|
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 |
4.31e-180 |
|
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: 500.93 E-value: 4.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 38 VATVLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGlgggDCRVKIATKANPWDGKSL 114
Cdd:cd19075 1 PKIILGTMTFGsqgRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLG----ERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 115 KPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPT 194
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 195 VYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgKQPVGRFFGNS-WAETYRNRFWKEHHFQAI 273
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSED--KAGGGRFDPNNaLGKLYRDRYWKPSYFEAL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380790393 274 ALVEKALQaAYGtsvPSMTSAALRWMYHHSQLQGAHGDTVILGMSSLEQLEQNLTATEEGPLEPAVVDAFNQAW 347
Cdd:cd19075 235 EKVEEAAE-KEG---ISLAEAALRWLYHHSALDGEKGDGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
42-347 |
1.30e-62 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 202.33 E-value: 1.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:COG0667 18 LGTMTFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRPRDD--VVIATKVgrrmgPGPNGRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 114 LKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsnGWIVP 193
Cdd:COG0667 96 LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 194 TVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKqpvgrffGNSWAETYRNRFWKEHHFQAI 273
Cdd:COG0667 174 VAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPE-------GDRAATNFVQGYLTERNLALV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380790393 274 ALVeKALQAAYGTSVPSMtsaALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATEEgPLEPAVVDAFNQAW 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 ... |
41-327 |
2.36e-57 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 186.19 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKA-----NPWDGKSLK 115
Cdd:cd06660 4 GLGTMTFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGNRD-DVVIATKGghppgGDPSRSRLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 116 PDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTV 195
Cdd:cd06660 83 PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 196 YQGMYN-ATTRQVETELLPCLRHFGLRFYAYNPLAGGLltgkykyedkdgkqpvgrffgnswaetyrnrfwkehhfqaia 274
Cdd:cd06660 163 VQPQYSlLDRSPMEEELLDWAEENGLPLLAYSPLARGP------------------------------------------ 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 380790393 275 lvekalqaaygtsvpsmTSAALRWMYHHSqlqgaHGDTVILGMSSLEQLEQNL 327
Cdd:cd06660 201 -----------------AQLALAWLLSQP-----FVTVPIVGARSPEQLEENL 231
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
42-331 |
2.30e-56 |
|
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: 186.24 E-value: 2.30e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKA------NPWD-GK 112
Cdd:cd19087 18 LGTMNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIA-----GRRddIVLATKVfgpmgdDPNDrGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 113 SLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIV 192
Cdd:cd19087 93 SRR--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 193 PTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNswaETYRNRFWKEHHFQA 272
Cdd:cd19087 171 FVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYG---KGKRPESGRLVER---ARYQARYGLEEYRDI 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 380790393 273 IALVEkALQAAYGTSVPSMtsaALRWMYHHSQLQGAhgdtvILGMSSLEQLEQNLTATE 331
Cdd:cd19087 245 AERFE-ALAAEAGLTPASL---ALAWVLSHPAVTSP-----IIGPRTLEQLEDSLAALE 294
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
41-344 |
1.49e-53 |
|
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: 178.95 E-value: 1.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD-------GQSETILGGLGLGLGGGDcRVKIATKANPW---D 110
Cdd:cd19081 13 CLGTMVFGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRGKRD-RVVIATKVGFPmgpN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 111 GKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGW 190
Cdd:cd19081 92 GPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 191 IVPTVYQGMYNATTRQ-VETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgnsWAETYRNRFWKEHH 269
Cdd:cd19081 172 PRYVSLQPEYNLVDREsFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGST--------RRGEAAKRYLNERG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 380790393 270 FQAIALVEkALQAAYGTsvpSMTSAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATeEGPLEPAVVDAFN 344
Cdd:cd19081 244 LRILDALD-EVAAEHGA---TPAQVALAWLLARPGV-----TAPIAGARTVEQLEDLLAAA-GLRLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
41-347 |
1.06e-51 |
|
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain regulatory domains - these are reported to have oxidoreductase activity.
Pssm-ID: 425554 [Multi-domain] Cd Length: 290 Bit Score: 173.27 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMG---RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPWDGK---SL 114
Cdd:pfam00248 2 GLGTWQLGggwGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpsGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 115 KPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEIctlcKSNGWIVPT 194
Cdd:pfam00248 82 SKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA----LTKGKIPIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 195 VYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETYrnrfwkehhfQAIA 274
Cdd:pfam00248 158 AVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTPLNL----------EALE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380790393 275 LVEKaLQAAYGTsvpSMTSAALRWMYHHSQlqgahGDTVILGMSSLEQLEQNLTATeEGPLEPAVVDAFNQAW 347
Cdd:pfam00248 228 ALEE-IAKEHGV---SPAQVALRWALSKPG-----VTIPIPGASNPEQLEDNLGAL-EFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
64-331 |
9.56e-51 |
|
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: 171.17 E-value: 9.56e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDG-----KSLKPDSLRSQLETSLKRLQCPRVDL 137
Cdd:cd19084 35 IDLGINFFDTAPVYGFGHSEEILGKALKGRRD---DVVIATKcGLRWDGgkgvtKDLSPESIRKEVEQSLRRLQTDYIDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 138 FYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwivPTVYQGMYNATTRQVETELLPCLRH 217
Cdd:cd19084 112 YQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVSLQPPYSMLEREIEEELLPYCRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 218 FGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNswaetYRNRFWKehHFQAIALVEKALQAAYGTSVPSMtsaALR 297
Cdd:cd19084 186 NGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPF-----FRGENFE--KNLEIVDKLKEIAEKYGKSLAQL---AIA 255
|
250 260 270
....*....|....*....|....*....|....
gi 380790393 298 WMYHHSQLqgahgDTVILGMSSLEQLEQNLTATE 331
Cdd:cd19084 256 WTLAQPGV-----TSAIVGAKNPEQLEENAGALD 284
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-331 |
5.23e-50 |
|
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: 169.71 E-value: 5.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTM----EMGRRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK----ANPWD--- 110
Cdd:cd19080 15 LGTMtfgtEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRD---RIVLATKytmnRRPGDpna 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 111 -GKSLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNG 189
Cdd:cd19080 92 gGNHRK--NLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 190 WIVPTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKY-KYEDKDGKQPVGRFFGNSwAETYRNrfwkeh 268
Cdd:cd19080 170 WSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYqRGEEGRAGEAKGVTVGFG-KLTERN------ 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380790393 269 hfqaIALVEKALQAAYGTSVpSMTSAALRWMYHHSQlqgahGDTVILGMSSLEQLEQNLTATE 331
Cdd:cd19080 243 ----WAIVDVVAAVAEELGR-SAAQVALAWVRQKPG-----VVIPIIGARTLEQLKDNLGALD 295
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
64-331 |
1.37e-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: 158.16 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANPWDGKSLKPDSL-RSQL----ETSLKRLQCPRVDLF 138
Cdd:cd19091 49 LDAGINFFDTADVYSEGESEEILGKALKGRRD---DVLIATKVRGRMGEGPNDVGLsRHHIiravEASLKRLGTDYIDLY 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHF 218
Cdd:cd19091 126 QLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYrnRFWKEHHFQAI-ALVEKAlqAAYGTSVPsmtSAALR 297
Cdd:cd19091 206 GVGLLVWSPLAGGLLSGKYR---RGQPAPEGSRLRRTGFDFP--PVDRERGYDVVdALREIA--KETGATPA---QVALA 275
|
250 260 270
....*....|....*....|....*....|....
gi 380790393 298 WMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATE 331
Cdd:cd19091 276 WL-----LSRPTVSSVIIGARNEEQLEDNLGAAG 304
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
64-346 |
4.22e-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: 148.50 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPwdgKSLKPDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19085 33 LDAGINFFDTAEAYGDGHSEEVLGKALK-----GRRddVVIATKVSP---DNLTPEDVRKSCERSLKRLGTDYIDLYQIH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 APDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwivPTVYQGMYNATTRQVETELLPCLRHFGLR 221
Cdd:cd19085 105 WPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCREHGIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 222 FYAYNPLAGGLLTGKYkyeDKDGKQPVGR--------FFGNSWAETyrnrfwkehhFQAIALVeKALQAAYGTsvpSMTS 293
Cdd:cd19085 179 VLAYSPLAQGLLTGKF---SSAEDFPPGDartrlfrhFEPGAEEET----------FEALEKL-KEIADELGV---TMAQ 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 380790393 294 AALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATEEgPLEPAVVDAFNQA 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 |
7.06e-42 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 148.50 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKANP-----WDGKSLKPDSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19079 45 LDLGINFFDTANVYSGGASEEILGRALKEFAPRD-EVVIATKVYFpmgdgPNGRGLSRKHIMAEVDASLKRLGTDYIDLY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHF 218
Cdd:cd19079 124 QIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSWAETYRnrfwKEHHFQAIALVEKaLQAAYGTsvpSMTSAALRW 298
Cdd:cd19079 204 GIGVIPWSPLARGRLARPWG---DTTERRRSTTDTAKLKYDYF----TEADKEIVDRVEE-VAKERGV---SMAQVALAW 272
|
250 260 270
....*....|....*....|....*....|...
