cd19105 221 LKWVLSNPRV-----DTVVPGMRNFAELEENLAA 249
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
63-333 |
4.45e-15 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 74.13 E-value: 4.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 63 FLERGHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSlkPDSVRSQLETSLKRLQCPQVDLFYLHA 142
Cdd:cd19096 30 AIDAGINYFDTAYGYGGGKSEEILGEALKEGPRE--KFYLATKLPPWSVKS--AEDFRRILEESLKRLGVDYIDFYLLHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 143 PDHGTPVEETLH-----ACQRLHQEGKFVELGLSNYASWEVaeICTLCKSNGW---ILPtvyqgmYNAtTRQVETELFPC 214
Cdd:cd19096 106 LNSPEWLEKARKgglleFLEKAKKEGLIRHIGFSFHDSPEL--LKEILDSYDFdfvQLQ------YNY-LDQENQAGRPG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 215 LRH---FGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrffgnswaetyrnrfwkehhfeaiALVEKALQAAYGASAPSV 291
Cdd:cd19096 177 IEYaakKGMGVIIMEPLKGGGLA---------------------------------------NNPPEALAILCGAPLSPA 217
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 41327764 292 tSAALRWMYHHsqlQGAHgdAVILGMSSLEQLEQNLAATEEG 333
Cdd:cd19096 218 -EWALRFLLSH---PEVT--TVLSGMSTPEQLDENIAAADEF 253
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-336 |
4.82e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 74.68 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwDGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19103 42 MAAGLNLWDTAAVYGMGASEKILGEFLKRYPRED--YIISTKFTP-QIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 dhgTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGWILPTVyQGMYNATTRQVETE--LFPCLRHfGLR 221
Cdd:cd19103 119 ---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSLLYRSSEEAgiLDYCKEN-GIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 222 FYAYNPLAGGLLTGKYkyedkDGKQPVGRffGNSWAETYrNRFWKEhhFEAIALVEKALQAAYGASAPSVTSAALRwmyh 301
Cdd:cd19103 194 FFAYMVLEQGALSGKY-----DTKHPLPE--GSGRAETY-NPLLPQ--LEELTAVMAEIGAKHGASIAQVAIAWAI---- 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 41327764 302 hsqlqgAHGDAVILGMSSLEQLEQ-------NLAATEEGPLE 336
Cdd:cd19103 260 ------AKGTTPIIGVTKPHHVEDaaraasiTLTDDEIKELE 295
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
102-329 |
9.69e-15 |
|
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: 72.90 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAP------DHGTPVEETLHACQRLHQEGKFVELGLSNYAS 175
Cdd:cd19071 59 ITTKLWPTD---HGYERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 176 WEVAEICTLCKsngwILPTVYQGMYNATTRQVETELFpCLRHfGLRFYAYNPLAGGlltgkykyedkdgkqpvgrffgns 255
Cdd:cd19071 136 EHLEELLAAAR----IKPAVNQIELHPYLQQKELVEF-CKEH-GIVVQAYSPLGRG------------------------ 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 41327764 256 waetyRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsaALRWmyhhsQLQgaHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19071 186 -----RRPLLDDPVLKEIA-------KKYGKTPAQV---LLRW-----ALQ--RGVVVIPKSSNPERIKENLDV 237
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
99-348 |
1.05e-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: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 99 RVKIATKANPWdgkSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHgtpvEETLH----------ACQRLHQEGKFVEL 168
Cdd:COG1453 69 KVILATKLPPW---VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNT----EEDLEkvlkpggaleALEKAKAEGKIRHI 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 169 GLSNYASWEVAEicTLCKSNGWilpTVYQGMYNA--TTRQVETELFPCLRHFGLRFYAYNPLAGGLLTgkykyedkdgkq 246
Cdd:COG1453 142 GFSTHGSLEVIK--EAIDTGDF---DFVQLQYNYldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA------------ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 247 pvgrffgnswaetyrnrfwkEHHFEAIALVEKALqaaygasapSVTSAALRWMYHHSQLqgahgDAVILGMSSLEQLEQN 326
Cdd:COG1453 205 --------------------NPPEKLVELLCPPL---------SPAEWALRFLLSHPEV-----TTVLSGMSTPEQLDEN 250
|
250 260
....*....|....*....|....*.
