|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-324 |
0e+00 |
|
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: 543.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVIS 80
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19143 81 TKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIYVK 239
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKyGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 240 HFYQqilgdpEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEVEQ 319
Cdd:cd19143 241 DRKE------ELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVME 314
|
....*
gi 124399033 320 KIESI 324
Cdd:cd19143 315 KIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-307 |
1.30e-121 |
|
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: 352.28 E-value: 1.30e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQDIVISTKIYGGDGn 89
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWP--RESYVISTKVFWPTG- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 DFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICD 169
Cdd:cd19074 78 PGPNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 170 RLSLHKPVVEQPQYNMMVRDRFEWEYESVFASGYGSTIWSPLYQGLLTGKYNDDIL--ADGRFNNSDNiyvKHFYQQILG 247
Cdd:cd19074 158 QFGLIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPppSRSRATDEDN---RDKKRRLLT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 248 DpekrtKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSV 307
Cdd:cd19074 235 D-----ENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-329 |
3.01e-105 |
|
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: 311.34 E-value: 3.01e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNT--KIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQDIV 78
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWGGVDEAEaiAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRP--RDDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTKIyGGDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:COG0667 79 IATKV-GRRMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 159 QQIHQAIGICDrlSLHKPVVEQPQYNMMVRdRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDD--ILADGRFNNSdn 235
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDR-SAEEELLPAARElGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATN-- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 236 iyvkhfyqqiLGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITK 315
Cdd:COG0667 233 ----------FVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE--LSA 300
|
330
....*....|....
gi 124399033 316 EVEQKIESILSNKP 329
Cdd:COG0667 301 EDLAALDAALAAVP 314
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
3-317 |
5.96e-91 |
|
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: 274.71 E-value: 5.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVISTK 82
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 83 IY-GGDGNdfpNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQI 161
Cdd:cd19141 82 IFwGGKAE---TERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 162 HQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIYVKh 240
Cdd:cd19141 159 MEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKiGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLK- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 241 fyQQILGDPEKRTkiQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEV 317
Cdd:cd19141 238 --EKILSEEGRRQ--QAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-329 |
1.19e-88 |
|
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: 269.55 E-value: 1.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVIS 80
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGNDfpNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19160 83 TKIYWGGQAE--TERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIYVK 239
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKiGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 240 HFYQQilgdpEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEVEQ 319
Cdd:cd19160 241 EKVQS-----EEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVM 315
|
330
....*....|
gi 124399033 320 KIESILSNKP 329
Cdd:cd19160 316 EIDALLGNKP 325
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-329 |
5.31e-88 |
|
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: 267.68 E-value: 5.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVIS 80
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGNDfpNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19159 81 TKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIYVK 239
Cdd:cd19159 159 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 240 hfyQQILGdpEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEVEQ 319
Cdd:cd19159 239 ---ERIVS--EEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVN 313
|
330
....*....|
gi 124399033 320 KIESILSNKP 329
Cdd:cd19159 314 EIDNILRNKP 323
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-324 |
1.02e-84 |
|
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: 258.66 E-value: 1.02e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYG--NWVNSDDKDTqdrNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIV 78
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGtmNFGGRTDEET---SFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTKIYGGDGNDfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:cd19087 75 LATKVFGPMGDD-PNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 159 QQIHQAIGICDRLSLHKPVVEQPQYNMMVRdRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYnddilADGRFNNSDNIY 237
Cdd:cd19087 154 WQIAKAQGIAARRGLLRFVSEQPMYNLLKR-QAELEILPAARAyGLGVIPYSPLAGGLLTGKY-----GKGKRPESGRLV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 238 VKHFYQQILGDPEKRTKIQnqlkQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEV 317
Cdd:cd19087 228 ERARYQARYGLEEYRDIAE----RFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT--LTPEL 301
|
....*..
gi 124399033 318 EQKIESI 324
Cdd:cd19087 302 LAEIDEL 308
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-329 |
2.74e-81 |
|
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: 250.39 E-value: 2.74e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVIS 80
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGNDfpNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19158 81 TKIFWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIYVK 239
Cdd:cd19158 159 IMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 240 hfyQQILGDPEKRTkiQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEVEQ 319
Cdd:cd19158 239 ---DKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVH 313
|
330
....*....|
gi 124399033 320 KIESILSNKP 329
Cdd:cd19158 314 EIDSILGNKP 323
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
2-309 |
6.15e-81 |
|
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: 249.04 E-value: 6.15e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 2 EYRRLGATGLKVSAI-----SYG----NWVNSDDKDTQdrntKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlNV 72
Cdd:cd19079 1 EYVRLGNSGLKVSRLclgcmSFGdpkwRPWVLDEEESR----PIIKRALDLGINFFDTANVYSGGASEEILGRALKE-FA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 73 QRQDIVISTKIYGgDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWG 152
Cdd:cd19079 76 PRDEVVIATKVYF-PMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 153 TSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRdrfEWEYESV---FASGYGSTIWSPLYQGLLTGKYNDdilaDGR 229
Cdd:cd19079 155 ASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYR---EEEREMIplcEEEGIGVIPWSPLARGRLARPWGD----TTE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 230 FNNSDNIYVKHFYqqiLGDPEKRTKIqnqLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQV 309
Cdd:cd19079 228 RRRSTTDTAKLKY---DYFTEADKEI---VDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-319 |
7.36e-80 |
|
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: 246.76 E-value: 7.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYG------------NWVNSDDKDTqdrnTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALK 68
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGtmtfgggggffgAWGGVDQEEA----DRLVDIALDAGINFFDTADVYSEGESEEILGKALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 69 TLnvqRQDIVISTKIYGGDGNDfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLA 148
Cdd:cd19091 77 GR---RDDVLIATKVRGRMGEG-PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 149 HYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDrFEWEYESV-FASGYGSTIWSPLYQGLLTGKY-NDDILA 226
Cdd:cd19091 153 RYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLaLDQGVGLLVWSPLAGGLLSGKYrRGQPAP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 227 DGRFNNSDNIYvkhfyqqilGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKS 306
Cdd:cd19091 232 EGSRLRRTGFD---------FPPVDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGA 302
|
330
....*....|...
gi 124399033 307 VQvVKLITKEVEQ 319
Cdd:cd19091 303 AG-LSLTPEEIAR 314
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-329 |
2.22e-79 |
|
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: 245.45 E-value: 2.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVIS 80
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19142 81 TKIYWSYG---SEERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESVF-ASGYGSTIWSPLYQGLLTGKynDDILADGRFNNSDNIYVK 239
Cdd:cd19142 158 IMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYnKVGVGLITWSPLSLGLDPGI--SEETRRLVTKLSFKSSKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 240 HFYQQILGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEVEQ 319
Cdd:cd19142 236 KVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVME 315
|
330
....*....|
gi 124399033 320 KIESILSNKP 329
Cdd:cd19142 316 ELERILDNKP 325
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-317 |
3.31e-78 |
|
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: 241.78 E-value: 3.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYG--DGKAEIHLGHALKT-LNVQRQDIVI 79
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGppPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 80 STKI-YG-GDGndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWT 157
Cdd:cd19089 81 STKAgYGmWPG---PYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 158 AQQIHQAIGICDRLSLhKPVVEQPQYNMMVRDRFEWEYESVFASGYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDniy 237
Cdd:cd19089 158 GAKARRAIALLRELGV-PLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAES--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 238 vkhfyqQILGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEV 317
Cdd:cd19089 234 ------KFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLDFSEEEL 307
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-322 |
7.36e-71 |
|
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: 222.79 E-value: 7.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWV-------NSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqRQDIVISTK 82
Cdd:cd19084 1 DLKVSRIGLGTWAiggtwwgEVDDQESIE----AIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 83 iYGGDGNDFPNSKY-LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQI 161
Cdd:cd19084 74 -CGLRWDGGKGVTKdLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 162 HQAIgicdrlSLHKPVVEQPQYNMMVRDrfewEYESVF----ASGYGSTIWSPLYQGLLTGKYNDdilaDGRFNNSDNIY 237
Cdd:cd19084 153 EEAR------KYGPIVSLQPPYSMLERE----IEEELLpycrENGIGVLPYGPLAQGLLTGKYKK----EPTFPPDDRRS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 238 VKHFYQqilgdPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEV 317
Cdd:cd19084 219 RFPFFR-----GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWE--LTEEE 291
|
....*
gi 124399033 318 EQKIE 322
Cdd:cd19084 292 LKEID 296
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
2-308 |
3.64e-69 |
|
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: 218.81 E-value: 3.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 2 EYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGD--GKAEIHLGHALKT-LNVQRQDIV 78
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPppGSAEENFGRILKEdLKPYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTKI--YGGDGndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEW 156
Cdd:cd19151 81 ISTKAgyTMWPG---PYGDWGSKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 157 TAQQIHQAIGICDRLSLhKPVVEQPQYNMMVRdrfeWEYESVFA----SGYGSTIWSPLYQGLLTGKYNDDILADGR--- 229
Cdd:cd19151 158 PPEEAREAAAILKDLGT-PCLIHQPKYSMFNR----WVEEGLLDvleeEGIGCIAFSPLAQGLLTDRYLNGIPEDSRaak 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 230 ---FNNSDNIyvkhfyqqilgDPEKRTKIqnqlKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKS 306
Cdd:cd19151 233 gssFLKPEQI-----------TEEKLAKV----RRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGA 297
|
..
gi 124399033 307 VQ 308
Cdd:cd19151 298 LD 299
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-319 |
6.93e-68 |
|
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: 215.54 E-value: 6.93e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 5 RLGATGLKVSAISYGNWV---NSDDKDTQDrntkiIQKAW-ELGINFFDTAEIYGD-------GKAEIHLGHALKTlNVQ 73
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMVfgwTADEETSFA-----LLDAFvDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKS-RGK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 74 RQDIVISTKIYGGDGndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGT 153
Cdd:cd19081 75 RDRVVIATKVGFPMG---PNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 154 SEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDRFEWEYESV-FASGYGSTIWSPLYQGLLTGKYNDDILADGRFNN 232
Cdd:cd19081 152 SNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLcREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 233 SDniyvkhFYQQILGDPEKRTkiqnqLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQvVKL 312
Cdd:cd19081 232 GE------AAKRYLNERGLRI-----LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAG-LRL 299
|
....*..
gi 124399033 313 ITKEVEQ 319
Cdd:cd19081 300 TDEEVAR 306
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-318 |
2.01e-63 |
|
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: 204.22 E-value: 2.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGD--GKAEIHLGHALKT-LNVQRQDIVI 79
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPppGSAEENFGRILREdFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 80 STKIyGGDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQ 159
Cdd:cd19150 82 STKA-GYDMWPGPYGEWGSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 160 QIHQAIGICDRLSLhkP-VVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDNIY 237
Cdd:cd19150 161 RTREAAAILRELGT--PlLIHQPSYNMLNRWVEESGLLDTLQElGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERSLS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 238 VKHFYQQILgdpekrtkiqNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKLITKEV 317
Cdd:cd19150 239 PKMLTEANL----------NSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLTFSADEL 308
|
.
