|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
10-318 |
1.92e-160 |
|
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: 450.85 E-value: 1.92e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPdeseGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQARWKERGLTLATKWYPHTPGAH 89
Cdd:cd19075 1 PKIILGTMTFGS----QGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERGFKIDTKANPGVGGGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 90 KADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPT 169
Cdd:cd19075 77 SPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 170 IYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKD-IPAEGRYSNQSSHGTLYRGRYFKDATFDALRL 248
Cdd:cd19075 157 VYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEdKAGGGRFDPNNALGKLYRDRYWKPSYFEALEK 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 249 IEPVAERHGLTMPEIAFRWIHHHSALNMKDNgrDGVIIGVSSLAQLENNLKDIQKGPLPQEVVDVLDQAW 318
Cdd:cd19075 237 VEEAAEKEGISLAEAALRWLYHHSALDGEKG--DGVILGASSLEQLEENLAALEKGPLPEEVVKAIDEAW 304
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
10-318 |
9.46e-75 |
|
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: 233.53 E-value: 9.46e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFG-----PDESEGARItslddFNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKW- 81
Cdd:COG0667 14 SRLGLGTMTFGgpwggVDEAEAIAI-----LDAALDA----GINFFDTADVYGPGRSEELLGEAlkGRPRDDVVIATKVg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 82 YPHTPGAHKADV----LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV 157
Cdd:COG0667 85 RRMGPGPNGRGLsrehIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ILCneRGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGrysnqSSHGTLYRGRY 237
Cdd:COG0667 165 AIA--EGLPPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEG-----DRAATNFVQGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 238 FKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNLKDIQkGPLPQEVVDVLDQA 317
Cdd:COG0667 238 LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGV-------TSVIPGARSPEQLEENLAAAD-LELSAEDLAALDAA 309
|
.
gi 1832818259 318 W 318
Cdd:COG0667 310 L 310
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
11-318 |
1.96e-62 |
|
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: 201.65 E-value: 1.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 11 RVILGLMTFGP--DESEGARItslddFNKCLDhlqqQGYNEVDTARVYVGGKQEAFTAQARWKERG-LTLATKWY----- 82
Cdd:cd19087 15 RLCLGTMNFGGrtDEETSFAI-----MDRALD----AGINFFDTADVYGGGRSEEIIGRWIAGRRDdIVLATKVFgpmgd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 -PHTPGAHKADVLREnLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCN 161
Cdd:cd19087 86 dPNDRGLSRRHIRRA-VEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 162 ERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQsshgTLYRGRYFKDA 241
Cdd:cd19087 165 RRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVER----ARYQARYGLEE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1832818259 242 TFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLK--DIqkgPLPQEVVDVLDQAW 318
Cdd:cd19087 241 YRDIAERFEALAAEAGLTPASLALAWVLSHPAVT-------SPIIGPRTLEQLEDSLAalEI---TLTPELLAEIDELF 309
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
9-315 |
2.67e-62 |
|
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: 201.29 E-value: 2.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 9 TPRVILGLMTFG--PDESEGARItslddfnkcLDHLQQQGYNEVDTARVY-------VGGKQEAFTAqaRW-KERG---- 74
Cdd:cd19081 9 VSPLCLGTMVFGwtADEETSFAL---------LDAFVDAGGNFIDTADVYsawvpgnAGGESETIIG--RWlKSRGkrdr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 75 LTLATKWYPHTPGAHK---ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAF 151
Cdd:cd19081 78 VVIATKVGFPMGPNGPglsRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 152 EVAEIVILCNERGWVRPTIYQAMYNAITR-NIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSshg 230
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSLQPEYNLVDReSFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGEA--- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 231 tlyRGRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNLKDIQkGPLPQEV 310
Cdd:cd19081 235 ---AKRYLNERGLRILDALDEVAAEHGATPAQVALAWLLARPGV-------TAPIAGARTVEQLEDLLAAAG-LRLTDEE 303
|
....*
gi 1832818259 311 VDVLD 315
Cdd:cd19081 304 VARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
12-318 |
3.81e-62 |
|
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: 200.23 E-value: 3.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 12 VILGLMTFGPDESEGARITSLDDFNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQA---RWKER-GLTLATKWYP---H 84
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEA----GINFIDTAEVYGDGKSEELLGEAlkdYPVKRdKVVIATKVPDgdgP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 85 TPGAHKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTafevAEIVILCNERG 164
Cdd:pfam00248 77 WPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFD----AEQIEKALTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 165 WVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHGTlyrgryfkDATFD 244
Cdd:pfam00248 153 KIPIVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGT--------PLNLE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 245 ALRLIEPVAERHGLTMPEIAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKdIQKGPLPQEVVDVLDQAW 318
Cdd:pfam00248 225 ALEALEEIAKEHGVSPAQVALRWA-------LSKPGVTIPIPGASNPEQLEDNLG-ALEFPLSDEEVARIDELL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
10-317 |
3.82e-58 |
|
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: 189.72 E-value: 3.82e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGA--RITSLDDFNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQARWKER-GLTLATKWYPHTP 86
Cdd:cd19085 2 SRLGLGCWQFGGGYWWGDqdDEESIATIHAALDA----GINFFDTAEAYGDGHSEEVLGKALKGRRdDVVIATKVSPDNL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 87 gahKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCnergwv 166
Cdd:cd19085 78 ---TPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 167 RPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRysNQSSHGTLYRGRYFKdATFDAL 246
Cdd:cd19085 149 RIDSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGD--ARTRLFRHFEPGAEE-ETFEAL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 247 RLIEPVAERHGLTMPEIAFRWIHHHsalnmkdNGRDGVIIGVSSLAQLENNLKDIQKgPLPQEVVDVLDQA 317
Cdd:cd19085 226 EKLKEIADELGVTMAQLALAWVLQQ-------PGVTSVIVGARNPEQLEENAAAVDL-ELSPSVLERLDEI 288
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
10-317 |
1.25e-55 |
|
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: 184.35 E-value: 1.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDD------FNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQA-RWKERGLTLATKWY 82
Cdd:cd19091 14 SELALGTMTFGGGGGFFGAWGGVDQeeadrlVDIALDA----GINFFDTADVYSEGESEEILGKAlKGRRDDVLIATKVR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 ------PHTPGAHKADVLREnLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEI 156
Cdd:cd19091 90 grmgegPNDVGLSRHHIIRA-VEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 157 VILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYktkdipaegRYSNQSSHGTLYRGR 236
Cdd:cd19091 169 LGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKY---------RRGQPAPEGSRLRRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 237 YFKDATFDALRL------IEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLK--DIQkgpLPQ 308
Cdd:cd19091 240 GFDFPPVDRERGydvvdaLREIAKETGATPAQVALAWLLSRPTVS-------SVIIGARNEEQLEDNLGaaGLS---LTP 309
|
....*....
gi 1832818259 309 EVVDVLDQA 317
Cdd:cd19091 310 EEIARLDKV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
17-299 |
1.49e-54 |
|
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: 180.87 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 17 MTFGP--DESEGARITslddfNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKWYPHTpGAHKAD 92
Cdd:cd19074 13 LTFGGqvDDEDAKACV-----RKAYDL----GINFFDTADVYAAGQAEEVLGKAlkGWPRESYVISTKVFWPT-GPGPND 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 93 V------LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWV 166
Cdd:cd19074 83 RglsrkhIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 167 RPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHGTLYRgRYFKDATFDAL 246
Cdd:cd19074 163 PPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRATDEDNRDKKR-RLLTDENLEKV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1832818259 247 RLIEPVAERHGLTMPEIAFRWIHHHSAlnmkdngRDGVIIGVSSLAQLENNLK 299
Cdd:cd19074 242 KKLKPIADELGLTLAQLALAWCLRNPA-------VSSAIIGASRPEQLEENVK 287
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
10-299 |
8.97e-52 |
|
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: 171.55 E-value: 8.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDDFnkcLDHlqqqGYNEVDTARVYVGGKQEAFTAQArWKERG----LTLATK----- 80
Cdd:cd06660 1 SRLGLGTMTFGGDGDEEEAFALLDAA---LEA----GGNFFDTADVYGDGRSERLLGRW-LKGRGnrddVVIATKgghpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 81 -WYPHTPGAHKADvLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVIL 159
Cdd:cd06660 73 gGDPSRSRLSPEH-IRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 160 CNERGWVRPTIYQAMYNAITRN-IETELIPACKRYGIDIVVYNPLAGGLfsgkyktkdipaegrysnqsshgtlyrgryf 238
Cdd:cd06660 152 AKAHGLPGFAAVQPQYSLLDRSpMEEELLDWAEENGLPLLAYSPLARGP------------------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 239 kdatfdalrliepvaerhgltmPEIAFRWIHHHSalnmkdnGRDGVIIGVSSLAQLENNLK 299
Cdd:cd06660 201 ----------------------AQLALAWLLSQP-------FVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
11-298 |
1.00e-51 |
|
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: 173.92 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 11 RVILGLMTFGpDESEGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQArWKERG----LTLATKWY---- 82
Cdd:cd19079 14 RLCLGCMSFG-DPKWRPWVLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRA-LKEFAprdeVVIATKVYfpmg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 --PHTPGAHKADVLREnLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILC 160
Cdd:cd19079 92 dgPNGRGLSRKHIMAE-VDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 161 NERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHgtlyrGRYFKD 240
Cdd:cd19079 171 EKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAKLK-----YDYFTE 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 241 ATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNL 298
Cdd:cd19079 246 ADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGV-------TAPIVGATKLEHLEDAV 296
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
11-315 |
9.41e-51 |
|
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: 171.25 E-value: 9.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 11 RVILGLMTFGPDESEGAritSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEA----FTAQARwkERgLTLATKWyphTP 86
Cdd:cd19080 12 PLALGTMTFGTEWGWGA---DREEARAMFDAYVEAGGNFIDTANNYTNGTSERllgeFIAGNR--DR-IVLATKY---TM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 87 GAHKADV---------LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV 157
Cdd:cd19080 83 NRRPGDPnaggnhrknLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARAN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKY-KTKDIPAEGRYSNQSSHGTlyrgr 236
Cdd:cd19080 163 TLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYqRGEEGRAGEAKGVTVGFGK----- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 237 yFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNMkdngrdgVIIGVSSLAQLENNLK--DIqkgPLPQEVVDVL 314
Cdd:cd19080 238 -LTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVI-------PIIGARTLEQLKDNLGalDL---TLSPEQLARL 306
|
.