gi 41327764 327 LAATEEG-PL---EPAVVDAFNQAWH 348
Cdd:COG1453 251 LKTADNLePLteeELAILERLAEELG 276
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-335 |
1.40e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.95 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGggdcRVKIATK--ANPWDGKSLKpDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19097 36 LKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKlpPLKEDKKEDE-AAIEASVEASLKRLKVDSLDGLLLH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 APD----HGTPVEETLHACQRlhqEGKFVELGLSNYASWEVAEICTLCKsngwilPTVYQGMYNA-TTRQVETELFPCLR 216
Cdd:cd19097 109 NPDdllkHGGKLVEALLELKK---EGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNIlDQRFLKSGLLAKLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 217 HFGLRFYAYNPLAGGLLTgkykyedKDGKQPVGRFfgnswaetyrnRFWKEHH--FEAIAlvekalqAAYGASAPsvtSA 294
Cdd:cd19097 180 KKGIEIHARSVFLQGLLL-------MEPDKLPAKF-----------APAKPLLkkLHELA-------KKLGLSPL---EL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 41327764 295 ALRWMYHHSqlqgaHGDAVILGMSSLEQLEQNLAATEEGPL 335
Cdd:cd19097 232 ALGFVLSLP-----EIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
64-331 |
6.33e-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: 71.05 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKA--------NPWDGKS--LKPDSVRSQLETSLKRLQCP 133
Cdd:cd19092 34 LELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCgirlgddpRPGRIKHydTSKEHILASVEGSLKRLGTD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 134 QVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVA---------------EICTLCksngwiLPTVYQG 198
Cdd:cd19092 114 YLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEllqsyldqplvtnqiELSLLH------TEAIDDG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 199 MynattrqveteLFPCLRHfGLRFYAYNPLAGglltgkykyedkdgkqpvGRFFGNSWAETYRNRfwkehhfeaiALVEK 278
Cdd:cd19092 188 T-----------LDYCQLL-DITPMAWSPLGG------------------GRLFGGFDERFQRLR----------AALEE 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 41327764 279 aLQAAYGASApsvTSAALRW-MYHHSQLQgahgdaVILGMSSLEQLEQNLAATE 331
Cdd:cd19092 228 -LAEEYGVTI---EAIALAWlLRHPARIQ------PILGTTNPERIRSAVKALD 271
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
64-233 |
7.71e-14 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 70.68 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19137 36 IELGYTHIDTAEMYGGGHTEELVGKAIKDFPRED--LFIVTKVWP---TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSngwilPTVY-QGMYNATTRQVETE-LFPCLRHFGLR 221
Cdd:cd19137 111 NPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-----PIVCnQVKYNLEDRDPERDgLLEYCQKNGIT 185
|
170
....*....|..
gi 41327764 222 FYAYNPLAGGLL 233
Cdd:cd19137 186 VVAYSPLRRGLE 197
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
63-329 |
9.24e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 71.09 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 63 FLERGHTELDTAFMYsdGQSETIL---GGLGLGLGGGDCRVKIATKANPWDGK-SLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19101 32 YVDAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVPDPGElTMTRAYVEAAIDRSLKRLGVDRLDLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAPDHGTP-VEETLHACQRLHQEGKFVELGLSNYASWEVAEICtlckSNGwiLPTVY-QGMYNATTRQVETELFP-CL 215
Cdd:cd19101 110 QFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----DAG--VPIVSnQVQYSLLDRRPENGMAAlCE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 216 RHfGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGRFFGNSWAETYRNRFWKEH----HFEAIALVEKALQAAYGASAPSV 291
Cdd:cd19101 184 DH-GIKLLAYGTLAGGLLSEKYL-----GVPEPTGPALETRSLQKYKLMIDEWggwdLFQELLRTLKAIADKHGVSIANV 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 41327764 292 tsaALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19101 258 ---AVRWV-----LDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
42-327 |
7.03e-13 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 68.73 E-value: 7.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMY-------SDGQSETILGGLGLGLGGGDcRVKIATK-ANPWDG-- 111
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSRE-KLIIASKvSGPSRNnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 112 KSLKPD------SVRSQLETSLKRLQCPQVDLFYLHAPDHGT--------------PVE---ETLHACQRLHQEGKFVEL 168
Cdd:PRK10625 97 KGIRPNqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRPTncfgklgyswtdsaPAVsllETLDALAEQQRAGKIRYI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 169 GLSNYASWEVAEICTLCKSNGwiLPTVY--QGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQ 246
Cdd:PRK10625 177 GVSNETAFGVMRYLHLAEKHD--LPRIVtiQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 247 PVG-------RFfgnswaetyrNRFWKEHHFEAIAlVEKALQAAYGASAPSVTSAALRwmyhhsqlQGAHGDAVILGMSS 319
Cdd:PRK10625 251 PAGarntlfsRF----------TRYSGEQTQKAVA-AYVDIAKRHGLDPAQMALAFVR--------RQPFVASTLLGATT 311
|
....*...