gi 124399033 318 E 318
Cdd:cd19150 309 A 309
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-325 |
3.69e-63 |
|
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: 202.93 E-value: 3.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 16 ISYGNWVNSDDKDTQDRNT--KIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVISTKIYGGDGndfPN 93
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEalEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDG---PW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 94 SKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAigicDRLSL 173
Cdd:pfam00248 78 PSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKA----LTKGK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 174 HKPVVEQPQYNmMVRDRFEWE-YESVFASGYGSTIWSPLYQGLLTGKYNDDIladgrfnnsDNIYVKHFYQQILGDPEKR 252
Cdd:pfam00248 154 IPIVAVQVEYN-LLRRRQEEElLEYCKKNGIPLIAYSPLGGGLLTGKYTRDP---------DKGPGERRRLLKKGTPLNL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124399033 253 TKIQNqlkqLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEVEQKIESIL 325
Cdd:pfam00248 224 EALEA----LEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFP--LSDEEVARIDELL 290
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-305 |
2.12e-57 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 185.80 E-value: 2.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 14 SAISYGNWVNSDDKDtQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVqRQDIVISTKIyGGDGNDFPN 93
Cdd:cd06660 1 SRLGLGTMTFGGDGD-EEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGN-RDDVVIATKG-GHPPGGDPS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 94 SKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSL 173
Cdd:cd06660 78 RSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 174 HKPVVEQPQYNMMVRDRFEWEYESVF-ASGYGSTIWSPLYQGLltgkynddiladgrfnnsdniyvkhfyqqilgdpekr 252
Cdd:cd06660 158 PGFAAVQPQYSLLDRSPMEEELLDWAeENGLPLLAYSPLARGP------------------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 124399033 253 tkiqnqlkqlgevakelgvtqAQLSLAWALKNKDVSTAITSATRPEQLEETVK 305
Cdd:cd06660 201 ---------------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-324 |
6.36e-57 |
|
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: 186.64 E-value: 6.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 13 VSAISYGNWVNSDD----KDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIVISTKIYGgdg 88
Cdd:cd19085 1 VSRLGLGCWQFGGGywwgDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVSP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 89 ndfpnsKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGIC 168
Cdd:cd19085 75 ------DNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 169 drlslhKPVVEQPQYNMMVRdrfEWEYEsVF----ASGYGSTIWSPLYQGLLTGKYNddilADGRFNNSDNIYvKHFyqq 244
Cdd:cd19085 149 ------RIDSNQLPYNLLWR---AIEYE-ILpfcrEHGIGVLAYSPLAQGLLTGKFS----SAEDFPPGDART-RLF--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 245 ILGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEVEQKIESI 324
Cdd:cd19085 211 RHFEPGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLE--LSPSVLERLDEI 288
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-319 |
1.92e-54 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 182.11 E-value: 1.92e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGD--GKAEIHLGHALKT-LNVQRQDI 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGPppGSAEENFGRLLREdFAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 78 VISTKIyGGDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWT 157
Cdd:PRK09912 93 IISTKA-GYDMWPGPYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 158 AQQIHQAIGICDRLSLhkP-VVEQPQYNMMVRdrfeWE-----YESVFASGYGSTIWSPLYQGLLTGKYNDDILADGRFN 231
Cdd:PRK09912 172 PERTQKMVELLREWKI--PlLIHQPSYNLLNR----WVdksglLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMH 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 232 NSDNiYVKHFYQQILGDPEkrtkiQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVK 311
Cdd:PRK09912 246 REGN-KVRGLTPKMLTEAN-----LNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLT 319
|
....*...
gi 124399033 312 LITKEVEQ 319
Cdd:PRK09912 320 FSTEELAQ 327
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-309 |
1.13e-51 |
|
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: 174.00 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYGNWV--------NSDDKDTqdrnTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqR 74
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggpwwgGSDDNES----IRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 75 QDIVISTKI----------YGGDGNDFPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIR 144
Cdd:cd19149 74 DKVVLATKCglrwdreggsFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 145 HGLAHYWGTSEWTAQQIHQAigicdrLSLHKPVVEQPQYNMMvrDRFEWEYESVFASGYGSTI--WSPLYQGLLTGKynd 222
Cdd:cd19149 154 QGKIRAIGASNVSVEQIKEY------VKAGQLDIIQEKYSML--DRGIEKELLPYCKKNNIAFqaYSPLEQGLLTGK--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 223 dILADGRFNNSDNIYVKHFYQqilgdPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEE 302
Cdd:cd19149 223 -ITPDREFDAGDARSGIPWFS-----PENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEE 296
|
....*..
gi 124399033 303 TVKSVQV 309
Cdd:cd19149 297 NAKAGDI 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-325 |
4.16e-51 |
|
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: 172.03 E-value: 4.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYG----NWVNSDDKDTQDrNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqRQDIVISTK--- 82
Cdd:cd19078 1 GLEVSAIGLGcmgmSHGYGPPPDKEE-MIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPF---RDQVVIATKfgf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 83 -IYGG-DGNDFPNSKYLSRKHLIEGlrnSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQ 160
Cdd:cd19078 77 kIDGGkPGPLGLDSRPEHIRKAVEG---SLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVET 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAIGICdrlslhkPVVE-QPQYNMMVRdrfewEYES-VF----ASGYGSTIWSPLYQGLLTGKYNddilADGRFNNSD 234
Cdd:cd19078 154 IRRAHAVC-------PVTAvQSEYSMMWR-----EPEKeVLptleELGIGFVPFSPLGKGFLTGKID----ENTKFDEGD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 235 NIYVKHFYQqilgdPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklIT 314
Cdd:cd19078 218 DRASLPRFT-----PEALEANQALVDLLKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIE--LT 290
|
330
....*....|.
gi 124399033 315 KEVEQKIESIL 325
Cdd:cd19078 291 PEELREIEDAL 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-324 |
1.19e-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: 168.90 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 13 VSAISYG--NWVNsddKDTQDRNTKIIQKAWELGINFFDTAEIY-------GDGKAEIHLGHALKTlNVQRQDIVISTKI 83
Cdd:cd19094 1 VSEICLGtmTWGE---QNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKK-KGNRDKVVLATKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 YG-GDGNDFPNSKY--LSRKHLIEGLRNSLKRLDTPYVDIVFAH---RY-------DY--------QTPLEETCRAFDWI 142
Cdd:cd19094 77 AGpGEGITWPRGGGtrLDRENIREAVEGSLKRLGTDYIDLYQLHwpdRYtplfgggYYtepseeedSVSFEEQLEALGEL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 143 IRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDRFE--WE---YESVfasgyGSTIWSPLYQGLLT 217
Cdd:cd19094 157 VKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEglAEachRENV-----GLLAYSPLAGGVLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 218 GKYND--DILADGRFNnsdnIYvKHFYQQILGDPEKRtkiqnQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSAT 295
Cdd:cd19094 232 GKYLDgaARPEGGRLN----LF-PGYMARYRSPQALE-----AVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGAT 301
|
330 340
....*....|....*....|....*....
gi 124399033 296 RPEQLEETVKSVQVVklITKEVEQKIESI 324
Cdd:cd19094 302 TLEQLKENIDAFDVP--LSDELLAEIDAV 328
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-310 |
2.51e-49 |
|
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: 167.40 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 4 RRLGATGLKVS-----AISYGN-WVNSDDKDTqdrNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqRQDI 77
Cdd:cd19080 1 RLLGRSGLRVSplalgTMTFGTeWGWGADREE---ARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN---RDRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 78 VISTK-IYGGDGNDfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEW 156
Cdd:cd19080 75 VLATKyTMNRRPGD-PNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 157 TAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDrFEWEYESVF-ASGYGSTIWSPLYQGLLTGKYNDDILADGRFNNSDN 235
Cdd:cd19080 154 PAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMArALGLGVTPWSPLGGGLLTGKYQRGEEGRAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124399033 236 IYVKHFyqqilgdPEKRTKIQnqlKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVV 310
Cdd:cd19080 233 VGFGKL-------TERNWAIV---DVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLT 297
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-310 |
2.65e-47 |
|
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: 162.00 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 2 EYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKI--IQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIVI 79
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPADEEESIatLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 80 STK----IYGGDGNDFPNSkylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSE 155
Cdd:cd19076 78 ATKfgivRDPGSGFRGVDG---RPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 156 WTAQQIHQAIGIcdrlslHKPVVEQPQYNMMVRDrFEweyESVFAS----GYGSTIWSPLYQGLLTGKY---NDDILADG 228
Cdd:cd19076 155 ASADTIRRAHAV------HPITAVQSEYSLWTRD-IE---DEVLPTcrelGIGFVAYSPLGRGFLTGAIkspEDLPEDDF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 229 RFNNSdniyvkhFYQqilgdPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQ 308
Cdd:cd19076 225 RRNNP-------RFQ-----GENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALD 292
|
..