gi 1832818259 315 D 315
Cdd:cd19080 307 D 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
45-315 |
1.04e-50 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 170.78 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 45 QGYNEVDTARVYVGGKQEAFTAQARWKERG-LTLATK----WYPHTPGAH--KADVLRENLERSLKELQTDQVDIFYLHA 117
Cdd:cd19084 37 LGINFFDTAPVYGFGHSEEILGKALKGRRDdVVIATKcglrWDGGKGVTKdlSPESIRKEVEQSLRRLQTDYIDLYQIHW 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 118 ADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwvrPTIYQAMYNAITRNIETELIPACKRYGIDI 197
Cdd:cd19084 117 PDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKYGP------IVSLQPPYSMLEREIEEELLPYCRENGIGV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 198 VVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHgtlYRGRYFKdATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNMk 277
Cdd:cd19084 191 LPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPF---FRGENFE-KNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTS- 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1832818259 278 dngrdgVIIGVSSLAQLENNLK--DIQkgpLPQEVVDVLD 315
Cdd:cd19084 266 ------AIVGAKNPEQLEENAGalDWE---LTEEELKEID 296
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
11-315 |
1.48e-49 |
|
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: 168.51 E-value: 1.48e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 11 RVILGLMTFGP--DESEGARItslddfnkcLDHLQQQGYNEVDTARVY-------VGGKQEAFTAqaRW-KERG----LT 76
Cdd:cd19094 3 EICLGTMTWGEqnTEAEAHEQ---------LDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIG--SWlKKKGnrdkVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 77 LATK---------WYPHTPGAHKADVLRENLERSLKELQTDQVDIFYLHAADR------------------SVPFAETLE 129
Cdd:cd19094 72 LATKvagpgegitWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRytplfgggyytepseeedSVSFEEQLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 130 AVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFS 209
Cdd:cd19094 152 ALGELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGLAEACHRENVGLLAYSPLAGGVLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 210 GKY-KTKDIPAEGRysnqsshGTLYRG---RYFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVI 285
Cdd:cd19094 232 GKYlDGAARPEGGR-------LNLFPGymaRYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVT-------STI 297
|
330 340 350
....*....|....*....|....*....|
gi 1832818259 286 IGVSSLAQLENNLKDIqKGPLPQEVVDVLD 315
Cdd:cd19094 298 IGATTLEQLKENIDAF-DVPLSDELLAEID 326
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
94-306 |
1.63e-43 |
|
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: 152.41 E-value: 1.63e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 94 LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGwVRPTIYQA 173
Cdd:cd19089 102 LLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 174 MYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHgtlyRGRYFKDATFDALRLIEPVA 253
Cdd:cd19089 181 RYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFL----TEEALTPEKLEQLRKLNKIA 256
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832818259 254 ERHGLTMPEIAFRWihhhsalNMKDNGRDGVIIGVSSLAQLENNLKDIQKGPL 306
Cdd:cd19089 257 AKRGQSLAQLALSW-------VLRDPRVTSVLIGASSPSQLEDNVAALKNLDF 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
37-317 |
5.47e-40 |
|
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: 143.51 E-value: 5.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 37 KCLDHlqqqGYNEVDTARVYVGGKQEAFTAQA----RWKERGLTLATKWYPHTPGAHKADV------LRENLERSLKELQ 106
Cdd:cd19143 39 AAYDA----GVNFFDNAEVYANGQSEEIMGQAikelGWPRSDYVVSTKIFWGGGGPPPNDRglsrkhIVEGTKASLKRLQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 107 TDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRN-IETE 185
Cdd:cd19143 115 LDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRErVEVE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 186 LIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIPAEGRYSNQSSHGTLYRGRYFKDATFDALRLIEPVAERHGLTMPEIAF 265
Cdd:cd19143 195 YAPLYEKYGLGTTTWSPLASGLLTGKY-NNGIPEGSRLALPGYEWLKDRKEELGQEKIEKVRKLKPIAEELGCSLAQLAI 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1832818259 266 RWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQKGP-LPQEVVDVLDQA 317
Cdd:cd19143 274 AWC-------LKNPNVSTVITGATKVEQLEENLKALEVLPkLTPEVMEKIEAI 319
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
10-299 |
3.53e-38 |
|
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: 137.68 E-value: 3.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEgaritslDDFNKCLDHLQQQGYNEVDTARVYvGGKQEAFTAQA---RW-KERG----LTLATK- 80
Cdd:cd19082 1 SRIVLGTADFGTRIDE-------EEAFALLDAFVELGGNFIDTARVY-GDWVERGASERvigEWlKSRGnrdkVVIATKg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 81 -----WYPHTPGAHKADvLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAE 155
Cdd:cd19082 73 ghpdlEDMSRSRLSPED-IRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 156 IVILCNERGWVRPTIYQAMYNAITRNIETELIPAC-----------KRYGIDIVVYNPLAGGLFSGKYKTKDIPAegrys 224
Cdd:cd19082 152 ANAYAKAHGLPGFAASSPQWSLARPNEPPWPGPTLvamdeemrawhEENQLPVFAYSSQARGFFSKRAAGGAEDD----- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1832818259 225 nqsshgTLYRGRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIhhhsaLNMKDNGRdgVIIGVSSLAQLENNLK 299
Cdd:cd19082 227 ------SELRRVYYSEENFERLERAKELAEEKGVSPTQIALAYV-----LNQPFPTV--PIIGPRTPEQLRDSLA 288
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
22-299 |
7.93e-38 |
|
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: 137.17 E-value: 7.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 22 DESEGARITslddfNKCLDhlqqQGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKwyphtpGAHK--------- 90
Cdd:cd19083 31 DEEEGKDLV-----REALD----NGVNLLDTAFIYGLGRSEELVGEVlkEYNRNEVVIATK------GAHKfggdgsvln 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 --ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEivilCNERGWVrp 168
Cdd:cd19083 96 nsPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKE----ANKDGYV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 169 TIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIP-AEGRYSNQSSHgtlYRGRYFKdATFDALR 247
Cdd:cd19083 170 DVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKY-TKDTKfPDNDLRNDKPL---FKGERFS-ENLDKVD 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 248 LIEPVAERHGLTMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNLK 299
Cdd:cd19083 245 KLKSIADEKGVTVAHLALAWYLTRPAI-------DVVIPGAKRAEQVIDNLK 289
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
45-317 |
1.45e-37 |
|
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: 136.65 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 45 QGYNEVDTARVYVGGKQEAFTAQA--RWKERgLTLATK----WYPHTP--GAHKADVLRENLERSLKELQTDQVDIFYLH 116
Cdd:cd19102 38 LGINWIDTAAVYGLGHSEEVVGRAlkGLRDR-PIVATKcgllWDEEGRirRSLKPASIRAECEASLRRLGVDVIDLYQIH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVIlcnergwVRPTIY-QAMYNAITRNIETELIPACKRYGI 195
Cdd:cd19102 117 WPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA-------IHPIASlQPPYSLLRRGIEAEILPFCAEHGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 196 DIVVYNPLAGGLFSGKYktkdipAEGRYSNQSSHGTLYRGRYFKDATFDA-LRLIE---PVAERHGLTMPEIAFRWIHHH 271
Cdd:cd19102 190 GVIVYSPMQSGLLTGKM------TPERVASLPADDWRRRSPFFQEPNLARnLALVDalrPIAERHGRTVAQLAIAWVLRR 263
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1832818259 272 SALNmkdngrdGVIIGVSSLAQLENNLK--DIQkgpLPQEVVDVLDQA 317
Cdd:cd19102 264 PEVT-------SAIVGARRPDQIDETVGaaDLR---LTPEELAEIEAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
10-299 |
2.20e-37 |
|
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: 136.19 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLM---TF--GPDESEGARItslddfnkcLDHLQQQGYNEVDTARVYVGGKQEAFTAQA--RWKERgLTLATKWY 82
Cdd:cd19076 13 SALGLGCMgmsAFygPADEEESIAT---------LHRALELGVTFLDTADMYGPGTNEELLGKAlkDRRDE-VVIATKFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 PH-TPGAH------KADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAE 155
Cdd:cd19076 83 IVrDPGSGfrgvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 156 IVIlcnergwVRP-TIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHgtlYR 234
Cdd:cd19076 163 AHA-------VHPiTAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNPR---FQ 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832818259 235 GRYFkDATFDALRLIEPVAERHGLTMPEIAFRWIHHhsalnmkdNGRDGVII-GVSSLAQLENNLK 299
Cdd:cd19076 233 GENF-DKNLKLVEKLEAIAAEKGCTPAQLALAWVLA--------QGDDIVPIpGTKRIKYLEENVG 289
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-299 |
9.39e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 131.30 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFGP--DESEGARItsLDDFnkcldhlQQQGYNEVDTARVY-------VGGKQEAFTAqaRW-KERG----LTLAT 79
Cdd:cd19752 5 LGTMYFGTrtDEETSFAI--LDRY-------VAAGGNFLDTANNYafwteggVGGESERLIG--RWlKDRGnrddVVIAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 80 K---------WYPHTPGAHKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTA 150
Cdd:cd19752 74 KvgagprdpdGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 151 FEVAEIVILCNERGWVRP-------TIYQAMYNA---ITRNIETELIPACKRYG-IDIVVYNPLAGGLfsgkYKTKDIPA 219
Cdd:cd19752 154 WRLERARQIARQQGWAEFsaiqqrhSYLRPRPGAdfgVQRIVTDELLDYASSRPdLTLLAYSPLLSGA----YTRPDRPL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 220 EGRYSNQsshGTLYRgryfkdatfdaLRLIEPVAERHGLTMPEIAFRWIHHhsalnmkdnGRDGVI--IGVSSLAQLENN 297
Cdd:cd19752 230 PEQYDGP---DSDAR-----------LAVLEEVAGELGATPNQVVLAWLLH---------RTPAIIplLGASTVEQLEEN 286
|
..
gi 1832818259 298 LK 299
Cdd:cd19752 287 LA 288
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
10-298 |
2.49e-34 |
|
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: 127.73 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFG-------PDESEGAritSLDDFNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQARwKERGLT----LA 78
Cdd:cd19093 3 SPLGLGTWQWGdrlwwgyGEYGDED---LQAAFDAALEA----GVNLFDTAEVYGTGRSERLLGRFL-KELGDRdevvIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 79 TKWYPhTPGAHKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETL-EAVNELHKEGKFVQLGLSNYTAFEVAEIV 157
Cdd:cd19093 75 TKFAP-LPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ILCNERGwVRPTIYQAMYNAITRNIET-ELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRysnqsshgtlyRGR 236
Cdd:cd19093 154 KALKERG-VPLASNQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGR-----------RRL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 237 YFK------DATFDALRLIepvAERHGLTMPEIAFRWIHHHSALnmkdngrdgVIIGVSSLAQLENNL 298
Cdd:cd19093 222 FGRknlekvQPLLDALEEI---AEKYGKTPAQVALNWLIAKGVV---------PIPGAKNAEQAEENA 277
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
10-310 |
6.57e-34 |
|
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: 126.13 E-value: 6.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEgariTSLDDFNKCLDHLQQQGYNEVDTARVYvgGKQEAFTAQA--RWKERGLTLATK--WYPHT 85
Cdd:cd19090 1 SALGLGTAGLGGVFGG----VDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAlaELPREPLVLSTKvgRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 86 PGAHKADVLRENLERSLKELQTDQVDIFYLHAADRsVPF------AETLEAVNELHKEGKFVQLGLSNYTAFEVAEI--- 156
Cdd:cd19090 75 TADYSADRVRRSVEESLERLGRDRIDLLMIHDPER-VPWvdilapGGALEALLELKEEGLIKHIGLGGGPPDLLRRAiet 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 157 ----VILCNERgwvrptiyqamYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKtkdipaegrysnqssHGTL 232
Cdd:cd19090 154 gdfdVVLTANR-----------YTLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPP---------------ERVR 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 233 YRGRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQkGPLPQEV 310
Cdd:cd19090 208 YTYRWLSPELLDRAKRLYELCDEHGVPLPALALRFL-------LRDPRISTVLVGASSPEELEQNVAAAE-GPLPEEL 277
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
37-299 |
2.31e-33 |
|
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: 125.46 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 37 KCLDHlqqqGYNEVDTARVYVGGKQEAFTAQARWKERG-LTLATK----W------YPHTPGAHK------ADVLRENLE 99
Cdd:cd19149 41 AALDL----GINLIDTAPAYGFGHSEEIVGKAIKGRRDkVVLATKcglrWdreggsFFFVRDGVTvyknlsPESIREEVE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 100 RSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwvrPTIYQAMYNAIT 179
Cdd:cd19149 117 QSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAGQ------LDIIQEKYSMLD 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 180 RNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEG--RYSNQsshgtlyrgRYFKDATFDALRLIE---PVAE 254
Cdd:cd19149 191 RGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGdaRSGIP---------WFSPENREKVLALLEkwkPLCE 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1832818259 255 RHGLTMPEIAFRWIHHHSalnmkdnGRDGVIIGVSSLAQLENNLK 299
Cdd:cd19149 262 KYGCTLAQLVIAWTLAQP-------GITSALCGARKPEQAEENAK 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
6-317 |
3.59e-31 |
|
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: 119.84 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 6 PSATPRV---ILGLMTFGPDESEGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQarW-KERG----LTL 77
Cdd:cd19146 5 PTAGVRVsplCLGAMSFGEAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGE--WmASRGnrdeMVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 78 ATKW-YPHTPGAHK----------ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLS 146
Cdd:cd19146 83 ATKYtTGYRRGGPIkiksnyqgnhAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 147 NYTAFevaeIVILCNE----RGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAgglfSGKYKTkdiPAEGR 222
Cdd:cd19146 163 DTPAW----VVSKANAyaraHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLG----QGQFRT---EEEFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 223 YSNQSshgtlyrGRYFKDATFDALRL---IEPVAERHGLTMPEIAFRWIHHHSALNMKdngrdgvIIGVSSLAQLENNLK 299
Cdd:cd19146 232 RRGRS-------GRKGGPQTEKERKVsekLEKVAEEKGTAITSVALAYVMHKAPYVFP-------IVGGRKVEHLKGNIE 297
|
330
....*....|....*...
gi 1832818259 300 DIQKgPLPQEVVDVLDQA 317
Cdd:cd19146 298 ALGI-SLSDEEIQEIEDA 314
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-299 |
4.19e-31 |
|
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: 118.10 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGpdeseGARITSLDDFNKCLDHLQ---QQGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKWYPH 84
Cdd:cd19072 5 PVLGLGTWGIG-----GGMSKDYSDDKKAIEALRyaiELGINLIDTAEMYGGGHAEELVGKAikGFDREDLFITTKVSPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 85 tpGAHKADVLREnLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV------- 157
Cdd:cd19072 80 --HLKYDDVIKA-AKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQsylkkgp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ILCNergwvrptiyQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKyktkdipaegrysnqsshgtlyrgry 237
Cdd:cd19072 157 IVAN----------QVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNA-------------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 238 fkdatfDALRLIEPVAERHGLTMPEIAFRWIHHHsalnmkdngrDGV--IIGVSSLAQLENNLK 299
Cdd:cd19072 201 ------KGSPLLDEIAKKYGKTPAQIALNWLISK----------PNViaIPKASNIEHLEENAG 248
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
10-299 |
5.85e-30 |
|
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: 115.01 E-value: 5.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFG--------PDESEGARItslddfnkcLDHLQQQGYNEVDTARVYVGGKQEAFTAQA--RWKErGLTLAT 79
Cdd:cd19088 2 SRLGYGAMRLTgpgiwgppADREEAIAV---------LRRALELGVNFIDTADSYGPDVNERLIAEAlhPYPD-DVVIAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 80 K--WYPHTPGAHKADV----LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYT---- 149
Cdd:cd19088 72 KggLVRTGPGWWGPDGspeyLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTvaqi 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 150 --AFEVAEIVILcnergwvrptiyQAMYNAITRNIEtELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysNQS 227
Cdd:cd19088 152 eeARAIVRIVSV------------QNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGG------------------DLA 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 228 SHGTLYRGryfkdatfdalrliepVAERHGLTMPEIAFRWIHHHSAlNMkdngrdGVIIGVSSLAQLENNLK 299
Cdd:cd19088 201 QPGGLLAE----------------VAARLGATPAQVALAWLLARSP-VM------LPIPGTSSVEHLEENLA 249
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-299 |
1.86e-29 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 115.00 E-value: 1.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFgpdeSEGA-RITSLDDFNKCLDHLQQQGYNEVDTARVYvGGKQE---AFTAQARWKERG---LTLATKWY 82
Cdd:cd19101 3 SRVINGMWQL----SGGHgGIRDEDAAVRAMAAYVDAGLTTFDCADIY-GPAEEligEFRKRLRRERDAaddVQIHTKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 PhTPGAHKAD--VLRENLERSLKELQTDQVDIFYLHAADRSVP-FAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV-- 157
Cdd:cd19101 78 P-DPGELTMTraYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREILda 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ---ILCNergwvrptiyQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSshgtLYR 234
Cdd:cd19101 157 gvpIVSN----------QVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSEKYLGVPEPTGPALETRS----LQK 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 235 GRYFKDAT-----F-DALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLK 299
Cdd:cd19101 223 YKLMIDEWggwdlFqELLRTLKAIADKHGVSIANVAVRWVLDQPGVA-------GVIVGARNSEHIDDNVR 286
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
75-316 |
1.06e-28 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 113.93 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 75 LTLATK-WYPHTPGAHKADVLRE----NLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYT 149
Cdd:PRK09912 92 LIISTKaGYDMWPGPYGSGGSRKyllaSLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 150 AFEVAEIVILCNErgWVRP-TIYQAMYNAITRNIE-TELIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIPAEGRYSNQS 227
Cdd:PRK09912 172 PERTQKMVELLRE--WKIPlLIHQPSYNLLNRWVDkSGLLDTLQNNGVGCIAFTPLAQGLLTGKY-LNGIPQDSRMHREG 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 228 SHGTLYRGRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQKGPLP 307
Cdd:PRK09912 249 NKVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWL-------LKDERVTSVLIGASRAEQLEENVQALNNLTFS 321
|
....*....