gi 380790393 299 MYHHSQlqgahGDTVILGMSSLEQLEQNLTATE 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 |
3.60e-40 |
|
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: 143.94 E-value: 3.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKA--NPW-----DGKSLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 174
Cdd:cd19089 80 ISTKAgyGMWpgpygDGGSRK--YLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 175 AWEVAEICTLCKSNGwiVP-TVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGRFFG 253
Cdd:cd19089 158 GAKARRAIALLRELG--VPlIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKY----LNGIPPDSRRAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 254 NSWaetyrnrFWKEHHFqAIALVEKALQ-----AAYGTSVPSMtsaALRWMYHHSQLQgahgdTVILGMSSLEQLEQNLT 328
Cdd:cd19089 232 ESK-------FLTEEAL-TPEKLEQLRKlnkiaAKRGQSLAQL---ALSWVLRDPRVT-----SVLIGASSPSQLEDNVA 295
|
250
....*....|
gi 380790393 329 ATEEGPLEPA 338
Cdd:cd19089 296 ALKNLDFSEE 305
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
64-329 |
8.10e-40 |
|
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: 142.35 E-value: 8.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGD----CRVKIATKANPWD-GKSLKpdSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19074 32 YDLGINFFDTADVYAAGQAEEVLGKALKGWPRESyvisTKVFWPTGPGPNDrGLSRK--HIFESIHASLKRLQLDYVDIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHF 218
Cdd:cd19074 110 YCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEEEVIPLCEKN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKYkyedKDGK-QPVGRFFGNSWaetyrNRFWKEHHF--QAIALVE--KALQAAYGTsvpSMTS 293
Cdd:cd19074 190 GIGLVVWSPLAQGLLTGKY----RDGIpPPSRSRATDED-----NRDKKRRLLtdENLEKVKklKPIADELGL---TLAQ 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 380790393 294 AALRWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTA 329
Cdd:cd19074 258 LALAWC-----LRNPAVSSAIIGASRPEQLEENVKA 288
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
64-332 |
3.88e-36 |
|
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: 132.93 E-value: 3.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATK-ANPWDGKSLK----PDSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19083 43 LDNGVNLLDTAFIYGLGRSEELVGEVLKEYNRNE--VVIATKgAHKFGGDGSVlnnsPEFLRSAVEKSLKRLNTDYIDLY 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEictlCKSNGWIvpTVYQGMYNATTRQVETELLPCLRHF 218
Cdd:cd19083 121 YIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE----ANKDGYV--DVLQGEYNLLQREAEEDILPYCVEN 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKY----KYEDKDGKQPVGRFFGnswaETYRNRFWKEHHFQAIAlvekalqAAYGTSVPSMtsa 294
Cdd:cd19083 195 NISFIPYFPLASGLLAGKYtkdtKFPDNDLRNDKPLFKG----ERFSENLDKVDKLKSIA-------DEKGVTVAHL--- 260
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 380790393 295 ALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTA-----TEE 332
Cdd:cd19083 261 ALAWYLTRPAI-----DVVIPGAKRAEQVIDNLKAldvtlTEE 298
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-331 |
9.01e-36 |
|
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: 132.03 E-value: 9.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKANP-WDGK-----SLKPDSLRSQLETSLKRLQCPRVDL 137
Cdd:cd19102 36 LDLGINWIDTAAVYGLGHSEEVVGRALKGLRD---RPIVATKCGLlWDEEgrirrSLKPASIRAECEASLRRLGVDVIDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 138 FYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTlcksngwIVP-TVYQGMYNATTRQVETELLPCLR 216
Cdd:cd19102 113 YQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPiASLQPPYSLLRRGIEAEILPFCA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 217 HFGLRFYAYNPLAGGLLTGKYkyedkdGKQPVGRFFGNSWAEtyRNRFWKEHHF-QAIALVE--KALQAAYGTSVPSMts 293
Cdd:cd19102 186 EHGIGVIVYSPMQSGLLTGKM------TPERVASLPADDWRR--RSPFFQEPNLaRNLALVDalRPIAERHGRTVAQL-- 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 380790393 294 aALRWMYHHSQLQGAhgdtvILGMSSLEQLEQNLTATE 331
Cdd:cd19102 256 -AIAWVLRRPEVTSA-----IVGARRPDQIDETVGAAD 287
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
64-331 |
3.27e-35 |
|
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: 130.41 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK-ANPWDGKSL------KPDSLRSQLETSLKRLQCPRVD 136
Cdd:cd19076 42 LELGVTFLDTADMYGPGTNEELLGKALKDRRD---EVVIATKfGIVRDPGSGfrgvdgRPEYVRAACEASLKRLGTDVID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 137 LFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTlcksngwIVP-TVYQGMYNATTRQVETELLPCL 215
Cdd:cd19076 119 LYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHA-------VHPiTAVQSEYSLWTRDIEDEVLPTC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 216 RHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGnswaetyrnRFWKEHHFQAIALVEK--ALQAAYGTSVPSMts 293
Cdd:cd19076 192 RELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNP---------RFQGENFDKNLKLVEKleAIAAEKGCTPAQL-- 260
|
250 260 270
....*....|....*....|....*....|....*....
gi 380790393 294 aALRWMYHhsqlQGAhgDTV-ILGMSSLEQLEQNLTATE 331
Cdd:cd19076 261 -ALAWVLA----QGD--DIVpIPGTKRIKYLEENVGALD 292
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
42-344 |
3.42e-35 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 131.15 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATKA------NP 108
Cdd:cd19094 6 LGTMTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKGNRD-KVVLATKVagpgegIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 109 W---DGKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDH------------------STPVEETLRACHQLHQEGKFVE 167
Cdd:cd19094 85 WprgGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRytplfgggyytepseeedSVSFEEQLEALGELVKAGKIRH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 168 LGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQp 247
Cdd:cd19094 165 IGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGAARPEG- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 248 vGRFF-GNSWAETYRNRFWKEHhfqAIALVEKALQAAYgtsvpSMTSAALRWMYHHSqlqgaHGDTVILGMSSLEQLEQN 326
Cdd:cd19094 244 -GRLNlFPGYMARYRSPQALEA---VAEYVKLARKHGL-----SPAQLALAWVRSRP-----FVTSTIIGATTLEQLKEN 309
|
330
....*....|....*...
gi 380790393 327 LTATeEGPLEPAVVDAFN 344
Cdd:cd19094 310 IDAF-DVPLSDELLAEID 326
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
72-342 |
1.37e-33 |
|
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: 126.56 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 72 DTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDS-------LRSQLETSLKRLQCPRVDLFYLHAPD 144
Cdd:cd19143 49 DNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIF-WGGGGPPPNDrglsrkhIVEGTKASLKRLQLDYVDLVFCHRPD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 145 HSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQ-VETELLPCLRHFGLRFY 223
Cdd:cd19143 128 PATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVEYAPLYEKYGLGTT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 224 AYNPLAGGLLTGKYkyedKDGKQPVGRFFGNSWaetyrnrFWKEHHFQA-----IALVEKALQAA--YGTSVPSMtsaAL 296
Cdd:cd19143 208 TWSPLASGLLTGKY----NNGIPEGSRLALPGY-------EWLKDRKEElgqekIEKVRKLKPIAeeLGCSLAQL---AI 273
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 380790393 297 RWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATEEGP-LEPAVVDA 342
Cdd:cd19143 274 AWC-----LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEK 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
34-324 |
3.39e-32 |
|
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: 122.42 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 34 PPPRVAtvLGTMEMGRRM----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATKAN-P 108
Cdd:cd19148 3 PVSRIA--LGTWAIGGWMwggtDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYGKRD-RVVIATKVGlE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 109 WDGKSLK-----PDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAA------WE 177
Cdd:cd19148 80 WDEGGEVvrnssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPeqmetfRK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 178 VAEICTLcksngwivptvyQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGK----YKYEDKDGKQPVGRFFG 253
Cdd:cd19148 160 VAPLHTV------------QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKmtkdTKFEGDDLRRTDPKFQE 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380790393 254 nswaetyrNRFwkEHHFQAIALVEKALQAAYGTSVPSMtsaALRWMYHHSqlqgahGDTVIL-GMSSLEQLE 324
Cdd:cd19148 228 --------PRF--SQYLAAVEELDKLAQERYGKSVIHL---AVRWLLDQP------GVSIALwGARKPEQLD 280
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
41-331 |
4.10e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 122.06 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYS-------DGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19752 4 CLGTMYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGNRD-DVVIATKvgagprdp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 106 -ANPWDGKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTL 184
Cdd:cd19752 83 dGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 185 CKSNGWIVPTVYQ----------GMYNATTRQVETELLPCLR-HFGLRFYAYNPLAGGLltgkykYEDKDGKQPvgrffg 253