gi 124399033 309 VV 310
Cdd:cd19076 293 VV 294
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-324 |
2.11e-44 |
|
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: 154.50 E-value: 2.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 4 RRLGATGLKVSAISYGN--------WVNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQ 75
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTnavgghnlYPNLDEEEGKD----LVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYN--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 76 DIVISTK---IYGGDGNDFPNSkylsRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWG 152
Cdd:cd19083 76 EVVIATKgahKFGGDGSVLNNS----PEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 153 TSEWTAQQIHQA--IGICDrlslhkpvVEQPQYNMMVRDRFEWEYESVFASGYGSTIWSPLYQGLLTGKYNDDI-LADGR 229
Cdd:cd19083 152 VSNFSLEQLKEAnkDGYVD--------VLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTkFPDND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 230 FNNSDNIYVKHFYQQILGDPEKrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQV 309
Cdd:cd19083 224 LRNDKPLFKGERFSENLDKVDK----------LKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV 293
|
330
....*....|....*
gi 124399033 310 VklITKEVEQKIESI 324
Cdd:cd19083 294 T--LTEEEIAFIDAL 306
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
42-313 |
1.39e-42 |
|
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: 149.63 E-value: 1.39e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 42 ELGINFFDTAEIYGDGKAEIHLGHALktlnVQRQDIVISTKIYGGDGNDfpnskyLSRKHLIEGLRNSLKRLDTPYVDIV 121
Cdd:cd19075 31 ERGHTEIDTARVYPDGTSEELLGELG----LGERGFKIDTKANPGVGGG------LSPENVRKQLETSLKRLKVDKVDVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 122 FAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRD------------ 189
Cdd:cd19075 101 YLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITRQvetelfpclrkl 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 190 --RFeweyesvFAsgygstiWSPLYQGLLTGKY--NDDILADGRFnNSDNIYVKHfYQQILGDPEkrtkIQNQLKQLGEV 265
Cdd:cd19075 181 giRF-------YA-------YSPLAGGFLTGKYkySEDKAGGGRF-DPNNALGKL-YRDRYWKPS----YFEALEKVEEA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 266 AKELGVTQAQLSLAW-----ALKNKDVSTAITSATRPEQLEETVKSVQ-------VVKLI 313
Cdd:cd19075 241 AEKEGISLAEAALRWlyhhsALDGEKGDGVILGASSLEQLEENLAALEkgplpeeVVKAI 300
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-306 |
2.11e-41 |
|
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: 144.54 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 11 LKVSAISYGNWV--NSDDKDTQDRN-TKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIVISTKIyGGD 87
Cdd:cd19086 1 LEVSEIGFGTWGlgGDWWGDVDDAEaIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKF-GNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 88 GNDFPN-SKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQ-TPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAI 165
Cdd:cd19086 77 FDGGPErPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEvLDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 166 --GICDrlslhkpvVEQPQYNMMVRDRFEWEYESVFASGYGSTIWSPLYQGLLTGKYnddiladgrfnnsdniyvkhfyq 243
Cdd:cd19086 157 rrGGID--------VVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGKL----------------------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 124399033 244 qilgdpekrtkiqnqlkqlgevakelgvtqAQLSLAWALKNKDVSTAITSATRPEQLEETVKS 306
Cdd:cd19086 206 ------------------------------AQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-308 |
1.67e-40 |
|
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: 143.14 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNW----VNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKtlNVQRQDIVISTKIYg 85
Cdd:cd19072 1 GEEVPVLGLGTWgiggGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIK--GFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 gdgndfPNskYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAI 165
Cdd:cd19072 78 ------PD--HLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 166 GICDRlslHKPVVEQPQYNMMVR----DRFEWEYE---SVFAsgygstiWSPLYQGLLTGKYNDDILAdgrfnnsdniyv 238
Cdd:cd19072 150 SYLKK---GPIVANQVEYNLFDReeesGLLPYCQKngiAIIA-------YSPLEKGKLSNAKGSPLLD------------ 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 239 khfyqqilgdpekrtkiqnqlkqlgEVAKELGVTQAQLSLAWaLKNKDVSTAITSATRPEQLEETVKSVQ 308
Cdd:cd19072 208 -------------------------EIAKKYGKTPAQIALNW-LISKPNVIAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
6-325 |
3.77e-40 |
|
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: 143.20 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 6 LGATGLKVSAISYGN----WVNSDDKDTqdrnTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqRQDIVIST 81
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggWGPQDDRDS----IAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVAT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 82 K---IYGGDGndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:cd19102 74 KcglLWDEEG---RIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 159 QQIH--QAIGICDRLslhkpvveQPQYNMMVRD------RFEWEYesvfasGYGSTIWSPLYQGLLTGKYNDDILA---- 226
Cdd:cd19102 151 DQMKrcQAIHPIASL--------QPPYSLLRRGieaeilPFCAEH------GIGVIVYSPMQSGLLTGKMTPERVAslpa 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 227 -DGRFNNSDniyvkhFYQQILGdpeKRTKIQNQLKQlgeVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVK 305
Cdd:cd19102 217 dDWRRRSPF------FQEPNLA---RNLALVDALRP---IAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVG 284
|
330 340
....*....|....*....|
gi 124399033 306 SVQVVklITKEVEQKIESIL 325
Cdd:cd19102 285 AADLR--LTPEELAEIEALL 302
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-283 |
3.51e-39 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 140.67 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNW-VNSDDKDTQDRNTKIiQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVI 79
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMrLGEWDLSPAEAAALI-EAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 80 STK---IYGGDGNDFPNSKY-LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSE 155
Cdd:COG4989 80 QTKcgiRLPSEARDNRVKHYdTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 156 WTAQQIhqaigicdRL---SLHKP-VVEQPQYNMMVRDRFEweyesvfasgyGSTI------------WSPLYQGLLTGK 219
Cdd:COG4989 160 FTPSQF--------ELlqsALDQPlVTNQIELSLLHTDAFD-----------DGTLdycqlngitpmaWSPLAGGRLFGG 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124399033 220 YNDDiladgrfnnsdniyvkhfyqqilgdpEKRTKiqnqlKQLGEVAKELGVTQAQLSLAWALK 283
Cdd:COG4989 221 FDEQ--------------------------FPRLR-----AALDELAEKYGVSPEAIALAWLLR 253
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
17-318 |
3.06e-38 |
|
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: 138.13 E-value: 3.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 17 SYGNWVNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVqRQDIVISTKIYGgdgndFPNSky 96
Cdd:cd19093 16 LWWGYGEYGDEDLQA----AFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGD-RDEVVIATKFAP-----LPWR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 97 LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYD-YQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIgicDRLSLHK 175
Cdd:cd19093 84 LTRRSVVKALKASLERLGLDSIDLYQLHWPGpWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAH---KALKERG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 176 --PVVEQPQYNMMVRDRFEWEYESVfASGYGSTI--WSPLYQGLLTGKYNDDILADGRfnnsdniYVKHFYQQILgdpek 251
Cdd:cd19093 161 vpLASNQVEYSLLYRDPEQNGLLPA-CDELGITLiaYSPLAQGLLTGKYSPENPPPGG-------RRRLFGRKNL----- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 252 rTKIQNQLKQLGEVAKELGVTQAQLSLAWaLKNKDVsTAITSATRPEQLEETVKSVQvVKLITKEVE 318
Cdd:cd19093 228 -EKVQPLLDALEEIAEKYGKTPAQVALNW-LIAKGV-VPIPGAKNAEQAEENAGALG-WRLSEEEVA 290
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-307 |
2.16e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 134.63 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVnsddkdTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnVQRQDIVIS 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGG------LPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKG--LRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 81 TKIYGGDGNDfpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPL---EETCRAFDWIIRHGLAHYWGTSE-- 155
Cdd:cd19105 73 TKASPRLDKK-------DKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFSThd 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 156 WTAQQIHQAIGiCDRLSlhkpvVEQPQYNMMvrdRFEWEYESVFASGYGSTIwsplyqGLLTGKynddILADGrfnnsdn 235
Cdd:cd19105 146 NMAEVLQAAIE-SGWFD-----VIMVAYNFL---NQPAELEEALAAAAEKGI------GVVAMK----TLAGG------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124399033 236 iyvkhfYQQILGDPEKRTKiqnqlkqlgevakelGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSV 307
Cdd:cd19105 200 ------YLQPALLSVLKAK---------------GFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
26-305 |
8.63e-37 |
|
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: 134.22 E-value: 8.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 26 DKDTQDRNTKIIQKAWELGINFFDTAEIYGD----GKAEIHLGHALKTLNVqRQDIVISTKiyGG-DGNDFPNSKYLSRK 100
Cdd:cd19082 12 TRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRGN-RDKVVIATK--GGhPDLEDMSRSRLSPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 101 HLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQ 180
Cdd:cd19082 89 DIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 181 PQYNMMVRDRFEWEYES------------------VFAsgygstiWSPLYQGLLTGKYN----DDILADGRFNNSDNIyv 238
Cdd:cd19082 169 PQWSLARPNEPPWPGPTlvamdeemrawheenqlpVFA-------YSSQARGFFSKRAAggaeDDSELRRVYYSEENF-- 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 239 khfyqqilgdpEKRTKIQnqlkqlgEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVK 305
Cdd:cd19082 240 -----------ERLERAK-------ELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLA 288
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-309 |
1.41e-35 |
|
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: 130.75 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 8 ATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQRQDIVISTK--IYG 85
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 GDGNDFPNSKY--LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIH- 162
Cdd:cd19092 81 GDDPRPGRIKHydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIEl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 163 -QAigicdRLSlHKPVVEQPQYNMMvrdRFEWEYESV--FASGYGSTI--WSPLYQGLLTGkynddiladgrfnnsdniy 237
Cdd:cd19092 161 lQS-----YLD-QPLVTNQIELSLL---HTEAIDDGTldYCQLLDITPmaWSPLGGGRLFG------------------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124399033 238 vkhfyqqilgdpEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQV 309
Cdd:cd19092 213 ------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
44-307 |
2.05e-33 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 125.14 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 44 GINFFDTAEIYG-------DGKAEIHLGHALKTLNVqRQDIVISTKI---YGGDGNDFPNSKYLSRKHLIEGLRNSLKRL 113
Cdd:cd19752 30 GGNFLDTANNYAfwteggvGGESERLIGRWLKDRGN-RDDVVIATKVgagPRDPDGGPESPEGLSAETIEQEIDKSLRRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 114 DTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNmMVRDRFEW 193
Cdd:cd19752 109 GTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHS-YLRPRPGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 194 EYESVFASG-----YGS-----TIWSplYQGLLTGKY-NDDILADGRFNNSDNiyvkhfyqqilgdpekrtkiQNQLKQL 262
Cdd:cd19752 188 DFGVQRIVTdelldYASsrpdlTLLA--YSPLLSGAYtRPDRPLPEQYDGPDS--------------------DARLAVL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 124399033 263 GEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSV 307
Cdd:cd19752 246 EEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-324 |
1.15e-32 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 123.91 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 2 EYRRLGATGLKVSAISYGN------WVNSDDkDTQDRntkIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvqRQ 75
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGggigglMGRTTR-EEQIA---AVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 76 DIVISTKIygGDGNDFPNSKYlsrKHLIEGLRNSLKRLDTPYVDIVFAH------RYDYQTP---------LEETCRAFD 140
Cdd:cd19104 74 GPYITTKV--RLDPDDLGDIG---GQIERSVEKSLKRLKRDSVDLLQLHnrigdeRDKPVGGtlsttdvlgLGGVADAFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 141 WIIRHGLAHYWGTSEW-TAQQIHQAIGiCDRLSLhkpvVEQPqYNMMVRDRFEWEYESVFASGYGSTI------------ 207
Cdd:cd19104 149 RLRSEGKIRFIGITGLgNPPAIRELLD-SGKFDA----VQVY-YNLLNPSAAEARPRGWSAQDYGGIIdaaaehgvgvmg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 208 WSPLYQGLLTGKYNDDILADgrfNNSDNIYVKHFyqqilgdpekrtkiqNQLKQLGEVAKELGVTQAQLSLAWALKNKDV 287
Cdd:cd19104 223 IRVLAAGALTTSLDRGREAP---PTSDSDVAIDF---------------RRAAAFRALAREWGETLAQLAHRFALSNPGV 284
|
330 340 350
....*....|....*....|....*....|....*..
gi 124399033 288 STAITSATRPEQLEETVKSVQVVKLiTKEVEQKIESI 324
Cdd:cd19104 285 STVLVGVKNREELEEAVAAEAAGPL-PAENLARLEAL 320
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-316 |
2.73e-32 |
|
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: 121.59 E-value: 2.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 8 ATGLKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIVISTKIYggd 87
Cdd:cd19138 6 PDGTKVPALGQGTWYMGEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 88 gndfP-NSkylSRKHLIEGLRNSLKRLDTPYVDIVFAH-RYDYqtPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAI 165
Cdd:cd19138 80 ----PsNA---SRQGTVRACERSLRRLGTDYLDLYLLHwRGGV--PLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELW 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 166 GIcdrLSLHKPVVEQPQYNMMVR----DRFEWEYE-SVFASGYgstiwSPLYQGlltgkyndDILADGRFNNSDniyvkh 240
Cdd:cd19138 151 AV---PGGGNCAANQVLYNLGSRgieyDLLPWCREhGVPVMAY-----SPLAQG--------GLLRRGLLENPT------ 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124399033 241 fyqqilgdpekrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVsTAITSATRPEQLEETVKSVQVVklITKE 316
Cdd:cd19138 209 ---------------------LKEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADLE--LTEE 260
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-307 |
6.24e-32 |
|
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: 121.12 E-value: 6.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYG------NWVNSDDKDTqdrnTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKtlNVQR 74
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGasplggVFGPVDEEEA----IRTVHEALDSGINYIDTAPWYGQGRSETVLGKALK--GIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 75 QDIVISTKI--YGGDGN---DFpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTP----LEETCRAFDWIIRH 145
Cdd:cd19163 75 DSYYLATKVgrYGLDPDkmfDF------SAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSldqiLNETLPALQKLKEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 146 GLAHYwgtsewtaqqihqaIGICDR-LSLHKPVVEQPQ-----------YNMMvrDRFEWEYESVFAS-GYGSTIWSPLY 212
Cdd:cd19163 149 GKVRF--------------IGITGYpLDVLKEVLERSPvkidtvlsychYTLN--DTSLLELLPFFKEkGVGVINASPLS 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 213 QGLLTGKynddiladgrfnnsdniyvkhfyqqilGDPE---KRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVST 289
Cdd:cd19163 213 MGLLTER---------------------------GPPDwhpASPEIKEACAKAAAYCKSRGVDISKLALQFALSNPDIAT 265
|
330
....*....|....*...