gi 41327764 320 LEQLEQNL 327
Cdd:PRK10625 312 MEQLKTNI 319
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
42-329 |
2.92e-12 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 65.72 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:cd19095 5 LGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDD--LFIATKVgthgeGGRDRKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 114 LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYAswevAEICTLCKSNgwiLP 193
Cdd:cd19095 81 FSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASG---VF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 194 TVYQGMYNATTRQVEtELFPCLRHFGLRFYAYNPLAGGLLtgkykyedkdgkqpvgrffgnswaetyrnrFWKEHHFEAI 273
Cdd:cd19095 154 DVVQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRL------------------------------RRRVRRRPLY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 274 ALVEKALQAAYGASAPSVTSAALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAA 329
Cdd:cd19095 203 ADYARRPEFAAEIGGATWAQAALRFVLSHPGV-----SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
64-186 |
5.10e-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: 62.52 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDCR---VKIATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYL 140
Cdd:cd19111 27 LFVGYRHIDTALSY--QNEKAIGEALKWWLKNGKLKreeVFITTKLPPVY---LEFKDTEKSLEKSLENLKLPYVDLYLI 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 41327764 141 HAP-------------DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCK 186
Cdd:cd19111 102 HHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
109-329 |
2.01e-10 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 61.10 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 109 WDGKSLKPDS----VRSQLETSLKRLQCPQ-VDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSnyaswEV-AEic 182
Cdd:cd19077 82 LDPDTLRPDGspeaVRKSIENILRALGGTKkIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLS-----EVsAE-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 183 TLCKSNGWILPTVYQGMYNATTRQVET-ELFPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSwaetyr 261
Cdd:cd19077 155 TIRRAHAVHPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIK---SLADIPEGDFRRHL------ 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327764 262 NRFWKEhHFEA-IALVE--KALQAAYGASAPSVtsaALRWMYHHSqlqgahGDAV--ILGMSSLEQLEQNLAA 329
Cdd:cd19077 226 DRFNGE-NFEKnLKLVDalQELAEKKGCTPAQL---ALAWILAQS------GPKIipIPGSTTLERVEENLKA 288
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
102-329 |
8.70e-10 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 59.40 E-value: 8.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKANpWDGKS----LKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHACQRLHQEGKFVELGLSNYASWE 177
Cdd:cd19142 79 VSTKIY-WSYGSeergLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 178 VAEICTLCKSNGWILPTVYQGMYNATTRQ-VETELFPCLRHFGLRFYAYNPLAGGLLTGK--------YKYEDKDGKQPV 248
Cdd:cd19142 158 IMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVGLITWSPLSLGLDPGIseetrrlvTKLSFKSSKYKV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 249 GRFFGNSWAETYRNrfwKEHHFEAIALVEKalqaaYGAsapSVTSAALRWmyhhsQLQGAHGDAVILGMSSLEQLEQNLA 328
Cdd:cd19142 238 GSDGNGIHEETRRA---SHKLRELSLIAER-----LGC---DLTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQLN 301
|
.