gi 1832818259 308 QEVVDVLDQ 316
Cdd:PRK09912 322 TEELAQIDQ 330
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
44-315 |
2.22e-27 |
|
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: 109.75 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEAFTA----QARWKERGLTLATKWYphtpGAHKADVLR--------ENLERSLKELQTDQVD 111
Cdd:cd19159 42 ESGVNLFDTAEVYAAGKAEVILGsiikKKGWRRSSLVITTKLY----WGGKAETERglsrkhiiEGLKGSLQRLQLEYVD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 112 IFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITR-NIETELIPAC 190
Cdd:cd19159 118 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELY 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 191 KRYGIDIVVYNPLAGGLFSGKYKTkDIPaegrysnQSSHGTLYRGRYFKDATFD--------ALRLIEPVAERHGLTMPE 262
Cdd:cd19159 198 HKIGVGAMTWSPLACGIISGKYGN-GVP-------ESSRASLKCYQWLKERIVSeegrkqqnKLKDLSPIAERLGCTLPQ 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 263 IAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQKGP-LPQEVVDVLD 315
Cdd:cd19159 270 LAVAWC-------LRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEID 316
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
44-302 |
3.10e-27 |
|
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: 109.07 E-value: 3.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEAFTAQ----ARWKERGLTLATKWYphtpGAHKADVLR--------ENLERSLKELQTDQVD 111
Cdd:cd19141 41 ENGINLFDTAEVYAAGKAEIVLGKilkkKGWRRSSYVITTKIF----WGGKAETERglsrkhiiEGLKASLERLQLEYVD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 112 IFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITR-NIETELIPAC 190
Cdd:cd19141 117 IVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQReKVEMQLPELF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 191 KRYGIDIVVYNPLAGGLFSGKYKTKdIPAegrysnqSSHGTLYRGRYFKDATFDA--------LRLIEPVAERHGLTMPE 262
Cdd:cd19141 197 HKIGVGAMTWSPLACGILSGKYDDG-VPE-------YSRASLKGYQWLKEKILSEegrrqqakLKELQIIADRLGCTLPQ 268
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1832818259 263 IAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQ 302
Cdd:cd19141 269 LAIAWC-------LKNEGVSSVLLGASSTEQLYENLQAIQ 301
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
14-310 |
7.16e-27 |
|
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: 107.90 E-value: 7.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLM----TFGPDESEGARITslddfnkCLDHLQQQGYNEVDTARVYVGGKQEAFTAQA---RWKERgLTLATKWYPHTP 86
Cdd:cd19145 17 LGCMglsgDYGAPKPEEEGIA-------LIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAlkdGPREK-VQLATKFGIHEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 87 GAHKADV------LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVaeivilc 160
Cdd:cd19145 89 GGSGVEVrgdpayVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTI------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 161 nERGW-VRP-TIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSNqsshgTLYRgryF 238
Cdd:cd19145 162 -RRAHaVHPiTAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRK-----SHPR---F 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1832818259 239 KDATFD----ALRLIEPVAERHGLTMPEIAFRWIHHHsalnmkdnGRDGV-IIGVSSLAQLENNLKDIQKGPLPQEV 310
Cdd:cd19145 233 QGENLEknkvLYERVEALAKKKGCTPAQLALAWVLHQ--------GEDVVpIPGTTKIKNLNQNIGALSVKLTKEDL 301
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
44-273 |
1.03e-26 |
|
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: 106.56 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEAFTAQARWKERG-LTLATKWYPHTpgAHKADVLReNLERSLKELQTDQVDIFYLHAadR-S 121
Cdd:cd19138 40 DLGMTLIDTAEMYGDGGSEELVGEAIRGRRDkVFLVSKVLPSN--ASRQGTVR-ACERSLRRLGTDYLDLYLLHW--RgG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 122 VPFAETLEAVNELHKEGKFVQLGLSNytaFEVAEIVILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYN 201
Cdd:cd19138 115 VPLAETVAAMEELKKEGKIRAWGVSN---FDTDDMEELWAVPGGGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYS 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 202 PLAGGlfsgkyktkDIPAEGRYSNQsshgtlyrgryfkdatfdalRLIEpVAERHGLTMPEIAFRWIHHHSA 273
Cdd:cd19138 192 PLAQG---------GLLRRGLLENP--------------------TLKE-IAARHGATPAQVALAWVLRDGN 233
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
98-303 |
5.16e-26 |
|
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: 105.56 E-value: 5.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 98 LERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGwVRPTIYQAMYNA 177
Cdd:cd19151 107 LDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSM 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 178 ITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIPAEGRysnQSSHGTLYRGRYFKDATFDALRLIEPVAERHG 257
Cdd:cd19151 186 FNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTDRY-LNGIPEDSR---AAKGSSFLKPEQITEEKLAKVRRLNEIAQARG 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1832818259 258 LTMPEIAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQK 303
Cdd:cd19151 262 QKLAQMALAWV-------LRNKRVTSVLIGASKPSQIEDAVGALDN 300
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
98-303 |
6.89e-26 |
|
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: 105.23 E-value: 6.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 98 LERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGwVRPTIYQAMYNA 177
Cdd:cd19150 107 LDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNM 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 178 ITRNIE-TELIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIPAEGRysnqSSHGTLYRGRYFKDATFDALRLIEPVAERH 256
Cdd:cd19150 186 LNRWVEeSGLLDTLQELGVGCIAFTPLAQGLLTDKY-LNGIPEGSR----ASKERSLSPKMLTEANLNSIRALNEIAQKR 260
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1832818259 257 GLTMPEIAFRWIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQK 303
Cdd:cd19150 261 GQSLAQMALAWV-------LRDGRVTSALIGASRPEQLEENVGALDN 300
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
12-268 |
9.42e-26 |
|
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: 104.70 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 12 VILGLMTFGPDESEgaritSLDDFNKCLDhlqqQGYNEVDTARVYVGGKQEAFTAQArWKERG----LTLATK----WYP 83
Cdd:cd19148 13 AIGGWMWGGTDEKE-----AIETIHKALD----LGINLIDTAPVYGFGLSEEIVGKA-LKEYGkrdrVVIATKvgleWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 84 HTP---GAHKADVLREnLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYT-----AFEVAE 155
Cdd:cd19148 83 GGEvvrNSSPARIRKE-VEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSpeqmeTFRKVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 156 IVILCnergwvrptiyQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYkTKDIPAEG---RYSNQSSHGTL 232
Cdd:cd19148 162 PLHTV-----------QPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKM-TKDTKFEGddlRRTDPKFQEPR 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 1832818259 233 YrGRYfkdatFDALRLIEPVA-ERHGLTMPEIAFRWI 268
Cdd:cd19148 230 F-SQY-----LAAVEELDKLAqERYGKSVIHLAVRWL 260
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
14-315 |
2.08e-25 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 104.55 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFGPDESEGaritsldDFNKCLDHLQQQGYNEVDTARVY-VGGKQE--AFTAQ--ARW-KERG----LTLATKWYP 83
Cdd:PRK10625 18 LGTMTFGEQNSEA-------DAHAQLDYAVAQGINLIDVAEMYpVPPRPEtqGLTETyiGNWlAKRGsrekLIIASKVSG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 84 HTPGAHKA---------DVLRENLERSLKELQTDQVDIFYLHAADR-----------------SVPFAETLEAVNELHKE 137
Cdd:PRK10625 91 PSRNNDKGirpnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQRptncfgklgyswtdsapAVSLLETLDALAEQQRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 138 GKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDI 217
Cdd:PRK10625 171 GKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 218 PAEGRysnqsshGTLYR--GRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLE 295
Cdd:PRK10625 251 PAGAR-------NTLFSrfTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVA-------STLLGATTMEQLK 316
|
330 340
....*....|....*....|
gi 1832818259 296 NNLkDIQKGPLPQEVVDVLD 315
Cdd:PRK10625 317 TNI-ESLHLTLSEEVLAEIE 335
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
14-299 |
3.54e-25 |
|
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: 101.79 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFGPDESEGariTSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQArWKERG--LTLATK----WYPHTPG 87
Cdd:cd19086 8 FGTWGLGGDWWGD---VDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKA-LKGRRdkVVIATKfgnrFDGGPER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 88 AHK--ADVLRENLERSLKELQTDQVDIFYLHAADRSV-PFAETLEAVNELHKEGKFVQLGLSnytaFEVAEIVILCNERG 164
Cdd:cd19086 84 PQDfsPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVlDNDELFEALEKLKQEGKIRAYGVS----VGDPEEALAALRRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 165 WVRpTIyQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGKyktkdipaegrysnqsshgtlyrgryfkdatfd 244
Cdd:cd19086 160 GID-VV-QVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGK--------------------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1832818259 245 alrliepvaerhgltMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNLK 299
Cdd:cd19086 205 ---------------LAQAALRFILSHPAV-------STVIPGARSPEQVEENAA 237
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
44-315 |
1.76e-24 |
|
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: 101.70 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEA----FTAQARWKERGLTLATKWYPHTPGAHKADVLR----ENLERSLKELQTDQVDIFYL 115
Cdd:cd19158 42 DNGINLFDTAEVYAAGKAEVvlgnIIKKKGWRRSSLVITTKIFWGGKAETERGLSRkhiiEGLKASLERLQLEYVDVVFA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 116 HAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITR-NIETELIPACKRYG 194
Cdd:cd19158 122 NRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQReKVEVQLPELFHKIG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 195 IDIVVYNPLAGGLFSGKYKTKDIPaegrYSNQSSHGTlyrgRYFKDATFD--------ALRLIEPVAERHGLTMPEIAFR 266
Cdd:cd19158 202 VGAMTWSPLACGIVSGKYDSGIPP----YSRASLKGY----QWLKDKILSeegrrqqaKLKELQAIAERLGCTLPQLAIA 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1832818259 267 WIhhhsalnMKDNGRDGVIIGVSSLAQLENNLKDIQKGP-LPQEVVDVLD 315
Cdd:cd19158 274 WC-------LRNEGVSSVLLGASNAEQLMENIGAIQVLPkLSSSIVHEID 316
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
46-299 |
2.40e-24 |
|
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: 99.65 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVY-----VGgkqEAFTAQARWKERgLTLATK-WYPHtpgaHKADVLRENLERSLKELQTDQVDIFYLHAAD 119
Cdd:cd19073 27 GYRHIDTAEIYnneaeVG---EAIAESGVPRED-LFITTKvWRDH----LRPEDLKKSVDRSLEKLGTDYVDLLLIHWPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 120 RSVPFAETLEAVNELHKEGKFVQLGLSNYT------AFEVAEIVILCNErgwVR--PTIYQAmynaitrnietELIPACK 191
Cdd:cd19073 99 PTVPLEETLGALKELKEAGKVKSIGVSNFTielleeALDISPLPIAVNQ---VEfhPFLYQA-----------ELLEYCR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 192 RYGIDIVVYNPLAgglfsgkyktkdipaegrysnqsshgtlyRGRYFKDATfdalrlIEPVAERHGLTMPEIAFRWIHHH 271
Cdd:cd19073 165 ENDIVITAYSPLA-----------------------------RGEVLRDPV------IQEIAEKYDKTPAQVALRWLVQK 209
|
250 260
....*....|....*....|....*...
gi 1832818259 272 SALnmkdngrdgVIIGVSSLAQLENNLK 299
Cdd:cd19073 210 GIV---------VIPKASSEDHLKENLA 228
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
10-298 |
6.02e-24 |
|
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: 100.21 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTF----GPDESEGARItslddfnKCLDHLQQQGYNEVDTARVYVGGKQE--AFTAQARWKERGLTLATKW-- 81
Cdd:cd19144 14 PALGFGAMGLsafyGPPKPDEERF-------AVLDAAFELGCTFWDTADIYGDSEELigRWFKQNPGKREKIFLATKFgi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 82 -YPHTPGAHKAD----VLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVaei 156
Cdd:cd19144 87 eKNVETGEYSVDgspeYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETL--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 157 vilcnERGW-VRP-TIYQAMYNAITRNIET---ELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGRYSnqsshgt 231
Cdd:cd19144 164 -----RRAHaVHPiAAVQIEYSPFSLDIERpeiGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFR------- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 232 LYRGRYFKDATFDALRL---IEPVAERHGLTMPEIAFRWIHHHsalnmkdnGRDGVII-GVSSLAQLENNL 298
Cdd:cd19144 232 RMAPRFQAENFPKNLELvdkIKAIAKKKNVTAGQLTLAWLLAQ--------GDDIIPIpGTTKLKRLEENL 294
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
45-270 |
1.46e-23 |
|
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: 98.84 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 45 QGYNEVDTARVYVGGKQEAF--TAQARWKERgLTLATKW-------YPHTPGAH-KADVLRENLERSLKELQTDQVDIFY 114
Cdd:cd19078 37 LGITFFDTAEVYGPYTNEELvgEALKPFRDQ-VVIATKFgfkidggKPGPLGLDsRPEHIRKAVEGSLKRLQTDYIDLYY 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 115 LHAADRSVPFAETLEAVNELHKEGKFVQLGLSnytafEVAEIVIlcnERGW-VRP-TIYQAMYNAITRNIETELIPACKR 192
Cdd:cd19078 116 QHRVDPNVPIEEVAGTMKELIKEGKIRHWGLS-----EAGVETI---RRAHaVCPvTAVQSEYSMMWREPEKEVLPTLEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 193 YGIDIVVYNPLAGGLFSGKYKTkdipaegrysNQSSHGTLYRGRY--FKDATFDA----LRLIEPVAERHGLTMPEIAFR 266
Cdd:cd19078 188 LGIGFVPFSPLGKGFLTGKIDE----------NTKFDEGDDRASLprFTPEALEAnqalVDLLKEFAEEKGATPAQIALA 257
|
....