gi 124399033 290 AITSATRPEQLEETVKSV 307
Cdd:cd19163 266 TLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-325 |
3.09e-31 |
|
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: 119.72 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWV-------NSDDKdtQDRNTkiIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvQRQDIVISTK 82
Cdd:cd19148 1 DLPVSRIALGTWAiggwmwgGTDEK--EAIET--IHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 83 I---YGGDGNDFPNSkylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQ 159
Cdd:cd19148 76 VgleWDEGGEVVRNS---SPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 160 QIhqaigicDRLSLHKPV-VEQPQYNMmvrdrFEWEYES-----VFASGYGSTIWSPLYQGLLTGKYN-DDILADGRFNN 232
Cdd:cd19148 153 QM-------ETFRKVAPLhTVQPPYNL-----FEREIEKdvlpyARKHNIVTLAYGALCRGLLSGKMTkDTKFEGDDLRR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 233 SDNIYVKHFYQQILGDPEkrtkiqnQLKQLgevAKE-LGVTQAQLSLAWALKNKDVSTAITSATRPEQLEEtVKSVQVVK 311
Cdd:cd19148 221 TDPKFQEPRFSQYLAAVE-------ELDKL---AQErYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDA-VDEVFGWS 289
|
330
....*....|....
gi 124399033 312 LiTKEVEQKIESIL 325
Cdd:cd19148 290 L-NDEDMKEIDAIL 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-308 |
5.28e-31 |
|
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: 118.43 E-value: 5.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 14 SAISYGN-WVNSDDKD-TQDRNTKIIQKAWELGINFFDTAEIYGDgkAEIHLGHALKTlnVQRQDIVISTKI--YGGDGN 89
Cdd:cd19090 1 SALGLGTaGLGGVFGGvDDDEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAE--LPREPLVLSTKVgrLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 DFpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCR--AFDWIIR---HGLAHYWGTSEWTAQQIHQA 164
Cdd:cd19090 77 DY------SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILAPggALEALLElkeEGLIKHIGLGGGPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 165 I--GICDRLSLHKpvveqpQYNMMVRDRFeweyESVF--ASGYGSTIW--SPLYQGLLTGKYNDdiladgrfnnsdniYV 238
Cdd:cd19090 151 IetGDFDVVLTAN------RYTLLDQSAA----DELLpaAARHGVGVInaSPLGMGLLAGRPPE--------------RV 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 239 KHFYQQILgdpekrTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQ 308
Cdd:cd19090 207 RYTYRWLS------PELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-329 |
8.42e-31 |
|
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: 119.08 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNS---DDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQDI 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSafyGPPKPDEERFAVLDAAFELGCTFWDTADIYGDSEELIGRWFKQNPGK--REKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 78 VISTKiYGG-----DGNDFPNSkylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWG 152
Cdd:cd19144 79 FLATK-FGIeknveTGEYSVDG---SPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 153 TSEWTAQQIHQAIGIcdrlslhKPV-------------VEQPQYNMMVRDRfeweyesvfASGYGSTIWSPLYQGLLTGK 219
Cdd:cd19144 155 LSECSAETLRRAHAV-------HPIaavqieyspfsldIERPEIGVLDTCR---------ELGVAIVAYSPLGRGFLTGA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 220 YND-DILADGRFNNsdniYVKHFyqqilgDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPE 298
Cdd:cd19144 219 IRSpDDFEEGDFRR----MAPRF------QAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLK 288
|
330 340 350
....*....|....*....|....*....|.
gi 124399033 299 QLEETVKSVQvVKLiTKEVEQKIESILSNKP 329
Cdd:cd19144 289 RLEENLGALK-VKL-TEEEEKEIREIAEEAE 317
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-309 |
3.35e-30 |
|
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: 115.75 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNW----VNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKtlNVQRQDIVISTKIYg 85
Cdd:cd19137 1 GEKIPALGLGTWgiggFLTPDYSRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIK--DFPREDLFIVTKVW- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 gdgndfpnSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAI 165
Cdd:cd19137 78 --------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 166 GICdrlslHKP-VVEQPQYNMMVRDrfeweyesvfasgygstiwsPLYQGLLtgkynddiladgRFNNSDNIYVKHFyqq 244
Cdd:cd19137 150 SKS-----QTPiVCNQVKYNLEDRD--------------------PERDGLL------------EYCQKNGITVVAY--- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 245 ilgDPEKRT--KIQNQLKQlgeVAKELGVTQAQLSLAWALKNKDVsTAITSATRPEQLEETVKSVQV 309
Cdd:cd19137 190 ---SPLRRGleKTNRTLEE---IAKNYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKENLKATEI 249
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
10-302 |
2.46e-28 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 110.53 E-value: 2.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWvNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGdgkAEIHLGHALKTLNVQRQDIVISTKIYGGDgn 89
Cdd:COG0656 2 GVEIPALGLGTW-QLPGEEAAA----AVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASGVPREELFVTTKVWNDN-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 dfpnskyLSRKHLIEGLRNSLKRLDTPYVDIVFAH-RYDYqtPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGIC 168
Cdd:COG0656 72 -------HGYDDTLAAFEESLERLGLDYLDLYLIHwPGPG--PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 169 DrlslHKPVVEQPQYNMmvrdrFEWEYESV-FASGYGSTI--WSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQI 245
Cdd:COG0656 143 G----VKPAVNQVELHP-----YLQQRELLaFCREHGIVVeaYSPLGRG-----------------------------KL 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 246 LGDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALkNKDVStAITSATRPEQLEE 302
Cdd:COG0656 185 LDDPV-----------LAEIAEKHGKTPAQVVLRWHL-QRGVV-VIPKSVTPERIRE 228
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-305 |
2.06e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYG--NWVNSDdkdtQDRNTKIIQKAWELGINFFDTAeiYGDGKAEIHLGHALKTLnvqRQDIV 78
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGgmRLPRKD----EEEAEALIRRAIDNGINYIDTA--RGYGDSEEFLGKALKGP---RDKVI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTKIyggdgndfpNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH----RYDYQTPLEETcRAFDWI--------IRHg 146
Cdd:COG1453 72 LATKL---------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHglntEEDLEKVLKPG-GALEALekakaegkIRH- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 147 lahywgtsewtaqqihqaIGIC--DRLSLHKPVVE-------QPQYNMM-VRDRFEWE-YESVFASGYGSTIWSPlyqgl 215
Cdd:COG1453 141 ------------------IGFSthGSLEVIKEAIDtgdfdfvQLQYNYLdQDNQAGEEaLEAAAEKGIGVIIMKP----- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 216 ltgkynddiLADGRFNNsdniyvkhfyqqilgDPEKRTKIqnqlkqlgevaKELGVTQAQLSLAWALKNKDVSTAITSAT 295
Cdd:COG1453 198 ---------LKGGRLAN---------------PPEKLVEL-----------LCPPLSPAEWALRFLLSHPEVTTVLSGMS 242
|
330
....*....|
gi 124399033 296 RPEQLEETVK 305
Cdd:COG1453 243 TPEQLDENLK 252
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-124 |
5.43e-27 |
|
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: 106.41 E-value: 5.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYGNWVNSddKDTQDRNTKIIQKAWELGINFFDTAEIYGDgkAEIHLGHALKTlnvQRQDIVISTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLG--RLSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 124399033 83 IYGGDGNDFpnskylsRKHliegLRNSLKRLDTPYVDIVFAH 124
Cdd:cd19100 74 TGARDYEGA-------KRD----LERSLKRLGTDYIDLYQLH 104
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-310 |
6.43e-27 |
|
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: 106.92 E-value: 6.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 13 VSAISYGNW------VNSDDKDtQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTlnvQRQDIVISTKI--- 83
Cdd:cd19088 1 VSRLGYGAMrltgpgIWGPPAD-REEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGglv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 YGGDGNDFPNSkylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQ 163
Cdd:cd19088 77 RTGPGWWGPDG---SPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 164 AIGICDRLSLhkpvveQPQYNMMVRDRfeweyESVFAS----GYGSTIWSPLyqglltgkynddiladGRFnnsdniyvk 239
Cdd:cd19088 154 ARAIVRIVSV------QNRYNLANRDD-----EGVLDYceaaGIAFIPWFPL----------------GGG--------- 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124399033 240 hfyqqilGDPEKRTKiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVV 310
Cdd:cd19088 198 -------DLAQPGGL-------LAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLR 254
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-319 |
1.13e-26 |
|
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: 107.13 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 4 RRLGATGLKVSAISYG-----NWVNSDDKDTQdrNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvQRQDIV 78
Cdd:cd19145 3 VKLGSQGLEVSAQGLGcmglsGDYGAPKPEEE--GIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDG--PREKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTK--IYGGDGndfpnSKYLSR---KHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGT 153
Cdd:cd19145 79 LATKfgIHEIGG-----SGVEVRgdpAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 154 SEWTAQQIHQAIGIcdrlslHKPVVEQPQYNMMVRDRFEWEYESVFASGYGSTIWSPLYQGLLTGKyndDILADgrfNNS 233
Cdd:cd19145 154 SEASADTIRRAHAV------HPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEE---LLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 234 DNIYVKHF--YQQilgdpEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQvVK 311
Cdd:cd19145 222 NSDVRKSHprFQG-----ENLEKNKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALS-VK 295
|
....*...
gi 124399033 312 LITKEVEQ 319
Cdd:cd19145 296 LTKEDLKE 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
6-306 |
1.08e-25 |
|
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: 103.47 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 6 LGATGLkvsaisYGNWVNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDgkAEIHLGHALKTLnvQRQDIVISTKI-- 83
Cdd:cd19095 5 LGTSGI------GRVWGVPSEAEAAR----LLNTALDLGINLIDTAPAYGR--SEERLGRALAGL--RRDDLFIATKVgt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 ---YGGDGNDFpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYwgtsewtaqq 160
Cdd:cd19095 71 hgeGGRDRKDF------SPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRY---------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 ihqaIGICDRLSLHKPVVE-------QPQYNMMVRDRfeweyESVF----ASGYGSTIWSPLYQGLLTGKYNDDILADgr 229
Cdd:cd19095 135 ----IGVSGDGEELEAAIAsgvfdvvQLPYNVLDREE-----EELLplaaEAGLGVIVNRPLANGRLRRRVRRRPLYA-- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124399033 230 fnnsdniyvkhfyqqilgdpekrtkiqnQLKQLGEVAKELGV-TQAQLSLAWALKNKDVSTAITSATRPEQLEETVKS 306
Cdd:cd19095 204 ----------------------------DYARRPEFAAEIGGaTWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-326 |
1.15e-23 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 99.08 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 3 YRRLGATGLKVSAISYG--------NWVNSDDKdtqdrnTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQR 74
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGasplgsvfGPVSEEDA------IASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 75 QDIVISTKI--YgGDGNDFpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQT---PLEETCRAFDWIIRHGLAH 149
Cdd:PLN02587 75 EKYVVSTKCgrY-GEGFDF------SAERVTKSVDESLARLQLDYVDILHCHDIEFGSldqIVNETIPALQKLKESGKVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 150 YWGTSEWTaqqihqaIGIC----DRLSLHKPVVEQPQYNMMVRDRFEWEYESVFAS-GYGSTIWSPLYQGLLTGKynddi 224
Cdd:PLN02587 148 FIGITGLP-------LAIFtyvlDRVPPGTVDVILSYCHYSLNDSSLEDLLPYLKSkGVGVISASPLAMGLLTEN----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 225 ladgrfnnsdniyvkhfyqqilGDPE---KRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLE 301
Cdd:PLN02587 216 ----------------------GPPEwhpAPPELKSACAAAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVE 273
|
330 340
....*....|....*....|....*..