gi 41327764 329 A 329
Cdd:cd19142 302 S 302
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-328 |
1.84e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 58.10 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSE-----TILGGLGLGLGGGDcRVKIATKA-----------NPW------------------ 109
Cdd:cd19099 31 LDSGINVIDTAINYRGGRSErligkALRELIEKGGIKRD-EVVIVTKAgyipgdgdeplRPLkyleeklgrglidvadsa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 110 -DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPV----------EETLHACQRLHQEGKfvelgLSNY--ASW 176
Cdd:cd19099 110 gLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLElgeeefydrlEEAFEALEEAVAEGK-----IRYYgiSTW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 177 EVAEI---------------------------------CTLCKSNGWILPTVYQGMYnattrqveTELFPCLRHFGLRFY 223
Cdd:cd19099 185 DGFRAppalpghlsleklvaaaeevggdnhhfkviqlpLNLLEPEALTEKNTVKGEA--------LSLLEAAKELGLGVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 224 AYNPLAGGLLTGKykyedkdgkqpvgrffgnswaetyRNRFWKEHHFEAIALVEKALQAAygASAPSVTSaalrwmyhhs 303
Cdd:cd19099 257 ASRPLNQGQLLGE------------------------LRLADLLALPGGATLAQRALQFA--RSTPGVDS---------- 300
|
330 340
....*....|....*....|....*
gi 41327764 304 qlqgahgdaVILGMSSLEQLEQNLA 328
Cdd:cd19099 301 ---------ALVGMRRPEHVDENLA 316
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
64-336 |
4.36e-09 |
|
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: 56.79 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGggdcRVK--IATKA-----NPWDGKSLKPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19163 43 LDSGINYIDTAPWYGQGRSETVLGKALKGIP----RDSyyLATKVgryglDPDKMFDFSAERITKSVEESLKRLGLDYID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 137 LFYLH----APDHGTPVEETLHACQRLHQEGKFVELGLSNY---ASWEVAE--------ICTLCKSNgwilptvyqgMYN 201
Cdd:cd19163 119 IIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGITGYpldVLKEVLErspvkidtVLSYCHYT----------LND 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 202 ATTrqveTELFPCLRHFGLRFYAYNPLAGGLLTgkykyedKDGKQPvgrffgnswaetyrnrfWKEHHFEAIALVEKAlq 281
Cdd:cd19163 189 TSL----LELLPFFKEKGVGVINASPLSMGLLT-------ERGPPD-----------------WHPASPEIKEACAKA-- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 282 AAYGASAPSVTSA-ALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEGPLE 336
Cdd:cd19163 239 AAYCKSRGVDISKlALQFALSNPDI-----ATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
64-328 |
8.70e-09 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 55.73 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcRVKIATKANPWDgksLKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19140 31 LELGYRHIDTAQMY--GNEAQVGEAIAASGVPRD-ELFLTTKVWPDN---YSPDDFLASVEESLRKLRTDYVDLLLLHWP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSngwilPTVyqgmynatTRQVE-------TELFPCLR 216
Cdd:cd19140 105 NKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSEA-----PLF--------TNQVEyhpyldqRKLLDAAR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 217 HFGLRFYAYNPLAgglltgkykyedkdgkqpvgrffgnswaetyRNRFWKEHHFEAIAlvekalqAAYGASAPSVtsaAL 296
Cdd:cd19140 172 EHGIALTAYSPLA-------------------------------RGEVLKDPVLQEIG-------RKHGKTPAQV---AL 210
|
250 260 270
....*....|....*....|....*....|..
gi 41327764 297 RWMyhhsqLQGAhGDAVILGMSSLEQLEQNLA 328
Cdd:cd19140 211 RWL-----LQQE-GVAAIPKATNPERLEENLD 236
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-347 |
1.03e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 56.12 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKA--NPWDGKSLKpDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19104 42 LDLGINFFDTAPSYGDGKSEENLGRALKGLPA---GPYITTKVrlDPDDLGDIG-GQIERSVEKSLKRLKRDSVDLLQLH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 ---------------APDHGTPVEETLHACQRLHQEGKFVELGLSnyaswevaeictlcksnGWilptvyqGMYNATTRQ 206
Cdd:cd19104 118 nrigderdkpvggtlSTTDVLGLGGVADAFERLRSEGKIRFIGIT-----------------GL-------GNPPAIREL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 207 VETELFPClrhfglrFYAY----NPLAGGLLTGKYKYEDKDG------KQPVG----RFFGNSWAETYRNRFWKEHHFEA 272
Cdd:cd19104 174 LDSGKFDA-------VQVYynllNPSAAEARPRGWSAQDYGGiidaaaEHGVGvmgiRVLAAGALTTSLDRGREAPPTSD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 273 IALVE-----KALQAAYGASAPSVTSAALRWMYHHSQLqgahgDAVILGMSSLEQLEQNLAATEEGPLEPAVVDAFNQAW 347