gi 1832818259 267 WIHH 270
Cdd:cd19078 258 WLLA 261
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
44-313 |
3.27e-23 |
|
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: 98.13 E-value: 3.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEA----FTAQARWKERGLTLATKWYPHTPGAHKADVLR----ENLERSLKELQTDQVDIFYL 115
Cdd:cd19160 44 EHGVNLFDTAEVYAAGKAERtlgnILKSKGWRRSSYVVTTKIYWGGQAETERGLSRkhiiEGLRGSLDRLQLEYVDIVFA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 116 HAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRN-IETELIPACKRYG 194
Cdd:cd19160 124 NRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEMQLPELYHKIG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 195 IDIVVYNPLAGGLFSGKYkTKDIPAEGRYSNQSSHgTLYRGRYFKDATFDALRLIE--PVAERHGLTMPEIAFRWIhhhs 272
Cdd:cd19160 204 VGSVTWSPLACGLITGKY-DGRVPDTCRAAVKGYQ-WLKEKVQSEEGKKQQAKVKElhPIADRLGCTVAQLAIAWC---- 277
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1832818259 273 alnMKDNGRDGVIIGVSSLAQLENNLKDIQKGP--LPQEVVDV 313
Cdd:cd19160 278 ---LRSEGVSSVLLGVSSAEQLIENLGSIQVLSqlTPQTVMEI 317
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-299 |
3.58e-23 |
|
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: 96.50 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKWYPHTPGAHKADVLREnLERSLKELQTDQVDIFYLHAADRS 121
Cdd:cd19105 36 DLGINYFDTAEGYGNGNSEEIIGEAlkGLRRDKVFLATKASPRLDKKDKAELLKS-VEESLKRLQTDYIDIYQLHGVDTP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 122 VP---FAETLEAVNELHKEGKFVQLGLSnyTAFEVAEIVILCNERGWVrpTIYQAMYNAITRNIE-TELIPACKRYGIDI 197
Cdd:cd19105 115 EErllNEELLEALEKLKKEGKVRFIGFS--THDNMAEVLQAAIESGWF--DVIMVAYNFLNQPAElEEALAAAAEKGIGV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 198 VVYNPLAGGLFSGKyktkdipaegrysnqsshgtlyRGRYFKDATFdalrliepvaerhglTMPEIAFRWIHHHSALnmk 277
Cdd:cd19105 191 VAMKTLAGGYLQPA----------------------LLSVLKAKGF---------------SLPQAALKWVLSNPRV--- 230
|
250 260
....*....|....*....|..
gi 1832818259 278 dngrDGVIIGVSSLAQLENNLK 299
Cdd:cd19105 231 ----DTVVPGMRNFAELEENLA 248
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
6-259 |
1.15e-22 |
|
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: 96.43 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 6 PSATPRV---ILGLMTFGPDESEGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQarW-KERG----LTL 77
Cdd:cd19147 4 KTAGIRVsplILGAMSIGDAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGE--WmKSRKnrdqIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 78 ATKWYPHTP-------------GAHKADvLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLG 144
Cdd:cd19147 82 ATKFTTDYKayevgkgkavnycGNHKRS-LHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 145 LSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRNIETELIPACKRYGIDIVVYNPLAGglfsGKYKTKDIPAEgRYS 224
Cdd:cd19147 161 VSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGG----GKFQSKKAVEE-RKK 235
|
250 260 270
....*....|....*....|....*....|....*
gi 1832818259 225 NQSSHGTLYRGRYFKDATFDALRLIEPVAERHGLT 259
Cdd:cd19147 236 NGEGLRSFVGGTEQTPEEVKISEALEKVAEEHGTE 270
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
13-317 |
3.97e-22 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 93.97 E-value: 3.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTFGPDESEGARI--TSLDDfnkcldhlqqqGYNEVDTARVY-----VGgkqEAFtaqarwKERG-----LTLATK 80
Cdd:COG0656 7 ALGLGTWQLPGEEAAAAvrTALEA-----------GYRHIDTAAMYgneegVG---EAI------AASGvpreeLFVTTK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 81 -WyphtPGAHKADVLRENLERSLKELQTDQVDIFYLHAAdRSVPFAETLEAVNELHKEGKFVQLGLSNYT------AFEV 153
Cdd:COG0656 67 vW----NDNHGYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDpehleeLLAE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 154 AEIVILCNergwvrptiyQAMYNAITRniETELIPACKRYGIDIVVYNPLAgglfsgkyktkdipaegrysnqsshgtly 233
Cdd:COG0656 142 TGVKPAVN----------QVELHPYLQ--QRELLAFCREHGIVVEAYSPLG----------------------------- 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 234 RGRYFKDATfdalrlIEPVAERHGLTMPEIAFRWIHHHSALnmkdngrdgVIIGVSSLAQLENNLkDIQKGPLPQEVVDV 313
Cdd:COG0656 181 RGKLLDDPV------LAEIAEKHGKTPAQVVLRWHLQRGVV---------VIPKSVTPERIRENL-DAFDFELSDEDMAA 244
|
....
gi 1832818259 314 LDQA 317
Cdd:COG0656 245 IDAL 248
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-299 |
4.01e-22 |
|
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: 93.84 E-value: 4.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFG-----PDESEGARItslddfnkcLDHLQQQGYNEVDTARVYvGGKQE---AFTAQARWKErgLTLATK-WYPH 84
Cdd:cd19095 5 LGTSGIGrvwgvPSEAEAARL---------LNTALDLGINLIDTAPAY-GRSEErlgRALAGLRRDD--LFIATKvGTHG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 85 TPGAHKADV----LRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTafEVAEIVILC 160
Cdd:cd19095 73 EGGRDRKDFspaaIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDG--EELEAAIAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 161 NERGWVrptiyQAMYNAITRNIEtELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAegrysnqsshgtlyrgryfkd 240
Cdd:cd19095 151 GVFDVV-----QLPYNVLDREEE-ELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYA--------------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1832818259 241 atfDALRLIEPVAERHGLTMPEIAFRWIHHHSALNMkdngrdgVIIGVSSLAQLENNLK 299
Cdd:cd19095 204 ---DYARRPEFAAEIGGATWAQAALRFVLSHPGVSS-------AIVGTTNPEHLEENLA 252
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
46-268 |
1.42e-21 |
|
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: 92.32 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvGGKQEAFTAQARWK-ERG-LTLATK-WYPHtpgAHKADVLREnLERSLKELQTDQVDIFYLHAADRSV 122
Cdd:cd19140 34 GYRHIDTAQMY-GNEAQVGEAIAASGvPRDeLFLTTKvWPDN---YSPDDFLAS-VEESLRKLRTDYVDLLLLHWPNKDV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 123 PFAETLEAVNELHKEGKFVQLGLSNYT------AFEVAEIVILCNergwvrptiyQAMYNAITRniETELIPACKRYGID 196
Cdd:cd19140 109 PLAETLGALNEAQEAGLARHIGVSNFTvallreAVELSEAPLFTN----------QVEYHPYLD--QRKLLDAAREHGIA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 197 IVVYNPLAgglfsgkyktkdipaegrysnqsshgtlyRGRYFKDAtfdalrLIEPVAERHGLTMPEIAFRWI 268
Cdd:cd19140 177 LTAYSPLA-----------------------------RGEVLKDP------VLQEIGRKHGKTPAQVALRWL 213
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
11-273 |
1.48e-21 |
|
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: 93.00 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 11 RVILGLMTFGPDESEGARITSLddFNKCLDHlqqqGYNEVDTARVYVGGKQEAFTAQARWKERGL----TLATK-----W 81
Cdd:cd19092 8 RLVLGCMRLADWGESAEELLSL--IEAALEL----GITTFDHADIYGGGKCEELFGEALALNPGLrekiEIQTKcgirlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 82 YPHTPGAHK-----ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVA-- 154
Cdd:cd19092 82 DDPRPGRIKhydtsKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEll 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 155 ----EIVILCNergwvrptiyQAMYNAI-TRNIETELIPACKRYGIDIVVYNPLAGGLFSGKyktkdipaegrysnqssh 229
Cdd:cd19092 162 qsylDQPLVTN----------QIELSLLhTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFGG------------------ 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1832818259 230 gtlyrgryFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSA 273
Cdd:cd19092 214 --------FDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPA 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-318 |
4.67e-21 |
|
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: 91.94 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 30 TSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQA-RWKERGLTLATKW-YPHTPGAHKADVLRENLERSLKELQT 107
Cdd:cd19104 29 TTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRAlKGLPAGPYITTKVrLDPDDLGDIGGQIERSVEKSLKRLKR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 108 DQVDIFYLH---AADRSVPFAETL------------EAVNELHKEGKFVQLGLsnyTAFEVAEIVILCNERGwvRPTIYQ 172
Cdd:cd19104 109 DSVDLLQLHnriGDERDKPVGGTLsttdvlglggvaDAFERLRSEGKIRFIGI---TGLGNPPAIRELLDSG--KFDAVQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 173 AMYN------AITRNIET------ELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPaegrysnQSSHGTLYRGRYFKD 240
Cdd:cd19104 184 VYYNllnpsaAEARPRGWsaqdygGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREA-------PPTSDSDVAIDFRRA 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 241 ATFDALrliepvAERHGLTMPEIAFRWihhhsALNMKdnGRDGVIIGVSSLAQLENNLKDIQKGPLPQEVVDVLDQAW 318
Cdd:cd19104 257 AAFRAL------AREWGETLAQLAHRF-----ALSNP--GVSTVLVGVKNREELEEAVAAEAAGPLPAENLARLEALW 321
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
21-306 |
1.80e-20 |
|
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: 89.51 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 21 PDESEGARItslddfnkcLDHLQQQGYNEVDTARVYvgGKQEAFTAQARWKERGLTLATKwYPHTPGAHK--ADVLRENL 98
Cdd:cd19097 23 PSEKEAKKI---------LEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKIITK-LPPLKEDKKedEAAIEASV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 99 ERSLKELQTDQVDIFYLH-AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTaFEVAEIVILCNergwvRPTIYQAMYNA 177
Cdd:cd19097 91 EASLKRLKVDSLDGLLLHnPDDLLKHGGKLVEALLELKKEGLIRKIGVSVYS-PEELEKALESF-----KIDIIQLPFNI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 178 IT-RNIETELIPACKRYGIDIV---VYnpLAGGLFSgkyKTKDIPAegrysnqsshgtlyrgrYFKDATfDALRLIEPVA 253
Cdd:cd19097 165 LDqRFLKSGLLAKLKKKGIEIHarsVF--LQGLLLM---EPDKLPA-----------------KFAPAK-PLLKKLHELA 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1832818259 254 ERHGLTMPEIAFRWIHHHSALnmkdngrDGVIIGVSSLAQLENNLKDIQKGPL 306
Cdd:cd19097 222 KKLGLSPLELALGFVLSLPEI-------DKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
86-303 |
3.88e-20 |
|
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: 89.22 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 86 PGAHKADVLRENLERSLKEL-----QTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV--- 157
Cdd:cd19077 84 PDTLRPDGSPEAVRKSIENIlralgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHavh 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 -ILCNErgwvrptiyqAMYNAITRNIET-ELIPACKRYGIDIVVYNPLAGGLFSGKYKT-KDIPaEG---RYSNQSSHGT 231
Cdd:cd19077 164 pIAAVE----------VEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIKSlADIP-EGdfrRHLDRFNGEN 232
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 232 LyrgryfkDATFDALRLIEPVAERHGLTMPEIAFRWIhhhsalnmKDNGRDGV--IIGVSSLAQLENNLKDIQK 303
Cdd:cd19077 233 F-------EKNLKLVDALQELAEKKGCTPAQLALAWI--------LAQSGPKIipIPGSTTLERVEENLKAANV 291
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-299 |
1.10e-19 |
|
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: 86.77 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGP-DESEGARItslddFNKCLDHlqqqGYNEVDTARVYvgGKQEAFTAQArWKER--GLTLATKwyphTp 86
Cdd:cd19100 12 SRLGFGGGPLGRlSQEEAAAI-----IRRALDL----GINYFDTAPSY--GDSEEKIGKA-LKGRrdKVFLATK----T- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 87 GAHKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAET------LEAVNELHKEGKFVQLGLSNYTaFEVAEIVIlc 160
Cdd:cd19100 75 GARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVfgpggaLEALLEAKEEGKIRFIGISGHS-PEVLLRAL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 161 nERGWVRpTIyQAMYNAI---TRNIETELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysnqsshgtlyrgry 237
Cdd:cd19100 152 -ETGEFD-VV-LFPINPAgdhIDSFREELLPLAREKGVGVIAMKVLAGG------------------------------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 238 fkdatfdalRLIEPVAERhgltmPEIAFRWihhhsALNMKDNgrDGVIIGVSSLAQLENNLK 299
Cdd:cd19100 198 ---------RLLSGDPLD-----PEQALRY-----ALSLPPV--DVVIVGMDSPEELDENLA 238
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-267 |
1.75e-19 |
|
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: 87.39 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 9 TPRVILGLMTFGPDESEGARI----TSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQ--ARWKERGLTLATKWY 82
Cdd:cd19103 4 LPKIALGTWSWGSGGAGGDQVfgnhLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEflKRYPREDYIISTKFT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 83 PHtpGAH-KADVLRENLERSLKELQTDQVDIFYLH-AADrsVPfAETLEAVnELHKEGKFVQLGLSNytaFEVAEIV--- 157
Cdd:cd19103 84 PQ--IAGqSADPVADMLEGSLARLGTDYIDIYWIHnPAD--VE-RWTPELI-PLLKSGKVKHVGVSN---HNLAEIKran 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 -ILcnERGWVRPTIYQAMYNAITRNIETELIPA-CKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEGrysnqSSHGTLYRG 235
Cdd:cd19103 155 eIL--AKAGVSLSAVQNHYSLLYRSSEEAGILDyCKENGITFFAYMVLEQGALSGKYDTKHPLPEG-----SGRAETYNP 227
|
250 260 270
....*....|....*....|....*....|..