gi 124399033 302 ETVKSVQVVKL--ITKEVEQKIESILS 326
Cdd:PLN02587 274 ENVAAATELETsgIDEELLSEVEAILA 300
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-302 |
2.40e-22 |
|
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: 94.25 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKdtqdrNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYggdgn 89
Cdd:cd19140 5 GVRIPALGLGTYPLTGEE-----CTRAVEHALELGYRHIDTAQMYGN---EAQVGEAIAASGVPRDELFLTTKVW----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 dFPNskyLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIgicd 169
Cdd:cd19140 72 -PDN---YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAV---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 170 RLSLHKPVVEQPQYNMMVRDRfeweyeSVFAS----GYGSTIWSPlyqglltgkynddiLADGRfnnsdniyvkhfyqqI 245
Cdd:cd19140 144 ELSEAPLFTNQVEYHPYLDQR------KLLDAarehGIALTAYSP--------------LARGE---------------V 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 246 LGDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVStAITSATRPEQLEE 302
Cdd:cd19140 189 LKDPV-----------LQEIGRKHGKTPAQVALRWLLQQEGVA-AIPKATNPERLEE 233
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-310 |
1.05e-21 |
|
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: 93.46 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYG----NWvnSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHL---GHALKTLNVQRQDIVIST 81
Cdd:cd19077 1 NGKLVGPIGLGlmglTW--RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLkllARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 82 KiyGG--DGNDFPNSkylSRKHLIEGLRNSLKRLD-TPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:cd19077 79 K--GGldPDTLRPDG---SPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 159 QQIHQAigicdrLSLHKPVVEQPQYNMMVRDRFEWE-YESVFASGYGSTIWSPLYQGLLTGKY-NDDILADGRFnnsdNI 236
Cdd:cd19077 154 ETIRRA------HAVHPIAAVEVEYSLFSREIEENGvLETCAELGIPIIAYSPLGRGLLTGRIkSLADIPEGDF----RR 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124399033 237 YVKHFyqqilgDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALK-NKDVSTAITSATRPEQLEETVKSVQVV 310
Cdd:cd19077 224 HLDRF------NGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAqSGPKIIPIPGSTTLERVEENLKAANVE 292
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-324 |
1.18e-21 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 94.15 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLGATGLKVSAISYGNWVNSDDKDTQDRNTKIiQKAWELGINFFDTAEIY-------GDGKAEIHLGHALKTLNvQ 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMTFGEQNSEADAHAQL-DYAVAQGINLIDVAEMYpvpprpeTQGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 74 RQDIVISTKIYG-GDGNDF---PNsKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH--------------RYDYQTP---L 132
Cdd:PRK10625 79 REKLIIASKVSGpSRNNDKgirPN-QALDRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgySWTDSAPavsL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 133 EETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDrFE------WEYESVFASGYgst 206
Cdd:PRK10625 158 LETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEvglaevSQYEGVELLAY--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 207 iwSPLYQGLLTGKYNDDILADGRFNNSDNIYVKHFYQQilgdpekrtkIQNQLKQLGEVAKELGVTQAQLSLAWALKNKD 286
Cdd:PRK10625 234 --SCLAFGTLTGKYLNGAKPAGARNTLFSRFTRYSGEQ----------TQKAVAAYVDIAKRHGLDPAQMALAFVRRQPF 301
|
330 340 350
....*....|....*....|....*....|....*...
gi 124399033 287 VSTAITSATRPEQLEETVKSVQVVklITKEVEQKIESI 324
Cdd:PRK10625 302 VASTLLGATTMEQLKTNIESLHLT--LSEEVLAEIEAV 337
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
36-308 |
1.77e-21 |
|
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: 93.16 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 36 IIQKAWELGINFFDTAEIYGDGKAEIHLGHALKtlNVQRQDIVISTKIygG------------DGNDFPNS-------KY 96
Cdd:cd19161 25 TLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLR--EKPRDEFVLSTKV--GrllkparegsvpDPNGFVDPlpfeivyDY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 97 lSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGlaHYWGTSEWTAQQIHQAIG-------ICD 169
Cdd:cd19161 101 -SYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKERHHFAQLMSG--GFKALEELKKAGVIKAFGlgvnevqICL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 170 RLSlhkpvvEQPQYN-MMVRDRFeweyesvfaSGYGSTIWSPLYQG--------LLTGKYNDDILADGRFNNSdniyvkh 240
Cdd:cd19161 178 EAL------DEADLDcFLLAGRY---------SLLDQSAEEEFLPRceqrgtslVIGGVFNSGILATGTKSGA------- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124399033 241 FYQQILGDPEkrtkIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQ 308
Cdd:cd19161 236 KFNYGDAPAE----IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQ 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-325 |
4.45e-21 |
|
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: 92.10 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVS-----AISYGN-WVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvQRQDIVISTKI 83
Cdd:cd19146 8 GVRVSplclgAMSFGEaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 ---YGGDGNDFPNSKYL--SRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:cd19146 87 ttgYRRGGPIKIKSNYQgnHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 159 QQIHQAIGICDRLSLHKPVVEQPQYNMMVRDrFEWEYESV-FASGYGSTIWSPLYQGlltgkyndDILADGRFNNSDNIY 237
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAAFRD-FERDILPMcEAEGMALAPWGVLGQG--------QFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 238 VKHFYQQilgdpEKRTKIQnqlKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEV 317
Cdd:cd19146 238 RKGGPQT-----EKERKVS---EKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGIS--LSDEE 307
|
....*...
gi 124399033 318 EQKIESIL 325
Cdd:cd19146 308 IQEIEDAY 315
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-319 |
5.22e-21 |
|
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: 91.14 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGN---WVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGG 86
Cdd:cd19120 1 GSKIPAIAFGTgtaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYGN---EKEVGEALKESGVPREDLFITTKVSPG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 87 DGNdfpnskylsrkhlIEG-LRNSLKRLDTPYVDIVFAH----RYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQI 161
Cdd:cd19120 78 IKD-------------PREaLRKSLAKLGVDYVDLYLIHspffAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 162 HQAIGICDrlslHKPVVEQPQYNMMVRDRFE--WEY---ESVFASGYGSTiwSPLYQGlltgkynddilADGRFNnsdni 236
Cdd:cd19120 145 EELLDTAK----IKPAVNQIEFHPYLYPQQPalLEYcreHGIVVSAYSPL--SPLTRD-----------AGGPLD----- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 237 yvkhfyqqilgdpekrtkiqnqlKQLGEVAKELGVTQAQLSLAWALKnKDVsTAITSATRPEQLEETVKsVQVVKLITKE 316
Cdd:cd19120 203 -----------------------PVLEKIAEKYGVTPAQVLLRWALQ-KGI-VVVTTSSKEERMKEYLE-AFDFELTEEE 256
|
...
gi 124399033 317 VEQ 319
Cdd:cd19120 257 VEE 259
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-302 |
5.28e-19 |
|
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: 85.02 E-value: 5.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 15 AISYGNWvnsddKDTQDRNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYggdgndfpnS 94
Cdd:cd19073 3 ALGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIYNN---EAEVGEAIAESGVPREDLFITTKVW---------R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 95 KYLSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLslh 174
Cdd:cd19073 66 DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 175 kPVVEQPQYNMMVRDRFEWEYesvfASGYGSTI--WSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQILGDPEkr 252
Cdd:cd19073 143 -IAVNQVEFHPFLYQAELLEY----CRENDIVItaYSPLARG-----------------------------EVLRDPV-- 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 124399033 253 tkiqnqlkqLGEVAKELGVTQAQLSLAWaLKNKDVStAITSATRPEQLEE 302
Cdd:cd19073 187 ---------IQEIAEKYDKTPAQVALRW-LVQKGIV-VIPKASSEDHLKE 225
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-323 |
2.70e-18 |
|
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: 83.92 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 36 IIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQDIVISTKiyggdgndF-PNSKYLSRKHLIEGLRNSLKRLD 114
Cdd:cd19103 37 VFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRYP--REDYIISTK--------FtPQIAGQSADPVADMLEGSLARLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 115 TPYVDIVFAHRydyQTPLEE-TCRAFDwIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVeQPQYNMMVRDrfeW 193
Cdd:cd19103 107 TDYIDIYWIHN---PADVERwTPELIP-LLKSGKVKHVGVSNHNLAEIKRANEILAKAGVSLSAV-QNHYSLLYRS---S 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 194 EYESVFASGYGSTI----WSPLYQGLLTGKYNddiladgrfnnsdniyVKHFYQQILGDPEKRTKIQNQLKQL----GEV 265
Cdd:cd19103 179 EEAGILDYCKENGItffaYMVLEQGALSGKYD----------------TKHPLPEGSGRAETYNPLLPQLEELtavmAEI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124399033 266 AKELGVTQAQLSLAWAL-KNkdvSTAITSATRPEQLEETVKSVQvVKLITKEVEQkIES 323
Cdd:cd19103 243 GAKHGASIAQVAIAWAIaKG---TTPIIGVTKPHHVEDAARAAS-ITLTDDEIKE-LEQ 296
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
17-312 |
4.81e-18 |
|
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: 82.58 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 17 SYGnWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDgkAEIHLGHALKTLnvqrQDIVISTKIyggdgNDFPNSKY 96
Cdd:cd19097 13 DYG-IANKSGKPSEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRL----DKFKIITKL-----PPLKEDKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 97 LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYqtpLEETCRA-FDWIIRH---GLAHYWGTSEWTAQQIHQAigicdrLS 172
Cdd:cd19097 81 EDEAAIEASVEASLKRLKVDSLDGLLLHNPDD---LLKHGGKlVEALLELkkeGLIRKIGVSVYSPEELEKA------LE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 173 LHKPVVEQPQYNMMvrDRfEWEYESVFASGYGSTIW----SPLYQGLLtgkynddiladgrFNNSDNIyvkhfyqqilgd 248
Cdd:cd19097 152 SFKIDIIQLPFNIL--DQ-RFLKSGLLAKLKKKGIEiharSVFLQGLL-------------LMEPDKL------------ 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124399033 249 PEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVKL 312
Cdd:cd19097 204 PAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-306 |
9.51e-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: 81.45 E-value: 9.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 14 SAISYG------NWVNSDDkdtQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKtlNVQRQDIVISTKIyggd 87
Cdd:cd19096 1 SVLGFGtmrlpeSDDDSID---EEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALK--EGPREKFYLATKL---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 88 gndfPNSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH---RYDYQTPLEEtCRAFDWIIR---HGLAHYWG-TSEWTAQQ 160
Cdd:cd19096 72 ----PPWSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPEWLEKARK-GGLLEFLEKakkEGLIRHIGfSFHDSPEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 161 IHQAI--GICDRLSLHkpvveqpqYNMMVRDRFEWE--YESVFASGYGSTIWSPLYQGLLTgkynddiladgrfnnsdni 236
Cdd:cd19096 147 LKEILdsYDFDFVQLQ--------YNYLDQENQAGRpgIEYAAKKGMGVIIMEPLKGGGLA------------------- 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 237 yvkhfyqqilgdpekrtkiqNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKS 306
Cdd:cd19096 200 --------------------NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-302 |
1.99e-17 |
|
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: 80.60 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 15 AISYGNWvNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIyggdgndfpNS 94
Cdd:cd19071 3 LIGLGTY-KLKPEETAE----AVLAALEAGYRHIDTAAAYGN---EAEVGEAIRESGVPREELFITTKL---------WP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 95 KYLSRKHLIEGLRNSLKRLDTPYVDIVFAH------RYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGIC 168
Cdd:cd19071 66 TDHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 169 DrlslHKPVVEQpqynmmvrdrFEweyesvfasgygstiWSPLYQglltgkyNDDILAdgrFNNSDNIYV------KHFY 242
Cdd:cd19071 146 R----IKPAVNQ----------IE---------------LHPYLQ-------QKELVE---FCKEHGIVVqaysplGRGR 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 243 QQILGDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALkNKDVSTaITSATRPEQLEE 302
Cdd:cd19071 187 RPLLDDPV-----------LKEIAKKYGKTPAQVLLRWAL-QRGVVV-IPKSSNPERIKE 233
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-158 |
4.03e-17 |
|
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: 80.82 E-value: 4.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 11 LKVSAISYGNWVNSDDKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTL----NVQRQDIVISTKiyGG 86
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTK--AG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 87 ---DGNDFPNSKY-----------------------LSRKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTP--------- 131
Cdd:cd19099 79 yipGDGDEPLRPLkyleeklgrglidvadsaglrhcISPAYLEDQIERSLKRLGLDTIDLYLLHNPEEQLLelgeeefyd 158
|
170 180
....*....|....*....|....*...