Cdd:cd19104 247 SDVAIdfrraAAFRALAREWGETLAQLAHRFALSNPGV-----STVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-328 |
4.22e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 53.25 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSET-----ILgglglglgggDCR--VKIATKANPWDgkslkPDSVRSQLETSLKRLQCPQVD 136
Cdd:cd19100 37 LDLGINYFDTAPSY--GDSEEkigkaLK----------GRRdkVFLATKTGARD-----YEGAKRDLERSLKRLGTDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 137 LFYLHAPDHGTPVEET------LHACQRLHQEGKFVELGLSNYaSWEVAEicTLCKSNGW--ILPTV-YQGMYNattRQV 207
Cdd:cd19100 100 LYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISGH-SPEVLL--RALETGEFdvVLFPInPAGDHI---DSF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 208 ETELFP-CLRHfGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrffgNSWAETYRnrfwkehhfeaialvekalqaayga 286
Cdd:cd19100 174 REELLPlAREK-GVGVIAMKVLAGGRLL-------------------SGDPLDPE------------------------- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 41327764 287 sapsvtsAALRWMyhhsqLQGAHGDAVILGMSSLEQLEQNLA 328
Cdd:cd19100 209 -------QALRYA-----LSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
113-329 |
4.33e-08 |
|
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: 53.51 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 113 SLKPDSVRSQLETSLKRLQCPQVDLFYLH--APDHGTPVEETLHACQRLHQEGKFVELGLSNYAswevaeICTLCKSNGW 190
Cdd:cd19139 67 NLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFT------IALLDEAIAV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 191 IlptvyqGMYNATTRQVetELFP----------CLRHfGLRFYAYNPLAGGlltgkykyedKDGKQPVgrffgnswaety 260
Cdd:cd19139 141 V------GAGAIATNQI--ELSPylqnrklvahCKQH-GIHVTSYMTLAYG----------KVLDDPV------------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327764 261 rnrfwkehhFEAIAlvekalqAAYGASAPSVtsaALRWMYHhsqlqgaHGDAVILGMSSLEQLEQNLAA 329
Cdd:cd19139 190 ---------LAAIA-------ERHGATPAQI---ALAWAMA-------RGYAVIPSSTKREHLRSNLLA 232
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
102-234 |
1.26e-07 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 52.25 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKANPWDGKSlkpDSVRSQLETSLKRLQCPQVDLFYLHAP-----DHGTPVE-----ETLHACQRLHQEGKFVELGLS 171
Cdd:cd19136 64 ITSKLAPKDQGY---EKARAACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVS 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327764 172 NYASWEVAEICTLCKsngwILPTVYQGMYNAttRQVETELFPCLRHFGLRFYAYNPLAGGLLT 234
Cdd:cd19136 141 NYTVRHLEELLKYCE----VPPAVNQVEFHP--HLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
117-247 |
1.33e-07 |
|
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: 51.99 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLH--APDHGTPVeETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPT 194
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHwpVPAQDKYV-ETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG----VVPV 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 195 VYQGMYNATTRQVETELFpCLRHfGLRFYAYNPLA-GGLLTGKY--KYEDKDGKQP 247
Cdd:cd19131 155 VNQIELHPRFQQRELRAF-HAKH-GIQTESWSPLGqGGLLSDPVigEIAEKHGKTP 208
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
64-346 |
1.61e-07 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 51.85 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDgQSETILGGLGLGLGGGDcrVKIATKANPwdgkslKPDSVRSQLETSLKRLQCPQVDLFYLHAP 143
Cdd:cd19120 35 LKAGFRHIDTAEMYGN-EKEVGEALKESGVPRED--LFITTKVSP------GIKDPREALRKSLAKLGVDYVDLYLIHSP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 144 ----DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQGMYNATTRQVETELFPCLRHFG 219
Cdd:cd19120 106 ffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPYLYPQQPALLEYCREHG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 220 LRFYAYNPLAgglltgkykyedkdgkqPVGRFFGnswaetyrnrfwkehhfEAIALVEKALQAAYGASAPSVtsaALRWM 299
Cdd:cd19120 182 IVVSAYSPLS-----------------PLTRDAG-----------------GPLDPVLEKIAEKYGVTPAQV---LLRWA 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 41327764 300 YhhsqlqgAHGDAVILGMSSLEQLEQNLAAtEEGPLEPAVVDAFNQA 346
Cdd:cd19120 225 L-------QKGIVVVTTSSKEERMKEYLEA-FDFELTEEEVEEIDKA 263
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
109-228 |
2.13e-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: 52.00 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 109 WDGKSlKPDSVRSQLETSLKRLQCPQVDLFYLHAP---DHG----------------TPVEETLHACQRLHQEGKFVELG 169