gi 1832818259 236 RyfKDATFDALRLIEPVAERHGLTMPEIAFRW 267
Cdd:cd19103 228 L--LPQLEELTAVMAEIGAKHGASIAQVAIAW 257
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-220 |
1.88e-19 |
|
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: 86.47 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTFGPDESEGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKWYPHTpgAHK 90
Cdd:cd19137 6 ALGLGTWGIGGFLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAikDFPREDLFIVTKVWPTN--LRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 ADVLReNLERSLKELQTDQVDIFYLHAADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNErgwvrPTI 170
Cdd:cd19137 84 DDLLR-SLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-----PIV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 171 Y-QAMYNAITRNIETE-LIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAE 220
Cdd:cd19137 158 CnQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGLEKTNRTLEEIAKN 209
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
29-317 |
5.48e-19 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 86.80 E-value: 5.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 29 ITSLDDFNKCLDHLQQQGYNEVDTARVYvgGKQEAFTAQA--RWKERgLTLATKWYPHTpgaHKADVLRENLERSLKELQ 106
Cdd:COG1453 25 RKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKAlkGPRDK-VILATKLPPWV---RDPEDMRKDLEESLKRLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 107 TDQVDIFYLHAADRSVPFAET------LEAVNELHKEGKFVQLGLSNYTAFEVAEIVIlcnERGWVRpTIyQAMYNAITR 180
Cdd:COG1453 99 TDYIDLYLIHGLNTEEDLEKVlkpggaLEALEKAKAEGKIRHIGFSTHGSLEVIKEAI---DTGDFD-FV-QLQYNYLDQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 181 N--IETELIPACKRYGIDIVVYNPLAGGLFsgkyktkdipaegrysnqsshgtlyrgryfkdatfdaLRLIEPVAE--RH 256
Cdd:COG1453 174 DnqAGEEALEAAAEKGIGVIIMKPLKGGRL-------------------------------------ANPPEKLVEllCP 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1832818259 257 GLTMPEIAFRWIhhhsaLNMKDNgrDGVIIGVSSLAQLENNLKDIQKG-PLPQEVVDVLDQA 317
Cdd:COG1453 217 PLSPAEWALRFL-----LSHPEV--TTVLSGMSTPEQLDENLKTADNLePLTEEELAILERL 271
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
10-315 |
5.64e-19 |
|
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: 84.84 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDdfnkcldhlqqQGYNEVDTARVYvggKQEAFTAQArWKERGLT-----LATK-Wyp 83
Cdd:cd19071 2 PLIGLGTYKLKPEETAEAVLAALE-----------AGYRHIDTAAAY---GNEAEVGEA-IRESGVPreelfITTKlW-- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 84 htPGAHKADVLRENLERSLKELQTDQVDIFYLH------AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV 157
Cdd:cd19071 65 --PTDHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ilcnERGWVRPTIYQAMYNAITRNIetELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysnqsshgtlyRGRY 237
Cdd:cd19071 143 ----AAARIKPAVNQIELHPYLQQK--ELVEFCKEHGIVVQAYSPLGRG---------------------------RRPL 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 238 FKDATfdalrlIEPVAERHGLTMPEIAFRWIHHHsalnmkdngrdGVII--GVSSLAQLENNLkDIQKGPLPQEVVDVLD 315
Cdd:cd19071 190 LDDPV------LKEIAKKYGKTPAQVLLRWALQR-----------GVVVipKSSNPERIKENL-DVFDFELSEEDMAAID 251
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
46-302 |
8.55e-19 |
|
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: 85.59 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYVGGKQE----AFTAQARWKERGLTLATKWYPHTpGAHKADVLR----ENLERSLKELQTDQVDIFYLHA 117
Cdd:cd19142 44 GINYFDTSDAFTSGQAEtelgRILKKKGWKRSSYIVSTKIYWSY-GSEERGLSRkhiiESVRASLRRLQLDYIDIVIIHK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 118 ADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGWVRPTIYQAMYNAITRN-IETELIPACKRYGID 196
Cdd:cd19142 123 ADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREkMELYMPELYNKVGVG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 197 IVVYNPLAGGLFSGKYKTKDIPAEGRYSNQSSHGTLYRGR----YFKDATfDALRLIEPVAERHGLTMPEIAFRWihhhs 272
Cdd:cd19142 203 LITWSPLSLGLDPGISEETRRLVTKLSFKSSKYKVGSDGNgiheETRRAS-HKLRELSLIAERLGCDLTQLLIAW----- 276
|
250 260 270
....*....|....*....|....*....|
gi 1832818259 273 alNMKDNGRDGVIIGVSSLAQLENNLKDIQ 302
Cdd:cd19142 277 --SLKNENVQCVLIGASSLEQLYSQLNSLQ 304
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-299 |
1.42e-18 |
|
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: 83.76 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFgpDESEGARItsldDFNKCLDHLQQ---QGYNEVDTARVYVGGKQEAFTAQA--RWKERGLTLATKWYPHTPga 88
Cdd:cd19096 5 FGTMRL--PESDDDSI----DEEKAIEMIRYaidAGINYFDTAYGYGGGKSEEILGEAlkEGPREKFYLATKLPPWSV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 89 HKADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAET-----LEAVNELHKEGKFVQLGLSNYTAFEVAEIVIlcNER 163
Cdd:cd19096 77 KSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKArkgglLEFLEKAKKEGLIRHIGFSFHDSPELLKEIL--DSY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 164 GWVRPTIYqamYNAITRNIE--TELIPACKRYGIDIVVYNPLAGGLFsgkyktkdipaegrysnqsshgtLYRGRYFKDA 241
Cdd:cd19096 155 DFDFVQLQ---YNYLDQENQagRPGIEYAAKKGMGVIIMEPLKGGGL-----------------------ANNPPEALAI 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 242 TFDAlrliepvaerhGLTMPEIAFRWIHHHSALNMkdngrdgVIIGVSSLAQLENNLK 299
Cdd:cd19096 209 LCGA-----------PLSPAEWALRFLLSHPEVTT-------VLSGMSTPEQLDENIA 248
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-316 |
1.56e-17 |
|
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: 81.14 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTFgpdesegaRITSLDDFNKCLDHLQQQGYNEVDTARVY-----VGGKQEAFTAQARWKERGLTLATKWYPHTPG 87
Cdd:cd19136 3 ILGLGTF--------RLRGEEEVRQAVDAALKAGYRLIDTASVYrneadIGKALRDLLPKYGLSREDIFITSKLAPKDQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 88 AHKAdvlRENLERSLKELQTDQVDIFYLH--------------AADRsvpfAETLEAVNELHKEGKFVQLGLSNYTAFEV 153
Cdd:cd19136 75 YEKA---RAACLGSLERLGTDYLDLYLIHwpgvqglkpsdprnAELR----RESWRALEDLYKEGKLRAIGVSNYTVRHL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 154 AEIVILCNergwVRPTIYQAMYNAitRNIETELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysnqsshgtly 233
Cdd:cd19136 148 EELLKYCE----VPPAVNQVEFHP--HLVQKELLKFCKDHGIHLQAYSSLGSG--------------------------- 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 234 RGRYFKDATFDAlrliepVAERHGLTMPEIAFRWIHHHSAlnmkdngrdGVIIGVSSLAQLENNLkDIQKGPLPQEVVDV 313
Cdd:cd19136 195 DLRLLEDPTVLA------IAKKYGRTPAQVLLRWALQQGI---------GVIPKSTNPERIAENI-KVFDFELSEEDMAE 258
|
...
gi 1832818259 314 LDQ 316
Cdd:cd19136 259 LNA 261
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
10-310 |
1.62e-17 |
|
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: 81.64 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGpdeseGARITSLDDFNKCLDHLQQQGYNEVDTARVYVGGKQEAF--TAQARWKERGLTLATK--WYPHT 85
Cdd:cd19162 1 PRLGLGAASLG-----NLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRlgAALARHPRAEYVVSTKvgRLLEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 86 PGAHK-----------ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFA--ETLEAVNELHKEGKFVQLGL---SNYT 149
Cdd:cd19162 76 GAAGRpagadrrfdfsADGIRRSIEASLERLGLDRLDLVFLHDPDRHLLQAltDAFPALEELRAEGVVGAIGVgvtDWAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 150 AFEVAEI----VILCNERgwvrptiyqamYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSgkyktKDIPAEGRYSN 225
Cdd:cd19162 156 LLRAARRadvdVVMVAGR-----------YTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILA-----TDDPAGDRYDY 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 226 QSSHGTLyrgryfkdatFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLkDIQKGP 305
Cdd:cd19162 220 RPATPEV----------LARARRLAAVCRRYGVPLPAAALQFPLRHPAVA-------SVVVGAASPAELRDNL-ALLRTP 281
|
....*
gi 1832818259 306 LPQEV 310
Cdd:cd19162 282 IPAEF 286
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
46-299 |
1.19e-14 |
|
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: 72.77 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvggKQEAFTAQA----RWKERGLTLATKWYPHTPGAHKadvLRENLERSLKELQTDQVDIFYLH--AAD 119
Cdd:cd19139 27 GYRHIDTAQIY---DNEAAVGQAiaesGVPRDELFITTKIWIDNLSKDK---LLPSLEESLEKLRTDYVDLTLIHwpSPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 120 RSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERgwvrptiyqamyNAITRNIE-------TELIPACKR 192
Cdd:cd19139 101 DEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAG------------AIATNQIElspylqnRKLVAHCKQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 193 YGIDIVVYNPLAgglfsgkyktkdipaegrysnqsshgtlyRGRYFKDATfdalrlIEPVAERHGLTMPEIAFRWIHHhs 272
Cdd:cd19139 169 HGIHVTSYMTLA-----------------------------YGKVLDDPV------LAAIAERHGATPAQIALAWAMA-- 211
|
250 260
....*....|....*....|....*...
gi 1832818259 273 alnmkdngRDGVIIGVSS-LAQLENNLK 299
Cdd:cd19139 212 --------RGYAVIPSSTkREHLRSNLL 231
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
44-207 |
1.70e-13 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 69.75 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVY-----VG-GKQEAFTAQARWKERGLTLATK-WYPHtpgaHKADVLRENLERSLKELQTDQVDIFYLH 116
Cdd:cd19118 31 KAGYRHLDLAKVYqnqheVGqALKELLKEEPGVKREDLFITSKlWNNS----HRPEYVEPALDDTLKELGLDYLDLYLIH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 ------------------------AADRSVPFAETLEAVNELHKEGKFVQLGLSNytaFEVAEIVILCNERGwVRPTIYQ 172
Cdd:cd19118 107 wpvafkptgdlnpltavptnggevDLDLSVSLVDTWKAMVELKKTGKVKSIGVSN---FSIDHLQAIIEETG-VVPAVNQ 182
|
170 180 190
....*....|....*....|....*....|....*
gi 1832818259 173 AMYNAitRNIETELIPACKRYGIDIVVYNPLAGGL 207
Cdd:cd19118 183 IEAHP--LLLQDELVDYCKSKNIHITAYSPLGNNL 215
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
42-206 |
8.56e-13 |
|
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: 67.35 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 42 LQQQGYNEVDTARVYvggKQEAFTAQArWKERGLT-----LATKWYPHTPGAHKAdvlRENLERSLKELQTDQVDIFYLH 116
Cdd:cd19135 35 LKECGYRHIDTAKRY---GCEELLGKA-IKESGVPredlfLTTKLWPSDYGYEST---KQAFEASLKRLGVDYLDLYLLH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 AADRSVP-------FAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRniETELIPA 189
Cdd:cd19135 108 WPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS----VVPHVNQVEFHPFQN--PVELIEY 181
|
170
....*....|....*..