gi 124399033 132 -LEETCRAFDWIIRHGLAHYWGTSEWTA 158
Cdd:cd19099 159 rLEEAFEALEEAVAEGKIRYYGISTWDG 186
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
19-309 |
8.10e-17 |
|
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: 79.96 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 19 GN-WVNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvqRQDIVISTKIyG-------GDGND 90
Cdd:cd19152 11 GNlYEAVSDEEAKA----TLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKV-GrllvplqEVEPT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 91 FPNSKYLSRKHLI------EGLRN----SLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIR-----------HGLAH 149
Cdd:cd19152 84 FEPGFWNPLPFDAvfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKgafraleelreEGVIK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 150 YW--GTSEWT-AQQIHQAIG-----ICDRLSLhkpvVEQPQYnmmvrDRFeweYESVFASGYGSTIWSPlyqglltgkYN 221
Cdd:cd19152 164 AIglGVNDWEvILRILEEADldwvmLAGRYTL----LDHSAA-----REL---LPECEKRGVKVVNAGP---------FN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 222 DDILADGRFNNSDNiyvkhfYQQilGDPEkrtkIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLE 301
Cdd:cd19152 223 SGFLAGGDNFDYYE------YGP--APPE----LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVE 290
|
....*...
gi 124399033 302 ETVKSVQV 309
Cdd:cd19152 291 ENVALLAT 298
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-315 |
1.78e-16 |
|
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: 78.73 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 4 RRLGATGLKVSAIS---------YGNWVNSDDKDtqdrntKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNVQR 74
Cdd:cd19153 3 ETLEIALGNVSPVGlgtaalggvYGDGLEQDEAV------AIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 75 QDIVISTKI--YGGDGNDFpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAHRY---DYQTPLEETCRAFdwiirhglah 149
Cdd:cd19153 77 SSYTVATKVgrYRDSEFDY------SAERVRASVATSLERLHTTYLDVVYLHDIefvDYDTLVDEALPAL---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 150 ywgtSEWTAQQIHQAIGIC-----------DRLSLHKPVVEQPQYNMMVRDRFEWEYESVFASGYGSTIW--SPLYQGLL 216
Cdd:cd19153 141 ----RTLKDEGVIKRIGIAgypldtltratRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVInaSPLSMGLL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 217 TGKynddiladgrfnnsdniyvkhfyqqilgDPEKRTKIQNQLKQLGEVA----KELGVTQAQLSLAWALKNKD-VSTAI 291
Cdd:cd19153 217 TSQ----------------------------GPPPWHPASGELRHYAAAAdavcASVEASLPDLALQYSLAAHAgVGTVL 268
|
330 340
....*....|....*....|....
gi 124399033 292 TSATRPEQLEETVKSVQVVKLITK 315
Cdd:cd19153 269 LGPSSLAQLRSMLAAVDAVASLGA 292
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
34-124 |
2.13e-15 |
|
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: 75.39 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 34 TKIIQKAWELGINFFDTAEIYGDgkAEIHLGHALKTL--NVQRQDIVISTKI--YGGDGNDFpnskylSRKHLIEGLRNS 109
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYYGP--SEIILGRALKALrdEFPRDTYFIITKVgrYGPDDFDY------SPEWIRASVERS 108
|
90
....*....|....*
gi 124399033 110 LKRLDTPYVDIVFAH 124
Cdd:cd19164 109 LRRLHTDYLDLVYLH 123
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
40-312 |
2.30e-15 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 75.06 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 40 AWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYggdgndfpnSKYLSRKHLIEGLRNSLKRLDTPYVD 119
Cdd:PRK11172 25 ALELGYRAIDTAQIYDN---EAAVGQAIAESGVPRDELFITTKIW---------IDNLAKDKLIPSLKESLQKLRTDYVD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 120 IVFAH--RYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEQPQY--NMMVRDrfewey 195
Cdd:PRK11172 93 LTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPYlqNRKVVA------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 196 esvFASGYGSTIWSplYQGLLTGKynddiladgrfnnsdniyvkhfyqqILGDPekrtkiqnqlkQLGEVAKELGVTQAQ 275
Cdd:PRK11172 167 ---FAKEHGIHVTS--YMTLAYGK-------------------------VLKDP-----------VIARIAAKHNATPAQ 205
|
250 260 270
....*....|....*....|....*....|....*..
gi 124399033 276 LSLAWALKNKdvSTAITSATRPEQLEETVKSvQVVKL 312
Cdd:PRK11172 206 VILAWAMQLG--YSVIPSSTKRENLASNLLA-QDLQL 239
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
29-304 |
6.14e-15 |
|
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: 74.32 E-value: 6.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 29 TQDRNTKIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLnvQRQDIVISTKI-----YGGDGNDFPNSKY--LSRKH 101
Cdd:cd19162 17 GEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH--PRAEYVVSTKVgrllePGAAGRPAGADRRfdFSADG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 102 LIEGLRNSLKRLDTPYVDIVFAHRYD--YQTPLEETCRAFDWIIRHGLAhywgtsewtaqqihQAIGI-CDRLSLHKPVV 178
Cdd:cd19162 95 IRRSIEASLERLGLDRLDLVFLHDPDrhLLQALTDAFPALEELRAEGVV--------------GAIGVgVTDWAALLRAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 179 EQPQYN-MMVRDRF---EWEYESVF-----ASGYGSTIWSPLYQGLLTGkyndDILADGRFNnsdniyvkhfYQQIlgdp 249
Cdd:cd19162 161 RRADVDvVMVAGRYtllDRRAATELlplcaAKGVAVVAAGVFNSGILAT----DDPAGDRYD----------YRPA---- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 124399033 250 eKRTKIQnQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETV 304
Cdd:cd19162 223 -TPEVLA-RARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNL 275
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
34-319 |
1.05e-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: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 34 TKIIQKAWELGINFFDTAEIYgDGKAEIhlGHALKTLNVQRQDIVISTKIYggdgndFPNskyLSRKHLIEGLRNSLKRL 113
Cdd:cd19139 17 IDSVRTALELGYRHIDTAQIY-DNEAAV--GQAIAESGVPRDELFITTKIW------IDN---LSKDKLLPSLEESLEKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 114 DTPYVDIVFAH---RYDyQTPLEET----CRAFDwiirHGLAHYWGTSEWTAQQIHQAIGICDRLSLHKPVVEqpqynmm 186
Cdd:cd19139 85 RTDYVDLTLIHwpsPND-EVPVEEYigalAEAKE----QGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIE------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 187 vrdrfeweyesvfasgygstiWSPLYQglltgkynDDILADgrFNNSDNIYVKHF----YQQILGDPekrtkiqnqlkQL 262
Cdd:cd19139 153 ---------------------LSPYLQ--------NRKLVA--HCKQHGIHVTSYmtlaYGKVLDDP-----------VL 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 263 GEVAKELGVTQAQLSLAWALkNKDVStAITSATRPEQLEETVKSVQvVKLITKEVEQ 319
Cdd:cd19139 191 AAIAERHGATPAQIALAWAM-ARGYA-VIPSSTKREHLRSNLLALD-LTLDADDMAA 244
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
10-322 |
3.93e-12 |
|
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: 66.39 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVS-----AISYGN-WvnSDDKDTQDRNT--KIIQKAWELGINFFDTAEIYGDGKAEIHLGHALKTLNvQRQDIVIST 81
Cdd:cd19147 7 GIRVSplilgAMSIGDaW--SGFMGSMDKEQafELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 82 KiYGGDGNDFPNSKYLS-------RKHLIEGLRNSLKRLDTPYVDIVFAHRYDYQTPLEETCRAFDWIIRHGLAHYWGTS 154
Cdd:cd19147 84 K-FTTDYKAYEVGKGKAvnycgnhKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 155 EWTAQQIHQAIGICDRLSLHKPVVEQPQYNMMVRDrFEWEYESVfASGYGSTIwSPlYQGLLTGKYNDDILADGRFNNSD 234
Cdd:cd19147 163 DTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRD-FERDIIPM-ARHFGMAL-AP-WDVLGGGKFQSKKAVEERKKNGE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 235 NIyvkhfyQQILGDPEKRTKIQNQLKQLGEVAKELGVTQ-AQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklI 313
Cdd:cd19147 239 GL------RSFVGGTEQTPEEVKISEALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIK--L 310
|
....*....