Cdd:cd19752 163 ARQQGWAEFSAIQqrhsylrprpGADFGVQRIVTDELLDYASsRPDLTLLAYSPLLSGA------YTRPDRPLP------ 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380790393 254 nswaETYRNRFwKEHHFQAIALVEKALQAAYGTSVpsmtsaaLRWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATE 331
Cdd:cd19752 231 ----EQYDGPD-SDARLAVLEEVAGELGATPNQVV-------LAWL-----LHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
64-326 |
2.57e-30 |
|
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: 117.76 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKAN-PWDG---------------KSLKPDSLRSQLETSL 127
Cdd:cd19149 43 LDLGINLIDTAPAYGFGHSEEIVGKAIKGRRD---KVVLATKCGlRWDReggsfffvrdgvtvyKNLSPESIREEVEQSL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 128 KRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGWIvpTVYQGMYNATTRQV 207
Cdd:cd19149 120 KRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYV----KAGQL--DIIQEKYSMLDRGI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 208 ETELLP-CLRHfGLRFYAYNPLAGGLLTGKYKyedkdgkqPVGRFFGNSWaetyRNR---FWKEHHFQAIALVE--KALQ 281
Cdd:cd19149 194 EKELLPyCKKN-NIAFQAYSPLEQGLLTGKIT--------PDREFDAGDA----RSGipwFSPENREKVLALLEkwKPLC 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 380790393 282 AAYGTSVPSMtsaALRWMYHHSQLqgahgDTVILGMSSLEQLEQN 326
Cdd:cd19149 261 EKYGCTLAQL---VIAWTLAQPGI-----TSALCGARKPEQAEEN 297
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
42-331 |
5.02e-30 |
|
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: 115.40 E-value: 5.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGRRM-----DAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPWdgkSLKP 116
Cdd:cd19072 9 LGTWGIGGGMskdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFDRED--LFITTKVSPD---HLKY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsNGWIVptVY 196
Cdd:cd19072 84 DDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLK-KGPIV--AN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 197 QGMYNATTRQVETELLP-CLRHfGLRFYAYNPLAGGLLTGKYKYEDkdgkqpvgrffgnswaetyrnrfwkehhfqaiaL 275
Cdd:cd19072 161 QVEYNLFDREEESGLLPyCQKN-GIAIIAYSPLEKGKLSNAKGSPL---------------------------------L 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 380790393 276 VEkaLQAAYGtsvpsMTSA--ALRWMYHHSqlqgahGDTVILGMSSLEQLEQNLTATE 331
Cdd:cd19072 207 DE--IAKKYG-----KTPAqiALNWLISKP------NVIAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
41-331 |
1.80e-27 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 109.18 E-value: 1.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMYSD----GQSETILGGLGLGLGGGDcRVKIATKA-----NPWDG 111
Cdd:cd19082 4 VLGTADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGNRD-KVVIATKGghpdlEDMSR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 112 KSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNyaaWEVAEIC---TLCKSN 188
Cdd:cd19082 83 SRLSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASN---WSTERIAeanAYAKAH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 189 GWIVPTVYQGMYNATTRQVETELLPCL-------RHF----GLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWA 257
Cdd:cd19082 160 GLPGFAASSPQWSLARPNEPPWPGPTLvamdeemRAWheenQLPVFAYSSQARGFFSKRAAGGAEDDSELRRVYYSEENF 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380790393 258 ETYRNrfwkehhfqAIALVEKalqaaYGTSVpsmTSAALRWMYHHSQLQGAhgdtvILGMSSLEQLEQNLTATE 331
Cdd:cd19082 240 ERLER---------AKELAEE-----KGVSP---TQIALAYVLNQPFPTVP-----IIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
41-255 |
9.52e-27 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 107.99 E-value: 9.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 41 VLGTMEMG-------RRMDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK-------- 105
Cdd:cd19147 14 ILGAMSIGdawsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRKNRD-QIVIATKfttdykay 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 106 ------ANPWDGKSLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVA 179
Cdd:cd19147 93 evgkgkAVNYCGNHKR--SLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380790393 180 EICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGG-LLTGKYKYEDKDGKQPVGRFFGNS 255
Cdd:cd19147 171 AANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGLRSFVGGT 247
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
42-329 |
1.55e-26 |
|
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: 107.51 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGRR-------MDAPASAAAVRAFLERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVkIATK--------- 105
Cdd:cd19146 16 LGAMSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRGNRDEMV-LATKyttgyrrgg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 106 ----ANPWDGKSLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEI 181
Cdd:cd19146 95 pikiKSNYQGNHAK--SLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 182 CTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGlltgkyKYEDKDGKQPVGRFFGNSWAETyr 261
Cdd:cd19146 173 NAYARAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQG------QFRTEEEFKRRGRSGRKGGPQT-- 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 262 nrfwkEHHFQAIALVEKaLQAAYGTSVpsmTSAALRWMYHHSQLqgahgdtV--ILGMSSLEQLEQNLTA 329
Cdd:cd19146 245 -----EKERKVSEKLEK-VAEEKGTAI---TSVALAYVMHKAPY-------VfpIVGGRKVEHLKGNIEA 298
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
64-331 |
2.49e-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: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATK--------ANPWDGKSLKPDSLRSQLETSLKRLQCPRV 135
Cdd:cd19078 35 VELGITFFDTAEVYGPYTNEELVGEALKPFRD---QVVIATKfgfkidggKPGPLGLDSRPEHIRKAVEGSLKRLQTDYI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 136 DLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSnyaawEVAE--------ICTLcksngwivpTVYQGMYNATTRQV 207
Cdd:cd19078 112 DLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGVetirrahaVCPV---------TAVQSEYSMMWREP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 208 ETELLPCLRHFGLRFYAYNPLAGGLLTGKYkyeDKDGKqpvgrfFGnswAETYRN---RFWKEHHFQAIALVE--KALQA 282
Cdd:cd19078 178 EKEVLPTLEELGIGFVPFSPLGKGFLTGKI---DENTK------FD---EGDDRAslpRFTPEALEANQALVDllKEFAE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 380790393 283 AYGtsvpsMTSA--ALRWMYHhsqlQGAHgdTV-ILGMSSLEQLEQNLTATE 331
Cdd:cd19078 246 EKG-----ATPAqiALAWLLA----KKPW--IVpIPGTTKLSRLEENIGAAD 286
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
64-339 |
6.61e-25 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 102.25 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSLK--PDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19090 30 LDLGINYIDTAPAY--GDSEERLGLALAELPRE--PLVLSTKVGRLPEDTADysADRVRRSVEESLERLGRDRIDLLMIH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 APDHSTPVEET-----LRACHQLHQEGKFVELGLsnyAAWEVAEICTLCKSNGWIVPTVYQGmYNATTRQVETELLP-CL 215
Cdd:cd19090 106 DPERVPWVDILapggaLEALLELKEEGLIKHIGL---GGGPPDLLRRAIETGDFDVVLTANR-YTLLDQSAADELLPaAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 216 RHfGLRFYAYNPLAGGLLTGKYKyedkdgkqpvgrffgnSWAETYRNRFWKEHHFQAIALveKALQAAYGtsVPsMTSAA 295
Cdd:cd19090 182 RH-GVGVINASPLGMGLLAGRPP----------------ERVRYTYRWLSPELLDRAKRL--YELCDEHG--VP-LPALA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 380790393 296 LRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATeEGPLEPAV 339
Cdd:cd19090 240 LRFLLRDPRI-----STVLVGASSPEELEQNVAAA-EGPLPEEL 277
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
102-330 |
6.19e-24 |
|
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: 100.17 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKAN--PWDGK-----SLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 174
Cdd:cd19151 81 ISTKAGytMWPGPygdwgSKK--YLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 175 AWEVAEICTLCKSNGwiVPT-VYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKY---EDKDGKQPvgr 250
Cdd:cd19151 159 PEEAREAAAILKDLG--TPClIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNgipEDSRAAKG--- 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 251 ffgnswaetyrNRFWKEHHFQA--IALVEK--ALQAAYGTSVPSMtsaALRWMYHHSQLQgahgdTVILGMSSLEQLEQN 326
Cdd:cd19151 234 -----------SSFLKPEQITEekLAKVRRlnEIAQARGQKLAQM---ALAWVLRNKRVT-----SVLIGASKPSQIEDA 294
|
....
gi 380790393 327 LTAT 330
Cdd:cd19151 295 VGAL 298
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
102-329 |
8.20e-24 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 100.45 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKA--NPWDGKSLKPDS---LRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAW 176
Cdd:PRK09912 94 ISTKAgyDMWPGPYGSGGSrkyLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPE 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 177 EVAEICTLCKSngWIVP-TVYQGMYNATTRQVE-TELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGkqpvgrffgn 254
Cdd:PRK09912 174 RTQKMVELLRE--WKIPlLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQD---------- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 255 swaetyrNRFWKEHHfQAIALVEKALQAAYGTSV-----------PSMTSAALRWMYHHSQLQgahgdTVILGMSSLEQL 323
Cdd:PRK09912 242 -------SRMHREGN-KVRGLTPKMLTEANLNSLrllnemaqqrgQSMAQMALSWLLKDERVT-----SVLIGASRAEQL 308
|
....*.