gi 1832818259 190 CKRYGIDIVVYNPLAGG 206
Cdd:cd19135 182 CRDNNIVFEGYCPLAKG 198
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
46-267 |
2.53e-12 |
|
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: 66.10 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvggKQEAFTAQArWKERG-----LTLATKWYPHTPgahkaDVlRENLERSLKELQTDQVDIFYLH---- 116
Cdd:cd19120 38 GFRHIDTAEMY---GNEKEVGEA-LKESGvpredLFITTKVSPGIK-----DP-REALRKSLAKLGVDYVDLYLIHspff 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRNIETELIPACKRYGID 196
Cdd:cd19120 108 AKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPYLYPQQPALLEYCREHGIV 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 197 IVVYNPLAgglfsgkyktkdiPAegrysNQSSHGTLyrgryfkDATFDALrliepvAERHGLTMPEIAFRW 267
Cdd:cd19120 184 VSAYSPLS-------------PL-----TRDAGGPL-------DPVLEKI------AEKYGVTPAQVLLRW 223
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
46-267 |
4.67e-12 |
|
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: 65.83 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVY-----VG-GKQEAFTAQARwKERGLTLATK-WYP-HTPgahkADVlRENLERSLKELQTDQVDIFYLH- 116
Cdd:cd19125 37 GYRHIDCAAIYgnekeIGkALKKLFEDGVV-KREDLFITSKlWCTdHAP----EDV-PPALEKTLKDLQLDYLDLYLIHw 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 -----------AADRSVPF--AETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRNie 183
Cdd:cd19125 111 pvrlkkgahmpEPEEVLPPdiPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQ-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 184 TELIPACKRYGIDIVVYNPLAgglfsgkyktkdipaegrysnqSSHGTLYRGRYFKDATfdalrlIEPVAERHGLTMPEI 263
Cdd:cd19125 185 DKLHEFCKSKGIHLSAYSPLG----------------------SPGTTWVKKNVLKDPI------VTKVAEKLGKTPAQV 236
|
....
gi 1832818259 264 AFRW 267
Cdd:cd19125 237 ALRW 240
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
13-267 |
7.41e-12 |
|
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: 64.52 E-value: 7.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTF---GPDESEGARITSLDDfnkcldhlqqqGYNEVDTARVYvggKQEAFTAQArWKERG-----LTLATKWYPH 84
Cdd:cd19133 11 ILGFGVFqipDPEECERAVLEAIKA-----------GYRLIDTAAAY---GNEEAVGRA-IKKSGipreeLFITTKLWIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 85 TPGAHKAdvlRENLERSLKELQTDQVDIFYLHAadrsvPFA---ETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCN 161
Cdd:cd19133 76 DAGYEKA---KKAFERSLKRLGLDYLDLYLIHQ-----PFGdvyGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHNE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 162 ergwVRPTIYQamynaitrnIET-------ELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysnqsshgtlyR 234
Cdd:cd19133 148 ----VKPAVNQ---------IEThpfnqqiEAVEFLKKYGVQIEAWGPFAEG---------------------------R 187
|
250 260 270
....*....|....*....|....*....|...
gi 1832818259 235 GRYFKDAtfdalrLIEPVAERHGLTMPEIAFRW 267
Cdd:cd19133 188 NNLFENP------VLTEIAEKYGKSVAQVILRW 214
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
46-218 |
1.59e-11 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 64.06 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvGGKQEAFTAQARWKERG------LTLATKWYPHtpgAHKADVLRENLERSLKELQTDQVDIFYLHAA- 118
Cdd:cd19111 30 GYRHIDTALSY-QNEKAIGEALKWWLKNGklkreeVFITTKLPPV---YLEFKDTEKSLEKSLENLKLPYVDLYLIHHPc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 119 ------------DRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILcnerGWVRPTIYQAMYNAITRniETEL 186
Cdd:cd19111 106 gfvnkkdkgereLASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAY----AKVKPSNLQLECHAYLQ--QREL 179
|
170 180 190
....*....|....*....|....*....|..
gi 1832818259 187 IPACKRYGIDIVVYNPLAGGLFSGKYKTKDIP 218
Cdd:cd19111 180 RKFCNKKNIVVTAYAPLGSPGRANQSLWPDQP 211
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
44-267 |
5.10e-11 |
|
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: 62.81 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYvgGKQEAF-TAQARWKERG------LTLATKWYPHtpgAHKADVLRENLERSLKELQTDQVDIFYLH 116
Cdd:cd19154 36 KAGYRLIDTAFLY--QNEEAIgEALAELLEEGvvkredLFITTKLWTH---EHAPEDVEEALRESLKKLQLEYVDLYLIH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 A-------------------ADRSVPFAETLEAVNELHKEGKFVQLGLSNytaFEVAEIV-ILCNERgwVRPTIYQamyn 176
Cdd:cd19154 111 ApaafkddegesgtmengmsIHDAVDVEDVWRGMEKVYDEGLTKAIGVSN---FNNDQIQrILDNAR--VKPHNNQ---- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 177 aitrnIET-------ELIPACKRYGIDIVVYNPLAgglfsgkyktkdipAEGRYSNQSSHGTLYRGRYFKDATFDALrli 249
Cdd:cd19154 182 -----VEChlyfpqkELVEFCKKHNISVTSYATLG--------------SPGRANFTKSTGVSPAPNLLQDPIVKAI--- 239
|
250
....*....|....*...
gi 1832818259 250 epvAERHGLTMPEIAFRW 267
Cdd:cd19154 240 ---AEKHGKTPAQVLLRY 254
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
75-315 |
2.28e-10 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 60.75 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 75 LTLATK----------WYPhtpgAHKADVLRENLERSLKELQTDQVDI------FYLHA-ADRSVpfAETLEAVNELHKE 137
Cdd:PRK10376 83 LTIVTKvgarrgedgsWLP----AFSPAELRRAVHDNLRNLGLDVLDVvnlrlmGDGHGpAEGSI--EEPLTVLAELQRQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 138 GKFVQLGLSNYTAFEVAE---IV-ILCnergwvrptiYQAMYNAITRNiETELIPACKRYGIDIVVYNPLAGglFSgkyk 213
Cdd:PRK10376 157 GLVRHIGLSNVTPTQVAEarkIAeIVC----------VQNHYNLAHRA-DDALIDALARDGIAYVPFFPLGG--FT---- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 214 tkdiPAegrysnQSShgTLYRgryfkdatfdalrliepVAERHGLTMPEIAFRWIHHHSAlNMKdngrdgVIIGVSSLAQ 293
Cdd:PRK10376 220 ----PL------QSS--TLSD-----------------VAASLGATPMQVALAWLLQRSP-NIL------LIPGTSSVAH 263
|
250 260
....*....|....*....|....
gi 1832818259 294 LENNLK--DIQkgpLPQEVVDVLD 315
Cdd:PRK10376 264 LRENLAaaELV---LSEEVLAELD 284
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
7-267 |
3.14e-10 |
|
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: 59.69 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 7 SATPRVILGLMTFGPDESEGARITSLddfnkcldhlqQQGYNEVDTARVY---VG-GKQEAFTAQARwKErgLTLATK-W 81
Cdd:cd19131 8 NTIPQLGLGVWQVSNDEAASAVREAL-----------EVGYRSIDTAAIYgneEGvGKAIRASGVPR-EE--LFITTKlW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 82 yphtPGAHKADVLRENLERSLKELQTDQVDIFYLH----AADRsvpFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIV 157
Cdd:cd19131 74 ----NSDQGYDSTLRAFDESLRKLGLDYVDLYLIHwpvpAQDK---YVETWKALIELKKEGRVKSIGVSNFTIEHLQRLI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 158 ilcNERGwVRPTIYQamynaitrnIE-------TELIPACKRYGIDIVVYNPLAGglfsgkyktkdipaegrysnqsshg 230
Cdd:cd19131 147 ---DETG-VVPVVNQ---------IElhprfqqRELRAFHAKHGIQTESWSPLGQ------------------------- 188
|
250 260 270
....*....|....*....|....*....|....*..
gi 1832818259 231 tlyrGRYFKDATfdalrlIEPVAERHGLTMPEIAFRW 267
Cdd:cd19131 189 ----GGLLSDPV------IGEIAEKHGKTPAQVVIRW 215
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
19-209 |
1.49e-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: 58.33 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 19 FGP-DESEGARItslddFNKCLDhlqqQGYNEVDTARVYVGGKQEAFTAQARW--KERGLTLATKWYPHTPGAHK----- 90
Cdd:cd19163 27 FGPvDEEEAIRT-----VHEALD----SGINYIDTAPWYGQGRSETVLGKALKgiPRDSYYLATKVGRYGLDPDKmfdfs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 ADVLRENLERSLKELQTDQVDIFYLH----AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVilcnERGWV 166
Cdd:cd19163 98 AERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGITGYPLDVLKEVL----ERSPV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1832818259 167 RptIYQAM-YNAITRNIET--ELIPACKRYGIDIVVYNPLAGGLFS 209
Cdd:cd19163 174 K--IDTVLsYCHYTLNDTSllELLPFFKEKGVGVINASPLSMGLLT 217
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
1-203 |
4.89e-09 |
|
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: 56.62 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 1 MPLVvpsatprvilGLMTF--GPDESEGARITSLDdfnkcldhlqqQGYNEVDTARVY-----VG-GKQEAFTAQARWKE 72
Cdd:cd19106 7 MPLI----------GLGTWksKPGQVKAAVKYALD-----------AGYRHIDCAAVYgneqeVGeALKEKVGPGKAVPR 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 73 RGLTLATK-WypHTpgAHKADVLRENLERSLKELQTDQVDIFYLH---AADR----------------SVPFAETLEAVN 132
Cdd:cd19106 66 EDLFVTSKlW--NT--KHHPEDVEPALRKTLKDLQLDYLDLYLIHwpyAFERgdnpfpknpdgtirydSTHYKETWKAME 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 133 ELHKEGKFVQLGLSNYTAFEVAEIVilcnERGWVRPTIYQAM---YNAitrniETELIPACKRYGIDIVVYNPL 203
Cdd:cd19106 142 KLVDKGLVKAIGLSNFNSRQIDDIL----SVARIKPAVLQVEchpYLA-----QNELIAHCKARGLVVTAYSPL 206
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
91-299 |
7.87e-09 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 56.08 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 ADVLRENLERSLKELQTDQVDIFYLHAADRSVPFAETLE-----------AVNELHKEGKFVQLGL-SNytafeVAEIVI 158
Cdd:cd19152 102 YDGILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEhfaqaikgafrALEELREEGVIKAIGLgVN-----DWEVIL 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 159 LCNERG---WVrptiyqaM----YNAITRNIETELIPACKRYGIDIVVYNPLAGGLFSGkyktkdipaegrysnqSSHGT 231
Cdd:cd19152 177 RILEEAdldWV-------MlagrYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAG----------------GDNFD 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1832818259 232 LYRGRYFKDATFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLK 299
Cdd:cd19152 234 YYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVA-------SVAPGASSPERVEENVA 294
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
22-206 |
1.36e-08 |
|
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: 55.14 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 22 DESEGARITSLDDfnkcldhlqqqGYNEVDTARVYvggKQEAFTAQArWKERG-----LTLATKWYPHTPGAHKAdvlRE 96
Cdd:cd19126 23 DETERAVQTALEN-----------GYRSIDTAAIY---KNEEGVGEA-IRESGvpreeLFVTTKLWNDDQRARRT---ED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 97 NLERSLKELQTDQVDIFYLH--AADRsvpFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAM 174
Cdd:cd19126 85 AFQESLDRLGLDYVDLYLIHwpGKDK---FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVE 157
|
170 180 190
....*....|....*....|....*....|..
gi 1832818259 175 YNAITRNieTELIPACKRYGIDIVVYNPLAGG 206
Cdd:cd19126 158 FHPYLTQ--KELRGYCKSKGIVVEAWSPLGQG 187
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
41-203 |
4.95e-08 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 53.69 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 41 HLQQQGYNEVDTARVY-----VG-GKQEAFTAQARWKErgLTLATK-WYPHTPGAHKAdvlrenLERSLKELQTDQVDIF 113
Cdd:cd19121 33 HALKIGYRHIDGALCYqnedeVGeGIKEAIAGGVKRED--LFVTTKlWSTYHRRVELC------LDRSLKSLGLDYVDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 114 YLHAADRSVP----------------------FAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVilcnERGWVRPTIY 171
Cdd:cd19121 105 LVHWPVLLNPngnhdlfptlpdgsrdldwdwnHVDTWKQMEKVLKTGKTKAIGVSNYSIPYLEELL----KHATVVPAVN 180
|
170 180 190
....*....|....*....|....*....|..