gi 124399033 314 TKEVEQKIE 322
Cdd:cd19147 311 TPEEIEYLE 319
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
16-302 |
1.25e-11 |
|
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: 63.93 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 16 ISYGNWVNSDDKDTQdrntkIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGD-GNDFPns 94
Cdd:cd19131 13 LGLGVWQVSNDEAAS-----AVREALEVGYRSIDTAAIYGN---EEGVGKAIRASGVPREELFITTKLWNSDqGYDST-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 95 kylsrkhlIEGLRNSLKRLDTPYVDIVFAHrydYQTPLE----ETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDR 170
Cdd:cd19131 83 --------LRAFDESLRKLGLDYVDLYLIH---WPVPAQdkyvETWKALIELKKEGRVKSIGVSNFTIEHLQRLIDETGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 171 lslhKPVVEQ----PQYNMMVRDRFEWEYESVFASgygstiWSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQIL 246
Cdd:cd19131 152 ----VPVVNQielhPRFQQRELRAFHAKHGIQTES------WSPLGQG-----------------------------GLL 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124399033 247 GDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALKNKDVstAITSATRPEQLEE 302
Cdd:cd19131 193 SDP-----------VIGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAE 235
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-167 |
3.93e-11 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 62.90 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTQdrntkIIQKAWELGINFFDTAEIYGDGKAeihLGHALKTL----NVQRQDIVISTKIYg 85
Cdd:cd19111 1 GFPMPVIGLGTYQSPPEEVRA-----AVDYALFVGYRHIDTALSYQNEKA---IGEALKWWlkngKLKREEVFITTKLP- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 gdgndfpnSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH-------------RYDYQTPLEETCRAFDWIIRHGLAHYWG 152
Cdd:cd19111 72 --------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170
....*....|....*
gi 124399033 153 TSEWTAQQIHQAIGI 167
Cdd:cd19111 144 LSNFNPRQINKILAY 158
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-180 |
3.98e-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: 63.20 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvnsddKDTQDRNTKIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTL----NVQRQDIVISTKIY 84
Cdd:cd19154 8 NGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegVVKREDLFITTKLW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 85 ggdgndfpnSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH--------RYDYQT-----------PLEETCRAFDWIIRH 145
Cdd:cd19154 80 ---------THEHAPEDVEEALRESLKKLQLEYVDLYLIHapaafkddEGESGTmengmsihdavDVEDVWRGMEKVYDE 150
|
170 180 190
....*....|....*....|....*....|....*
gi 124399033 146 GLAHYWGTSEWTAQQIHQAIGICdrlsLHKPVVEQ 180
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNA----RVKPHNNQ 181
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-309 |
3.05e-09 |
|
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: 57.42 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 1 MEYRRLgATGLKVSAISYGNWvNSDDKDTQdrntKIIQKAWELGINFFDTAEIYGDgKAEI--HLGHALKTLNVQRQDIV 78
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTW-KSKPGEVG----QAVKQALEAGYRHIDCAAIYGN-EAEIgaALAEVFKEGKVKREDLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 79 ISTKIYggdgndfpNSKYLSrKHLIEGLRNSLKRLDTPYVDIVFAH--------------RYDY----QTPLEETCRAFD 140
Cdd:cd19123 74 ITSKLW--------NNSHAP-EDVLPALEKTLADLQLDYLDLYLMHwpvalkkgvgfpesGEDLlslsPIPLEDTWRAME 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 141 WIIRHGLAHYWGTSEWTAQQIHQAIG------ICDRLSLHkPVVEQPQYNMMVRDRfeweyesvfasGYGSTIWSPLyqg 214
Cdd:cd19123 145 ELVDKGLCRHIGVSNFSVKKLEDLLAtarikpAVNQVELH-PYLQQPELLAFCRDN-----------GIHLTAYSPL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 215 lltgkynddiladGRfnnsdniyvkhfyqqilGDPEKRTKIQNQLKQL-----GEVAKELGVTQAQLSLAWALKNKdvST 289
Cdd:cd19123 210 -------------GS-----------------GDRPAAMKAEGEPVLLedpviNKIAEKHGASPAQVLIAWAIQRG--TV 257
|
330 340
....*....|....*....|
gi 124399033 290 AITSATRPEQLEETVKSVQV 309
Cdd:cd19123 258 VIPKSVNPERIQQNLEAAEV 277
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-325 |
6.87e-09 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 56.45 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 42 ELGINFFDTAEIYGDgkAEIHLGHALKTL---NVQRQDIVISTKIYggdgnDFPNSKYLSRKHLIEGLRNSLKRLDTPYV 118
Cdd:cd19101 34 DAGLTTFDCADIYGP--AEELIGEFRKRLrreRDAADDVQIHTKWV-----PDPGELTMTRAYVEAAIDRSLKRLGVDRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 119 DIVFAHRYDYQTP-LEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQaigICDrlSLHKPVVEQPQYNMMVRdRFEWEYES 197
Cdd:cd19101 107 DLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLRE---ILD--AGVPIVSNQVQYSLLDR-RPENGMAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 198 VFAS------GYGStiwspLYQGLLTGKYNDdiLADGRFNNSDNiYVKHFYQQIL---GDPEkrtKIQNQLKQLGEVAKE 268
Cdd:cd19101 181 LCEDhgikllAYGT-----LAGGLLSEKYLG--VPEPTGPALET-RSLQKYKLMIdewGGWD---LFQELLRTLKAIADK 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 269 LGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVklITKEVEQKIESIL 325
Cdd:cd19101 250 HGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSFR--LDDEDRAAIDAVL 304
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
35-302 |
8.74e-09 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 55.72 E-value: 8.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 35 KIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTL----NVQRQDIVISTKIyggdgndfpNSKYLSRKHLIEGLRNSL 110
Cdd:cd19136 19 QAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyGLSREDIFITSKL---------APKDQGYEKARAACLGSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 111 KRLDTPYVDIVFAH-----RYDYQTPLEETCRAFDW-----IIRHGLAHYWGTSEWTAQQIHQAIGICDRlslhKPVVEQ 180
Cdd:cd19136 87 ERLGTDYLDLYLIHwpgvqGLKPSDPRNAELRRESWraledLYKEGKLRAIGVSNYTVRHLEELLKYCEV----PPAVNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 181 ----PQYNMmvRDRFEW-EYESVFASGYgstiwSPLYQGLLTgkynddiladgrfnnsdniyvkhfyqqILGDPEkrtki 255
Cdd:cd19136 163 vefhPHLVQ--KELLKFcKDHGIHLQAY-----SSLGSGDLR---------------------------LLEDPT----- 203
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 124399033 256 qnqlkqLGEVAKELGVTQAQLSLAWALKNkDVStAITSATRPEQLEE 302
Cdd:cd19136 204 ------VLAIAKKYGRTPAQVLLRWALQQ-GIG-VIPKSTNPERIAE 242
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-283 |
1.14e-08 |
|
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: 55.35 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKdtqdrNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGDGn 89
Cdd:cd19132 4 GTQIPAIGFGTYPLKGDE-----GVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKLPGRHH- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 dfpnskylSRKHLIEGLRNSLKRLDTPYVDIVFAH-------RYdyqtplEETCRAFDWIIRHGLAHYWGTSEWTAQQIh 162
Cdd:cd19132 75 --------GYEEALRTIEESLYRLGLDYVDLYLIHwpnpsrdLY------VEAWQALIEAREEGLVRSIGVSNFLPEHL- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 163 qaigicDRLSLH---KPVVEQ----PQYNMMVRDRFEWEYESVFASgygstiWSPLYQGlltgkynddiladgrfnnsdn 235
Cdd:cd19132 140 ------DRLIDEtgvTPAVNQielhPYFPQAEQRAYHREHGIVTQS------WSPLGRG--------------------- 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 124399033 236 iyvkhfyQQILGDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALK 283
Cdd:cd19132 187 -------SGLLDEP-----------VIKAIAEKHGKTPAQVVLRWHVQ 216
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
10-180 |
1.71e-08 |
|
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: 54.98 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTqdrnTKIIQKAWELGINFFDTAEIYGDgKAEIhlGHALKTL----NVQRQDIVISTKIYG 85
Cdd:cd19116 8 GNEIPAIALGTWKLKDDEGV----RQAVKHAIEAGYRHIDTAYLYGN-EAEV--GEAIREKiaegVVKREDLFITTKLWN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 gdgndfpnsKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH-------RYDYQTPLE---------ETCRAFDWIIRHGLAH 149
Cdd:cd19116 81 ---------SYHEREQVEPALRESLKRLGLDYVDLYLIHwpvafkeNNDSESNGDgslsdidylETWRGMEDLVKLGLTR 151
|
170 180 190
....*....|....*....|....*....|.
gi 124399033 150 YWGTSEWTAQQIHQAIgicdRLSLHKPVVEQ 180
Cdd:cd19116 152 SIGVSNFNSEQINRLL----SNCNIKPAVNQ 178
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-180 |
4.11e-08 |
|
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: 53.93 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvnsDDKDTQDRNTkiIQKAWELGINFFDTAEIYGDgkaEIHLGHALK-----TLNVQRQDIVISTKI 83
Cdd:cd19106 3 TGQKMPLIGLGTW---KSKPGQVKAA--VKYALDAGYRHIDCAAVYGN---EQEVGEALKekvgpGKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 YggdgndfpNSKYlsRKHLIEG-LRNSLKRLDTPYVDIVFAH--------------------RYDYqTPLEETCRAFDWI 142
Cdd:cd19106 75 W--------NTKH--HPEDVEPaLRKTLKDLQLDYLDLYLIHwpyafergdnpfpknpdgtiRYDS-THYKETWKAMEKL 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 124399033 143 IRHGLAHYWGTSEWTAQQIHQAIGICDrlslHKPVVEQ 180
Cdd:cd19106 144 VDKGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQ 177
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-318 |
4.94e-08 |
|
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: 53.68 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 16 ISYGNWVNSDDKDTQDrntkiIQKAWELGINFFDTAEIYGD----GKAeihLGHALKTLNVQRQDIVISTKIYggdgndf 91
Cdd:cd19128 4 LGFGTYKITESESKEA-----VKNAIKAGYRHIDCAYYYGNeafiGIA---FSEIFKDGGVKREDLFITSKLW------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 92 pnsKYLSRKHLI-EGLRNSLKRLDTPYVDIVFAH-------------------RYDYQTPLEETCRAFDWIIRHGLAHYW 151
Cdd:cd19128 69 ---PTMHQPENVkEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprddnqiQSLSKKPLEDTWRAMEQCVDEKLTKNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 152 GTSEWTAQQIHQAIGICDRlslhKPVVEQpqynmmvrdrfeweYESvfasgygstiwSPLYQglltgkyNDDILadgRFN 231
Cdd:cd19128 146 GVSNYSTKLLTDLLNYCKI----KPFMNQ--------------IEC-----------HPYFQ-------NDKLI---KFC 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 232 NSDNIYVKHfYQQILGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALK--NKDVSTAITSATrPEQLEETVKSVQv 309
Cdd:cd19128 187 IENNIHVTA-YRPLGGSYGDGNLTFLNDSELKALATKYNTTPPQVIIAWHLQkwPKNYSVIPKSAN-KSRCQQNFDIND- 263
|
....*....
gi 124399033 310 VKLITKEVE 318
Cdd:cd19128 264 LALTKEDMD 272
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-324 |
6.44e-08 |
|
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: 53.12 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvNSDDKDTQDRntkiIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTL----NVQRQDIVISTKIY 84
Cdd:cd19125 7 TGAKIPAVGLGTW-QADPGVVGNA----VKTAIKEGYRHIDCAAIYGN---EKEIGKALKKLfedgVVKREDLFITSKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 85 ggdgndfpnSKYLSRKHLIEGLRNSLKRLDTPYVDIVFAH-------------RYDY-QTPLEETCRAFDWIIRHGLAHY 150
Cdd:cd19125 79 ---------CTDHAPEDVPPALEKTLKDLQLDYLDLYLIHwpvrlkkgahmpePEEVlPPDIPSTWKAMEKLVDSGKVRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 151 WGTSEWTAQQIHQAIGICDRlslhKPVVEQ-------PQYNMmvrdrfeWEY---ESVFASGYgstiwSPlyqglltgky 220
Cdd:cd19125 150 IGVSNFSVKKLEDLLAVARV----PPAVNQvechpgwQQDKL-------HEFcksKGIHLSAY-----SP---------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 221 nddiladgrfnnsdniyvkhfyqqiLGDPEKRTKIQNQLKQ--LGEVAKELGVTQAQLSLAWALKNKdvSTAITSATRPE 298
Cdd:cd19125 204 -------------------------LGSPGTTWVKKNVLKDpiVTKVAEKLGKTPAQVALRWGLQRG--TSVLPKSTNEE 256
|
330 340
....*....|....*....|....*..