gi 380790393 324 EQNLTA 329
Cdd:PRK09912 309 EENVQA 314
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
64-329 |
2.31e-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: 98.07 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcRVKIATK--ANPWdgkSLKPDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19093 36 LEAGVNLFDTAEVYGTGRSERLLGRFLKELGDRD-EVVIATKfaPLPW---RLTRRSVVKALKASLERLGLDSIDLYQLH 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 APDH-STPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwIVPTVYQGMYNATTRQVET-ELLPCLRHFG 219
Cdd:cd19093 112 WPGPwYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQnGLLPACDELG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 220 LRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFGNSWAETyrnrfwkehhfQAIALVEKALQAAYGTsvpSMTSAALRWM 299
Cdd:cd19093 191 ITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKV-----------QPLLDALEEIAEKYGK---TPAQVALNWL 256
|
250 260 270
....*....|....*....|....*....|
gi 380790393 300 YhhsqlqgAHGDTVILGMSSLEQLEQNLTA 329
Cdd:cd19093 257 I-------AKGVVPIPGAKNAEQAEENAGA 279
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
65-329 |
1.45e-22 |
|
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: 96.36 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDSL-RSQ----LETSLKRLQCPRVDLFY 139
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIF-WGGKAETERGLsRKHiiegLKASLERLQLEYVDIVF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 140 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTR-QVETElLPCLRH- 217
Cdd:cd19141 120 ANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQ-LPELFHk 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 218 FGLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSW------AETYRNRFWKEHHFQAIAlvEKalqaaYGTSVP 289
Cdd:cd19141 199 IGVGAMTWSPLACGILSGKY----DDGVPEYSRasLKGYQWlkekilSEEGRRQQAKLKELQIIA--DR-----LGCTLP 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 380790393 290 SMTSAalrWMYHHsqlQGAHGdtVILGMSSLEQLEQNLTA 329
Cdd:cd19141 268 QLAIA---WCLKN---EGVSS--VLLGASSTEQLYENLQA 299
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
64-331 |
3.23e-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: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLgggDCRVKIATKA-------NPW--DGKslkPDSLRSQLETSLKRLQCPR 134
Cdd:cd19088 34 LELGVNFIDTADSYGPDVNERLIAEALHPY---PDDVVIATKGglvrtgpGWWgpDGS---PEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 135 VDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVpTVyQGMYNATTRQVETELLPC 214
Cdd:cd19088 108 IDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----IV-SV-QNRYNLANRDDEGVLDYC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 215 LRHfGLRFYAYNPLAGGLLTgkykyedkdgkQPVGRFfgnswaetyrnrfwkehhfqaialveKALQAAYGTSVPsmtSA 294
Cdd:cd19088 182 EAA-GIAFIPWFPLGGGDLA-----------QPGGLL--------------------------AEVAARLGATPA---QV 220
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 380790393 295 ALRWMYHHSQlqgahgdtVIL---GMSSLEQLEQNLTATE 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 |
1.01e-20 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 91.35 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDgqSETILGGLGLGLGGGDCRVKIATK----ANPWDGK---SLKPDSLRSQLETSLKRLQCPRVD 136
Cdd:cd19144 44 FELGCTFWDTADIYGD--SEELIGRWFKQNPGKREKIFLATKfgieKNVETGEysvDGSPEYVKKACETSLKRLGVDYID 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 137 LFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTlcksngwIVP-TVYQGMYNATTRQVET---ELL 212
Cdd:cd19144 122 LYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHA-------VHPiAAVQIEYSPFSLDIERpeiGVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 213 PCLRHFGLRFYAYNPLAGGLLTGKYKYEDKdgkqpvgrFFGNSWaETYRNRFWKEHHFQAIALVEKALQAAYGTSVPSmT 292
Cdd:cd19144 195 DTCRELGVAIVAYSPLGRGFLTGAIRSPDD--------FEEGDF-RRMAPRFQAENFPKNLELVDKIKAIAKKKNVTA-G 264
|
250 260 270
....*....|....*....|....*....|....*....
gi 380790393 293 SAALRWMYhhsqlqgAHGDTV--ILGMSSLEQLEQNLTA 329
Cdd:cd19144 265 QLTLAWLL-------AQGDDIipIPGTTKLKRLEENLGA 296
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
102-329 |
1.57e-19 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 87.89 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKA--NPWDGK-----SLKpdSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYA 174
Cdd:cd19150 81 ISTKAgyDMWPGPygewgSRK--YLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 175 AWEVAEICTLCKSngWIVPT-VYQGMYNATTRQVE-TELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGrff 252
Cdd:cd19150 159 PERTREAAAILRE--LGTPLlIHQPSYNMLNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKYL-----NGIPEG--- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 253 gnswaetyrNRFWKEHHFQAIALVE------KALQAAYGTSVPSMTSAALRWMyhhsqLQGAHGDTVILGMSSLEQLEQN 326
Cdd:cd19150 229 ---------SRASKERSLSPKMLTEanlnsiRALNEIAQKRGQSLAQMALAWV-----LRDGRVTSALIGASRPEQLEEN 294
|
...
gi 380790393 327 LTA 329
Cdd:cd19150 295 VGA 297
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
64-233 |
2.38e-19 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 86.53 E-value: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETIlgglgLGLGGGDCR--VKIATKANPWDGkslKPDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19138 39 IDLGMTLIDTAEMYGDGGSEEL-----VGEAIRGRRdkVFLVSKVLPSNA---SRQGTVRACERSLRRLGTDYLDLYLLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 APDhSTPVEETLRACHQLHQEGKFVELGLSNY------AAWEVAEIcTLCKSNgwivptvyQGMYNATTRQVETELLPCL 215
Cdd:cd19138 111 WRG-GVPLAETVAAMEELKKEGKIRAWGVSNFdtddmeELWAVPGG-GNCAAN--------QVLYNLGSRGIEYDLLPWC 180
|
170
....*....|....*....
gi 380790393 216 RHFGLRFYAYNPLA-GGLL 233
Cdd:cd19138 181 REHGVPVMAYSPLAqGGLL 199
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
64-329 |
4.83e-19 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 84.84 E-value: 4.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLglgggDCR--VKIATKANPWDGKSLK------PDSLRSQLETSLKRLQCPRV 135
Cdd:cd19086 34 LDLGINFFDTADVYGDGHSERLLGKALK-----GRRdkVVIATKFGNRFDGGPErpqdfsPEYIREAVEASLKRLGTDYI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 136 DLFYLH-APDHSTPVEETLRACHQLHQEGKFVELGLS---NYAAWEVAEictlcksNGWIVptVYQGMYNATTRQVETEL 211
Cdd:cd19086 109 DLYQLHnPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR-------RGGID--VVQVIYNLLDQRPEEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 212 LPCLRHFGLRFYAYNPLAGGLLTGKykyedkdgkqpvgrffgnswaetyrnrfwkehhfqaialvekalqaaygtsvpsM 291
Cdd:cd19086 180 FPLAEEHGVGVIARVPLASGLLTGK------------------------------------------------------L 205
|
250 260 270
....*....|....*....|....*....|....*...
gi 380790393 292 TSAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTA 329
Cdd:cd19086 206 AQAALRFILSHPAV-----STVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
67-329 |
1.37e-18 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 84.79 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 67 GHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATK---ANPWDGKSL---KPDSLRSQLETSLKRLQCPRVDLFYL 140
Cdd:cd19145 46 GVTFLDTSDIYGPNTNEVLLGKALKDGPRE--KVQLATKfgiHEIGGSGVEvrgDPAYVRAACEASLKRLDVDYIDLYYQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 141 HAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAwevaeiCTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHFGL 220
Cdd:cd19145 124 HRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASA------DTIRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 221 RFYAYNPLAGGLLTGKYKYE----DKDGKQPVGRFFGNSWaetyrnrfwkEHHFQAIALVEkALQAAYGTSvPSmtSAAL 296
Cdd:cd19145 198 GIVPYSPLGRGFFAGKAKLEelleNSDVRKSHPRFQGENL----------EKNKVLYERVE-ALAKKKGCT-PA--QLAL 263
|
250 260 270
....*....|....*....|....*....|....*
gi 380790393 297 RWMYHhsqlqgaHGDTV--ILGMSSLEQLEQNLTA 329
Cdd:cd19145 264 AWVLH-------QGEDVvpIPGTTKIKNLNQNIGA 291
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
65-334 |
2.51e-18 |
|
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: 84.71 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDSLRSQ-----LETSLKRLQCPRVDLFY 139
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLY-WGGKAETERGLSRKhiiegLKGSLQRLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 140 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRH-F 218
Cdd:cd19159 121 ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKYKYEDKDGKQPVGRFFgnSW------AETYRNRFWKEHHFQAIAlvEKalqaaYGTSVPSMt 292
Cdd:cd19159 201 GVGAMTWSPLACGIISGKYGNGVPESSRASLKCY--QWlkerivSEEGRKQQNKLKDLSPIA--ER-----LGCTLPQL- 270
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 380790393 293 saALRWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATEEGP 334
Cdd:cd19159 271 --AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
65-334 |
2.69e-18 |
|
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: 84.37 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDSLRSQ-----LETSLKRLQCPRVDLFY 139
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIF-WGGKAETERGLSRKhiiegLKASLERLQLEYVDVVF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 140 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQ-VETELLPCLRHF 218
Cdd:cd19158 121 ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 219 GLRFYAYNPLAGGLLTGKYkyedKDGKQPVGR--FFGNSW------AETYRNRFWKEHHFQAIAlvekalqAAYGTSVPS 290
Cdd:cd19158 201 GVGAMTWSPLACGIVSGKY----DSGIPPYSRasLKGYQWlkdkilSEEGRRQQAKLKELQAIA-------ERLGCTLPQ 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 380790393 291 MtsaALRWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATEEGP 334
Cdd:cd19158 270 L---AIAWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVLP 305
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
64-231 |
4.40e-17 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 79.62 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19073 24 LELGYRHIDTAEIY-NNEAEVGEAIAESGVPRED--LFITTKVWR---DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEictlCKSNGWIVPTVYQGMYNATTRQveTELLPCLRHFGLRFY 223
Cdd:cd19073 98 NPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEE----ALDISPLPIAVNQVEFHPFLYQ--AELLEYCRENDIVIT 171
|
....*...