gi 1832818259 172 QAMYNAITRniETELIPACKRYGIDIVVYNPL 203
Cdd:cd19121 181 QVENHPYLP--QQELVDFCKEKGILIEAYSPL 210
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
46-267 |
1.23e-07 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 52.39 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvggKQEAFTAQArWKERG-----LTLATK-W-----YPHTPGAhkadvlrenLERSLKELQTDQVDIFY 114
Cdd:cd19157 37 GYRSIDTAAIY---GNEEGVGKG-IKESGipreeLFITSKvWnadqgYDSTLKA---------FEASLERLGLDYLDLYL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 115 LHAADRSVpFAETLEAVNELHKEGKFVQLGLSNYTA------FEVAEIVilcnergwvrPTIYQAMYNAitRNIETELIP 188
Cdd:cd19157 104 IHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVhhledlLADAEIV----------PMVNQVEFHP--RLTQKELRD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 189 ACKRYGIDIVVYNPL-AGGLFsgkyktkDIPaegrysnqsshgtlyrgryfkdatfdalrLIEPVAERHGLTMPEIAFRW 267
Cdd:cd19157 171 YCKKQGIQLEAWSPLmQGQLL-------DNP-----------------------------VLKEIAEKYNKSVAQVILRW 214
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
13-268 |
1.37e-07 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 52.53 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTF-GPDEsegaritsldDFNKCLDHLQQQGYNEVDTARVY-----VGGKQEAFTAQARWKERGLTLATKWyphTP 86
Cdd:cd19155 14 VVGLGTWqSSPE----------EIETAVDTALEAGYRHIDTAYVYrneaaIGNVLKKWIDSGKVKREELFIVTKL---PP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 87 GAHKADVLRENLERSLKELQTDQVDIFYLHAA---------------------DRSVPFAETLEAVNELHKEGKFVQLGL 145
Cdd:cd19155 81 GGNRREKVEKFLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 146 SNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRniETELIPACKRYGIDIVVYNPLAGGLFSGKYKTKDIPAEgrysn 225
Cdd:cd19155 161 SNFNREQMARILKNAR----IKPANLQVELHVYLQ--QKDLVDFCSTHSITVTAYAPLGSPGAAHFSPGTGSPSG----- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1832818259 226 qsshgtlyrgryfkdATFDALR--LIEPVAERHGLTMPEIAFRWI 268
Cdd:cd19155 230 ---------------SSPDLLQdpVVKAIAERHGKSPAQVLLRWL 259
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
10-299 |
2.03e-07 |
|
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: 51.75 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDdfnkcldhlqqQGYNEVDTARVY-----VG-GKQEAFTaQARWKERGLTLATKWYP 83
Cdd:cd19128 2 PRLGFGTYKITESESKEAVKNAIK-----------AGYRHIDCAYYYgneafIGiAFSEIFK-DGGVKREDLFITSKLWP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 84 HTpgaHKADVLRENLERSLKELQTDQVDIFYLH-------------------AADRSVPFAETLEAVNELHKEGKFVQLG 144
Cdd:cd19128 70 TM---HQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 145 LSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRNieTELIPACKRYGIDIVVYNPLAgglfsgkyktkdipaegrys 224
Cdd:cd19128 147 VSNYSTKLLTDLLNYCK----IKPFMNQIECHPYFQN--DKLIKFCIENNIHVTAYRPLG-------------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1832818259 225 nqsshgtlyrGRYFKDA-TFDALRLIEPVAERHGLTMPEIAFRWiHHHSALNMKdngrdGVIIGVSSLAQLENNLK 299
Cdd:cd19128 201 ----------GSYGDGNlTFLNDSELKALATKYNTTPPQVIIAW-HLQKWPKNY-----SVIPKSANKSRCQQNFD 260
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
44-303 |
3.04e-07 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 51.17 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVYVGGKQEAFTAQA-RWKERG-LTLATK------------------WYPHTPGAHKAD-----VLReNL 98
Cdd:cd19161 31 DSGIRYFDTAPMYGHGLAEHRLGDFlREKPRDeFVLSTKvgrllkparegsvpdpngFVDPLPFEIVYDysydgIMR-SF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 99 ERSLKELQTDQVDIFYLHAADR--------SVPFAET----LEAVNELHKEG--KFVQLGLSNY----TAFEVAEI-VIL 159
Cdd:cd19161 110 EDSLQRLGLNRIDILYVHDIGVythgdrkeRHHFAQLmsggFKALEELKKAGviKAFGLGVNEVqiclEALDEADLdCFL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 160 CNERgwvrptiyqamYNAITRNIETELIPACKRYGIDIVVYNPLAGGLFS------GKYKTKDIPAEgrysnqsshgtly 233
Cdd:cd19161 190 LAGR-----------YSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILAtgtksgAKFNYGDAPAE------------- 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 234 rgryfkdaTFDALRLIEPVAERHGLTMPEIAFRWIHHHSALNmkdngrdGVIIGVSSLAQLENNLKDIQK 303
Cdd:cd19161 246 --------IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVA-------SVLTGARNPAQLRQNVEAFQT 300
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
13-267 |
3.82e-07 |
|
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: 50.74 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTF---GPDESEGARITSLDDfnkcldhlqqqGYNEVDTARVYvggKQEAFTAQA---RWKERGLT-----LATK- 80
Cdd:cd19116 13 AIALGTWklkDDEGVRQAVKHAIEA-----------GYRHIDTAYLY---GNEAEVGEAireKIAEGVVKredlfITTKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 81 WYPHtpgaHKADVLRENLERSLKELQTDQVDIFYLH----------------AADRSVPFAETLEAVNELHKEGKFVQLG 144
Cdd:cd19116 79 WNSY----HEREQVEPALRESLKRLGLDYVDLYLIHwpvafkenndsesngdGSLSDIDYLETWRGMEDLVKLGLTRSIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 145 LSNYTAFEVAEIVILCNergwVRPTIYQAMYNAitRNIETELIPACKRYGIDIVVYNPLagglfsGKYKTKdipaegrys 224
Cdd:cd19116 155 VSNFNSEQINRLLSNCN----IKPAVNQIEVHP--TLTQEKLVAYCQSNGIVVMAYSPF------GRLVPR--------- 213
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1832818259 225 nqsshGTLYRGRYFKDATFDALrliepvAERHGLTMPEIAFRW 267
Cdd:cd19116 214 -----GQTNPPPRLDDPTLVAI------AKKYGKTTAQIVLRY 245
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
56-206 |
4.71e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 50.78 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 56 YVGGKQEAFTAQARWKERGLTLATK-WYPHTPGAH--KADVLRENLERSLKELQTDQVDIFYLHAADRSVP--------- 123
Cdd:cd19099 79 YIPGDGDEPLRPLKYLEEKLGRGLIdVADSAGLRHciSPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefyd 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 124 -FAETLEAVNELHKEGKFVQLGLSNYTAFEV----------AEIVILCNERGWVRPTIY--QAMYN-----AITRNIE-- 183
Cdd:cd19099 159 rLEEAFEALEEAVAEGKIRYYGISTWDGFRAppalpghlslEKLVAAAEEVGGDNHHFKviQLPLNllepeALTEKNTvk 238
|
170 180
....*....|....*....|....*.
gi 1832818259 184 ---TELIPACKRYGIDIVVYNPLAGG 206
Cdd:cd19099 239 geaLSLLEAAKELGLGVIASRPLNQG 264
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
46-207 |
4.89e-07 |
|
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: 50.53 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVY-----VG-GKQEAFTAqARWKERGLTLATK-WYPHtpgaHKADVLRENLERSLKELQTDQVDIFYLHAA 118
Cdd:cd19129 32 GFRHFDCAERYrneaeVGeAMQEVFKA-GKIRREDLFVTTKlWNTN----HRPERVKPAFEASLKRLQLDYLDLYLIHTP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 119 --------------------DRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVilcnERGWVRPTIYQAMYNAI 178
Cdd:cd19129 107 fafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIF----EAARIKPAVVQVESHPY 182
|
170 180
....*....|....*....|....*....
gi 1832818259 179 TRniETELIPACKRYGIDIVVYNPLAGGL 207
Cdd:cd19129 183 LP--EWELLDFCKNHGIVLQAFAPLGHGM 209
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
44-269 |
6.70e-07 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 49.96 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 44 QQGYNEVDTARVY-----VG-GKQEAFTAQARWKERGLTLATKWYPHTpgAHKADVLrENLERSLKELQTDQVDIFYLH- 116
Cdd:cd19124 31 EVGYRHFDTAAAYgteeaLGeALAEALRLGLVKSRDELFVTSKLWCSD--AHPDLVL-PALKKSLRNLQLEYVDLYLIHw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 -----AADRSVPFAE----------TLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRn 181
Cdd:cd19124 108 pvslkPGKFSFPIEEedflpfdikgVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNPAWQ- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 182 iETELIPACKRYGIDIVVYNPLAGGlfsgkyktkdipaegrysnqsshGTlyrgRYFKDATFDALRLIEpVAERHGLTMP 261
Cdd:cd19124 183 -QKKLREFCKANGIHVTAYSPLGAP-----------------------GT----KWGSNAVMESDVLKE-IAAAKGKTVA 233
|
....*...
gi 1832818259 262 EIAFRWIH 269
Cdd:cd19124 234 QVSLRWVY 241
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
46-298 |
8.71e-07 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 49.84 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYVGGKQEAFTAQA----RWKERGLTLATKWYPHTPGAHK--ADVLRENLERSLKELQTDQVDIFYLHA-- 117
Cdd:cd19153 46 GINHFDTSPYYGAESSEAVLGKAlaalQVPRSSYTVATKVGRYRDSEFDysAERVRASVATSLERLHTTYLDVVYLHDie 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 118 -ADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERGwvrPTIYQAMYNAITRNIETELIPACKRYGID 196
Cdd:cd19153 126 fVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLDTLTRATRRCSPGS---LDAVLSYCHLTLQDARLESDAPGLVRGAG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 197 IVVYN--PLAGGLFSGKYKTKDIPAEGrysnqsshgtlyrgryfkdatfdALRLIEPVAERH----GLTMPEIAFRWihh 270
Cdd:cd19153 203 PHVINasPLSMGLLTSQGPPPWHPASG-----------------------ELRHYAAAADAVcasvEASLPDLALQY--- 256
|
250 260
....*....|....*....|....*...
gi 1832818259 271 hsALNMKdNGRDGVIIGVSSLAQLENNL 298
Cdd:cd19153 257 --SLAAH-AGVGTVLLGPSSLAQLRSML 281
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
46-203 |
1.18e-06 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 49.34 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVY-----VG-GKQEAFTAQARWKERGLTLATKWyphtPGAHKADVLRENLERSLKELQTDQVDIFYLH--- 116
Cdd:cd19107 30 GYRHIDCAYVYqneneVGeAIQEKIKEQVVKREDLFIVSKLW----CTFHEKGLVKGACQKTLSDLKLDYLDLYLIHwpt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 ---AADRSVP-------------FAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVilcNERGwvrptiyqAMYNAITR 180
Cdd:cd19107 106 gfkPGKELFPldesgnvipsdttFLDTWEAMEELVDEGLVKAIGVSNFNHLQIERIL---NKPG--------LKYKPAVN 174
|
170 180 190
....*....|....*....|....*....|
gi 1832818259 181 NIET-------ELIPACKRYGIDIVVYNPL 203
Cdd:cd19107 175 QIEChpyltqeKLIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
2-226 |
2.53e-06 |
|
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: 48.37 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 2 PLVVPSATPRVILGLMTFGPDESEGARITSLDdfnkcldhlqqQGYNEVDTARVY-----VG--------GKQEAFTAQA 68
Cdd:cd19130 3 VLNDGNSIPQLGYGVFKVPPADTQRAVATALE-----------VGYRHIDTAAIYgneegVGaaiaasgiPRDELFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 69 RWKERgltlatkwyphtpgaHKADVLRENLERSLKELQTDQVDIFYLH----AADRsvpFAETLEAVNELHKEGKFVQLG 144
Cdd:cd19130 72 LWNDR---------------HDGDEPAAAFAESLAKLGLDQVDLYLVHwptpAAGN---YVHTWEAMIELRAAGRTRSIG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 145 LSNytaFEVAEIVILCNERGWVrPTIYQ-AMYNAITRNIETElipACKRYGIDIVVYNPLA-GGLFSGKYKTKDIPAEGR 222
Cdd:cd19130 134 VSN---FLPPHLERIVAATGVV-PAVNQiELHPAYQQRTIRD---WAQAHDVKIEAWSPLGqGKLLGDPPVGAIAAAHGK 206
|
....
gi 1832818259 223 YSNQ 226
Cdd:cd19130 207 TPAQ 210
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
10-267 |
8.51e-06 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 46.72 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDDfnkcldhlqqqGYNEVDTARVYVGGKQ--EAFTAQARWKERgLTLATK-W--YPH 84
Cdd:cd19117 15 PAVGLGTWQSKPNEVAKAVEAALKA-----------GYRHIDTAAIYGNEEEvgQGIKDSGVPREE-IFITTKlWctWHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 85 TPgahkadvlRENLERSLKELQTDQVDIFYLHAADRSVP---------------------FAETLEAVNELHKEGKFVQL 143
Cdd:cd19117 83 RV--------EEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVKAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 144 GLSNYTAFEVAEivILCNERGWVRPTIYQAMYNAItrNIETELIPACKRYGIDIVVYNPLAgglfsgkyktkdipaegry 223
Cdd:cd19117 155 GVSNFSIKNLEK--LLASPSAKIVPAVNQIELHPL--LPQPKLVDFCKSKGIHATAYSPLG------------------- 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1832818259 224 snqSSHGTLYRgryfkdatfdaLRLIEPVAERHGLTMPEIAFRW 267
Cdd:cd19117 212 ---STNAPLLK-----------EPVIIKIAKKHGKTPAQVIISW 241
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
14-206 |
1.05e-05 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 46.72 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFGPDESEGaritsldDFNKCLDHLQQQGYNEVDTARVY-----VG-GKQEAFtAQARWKERGLTLATKWYPHTpg 87
Cdd:cd19119 15 LGLGTASPHEDRA-------EVKEAVEAAIKEGYRHIDTAYAYetedfVGeAIKRAI-DDGSIKREELFITTKVWPTF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 88 ahkADVLRENLERSLKELQTDQVDIFYLH-------------------------AADRSVPFAETLEAVNELHKEGKFVQ 142
Cdd:cd19119 85 ---YDEVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftpvnddgktRYAASGDHITTYKQLEKIYLDGRAKA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1832818259 143 LGLSNYTAFEVAEIVILCNergwVRPTIYQamynaitrnIET-------ELIPACKRYGIDIVVYNPLAGG 206
Cdd:cd19119 162 IGVSNYSIVYLERLIKECK----VVPAVNQ---------VELhphlpqmDLRDFCFKHGILVTAYSPLGSH 219
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
95-299 |
1.13e-05 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; 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: 381390 [Multi-domain] Cd Length: 298 Bit Score: 46.50 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 95 RENLERSLKELQTDQVDIFYLHAADrSVPFAETLEAVNELHK---EGKFVQLGLSNYTAFEVAEIVILCNERGwVRPT-- 169
Cdd:cd19164 102 RASVERSLRRLHTDYLDLVYLHDVE-FVADEEVLEALKELFKlkdEGKIRNVGISGYPLPVLLRLAELARTTA-GRPLda 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 170 -IYQAMYNaITRNIETELIPACKRYGIDIVVYN--PLAGGLFSgkyktkdiPAEGRYSNQSSHGtlyrgryFKDATFDAL 246
Cdd:cd19164 180 vLSYCHYT-LQNTTLLAYIPKFLAAAGVKVVLNasPLSMGLLR--------SQGPPEWHPASPE-------LRAAAAKAA 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1832818259 247 RLiepvAERHGLTMPEIAFRWihhhsALNmKDNGRDGVIIGVSSLAQLENNLK 299
Cdd:cd19164 244 EY----CQAKGTDLADVALRY-----ALR-EWGGEGPTVVGCSNVDELEEAVE 286
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
46-206 |
1.29e-05 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 45.97 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYvggKQEAFTAQArWKERG-----LTLATKWYPHTPGAHKAdvlRENLERSLKELQTDQVDIFYLHAAdR 120
Cdd:cd19156 36 GYRHIDTAAIY---KNEEGVGQG-IRESGvpreeVFVTTKLWNSDQGYEST---LAAFEESLEKLGLDYVDLYLIHWP-V 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 121 SVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAItrNIETELIPACKRYGIDIVVY 200
Cdd:cd19156 108 KGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQIELHPL--LTQEPLRKFCKEKNIAVEAW 181
|
....*.