Cdd:cd19106 75 WNTKH-HPEDVEPALRKTLKDLQLDYLDLYLIHWPyafERGdnpfpknpdgtirydsTHYKETWKAMEKLVDKGLVKAIG 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 170 LSNYASWEVAEICtlckSNGWILPTVYqgmynattrQVE-------TELFPCLRHFGLRFYAYNPL 228
Cdd:cd19106 154 LSNFNSRQIDDIL----SVARIKPAVL---------QVEchpylaqNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
102-298 |
3.07e-07 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 51.04 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKANPWDGKSlkpDSVRSQLETSLKRLQCPQVDLFYLHAP--DhgtpVEETLHACQRLHQEGKFVELGLSNYASWEVA 179
Cdd:cd19133 68 ITTKLWIQDAGY---EKAKKAFERSLKRLGLDYLDLYLIHQPfgD----VYGAWRAMEELYKEGKIRAIGVSNFYPDRLV 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 180 EICTLCKsngwILPTVYQGMYNATTRQVETELFpcLRHFGLRFYAYNPLAGGlltgkykyedkdgkqpvgrffgnswaet 259
Cdd:cd19133 141 DLILHNE----VKPAVNQIETHPFNQQIEAVEF--LKKYGVQIEAWGPFAEG---------------------------- 186
|
170 180 190
....*....|....*....|....*....|....*....
gi 41327764 260 yRNRFWKEHHFEAIAlvekalqAAYGASAPSVTsaaLRW 298
Cdd:cd19133 187 -RNNLFENPVLTEIA-------EKYGKSVAQVI---LRW 214
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
116-228 |
3.35e-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: 51.19 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 116 PDSVRSQLETSLKRLQCPQVDLFYLHAP------DHG--------TPVEETLHACQRLHQEGKFVELGLSNYASWEVAEI 181
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgAHMpepeevlpPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 41327764 182 CTLCKsngwILPTVYQGMYNATTRQveTELFPCLRHFGLRFYAYNPL 228
Cdd:cd19125 164 LAVAR----VPPAVNQVECHPGWQQ--DKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
117-233 |
3.54e-07 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 50.79 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPV-------EETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsng 189
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS--- 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 41327764 190 wILPTVYQGMYNATTRQVetELFPCLRHFGLRFYAYNPLAGGLL 233
Cdd:cd19135 160 -VVPHVNQVEFHPFQNPV--ELIEYCRDNNIVFEGYCPLAKGKA 200
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
117-329 |
3.89e-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: 47.74 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHG--TPVEETLHACQRLHQEGKFVELGLsnyASWEVAEICTLCKSNGW--IL 192
Cdd:cd19162 93 DGIRRSIEASLERLGLDRLDLVFLHDPDRHllQALTDAFPALEELRAEGVVGAIGV---GVTDWAALLRAARRADVdvVM 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 193 PTvyqGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGkykyedkdGKQPVGRFFGNSWAETYRNRfwkehhfeA 272
Cdd:cd19162 170 VA---GRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT--------DDPAGDRYDYRPATPEVLAR--------A 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 41327764 273 IALVEKAlqAAYGASAPsvtSAALRWMYHHSQLQgahgdAVILGMSSLEQLEQNLAA 329
Cdd:cd19162 231 RRLAAVC--RRYGVPLP---AAALQFPLRHPAVA-----SVVVGAASPAELRDNLAL 277
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
102-232 |
5.43e-06 |
|
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: 47.45 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 102 IATKAnpWDGKSlKPDSVRSQLETSLKRLQCPQVDLFYLHAP--------------------DHGTPVEETLHACQRLHQ 161
Cdd:cd19129 68 VTTKL--WNTNH-RPERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVD 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 41327764 162 EGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQgmYNATTRQVETELFPCLRHFGLRFYAYNPLAGGL 232
Cdd:cd19129 145 EGRCKAIGLSDVSLEKLREIFEAAR----IKPAVVQ--VESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
64-228 |
6.51e-06 |
|
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: 47.41 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdgQSETILGGLGLGLGGGDcRVK-----IATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19154 35 LKAGYRLIDTAFLY---QNEEAIGEALAELLEEG-VVKredlfITTKLWT---HEHAPEDVEEALRESLKKLQLEYVDLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAP-----------------DHGTPV--EETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQGM 199
Cdd:cd19154 108 LIHAPaafkddegesgtmengmSIHDAVdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVE 183
|
170 180
....*....|....*....|....*....