gi 380790393 224 AYNPLAGG 231
Cdd:cd19073 172 AYSPLARG 179
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
65-345 |
1.79e-16 |
|
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: 79.26 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 65 ERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANpWDGKSLKPDSLRSQ-----LETSLKRLQCPRVDLFY 139
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIY-WGGQAETERGLSRKhiiegLRGSLDRLQLEYVDIVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 140 LHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQ-VETElLPCLRH- 217
Cdd:cd19160 123 ANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQ-LPELYHk 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 218 FGLRFYAYNPLAGGLLTGkyKYEDKDGKQPVGRFFGNSW-AETYRNRFWKEHHFQAIALVEKALQaaYGTSVPSMtsaAL 296
Cdd:cd19160 202 IGVGSVTWSPLACGLITG--KYDGRVPDTCRAAVKGYQWlKEKVQSEEGKKQQAKVKELHPIADR--LGCTVAQL---AI 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 380790393 297 RWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTATEE-GPLEPAVVDAFNQ 345
Cdd:cd19160 275 AWC-----LRSEGVSSVLLGVSSAEQLIENLGSIQVlSQLTPQTVMEIDA 319
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
64-233 |
3.93e-16 |
|
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: 77.23 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwdgKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19137 36 IELGYTHIDTAEMYGGGHTEELVGKAIKDFPRED--LFIVTKVWP---TNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNgwIVptVYQGMYNATTRQVETE-LLPCLRHFGLRF 222
Cdd:cd19137 111 NPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQTP--IV--CNQVKYNLEDRDPERDgLLEYCQKNGITV 186
|
170
....*....|.
gi 380790393 223 YAYNPLAGGLL 233
Cdd:cd19137 187 VAYSPLRRGLE 197
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
99-348 |
3.05e-15 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 76.01 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 99 RVKIATKANPWdgkSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLR------ACHQLHQEGKFVELGLSN 172
Cdd:COG1453 69 KVILATKLPPW---VRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggaleALEKAKAEGKIRHIGFST 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 173 YAAWEVAEicTLCKSNGWivpTVYQGMYNA--TTRQVETELLPCLRHFGLRFYAYNPLAGGLLTgkykyedkdgkqpvgr 250
Cdd:COG1453 146 HGSLEVIK--EAIDTGDF---DFVQLQYNYldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA---------------- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 251 ffgnswaetyrnrfwkEHHFQAIALVEKALqaaygtsvpSMTSAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNL-TA 329
Cdd:COG1453 205 ----------------NPPEKLVELLCPPL---------SPAEWALRFLLSHPEV-----TTVLSGMSTPEQLDENLkTA 254
|
250 260
....*....|....*....|..
gi 380790393 330 TEEGPL---EPAVVDAFNQAWH 348
Cdd:COG1453 255 DNLEPLteeELAILERLAEELG 276
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-329 |
4.23e-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: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdCRVKIATKANPWDGKSlKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19105 35 LDLGINYFDTAEGYGNGNSEEIIGEALKGLRR--DKVFLATKASPRLDKK-DKAELLKSVEESLKRLQTDYIDIYQLHGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 DHSTP---VEETLRACHQLHQEGKFVELGLS-NYAAWEVAEicTLCKSnGWIvpTVYQGMYNATTRQVE-TELLP-CLRH 217
Cdd:cd19105 112 DTPEErllNEELLEALEKLKKEGKVRFIGFStHDNMAEVLQ--AAIES-GWF--DVIMVAYNFLNQPAElEEALAaAAEK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 218 fGLRFYAYNPLAGGLLTGKYKYEDKDGKqpvgrffgnswaetyrnrfwkehhfqaialvekalqaaygtsvPSMTSAALR 297
Cdd:cd19105 187 -GIGVVAMKTLAGGYLQPALLSVLKAKG-------------------------------------------FSLPQAALK 222
|
250 260 270
....*....|....*....|....*....|..
gi 380790393 298 WMYHHSQLqgahgDTVILGMSSLEQLEQNLTA 329
Cdd:cd19105 223 WVLSNPRV-----DTVVPGMRNFAELEENLAA 249
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
102-329 |
6.12e-15 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 73.55 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKANPWDgksLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHsTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEI 181
Cdd:COG0656 63 VTTKVWNDN---HGYDDTLAAFEESLERLGLDYLDLYLIHWPGP-GPYVETWRALEELYEEGLIRAIGVSNFDPEHLEEL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 182 CTLCKsngwIVPTVYQGMYNATTRQveTELLPCLRHFGLRFYAYNPLA-GGLLtgkykyedkdgKQPVgrffgnswaety 260
Cdd:COG0656 139 LAETG----VKPAVNQVELHPYLQQ--RELLAFCREHGIVVEAYSPLGrGKLL-----------DDPV------------ 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 380790393 261 rnrfwkehhFQAIAlvekalqAAYGTSVPsmtSAALRWmyhHSQlqgaHGDTVILGMSSLEQLEQNLTA 329
Cdd:COG0656 190 ---------LAEIA-------EKHGKTPA---QVVLRW---HLQ----RGVVVIPKSVTPERIRENLDA 232
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
64-331 |
7.61e-15 |
|
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: 73.74 E-value: 7.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKA--------NPWDGKS--LKPDSLRSQLETSLKRLQCP 133
Cdd:cd19092 34 LELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCgirlgddpRPGRIKHydTSKEHILASVEGSLKRLGTD 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 134 RVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAeictLCKSNgWIVPTVyqgmynatTRQVE----- 208
Cdd:cd19092 114 YLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIE----LLQSY-LDQPLV--------TNQIElsllh 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 209 TELLP------CLRHfGLRFYAYNPLAGglltgkykyedkdgkqpvGRFFGNSWAETYRNRfwkehhfqaiALVEKaLQA 282
Cdd:cd19092 181 TEAIDdgtldyCQLL-DITPMAWSPLGG------------------GRLFGGFDERFQRLR----------AALEE-LAE 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 380790393 283 AYGTsvpSMTSAALRW-MYHHSQLQgahgdtVILGMSSLEQLEQNLTATE 331
Cdd:cd19092 231 EYGV---TIEAIALAWlLRHPARIQ------PILGTTNPERIRSAVKALD 271
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
63-333 |
8.64e-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: 73.36 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 63 FLERGHTELDTAFMYSDGQSETILGGLGLGLGGGdcRVKIATKANPWDGKSlkPDSLRSQLETSLKRLQCPRVDLFYLHA 142
Cdd:cd19096 30 AIDAGINYFDTAYGYGGGKSEEILGEALKEGPRE--KFYLATKLPPWSVKS--AEDFRRILEESLKRLGVDYIDFYLLHG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 143 PDHSTpVEETLRACH------QLHQEGKFVELGLSNYAAWEVaeICTLCKSNGWIVPTVYqgmYNAtTRQVETELLPCLR 216
Cdd:cd19096 106 LNSPE-WLEKARKGGllefleKAKKEGLIRHIGFSFHDSPEL--LKEILDSYDFDFVQLQ---YNY-LDQENQAGRPGIE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 217 H---FGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrffgnswaetyrnrfwkehhfqaiALVEKALQAAYGTSVPSMtS 293
Cdd:cd19096 179 YaakKGMGVIIMEPLKGGGLA---------------------------------------NNPPEALAILCGAPLSPA-E 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 380790393 294 AALRWMYHHsqlQGAHgdTVILGMSSLEQLEQNLTATEEG 333
Cdd:cd19096 219 WALRFLLSH---PEVT--TVLSGMSTPEQLDENIAAADEF 253
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
42-332 |
1.16e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 74.12 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGRRMDAPASAAAVRAFLERGHTELDTAFMY-------SDGQSETILGGLGLGLGGGDcRVKIATK-ANPWDG-- 111
Cdd:PRK10625 18 LGTMTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRGSRE-KLIIASKvSGPSRNnd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 112 KSLKPD------SLRSQLETSLKRLQCPRVDLFYLHAPDH--------------STPVE---ETLRACHQLHQEGKFVEL 168
Cdd:PRK10625 97 KGIRPNqaldrkNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdSAPAVsllETLDALAEQQRAGKIRYI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 169 GLSNYAAWEVAEICTLCKSNGWIVPTVYQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYkyedKDGKQPV 248
Cdd:PRK10625 177 GVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKY----LNGAKPA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 249 G-------RFfgnswaetyrNRFWKEHHFQAIAlVEKALQAAYGTSVPSMTSAALRwmyhhsqlQGAHGDTVILGMSSLE 321
Cdd:PRK10625 253 GarntlfsRF----------TRYSGEQTQKAVA-AYVDIAKRHGLDPAQMALAFVR--------RQPFVASTLLGATTME 313
|
330
....*....|....*.
gi 380790393 322 QLE-----QNLTATEE 332
Cdd:PRK10625 314 QLKtniesLHLTLSEE 329
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
63-329 |
1.54e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 73.40 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 63 FLERGHTELDTAFMYsdGQSETIL---GGLGLGLGGGDCRVKIATKANPWDGK-SLKPDSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19101 32 YVDAGLTTFDCADIY--GPAEELIgefRKRLRRERDAADDVQIHTKWVPDPGElTMTRAYVEAAIDRSLKRLGVDRLDLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAPDHSTP-VEETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGwiVPTVY-QGMYNATTRQVETELLP-CL 215
Cdd:cd19101 110 QFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIL----DAG--VPIVSnQVQYSLLDRRPENGMAAlCE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 216 RHfGLRFYAYNPLAGGLLTGKYKyedkdGKQPVGRFFGNSWAETYRNRFWKEH----HFQAIALVEKALQAAYGTSVPSM 291
Cdd:cd19101 184 DH-GIKLLAYGTLAGGLLSEKYL-----GVPEPTGPALETRSLQKYKLMIDEWggwdLFQELLRTLKAIADKHGVSIANV 257
|
250 260 270
....*....|....*....|....*....|....*...