gi 1832818259 201 NPLAGG 206
Cdd:cd19156 182 SPLGQG 187
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
88-267 |
1.64e-05 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 45.86 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 88 AHKADVLRENLERSLKELQTDQVDIFYLH---AADRSVPF---------------AETLEAVNELHKEGKFVQLGLSNYT 149
Cdd:cd19123 82 SHAPEDVLPALEKTLADLQLDYLDLYLMHwpvALKKGVGFpesgedllslspiplEDTWRAMEELVDKGLCRHIGVSNFS 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 150 A------FEVAEIVILCNERGwVRPTIYQamynaitrnieTELIPACKRYGIDIVVYNPLAGGlfsgkyktkDIPAEGRY 223
Cdd:cd19123 162 VkkledlLATARIKPAVNQVE-LHPYLQQ-----------PELLAFCRDNGIHLTAYSPLGSG---------DRPAAMKA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1832818259 224 SNQSshgtlyrgRYFKDATfdalrlIEPVAERHGLTMPEIAFRW 267
Cdd:cd19123 221 EGEP--------VLLEDPV------INKIAEKHGASPAQVLIAW 250
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-206 |
2.67e-05 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 45.23 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLddfnkcldhlqQQGYNEVDTARVYvgGKQEAFTAQARWKE--RG-LTLATK-WYPHt 85
Cdd:cd19134 12 PVIGLGVGELSDDEAERSVSAAL-----------EAGYRLIDTAAAY--GNEAAVGRAIAASGipRGeLFVTTKlATPD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 86 pgaHKADVLRENLERSLKELQTDQVDIFYLH-AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCnerg 164
Cdd:cd19134 78 ---QGFTASQAACRASLERLGLDYVDLYLIHwPAGREGKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT---- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1832818259 165 WVRPTIYQAMYNAITRniETELIPACKRYGIDIVVYNPLAGG 206
Cdd:cd19134 151 FFTPAVNQIELHPLLN--QAELRKVNAQHGIVTQAYSPLGVG 190
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
19-203 |
3.23e-05 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 44.92 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 19 FGPDESEGARITSLDDFNKCLDhlqqQGYNEVDTARVY-----VGGKQEAFTAQ-ARWKERGLTLATKWYPHTpgaHKAD 92
Cdd:cd19122 14 FGTFANEGAKGETYAAVTKALD----VGYRHLDCAWFYlnedeVGDAVRDFLKEnPSVKREDLFICTKVWNHL---HEPE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 93 VLRENLERSLKELQTDQVDIFYLH---AA----DRSVPFAE----------------TLEAVNELHKEGKFVQLGLSNYT 149
Cdd:cd19122 87 DVKWSIDNSLKNLKLDYIDLFLVHwpiAAekndQRSPKLGPdgkyvilkdltenpepTWRAMEEIYESGKAKAIGVSNWT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1832818259 150 AFEVAEIVILCNergwVRPTIYQAMYNAITRNieTELIPACKRYGIDIVVYNPL 203
Cdd:cd19122 167 IPGLKKLLSFAK----VKPHVNQIEIHPFLPN--EELVDYCFSNDILPEAYSPL 214
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
46-205 |
3.25e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 44.95 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYVGGKQEAFTAQARWKE-----RGLTLATK-WYPhtpgAHKADVLRENLERSLKELQTDQVDIFYLH--- 116
Cdd:cd19110 30 GYRHFDCAYLYHNESEVGAGIREKIKEgvvrrEDLFIVSKlWCT----CHKKSLVKTACTRSLKALKLNYLDLYLIHwpm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 ---------AADRS---VP----FAETLEAVNELHKEGKFVQLGLSNYTAFEVAEIVILCNERgwVRPtiyqamynaITR 180
Cdd:cd19110 106 gfkpgepdlPLDRSgmvIPsdtdFLDTWEAMEDLVIEGLVKNIGVSNFNHEQLERLLNKPGLR--VKP---------VTN 174
|
170 180 190
....*....|....*....|....*....|..
gi 1832818259 181 NIE-------TELIPACKRYGIDIVVYNPLAG 205
Cdd:cd19110 175 QIEchpyltqKKLISFCQSRNVSVTAYRPLGG 206
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
14-274 |
7.98e-05 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 43.41 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 14 LGLMTFGPDESEGARitslddfnkCLDHLQQQGYNEVDTARVYV--GGKQEAFtAQARWKERGLTLATKwyphTPGA-HK 90
Cdd:cd19132 10 IGFGTYPLKGDEGVE---------AVVAALQAGYRLLDTAFNYEneGAVGEAV-RRSGVPREELFVTTK----LPGRhHG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 ADVLRENLERSLKELQTDQVDIFYLH----AADRSVpfaETLEAVNELHKEGKFVQLGLSNytaFEVAEIVILCNERGwV 166
Cdd:cd19132 76 YEEALRTIEESLYRLGLDYVDLYLIHwpnpSRDLYV---EAWQALIEAREEGLVRSIGVSN---FLPEHLDRLIDETG-V 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 167 RPTIYQ-AMYNAITRnieTELIPACKRYGIDIVVYNPLagglfsgkyktkdipaeGRYSNQSSHGTLYRgryfkdatfda 245
Cdd:cd19132 149 TPAVNQiELHPYFPQ---AEQRAYHREHGIVTQSWSPL-----------------GRGSGLLDEPVIKA----------- 197
|
250 260
....*....|....*....|....*....
gi 1832818259 246 lrliepVAERHGLTMPEIAFRWIHHHSAL 274
Cdd:cd19132 198 ------IAEKHGKTPAQVVLRWHVQLGVV 220
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
89-267 |
1.31e-04 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 43.20 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 89 HKADVLRENLERSLKELQTDQVDIFYLH---------------------AADR----SVPFAETLEAVNELHKEGKFVQL 143
Cdd:cd19113 82 HDPKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfycgDGDNfvyeDVPILDTWKALEKLVDAGKIKSI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 144 GLSNYTAFEVAEIVILCNergwVRPTIYQAMYNAITRniETELIPACKRYGIDIVVYNPLAGGLF--SGKYKTKDIPaeg 221
Cdd:cd19113 162 GVSNFPGALILDLLRGAT----IKPAVLQIEHHPYLQ--QPKLIEYAQKAGITITAYSSFGPQSFveLNQGRALNTP--- 232
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1832818259 222 rysnqsshgTLyrgryFKDATfdalrlIEPVAERHGLTMPEIAFRW 267
Cdd:cd19113 233 ---------TL-----FEHDT------IKSIAAKHNKTPAQVLLRW 258
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-267 |
3.35e-04 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 41.62 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 10 PRVILGLMTFGPDESEGARITSLDDfnkcldhlqqqGYNEVDTARVYVGGKQ--EAFTaQARWKERGLTLATKWYPHTPG 87
Cdd:cd19127 10 PALGLGVFQTPPEETADAVATALAD-----------GYRLIDTAAAYGNEREvgEGIR-RSGVDRSDIFVTTKLWISDYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 88 AHKAdvlRENLERSLKELQTDQVDIFYLHaadRSVP--FAETLEAVNELHK---EGKFVQLGLSNYTAFEVAEIVilcnE 162
Cdd:cd19127 78 YDKA---LRGFDASLRRLGLDYVDLYLLH---WPVPndFDRTIQAYKALEKllaEGRVRAIGVSNFTPEHLERLI----D 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 163 RGWVRPTIYQAMYNAITrnIETELIPACKRYGIDIVVYNPLAGGLFsgkYKTKDIPAegrysnqsshgtlyRGRYFKDAT 242
Cdd:cd19127 148 ATTVVPAVNQVELHPYF--SQKDLRAFHRRLGIVTQAWSPIGGVMR---YGASGPTG--------------PGDVLQDPT 208
|
250 260
....*....|....*....|....*
gi 1832818259 243 FDALrliepvAERHGLTMPEIAFRW 267
Cdd:cd19127 209 ITGL------AEKYGKTPAQIVLRW 227
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-299 |
4.54e-04 |
|
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: 381324 [Multi-domain] Cd Length: 318 Bit Score: 41.56 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 39 LDHLQQQGYNEVDTARVYvgGKQEAFTA---QARWKERG-LTLATKW---Y---------PHTPGAHKADVLRENLERSl 102
Cdd:cd19098 41 LDAAWAAGVRYFDAARSY--GRAEEFLGswlRSRNIAPDaVFVGSKWgytYtadwqvdaaVHEVKDHSLARLLKQWEET- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 103 KELQTDQVDIFYLHAADRSVPFAETLEAVNELH---KEGKFVQLGLSNYTAFEVAEIVILCNERGwVRP-TIYQAMYNAI 178
Cdd:cd19098 118 RSLLGKHLDLYQIHSATLESGVLEDADVLAALAelkAEGVKIGLSLSGPQQAETLRRALEIEIDG-ARLfDSVQATWNLL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 179 trniETELIPA---CKRYGIDIVVynplagglfsgkyktKDIPAEGRYSNQSShgtlyrgryfkDATFDALR-LIEPVAE 254
Cdd:cd19098 197 ----EQSAGEAleeAHEAGMGVIV---------------KEALANGRLTDRNP-----------SPELAPLMaVLKAVAD 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1832818259 255 RHGLTMPEIAFRWIHHHSALNMkdngrdgVIIGVSSLAQLENNLK 299
Cdd:cd19098 247 RLGVTPDALALAAVLAQPFVDV-------VLSGAATPEQLRSNLR 284
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
46-333 |
8.41e-04 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 40.55 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 46 GYNEVDTARVYVGGKQ------EAFTaQARWKERGLTLATKWYPHTPGahkadVLRENLERSLKELQTDQVDIFYLH--- 116
Cdd:cd19112 37 GYRHFDCAADYKNEKEvgealaEAFK-TGLVKREDLFITTKLWNSDHG-----HVIEACKDSLKKLQLDYLDLYLVHfpv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 117 --------------------AADRSVPFAETLEAVNELHKEGKFVQLGLSNYTAFEVAEivilCNERGWVRPTIYQamyn 176
Cdd:cd19112 111 atkhtgvgttgsalgedgvlDIDVTISLETTWHAMEKLVSAGLVRSIGISNYDIFLTRD----CLAYSKIKPAVNQ---- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 177 aitrnIET-------ELIPACKRYGIDIVVYNPLAGGLfsgkyktkdipaegrySNQSSHGTLyrgryfkdATFDALRLI 249
Cdd:cd19112 183 -----IEThpyfqrdSLVKFCQKHGISVTAHTPLGGAA----------------ANAEWFGSV--------SPLDDPVLK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 250 EpVAERHGLTMPEIAFRW-IHHHSAlnmkdngrdgVIIGVSSLAQLENNLK--DIQKGPLPQEVVDVLDQAWLIAKPtaP 326
Cdd:cd19112 234 D-LAKKYGKSAAQIVLRWgIQRNTA----------VIPKSSKPERLKENIDvfDFQLSKEDMKLIKSLDRKYRTNQP--A 300
|
....*..
gi 1832818259 327 NYWHLDL 333
Cdd:cd19112 301 KFWGIDL 307
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
13-116 |
8.98e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 40.68 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 13 ILGLMTFGPDE---SEGARITSLddfnkCLDhlqqQGYNEVDTARVY-----VGGKQEAFTAQARWKERGLTLATK-Wyp 83
Cdd:cd19108 13 VLGFGTYAPEEvpkSKALEATKL-----AID----AGFRHIDSAYLYqneeeVGQAIRSKIADGTVKREDIFYTSKlW-- 81
|
90 100 110
....*....|....*....|....*....|...
gi 1832818259 84 htPGAHKADVLRENLERSLKELQTDQVDIFYLH 116
Cdd:cd19108 82 --CTFHRPELVRPALEKSLKKLQLDYVDLYLIH 112
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
91-211 |
4.52e-03 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 38.61 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1832818259 91 ADVLRENLERSLKELQTDQVDIFYLH-----AADRSVpfAETLEAVNELHKEGKFVQLGLSNYTaFEVAEIVILCNERGW 165
Cdd:PLN02587 94 AERVTKSVDESLARLQLDYVDILHCHdiefgSLDQIV--NETIPALQKLKESGKVRFIGITGLP-LAIFTYVLDRVPPGT 170
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1832818259 166 VRPTIYQAMYNAITRNIEtELIPACKRYGIDIVVYNPLAGGLFSGK 211
Cdd:PLN02587 171 VDVILSYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTEN 215
|
|
| |