gi 41327764 200 YNATTRQVETELFpCLRHfGLRFYAYNPL 228
Cdd:cd19154 184 CHLYFPQKELVEF-CKKH-NISVTSYATL 210
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
117-329 |
8.89e-06 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 46.83 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPD---HGTPVEETLH--------ACQRLHQEGKFVELGL-SNyaSWEVAE-ICT 183
Cdd:cd19152 103 DGILRSIEDSLQRLGLSRIDLLSIHDPDedlAGAESDEHFAqaikgafrALEELREEGVIKAIGLgVN--DWEVILrILE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 184 LCKSNgWILptvYQGMYNATTRQVETELFPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgNSWAETYRNR 263
Cdd:cd19152 181 EADLD-WVM---LAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPA------PPELIARRDR 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41327764 264 FW---KEHHfeaIALVEKALQAAYgasAPSVTSaalrwmyhhsqlqgahgdAVILGMSSLEQLEQNLAA 329
Cdd:cd19152 251 IEalcEQHG---VSLAAAALQFAL---APPAVA------------------SVAPGASSPERVEENVAL 295
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
115-230 |
1.01e-05 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 46.36 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAP-------------------DHGTPVEETLHACQRLHQEGKFVELGLSNYAS 175
Cdd:cd19128 73 QPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYST 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41327764 176 WEVAEICTLCKsngwILPtvyqgmynaTTRQVETEL-FP-------CLRHfGLRFYAYNPLAG 230
Cdd:cd19128 153 KLLTDLLNYCK----IKP---------FMNQIECHPyFQndklikfCIEN-NIHVTAYRPLGG 201
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
117-231 |
1.23e-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: 46.23 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVeETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 196
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPVKGKYK-ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVN 155
|
90 100 110
....*....|....*....|....*....|....*
gi 41327764 197 QGMYNAttRQVETELFPCLRHFGLRFYAYNPLAGG 231
Cdd:cd19157 156 QVEFHP--RLTQKELRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
64-332 |
3.46e-05 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 44.83 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPW--DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLH 141
Cdd:cd19153 43 FAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYrdSEFDYSAERVRASVATSLERLHTTYLDVVYLH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 142 A---PDHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKSNGwilPTVYQGMYNATTRQVE-TELFPCLRH 217
Cdd:cd19153 123 DiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS---LDAVLSYCHLTLQDARlESDAPGLVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 218 -FGLRFYAYNPLAGGLLTGKykyedkdGKQPvgrffgnswaetyrnrfWKEHHFEaiaLVEKALQAAYGASAPSVTSAAL 296
Cdd:cd19153 200 gAGPHVINASPLSMGLLTSQ-------GPPP-----------------WHPASGE---LRHYAAAADAVCASVEASLPDL 252
|
250 260 270
....*....|....*....|....*....|....*.
gi 41327764 297 RWMYHHSQLQGAhgDAVILGMSSLEQLEQNLAATEE 332
Cdd:cd19153 253 ALQYSLAAHAGV--GTVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
117-233 |
4.08e-05 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 44.35 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTpVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 196
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVN 154
|
90 100 110
....*....|....*....|....*....|....*..
gi 41327764 197 QGMYNAttRQVETELFPCLRHFGLRFYAYNPLAGGLL 233
Cdd:cd19126 155 QVEFHP--YLTQKELRGYCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
64-228 |
7.89e-05 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 44.05 E-value: 7.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGdcRVK-----IATKANPwdgKSLKPDSVRSQLETSLKRLQCPQVDLF 138
Cdd:cd19155 35 LEAGYRHIDTAYVY--RNEAAIGNVLKKWIDSG--KVKreelfIVTKLPP---GGNRREKVEKFLLKSLEKLQLDYVDLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 139 YLHAP---------------------DHGTPVEETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVYQ 197
Cdd:cd19155 108 LIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR----IKPANLQ 183
|
170 180 190
....*....|....*....|....*....|.