gi 380790393 292 tsaALRWMyhhsqLQGAHGDTVILGMSSLEQLEQNLTA 329
Cdd:cd19101 258 ---AVRWV-----LDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-336 |
2.26e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 72.75 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDcrVKIATKANPwDGKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19103 42 MAAGLNLWDTAAVYGMGASEKILGEFLKRYPRED--YIISTKFTP-QIAGQSADPVADMLEGSLARLGTDYIDIYWIHNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 dhsTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGWIVPTVyQGMYNATTRQVETE--LLPCLRHfGLR 221
Cdd:cd19103 119 ---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSLLYRSSEEAgiLDYCKEN-GIT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 222 FYAYNPLAGGLLTGKYkyedkDGKQPVGRffGNSWAETYrNRFWKEHHfqAIALVEKALQAAYGTSVPSMTSAALRwmyh 301
Cdd:cd19103 194 FFAYMVLEQGALSGKY-----DTKHPLPE--GSGRAETY-NPLLPQLE--ELTAVMAEIGAKHGASIAQVAIAWAI---- 259
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 380790393 302 hsqlqgAHGDTVILGMSSLEQLEQ-------NLTATEEGPLE 336
Cdd:cd19103 260 ------AKGTTPIIGVTKPHHVEDaaraasiTLTDDEIKELE 295
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
42-329 |
1.56e-13 |
|
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: 69.57 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 42 LGTMEMGR---RMDAPASAAAVRAFLERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcrVKIATKA-----NPWDGKS 113
Cdd:cd19095 5 LGTSGIGRvwgVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGLRRDD--LFIATKVgthgeGGRDRKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 114 LKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAawevAEICTLCKSNgwiVP 193
Cdd:cd19095 81 FSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG----EELEAAIASG---VF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 194 TVYQGMYNATTRQVEtELLPCLRHFGLRFYAYNPLAGGLLtgkykyedkdgkqpvgrffgnswaetyrnrFWKEHHFQAI 273
Cdd:cd19095 154 DVVQLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRL------------------------------RRRVRRRPLY 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 380790393 274 ALVEKALQAAYGTSVPSMTSAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTA 329
Cdd:cd19095 203 ADYARRPEFAAEIGGATWAQAALRFVLSHPGV-----SSAIVGTTNPEHLEENLAA 253
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-335 |
1.25e-12 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 67.17 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGggdcRVKIATK--ANPWDGKSLKpDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19097 36 LKAGINTLDTAPAY--GDSEKVLGKFLKRLD----KFKIITKlpPLKEDKKEDE-AAIEASVEASLKRLKVDSLDGLLLH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 APD----HSTPVEETLRachQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwivPTVYQGMYNA-TTRQVETELLPCLR 216
Cdd:cd19097 109 NPDdllkHGGKLVEALL---ELKKEGLIRKIGVSVYSPEELEKALESFK------IDIIQLPFNIlDQRFLKSGLLAKLK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 217 HFGLRFYAYNPLAGGLLTgkykyedKDGKQPVGRFfgnswaetyrnRFWKEHH--FQAIAlvekalqAAYGTSVPSMtsa 294
Cdd:cd19097 180 KKGIEIHARSVFLQGLLL-------MEPDKLPAKF-----------APAKPLLkkLHELA-------KKLGLSPLEL--- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 380790393 295 ALRWMYHHSqlqgaHGDTVILGMSSLEQLEQNLTATEEGPL 335
Cdd:cd19097 232 ALGFVLSLP-----EIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
102-231 |
1.74e-12 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 66.35 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKANPWDgksLKPDSLRSQLETSLKRLQCPRVDLFYLHAP------DHSTPVEETLRACHQLHQEGKFVELGLSNYAA 175
Cdd:cd19071 59 ITTKLWPTD---HGYERVREALEESLKDLGLDYLDLYLIHWPvpgkegGSKEARLETWRALEELVDEGLVRSIGVSNFNV 135
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 380790393 176 WEVAEICTLCKsngwIVPTVYQGMYNATTRQVET-ELlpCLRHfGLRFYAYNPLAGG 231
Cdd:cd19071 136 EHLEELLAAAR----IKPAVNQIELHPYLQQKELvEF--CKEH-GIVVQAYSPLGRG 185
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
109-329 |
8.20e-12 |
|
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: 65.34 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 109 WDGKSLKPDS----LRSQLETSLKRLQCP-RVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSnyaawEV-AEic 182
Cdd:cd19077 82 LDPDTLRPDGspeaVRKSIENILRALGGTkKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLS-----EVsAE-- 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 183 TLCKSNGwIVP-TVYQGMYNATTRQVET-ELLPCLRHFGLRFYAYNPLAGGLLTGKYKyedKDGKQPVGRFFGNSwaety 260
Cdd:cd19077 155 TIRRAHA-VHPiAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIK---SLADIPEGDFRRHL----- 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380790393 261 rNRFWKEHHFQAIALVE--KALQAAYGtsvPSMTSAALRWMYHHSqlqgahGDTV--ILGMSSLEQLEQNLTA 329
Cdd:cd19077 226 -DRFNGENFEKNLKLVDalQELAEKKG---CTPAQLALAWILAQS------GPKIipIPGSTTLERVEENLKA 288
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
102-329 |
8.74e-12 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 65.18 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKANpWDGKS----LKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWE 177
Cdd:cd19142 79 VSTKIY-WSYGSeergLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 178 VAEICTLCKSNGWIVPTVYQGMYNATTRQ-VETELLPCLRHFGLRFYAYNPLAGGLLTGK--------YKYEDKDGKQPV 248
Cdd:cd19142 158 IMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVGLITWSPLSLGLDPGIseetrrlvTKLSFKSSKYKV 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 249 GRFFGNSWAETYRNrfwKEHHFQAIALVEKalqaaYGTsvpSMTSAALRWmyhhsQLQGAHGDTVILGMSSLEQLEQNLT 328
Cdd:cd19142 238 GSDGNGIHEETRRA---SHKLRELSLIAER-----LGC---DLTQLLIAW-----SLKNENVQCVLIGASSLEQLYSQLN 301
|
.
gi 380790393 329 A 329
Cdd:cd19142 302 S 302
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
64-186 |
7.88e-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: 62.13 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDCR---VKIATKANPWDgksLKPDSLRSQLETSLKRLQCPRVDLFYL 140
Cdd:cd19111 27 LFVGYRHIDTALSY--QNEKAIGEALKWWLKNGKLKreeVFITTKLPPVY---LEFKDTEKSLEKSLENLKLPYVDLYLI 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 380790393 141 HAP-------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK 186
Cdd:cd19111 102 HHPcgfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK 160
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-327 |
1.57e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 61.57 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSE-----TILGGLGLGLGGGDcRVKIATKA-----------NPW------------------ 109
Cdd:cd19099 31 LDSGINVIDTAINYRGGRSErligkALRELIEKGGIKRD-EVVIVTKAgyipgdgdeplRPLkyleeklgrglidvadsa 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 110 -DGKSLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPV----------EETLRACHQLHQEGK-------------- 164
Cdd:cd19099 110 gLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLElgeeefydrlEEAFEALEEAVAEGKiryygistwdgfra 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 165 ------FVELGLSNYAAWEVAE----------ICTLCKSNGWIVPTVYQGMYnattrqveTELLPCLRHFGLRFYAYNPL 228
Cdd:cd19099 190 ppalpgHLSLEKLVAAAEEVGGdnhhfkviqlPLNLLEPEALTEKNTVKGEA--------LSLLEAAKELGLGVIASRPL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 229 AGGLLTGKykyedkdgkqpvgrffgnswaetyRNRFWKEHHFQAIALVEKALQAAYGTSVPsmtsaalrwmyhhsqlqga 308
Cdd:cd19099 262 NQGQLLGE------------------------LRLADLLALPGGATLAQRALQFARSTPGV------------------- 298
|
330
....*....|....*....
gi 380790393 309 hgDTVILGMSSLEQLEQNL 327
Cdd:cd19099 299 --DSALVGMRRPEHVDENL 315
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
120-234 |
1.63e-09 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 58.03 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 120 RSQLETSLKRLQCPRVDLFYLHAP-----DHSTPVE-----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsng 189
Cdd:cd19136 79 RAACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYCE--- 155
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 380790393 190 wIVPTVYQGMYNAttRQVETELLPCLRHFGLRFYAYNPLAGGLLT 234
Cdd:cd19136 156 -VPPAVNQVEFHP--HLVQKELLKFCKDHGIHLQAYSSLGSGDLR 197
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
114-327 |
2.70e-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: 57.27 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 114 LKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRACHQLHQEGKFVELGLSNY------AAWEVAEICTLCKs 187
Cdd:cd19140 75 YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFtvallrEAVELSEAPLFTN- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 188 ngwivptvyQGMYNATTRQveTELLPCLRHFGLRFYAYNPLAgglltgkykyedkdgkqpvgrffgnswaetyRNRFWKE 267
Cdd:cd19140 154 ---------QVEYHPYLDQ--RKLLDAAREHGIALTAYSPLA-------------------------------RGEVLKD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380790393 268 HHFQAIAlvekalqAAYGtsvpsMTSA--ALRWMyhhsqLQGAhGDTVILGMSSLEQLEQNL 327
Cdd:cd19140 192 PVLQEIG-------RKHG-----KTPAqvALRWL-----LQQE-GVAAIPKATNPERLEENL 235
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
64-336 |
7.63e-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: 56.02 E-value: 7.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGggdcRVK--IATKA-----NPWDGKSLKPDSLRSQLETSLKRLQCPRVD 136
Cdd:cd19163 43 LDSGINYIDTAPWYGQGRSETVLGKALKGIP----RDSyyLATKVgryglDPDKMFDFSAERITKSVEESLKRLGLDYID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 137 LFYLH----APDHSTPVEETLRACHQLHQEGKFVELGLSNY--AAW-EVAE--------ICTLCKSNgwivptvyqgMYN 201
Cdd:cd19163 119 IIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGITGYplDVLkEVLErspvkidtVLSYCHYT----------LND 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 202 ATTrqveTELLPCLRHFGLRFYAYNPLAGGLLTgkykyedKDGKQPvgrffgnswaetyrnrfWKEHHFQAIALVEKAlq 281
Cdd:cd19163 189 TSL----LELLPFFKEKGVGVINASPLSMGLLT-------ERGPPD-----------------WHPASPEIKEACAKA-- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 380790393 282 AAYGTSVPSMTSA-ALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATEEGPLE 336
Cdd:cd19163 239 AAYCKSRGVDISKlALQFALSNPDI-----ATTLVGTASPENLRKNLEAAEEPLDA 289
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-327 |
1.05e-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: 55.18 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSET-----ILgglglglgggDCR--VKIATKANPWDgkslkPDSLRSQLETSLKRLQCPRVD 136
Cdd:cd19100 37 LDLGINYFDTAPSY--GDSEEkigkaLK----------GRRdkVFLATKTGARD-----YEGAKRDLERSLKRLGTDYID 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 137 LFYLHAPDHSTPVEET------LRACHQLHQEGKFVELGLS---NYAAWEVAEictlcksNGWI----VPTVYQGMYNat 203
Cdd:cd19100 100 LYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISghsPEVLLRALE-------TGEFdvvlFPINPAGDHI-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 204 tRQVETELLP-CLRHfGLRFYAYNPLAGGLLTgkykyedkdgkqpvgrffgNSWAETYRnrfwkehhfqaialvekalqa 282
Cdd:cd19100 171 -DSFREELLPlAREK-GVGVIAMKVLAGGRLL-------------------SGDPLDPE--------------------- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 380790393 283 aygtsvpsmtsAALRWMyhhsqLQGAHGDTVILGMSSLEQLEQNL 327
Cdd:cd19100 209 -----------QALRYA-----LSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
120-231 |
1.15e-08 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 55.27 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 120 RSQLETSLKRLQCPRVDLFYLHAPDHStpVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVyqgm 199
Cdd:cd19133 83 KKAFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE----VKPAV---- 152
|
90 100 110
....*....|....*....|....*....|....*....
gi 380790393 200 ynattRQVET-------ELLPCLRHFGLRFYAYNPLAGG 231
Cdd:cd19133 153 -----NQIEThpfnqqiEAVEFLKKYGVQIEAWGPFAEG 186
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
64-229 |
1.18e-08 |
|
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: 55.32 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDgQSETILGGLGLGLGGGDcrVKIATKANPwdgkslKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19120 35 LKAGFRHIDTAEMYGN-EKEVGEALKESGVPRED--LFITTKVSP------GIKDPREALRKSLAKLGVDYVDLYLIHSP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 ----DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVYQGMYNATTRQVETELLPCLRHFG 219
Cdd:cd19120 106 ffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPYLYPQQPALLEYCREHG 181
|
170
....*....|
gi 380790393 220 LRFYAYNPLA 229
Cdd:cd19120 182 IVVSAYSPLS 191
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
64-347 |
1.51e-08 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 55.35 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGgdcRVKIATKA--NPWDGKSLKpDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19104 42 LDLGINFFDTAPSYGDGKSEENLGRALKGLPA---GPYITTKVrlDPDDLGDIG-GQIERSVEKSLKRLKRDSVDLLQLH 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 ---------------APDHSTPVEETLRACHQLHQEGKFVELGLSnyaAWEVAE-ICTLCKSNGW---------IVPTVY 196
Cdd:cd19104 118 nrigderdkpvggtlSTTDVLGLGGVADAFERLRSEGKIRFIGIT---GLGNPPaIRELLDSGKFdavqvyynlLNPSAA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 197 QGMYNATTRQVETELLP-CLRHfGLRFYAYNPLAGGLLTGKykyEDKDGKQPVgrffgnswaeTYRNRFWKEHHfQAial 275
Cdd:cd19104 195 EARPRGWSAQDYGGIIDaAAEH-GVGVMGIRVLAAGALTTS---LDRGREAPP----------TSDSDVAIDFR-RA--- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380790393 276 veKALQAAYGTSVPSMTSAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNLTATEEGPLEPAVVDAFNQAW 347
Cdd:cd19104 257 --AAFRALAREWGETLAQLAHRFALSNPGV-----STVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
117-233 |
5.76e-08 |
|
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: 53.10 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPV-------EETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsng 189
Cdd:cd19135 83 ESTKQAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS--- 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 380790393 190 wIVPTVYQGMYNATTRQVetELLPCLRHFGLRFYAYNPLAGGLL 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 |
1.85e-07 |
|
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: 51.98 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDH--STPVEETLRACHQLHQEGKFVELGL---SNYAAWEVAEIctlcksNGWI 191
Cdd:cd19162 93 DGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVgvtDWAALLRAARR------ADVD 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 192 VPTVyQGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGkykyedkdGKQPVGRFFGNSWAETYRNRfwkehhFQ 271
Cdd:cd19162 167 VVMV-AGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILAT--------DDPAGDRYDYRPATPEVLAR------AR 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 380790393 272 AIAlvekALQAAYGTSVPsmtSAALRWMYHHSQLQgahgdTVILGMSSLEQLEQNLTA 329
Cdd:cd19162 232 RLA----AVCRRYGVPLP---AAALQFPLRHPAVA-----SVVVGAASPAELRDNLAL 277
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
117-247 |
3.13e-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: 50.83 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPdhsTPVE----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIV 192
Cdd:cd19131 80 DSTLRAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETG----VV 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 380790393 193 PTVYQGMYNATTRQVETELLpCLRHfGLRFYAYNPLA-GGLLTGKY--KYEDKDGKQP 247
Cdd:cd19131 153 PVVNQIELHPRFQQRELRAF-HAKH-GIQTESWSPLGqGGLLSDPVigEIAEKHGKTP 208
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
113-173 |
5.84e-07 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 50.04 E-value: 5.84e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 380790393 113 SLKPDSLRSQLETSLKRLQCPRVDLFYLH--APDHSTPVEETLRACHQLHQEGKFVELGLSNY 173
Cdd:cd19139 67 NLSKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNF 129
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
109-228 |
1.78e-06 |
|
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: 48.92 E-value: 1.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 109 WDGKSlKPDSLRSQLETSLKRLQCPRVDLFYLHAP------DH-------------STPVEETLRACHQLHQEGKFVELG 169
Cdd:cd19106 75 WNTKH-HPEDVEPALRKTLKDLQLDYLDLYLIHWPyafergDNpfpknpdgtirydSTHYKETWKAMEKLVDKGLVKAIG 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 380790393 170 LSNYAAWEVAEICtlckSNGWIVPTVYqgmynattrQVE-------TELLPCLRHFGLRFYAYNPL 228
Cdd:cd19106 154 LSNFNSRQIDDIL----SVARIKPAVL---------QVEchpylaqNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
117-231 |
2.87e-06 |
|
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: 48.16 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDhSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVY 196
Cdd:cd19157 81 DSTLKAFEASLERLGLDYLDLYLIHWPV-KGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVN 155
|
90 100 110
....*....|....*....|....*....|....*
gi 380790393 197 QGMYNAttRQVETELLPCLRHFGLRFYAYNPLAGG 231
Cdd:cd19157 156 QVEFHP--RLTQKELRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
116-228 |
4.17e-06 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 47.73 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 116 PDSLRSQLETSLKRLQCPRVDLFYLHAPDH--------------STPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEI 181
Cdd:cd19125 84 PEDVPPALEKTLKDLQLDYLDLYLIHWPVRlkkgahmpepeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDL 163
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 380790393 182 CTLCKsngwIVPTVYQGMYNATTRQveTELLPCLRHFGLRFYAYNPL 228
Cdd:cd19125 164 LAVAR----VPPAVNQVECHPGWQQ--DKLHEFCKSKGIHLSAYSPL 204
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
64-186 |
1.22e-05 |
|
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: 46.25 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdgQSETILGGLGLGLGGGDcRVK-----IATKANPwdgKSLKPDSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19154 35 LKAGYRLIDTAFLY---QNEEAIGEALAELLEEG-VVKredlfITTKLWT---HEHAPEDVEEALRESLKKLQLEYVDLY 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 380790393 139 YLHAP-----------------DHSTPV--EETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCK 186
Cdd:cd19154 108 LIHAPaafkddegesgtmengmSIHDAVdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR 174
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
115-230 |
1.38e-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: 45.98 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 115 KPDSLRSQLETSLKRLQCPRVDLFYLHAP-------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAA 175
Cdd:cd19128 73 QPENVKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYST 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 380790393 176 WEVAEICTLCKsngwIVPTVYQ---GMYNATTRQVETellpCLRHfGLRFYAYNPLAG 230
Cdd:cd19128 153 KLLTDLLNYCK----IKPFMNQiecHPYFQNDKLIKF----CIEN-NIHVTAYRPLGG 201
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
117-233 |
3.89e-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: 44.74 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLH--APDHstpVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPT 194
Cdd:cd19126 80 RRTEDAFQESLDRLGLDYVDLYLIHwpGKDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPA 152
|
90 100 110
....*....|....*....|....*....|....*....