gi 41327764 198 GMYNATTRQVETELFpCLRHfGLRFYAYNPL 228
Cdd:cd19155 184 VELHVYLQQKDLVDF-CSTH-SITVTAYAPL 212
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
72-341 |
2.10e-04 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 42.84 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 72 DTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPW-DGKSLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGT--- 147
Cdd:PLN02587 49 DTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKCGRYgEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSldq 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 148 PVEETLHACQRLHQEGKFVELGLSNYAswevAEICTlcksngWILPTVYQGM---------YNATTRQVEtELFPCLRHF 218
Cdd:PLN02587 129 IVNETIPALQKLKESGKVRFIGITGLP----LAIFT------YVLDRVPPGTvdvilsychYSLNDSSLE-DLLPYLKSK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 219 GLRFYAYNPLAGGLLTGKYKYEdkdgkqpvgrffgnsWaetyrnrfwkehHFEAIALVEKALQAAY--GASAPSVTSAAL 296
Cdd:PLN02587 198 GVGVISASPLAMGLLTENGPPE---------------W------------HPAPPELKSACAAAAThcKEKGKNISKLAL 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 41327764 297 RWMYHHSQLQgahgdAVILGMSSLEQLEQNLAATEEgpLEPAVVD 341
Cdd:PLN02587 251 QYSLSNKDIS-----TTLVGMNSVQQVEENVAAATE--LETSGID 288
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
117-233 |
2.42e-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: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 117 DSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVeETLHACQRLHQEGKFVELGLSNYASWEVAEICTLCKsngwILPTVY 196
Cdd:cd19156 80 ESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVN 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 41327764 197 QgmynattrqveTELFPCLRHFGLRFY---------AYNPLAGGLL 233
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) ... |
113-189 |
5.62e-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: 41.45 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 113 SLKPDSVRSQLETSLKRLQCPQVDLFYLHAPDHGTPVEETLHAcqrlHQEGKF----VELglsnYASWEVAEICT---LC 185
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPK----DENGKLifdtVDL----CATWEAMEKCKdagLA 155
|
....
gi 41327764 186 KSNG 189
Cdd:cd19108 156 KSIG 159
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
114-173 |
1.20e-03 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 40.01 E-value: 1.20e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 41327764 114 LKPDSVRSQLETSLKRLQCPQVDLFYLH--APDHGTPVEETLHACQRLHQEGKFVELGLSNY 173
Cdd:PRK11172 70 LAKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNF 131
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
64-173 |
3.91e-03 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 38.35 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcRVKIATKAnpWDGKSlKPDSVRSQLETSLKRLQCPQVDLFYLH-- 141
Cdd:cd19130 33 LEVGYRHIDTAAIY--GNEEGVGAAIAASGIPRD-ELFVTTKL--WNDRH-DGDEPAAAFAESLAKLGLDQVDLYLVHwp 106
|
90 100 110
....*....|....*....|....*....|..
gi 41327764 142 APDHGTPVeETLHACQRLHQEGKFVELGLSNY 173
Cdd:cd19130 107 TPAAGNYV-HTWEAMIELRAAGRTRSIGVSNF 137
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
115-331 |
7.68e-03 |
|
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: 37.78 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 115 KPDSVRSQLETSLKRLQCPQVDLFYLHAP---DHGT---------------PVEETLHACQRLHQEGKFVELGLSNYASW 176
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPvalKKGVgfpesgedllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 177 EVAEICTLCKsngwILPTVYQgmynattrqveTELFPCL---------RHFGLRFYAYNPLAggllTGKYKYEDKDGKQP 247
Cdd:cd19123 164 KLEDLLATAR----IKPAVNQ-----------VELHPYLqqpellafcRDNGIHLTAYSPLG----SGDRPAAMKAEGEP 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41327764 248 VgrffgnswaetyrnrfwkehHFEAIALVEKAlqAAYGASAPSVtsaALRWMYHhsqlqgaHGDAVILGMSSLEQLEQNL 327
Cdd:cd19123 225 V--------------------LLEDPVINKIA--EKHGASPAQV---LIAWAIQ-------RGTVVIPKSVNPERIQQNL 272
|
....
gi 41327764 328 AATE 331
Cdd:cd19123 273 EAAE 276
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
102-173 |
8.83e-03 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 37.36 E-value: 8.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 41327764 102 IATKAnpWDGKSLKPdsvRSQLETSLKRLQCPQVDLFYLHAPDhgtPVEET-LHACQR---LHQEGKFVELGLSNY 173
Cdd:PRK11565 73 ITTKL--WNDDHKRP---REALEESLKKLQLDYVDLYLMHWPV---PAIDHyVEAWKGmieLQKEGLIKSIGVCNF 140
|
|
| |