gi 380790393 195 VYQGMYNAttRQVETELLPCLRHFGLRFYAYNPLAGGLL 233
Cdd:cd19126 153 VNQVEFHP--YLTQKELRGYCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
64-332 |
4.14e-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: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDGQSETILGGLGLGLGGGDCRVKIATKANPW--DGKSLKPDSLRSQLETSLKRLQCPRVDLFYLH 141
Cdd:cd19153 43 FAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYrdSEFDYSAERVRASVATSLERLHTTYLDVVYLH 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 A---PDHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKSNGwivPTVYQGMYNATTRQVE-TELLPCLRH 217
Cdd:cd19153 123 DiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS---LDAVLSYCHLTLQDARlESDAPGLVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 218 -FGLRFYAYNPLAGGLLTGKykyedkdGKQPvgrffgnswaetyrnrfWK--EHHFQAIALVEKALQAAYGTSVPSMtsa 294
Cdd:cd19153 200 gAGPHVINASPLSMGLLTSQ-------GPPP-----------------WHpaSGELRHYAAAADAVCASVEASLPDL--- 252
|
250 260 270
....*....|....*....|....*....|....*...
gi 380790393 295 ALRWMYHHSQLQGahgdTVILGMSSLEQLEQNLTATEE 332
Cdd:cd19153 253 ALQYSLAAHAGVG----TVLLGPSSLAQLRSMLAAVDA 286
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
117-233 |
8.79e-05 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 43.66 E-value: 8.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVeETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVY 196
Cdd:cd19156 80 ESTLAAFEESLEKLGLDYVDLYLIHWPVKGKFK-DTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVN 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 380790393 197 QgmynattrqveTELLPCLRHFGLRFY---------AYNPLAGGLL 233
Cdd:cd19156 155 Q-----------IELHPLLTQEPLRKFckekniaveAWSPLGQGKL 189
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
102-232 |
1.49e-04 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 43.21 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 102 IATKAnpWDGKSlKPDSLRSQLETSLKRLQCPRVDLFYLHAP--------------------DHSTPVEETLRACHQLHQ 161
Cdd:cd19129 68 VTTKL--WNTNH-RPERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVD 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 380790393 162 EGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVYQgmYNATTRQVETELLPCLRHFGLRFYAYNPLAGGL 232
Cdd:cd19129 145 EGRCKAIGLSDVSLEKLREIFEAAR----IKPAVVQ--VESHPYLPEWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
117-327 |
2.18e-04 |
|
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: 42.60 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 117 DSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETL-----------RACHQLHQEGKFVELGL-SNyaAWEVAE-ICT 183
Cdd:cd19152 103 DGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDehfaqaikgafRALEELREEGVIKAIGLgVN--DWEVILrILE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 184 LCKSNGWIVPtvyqGMYNATTRQVETELLPCLRHFGLRFYAYNPLAGGLLTGKYKYEDKDGKQPvgrffgNSWAETYRNR 263
Cdd:cd19152 181 EADLDWVMLA----GRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAGGDNFDYYEYGPA------PPELIARRDR 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 380790393 264 FWkehhfqaialvekALQAAYGTSVPSmtsAALRWMYHHSQLqgahgDTVILGMSSLEQLEQNL 327
Cdd:cd19152 251 IE-------------ALCEQHGVSLAA---AALQFALAPPAV-----ASVAPGASSPERVEENV 293
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
115-231 |
4.70e-04 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 41.63 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 115 KPDSLRSQLETSLKRLQCPRVDLFYLHAP---------DHST---------PVEETLRACHQLHQEGKFVELGLSNYAAW 176
Cdd:cd19123 84 APEDVLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfPESGedllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVK 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380790393 177 EVAEICTLCKsngwIVPTVyqgmynattRQVE-------TELLPCLRHFGLRFYAYNPLAGG 231
Cdd:cd19123 164 KLEDLLATAR----IKPAV---------NQVElhpylqqPELLAFCRDNGIHLTAYSPLGSG 212
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
114-173 |
9.00e-04 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 40.39 E-value: 9.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 380790393 114 LKPDSLRSQLETSLKRLQCPRVDLFYLH--APDHSTPVEETLRACHQLHQEGKFVELGLSNY 173
Cdd:PRK11172 70 LAKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNF 131
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
64-228 |
9.80e-04 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 40.59 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGdcRVK-----IATKANPwdgKSLKPDSLRSQLETSLKRLQCPRVDLF 138
Cdd:cd19155 35 LEAGYRHIDTAYVY--RNEAAIGNVLKKWIDSG--KVKreelfIVTKLPP---GGNRREKVEKFLLKSLEKLQLDYVDLY 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 139 YLHAP---------------------DHSTPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVYQ 197
Cdd:cd19155 108 LIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR----IKPANLQ 183
|
170 180 190
....*....|....*....|....*....|.
gi 380790393 198 GMYNATTRQveTELLPCLRHFGLRFYAYNPL 228
Cdd:cd19155 184 VELHVYLQQ--KDLVDFCSTHSITVTAYAPL 212
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
64-233 |
3.19e-03 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 38.68 E-value: 3.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSDgqsETILGGLGLGLGGGDCRVKIATK-ANPWDGKSLKPDSLRSqletSLKRLQCPRVDLFYLH- 141
Cdd:cd19134 34 LEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKlATPDQGFTASQAACRA----SLERLGLDYVDLYLIHw 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 142 -APDHSTPVeETLRACHQLHQEGKFVELGLSNYAAWEVAEICtlckSNGWIVPTVYQgmynattrqveTELLPCLRHFGL 220
Cdd:cd19134 107 pAGREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLI----DLTFFTPAVNQ-----------IELHPLLNQAEL 170
|
170 180
....*....|....*....|..
gi 380790393 221 RFY---------AYNPLAGGLL 233
Cdd:cd19134 171 RKVnaqhgivtqAYSPLGVGRL 192
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
116-230 |
4.32e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 38.41 E-value: 4.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 116 PDSLRSQLETSLKRLQCPRVDL------FYLHAPDHStPVEETLRACHQLHQEGKFVELGLSNYAAWEVAEICTlcksng 189
Cdd:PRK10376 105 PAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARK------ 177
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 380790393 190 wIVPTV-YQGMYNATTRQvETELLPCLRHFGLRFYAYNPLAG 230
Cdd:PRK10376 178 -IAEIVcVQNHYNLAHRA-DDALIDALARDGIAYVPFFPLGG 217
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
113-189 |
5.37e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 38.37 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 113 SLKPDSLRSQLETSLKRLQCPRVDLFYLHAPDHSTPVEETLRAchqlHQEGKF----VELglsnYAAWEVAEICT---LC 185
Cdd:cd19108 84 FHRPELVRPALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPK----DENGKLifdtVDL----CATWEAMEKCKdagLA 155
|
....
gi 380790393 186 KSNG 189
Cdd:cd19108 156 KSIG 159
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
64-197 |
7.72e-03 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 37.65 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYSD----GQ--SETILGGLglglgggdcrVK-----IATKAnpwDGKSLKPDSLRSQLETSLKRLQC 132
Cdd:cd19116 35 IEAGYRHIDTAYLYGNeaevGEaiREKIAEGV----------VKredlfITTKL---WNSYHEREQVEPALRESLKRLGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 133 PRVDLFYLHAP------------DHSTPVE----ETLRACHQLHQEGKFVELGLSNYAAWEVAEICTLCKsngwIVPTVY 196
Cdd:cd19116 102 DYVDLYLIHWPvafkenndsesnGDGSLSDidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN----IKPAVN 177
|
.
gi 380790393 197 Q 197
Cdd:cd19116 178 Q 178
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
64-327 |
9.45e-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: 37.20 E-value: 9.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 64 LERGHTELDTAFMYsdGQSETILGGLGLGLGGGDcRVKIATKAnpWDGKSlKPDSLRSQLETSLKRLQCPRVDLFYLHAP 143
Cdd:cd19130 33 LEVGYRHIDTAAIY--GNEEGVGAAIAASGIPRD-ELFVTTKL--WNDRH-DGDEPAAAFAESLAKLGLDQVDLYLVHWP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 144 dhsTPVE----ETLRACHQLHQEGKFVELGLSNYaawEVAEICTLCKSNGwIVPTVYQ-----GMYNATTRQVETellpc 214
Cdd:cd19130 107 ---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNF---LPPHLERIVAATG-VVPAVNQielhpAYQQRTIRDWAQ----- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380790393 215 lRHfGLRFYAYNPLAGGLLTgkykyedkdGKQPVGRffgnswaetyrnrfwkehhfqaialvekaLQAAYGTSVpsmTSA 294
Cdd:cd19130 175 -AH-DVKIEAWSPLGQGKLL---------GDPPVGA-----------------------------IAAAHGKTP---AQI 211
|
250 260 270
....*....|....*....|....*....|...
gi 380790393 295 ALRWmyhHSQlqgaHGDTVILGMSSLEQLEQNL 327
Cdd:cd19130 212 VLRW---HLQ----KGHVVFPKSVRRERMEDNL 237
|
|
| |