gi 124399033 299 QLEEtvkSVQVVKL-ITKEVEQKIESI 324
Cdd:cd19125 257 RIKE---NIDVFDWsIPEEDFAKFSSI 280
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
42-302 |
7.27e-08 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 52.71 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 42 ELGINFFDTAEIYGdgkAEIHLGHALKTLNVQRQDIVISTKIYGGDgndfpnskYLSRKhLIEGLRNSLKRLDTPYVDIV 121
Cdd:cd19135 37 ECGYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTTKLWPSD--------YGYES-TKQAFEASLKRLGVDYLDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 122 FAHRYDYQTP-------LEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRLslhkPVVEQPQYNMMVRDRFEWE 194
Cdd:cd19135 105 LLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCSVV----PHVNQVEFHPFQNPVELIE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 195 Y---ESVFASGYgstiwSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQILGDPekrtKIQnqlkqlgEVAKELGV 271
Cdd:cd19135 181 YcrdNNIVFEGY-----CPLAKG-----------------------------KALEEP----TVT-------ELAKKYQK 215
|
250 260 270
....*....|....*....|....*....|.
gi 124399033 272 TQAQLSLAWALKNkDVSTaITSATRPEQLEE 302
Cdd:cd19135 216 TPAQILIRWSIQN-GVVT-IPKSTKEERIKE 244
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-124 |
9.95e-08 |
|
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: 52.50 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWVNSDDKdtqdrNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYggdg 88
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNE-----VAKAVEAALKAGYRHIDTAAIYGN---EEEVGQGIKDSGVPREEIFITTKLW---- 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 124399033 89 NDFpnskylsRKHLIEGLRNSLKRLDTPYVDIVFAH 124
Cdd:cd19117 78 CTW-------HRRVEEALDQSLKKLGLDYVDLYLMH 106
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-324 |
1.46e-07 |
|
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: 52.49 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvnsddKDTQDRNTKIIQKAWELGINFFDTAEIYGD----GKAeihLGHALKTLNVQRQDIVISTKIY 84
Cdd:cd19112 7 SGHKMPVIGLGVW-----RMEPGEIKELILNAIKIGYRHFDCAADYKNekevGEA---LAEAFKTGLVKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 85 GGDgndfpnskylsRKHLIEGLRNSLKRLDTPYVDIVFAH-----------------------RYDYQTPLEETCRAFDW 141
Cdd:cd19112 79 NSD-----------HGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWHAMEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 142 IIRHGLAHYWGTSEWTAQQIHQaigiCDRLSLHKPVVEQpqynMMVRDRFEWEYESVFASGYG--STIWSPLYQGLLtgk 219
Cdd:cd19112 148 LVSAGLVRSIGISNYDIFLTRD----CLAYSKIKPAVNQ----IETHPYFQRDSLVKFCQKHGisVTAHTPLGGAAA--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 220 yNDDiladgRFNnsdniyvkhfYQQILGDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALKNKDVstAITSATRPEQ 299
Cdd:cd19112 217 -NAE-----WFG----------SVSPLDDP-----------VLKDLAKKYGKSAAQIVLRWGIQRNTA--VIPKSSKPER 267
|
330 340
....*....|....*....|....*
gi 124399033 300 LEETVKsVQVVKLiTKEVEQKIESI 324
Cdd:cd19112 268 LKENID-VFDFQL-SKEDMKLIKSL 290
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
36-283 |
1.53e-07 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 52.28 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 36 IIQKAWELGINFFDTAEIYGDgkaeiHLGHAL--KTLNVQRQDIVISTKI---YGGDGNDFPNskyLSRKHLIEGLRNSL 110
Cdd:PRK10376 45 VLREAVALGVNHIDTSDFYGP-----HVTNQLirEALHPYPDDLTIVTKVgarRGEDGSWLPA---FSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 111 KRLDTPYVDIV-FAHRYDYQTP----LEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDrlslhkPVVEQPQYNM 185
Cdd:PRK10376 117 RNLGLDVLDVVnLRLMGDGHGPaegsIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIAE------IVCVQNHYNL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 186 MVRDrfeweyesvfasgygstiwsplyqglltgkynDDILADGRfnNSDNI-YVKHFyqqILGDpekRTKIQNQlkQLGE 264
Cdd:PRK10376 191 AHRA--------------------------------DDALIDAL--ARDGIaYVPFF---PLGG---FTPLQSS--TLSD 228
|
250
....*....|....*....
gi 124399033 265 VAKELGVTQAQLSLAWALK 283
Cdd:PRK10376 229 VAASLGATPMQVALAWLLQ 247
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
19-124 |
1.54e-07 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 19 GNWVNSDDKdtqdrNTKIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTLNVQRQDIVISTKIYGGDgndfpnskyls 98
Cdd:PRK11565 21 GVWQASNEE-----VITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKLWNDD----------- 81
|
90 100
....*....|....*....|....*.
gi 124399033 99 RKHLIEGLRNSLKRLDTPYVDIVFAH 124
Cdd:PRK11565 82 HKRPREALEESLKKLQLDYVDLYLMH 107
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
10-302 |
2.81e-07 |
|
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: 51.06 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWvNSDDKDTQdrntKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGD-G 88
Cdd:cd19130 7 GNSIPQLGYGVF-KVPPADTQ----RAVATALEVGYRHIDTAAIYGN---EEGVGAAIAASGIPRDELFVTTKLWNDRhD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 89 NDFPNSKYlsrkhlieglRNSLKRLDTPYVDIVFAHrydYQTPLE----ETCRAFDWIIRHGLAHYWGTSEWTAQQIHQA 164
Cdd:cd19130 79 GDEPAAAF----------AESLAKLGLDQVDLYLVH---WPTPAAgnyvHTWEAMIELRAAGRTRSIGVSNFLPPHLERI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 165 IGICDRLslhkPVVEQPQYNMMVRDRFEWEYESvfASGYGSTIWSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQ 244
Cdd:cd19130 146 VAATGVV----PAVNQIELHPAYQQRTIRDWAQ--AHDVKIEAWSPLGQG-----------------------------K 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 124399033 245 ILGDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALKNKdvSTAITSATRPEQLEE 302
Cdd:cd19130 191 LLGDP-----------PVGAIAAAHGKTPAQIVLRWHLQKG--HVVFPKSVRRERMED 235
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-302 |
3.82e-07 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 50.65 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTQdrntKIIQKAWELGINFFDTAEIYGDGKAeihLGHALKTLNVQRQDIVISTKIYggdgn 89
Cdd:cd19133 6 GVEMPILGFGVFQIPDPEECE----RAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKLW----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 90 dFPNSKYLSRKHLIEGlrnSLKRLDTPYVDIVFAHR--YDYqtplEETCRAFDWIIRHGLAHYWGTSEWTAQQIhqaigi 167
Cdd:cd19133 74 -IQDAGYEKAKKAFER---SLKRLGLDYLDLYLIHQpfGDV----YGAWRAMEELYKEGKIRAIGVSNFYPDRL------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 168 cDRLSLH---KPVVEQPQYNMmvrdrFEWEYESV-FASGYGSTI--WSPlyqglltgkynddiLADGRFNnsdniyvkhf 241
Cdd:cd19133 140 -VDLILHnevKPAVNQIETHP-----FNQQIEAVeFLKKYGVQIeaWGP--------------FAEGRNN---------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124399033 242 yqqILGDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKnKDVSTaITSATRPEQLEE 302
Cdd:cd19133 190 ---LFENPV-----------LTEIAEKYGKSVAQVILRWLIQ-RGIVV-IPKSVRPERIAE 234
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
15-300 |
6.25e-07 |
|
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: 50.24 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 15 AISYGNWVNSDDKDTQDrntkiIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGDgNDFPNS 94
Cdd:cd19134 13 VIGLGVGELSDDEAERS-----VSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKLATPD-QGFTAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 95 kylsrkhlIEGLRNSLKRLDTPYVDIVFAHrydYQTPLE----ETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGicdr 170
Cdd:cd19134 84 --------QAACRASLERLGLDYVDLYLIH---WPAGREgkyvDSWGGLMKLREEGLARSIGVSNFTAEHLENLID---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 171 LSLHKPVVEQ----PQYNMMVRDRFEWEYESVFASgygstiWSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQIL 246
Cdd:cd19134 149 LTFFTPAVNQielhPLLNQAELRKVNAQHGIVTQA------YSPLGVG-----------------------------RLL 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 124399033 247 GDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVstAITSATRPEQL 300
Cdd:cd19134 194 DNPA-----------VTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERI 234
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-124 |
8.70e-07 |
|
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: 49.72 E-value: 8.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWVNSDDKDTQDrntkiIQKAWELGINFFDTAEIYGDgKAEIhlGHALKTL-----NVQRQDIVISTKI 83
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAA-----VKIALKAGYRHLDLAKVYQN-QHEV--GQALKELlkeepGVKREDLFITSKL 74
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124399033 84 YggdgndfpNSKYlSRKHLIEGLRNSLKRLDTPYVDIVFAH 124
Cdd:cd19118 75 W--------NNSH-RPEYVEPALDDTLKELGLDYLDLYLIH 106
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-309 |
1.59e-06 |
|
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: 49.16 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWVNSDDKDtqdRNTKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTL-----NVQRQDIVISTKI 83
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKG---ETYAAVTKALDVGYRHLDCAWFYLN---EDEVGDAVRDFlkenpSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 YggdgndfpnsKYLSR-KHLIEGLRNSLKRLDTPYVDIVFAH------RYDYQTPL-----------------EETCRAF 139
Cdd:cd19122 79 W----------NHLHEpEDVKWSIDNSLKNLKLDYIDLFLVHwpiaaeKNDQRSPKlgpdgkyvilkdltenpEPTWRAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 140 DWIIRHGLAHYWGTSEWTAQQIHQAIGICDRlslhKPVVEQPQYNMMVRDRFEWEYesVFASGYGSTIWSPLyqglltGK 219
Cdd:cd19122 149 EEIYESGKAKAIGVSNWTIPGLKKLLSFAKV----KPHVNQIEIHPFLPNEELVDY--CFSNDILPEAYSPL------GS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 220 YNddiladgrfnnsdniyvkhfyqQILGDPEKrtkiQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVstAITSATRPEQ 299
Cdd:cd19122 217 QN----------------------QVPSTGER----VSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSR 268
|
330
....*....|
gi 124399033 300 LEETVKSVQV 309
Cdd:cd19122 269 IESNFKSIEL 278
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
31-216 |
2.94e-06 |
|
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: 47.82 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 31 DRNTKIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTLNVQRQDIVISTKIYGGDGNDfpnskylsrKHLIEGLRNSL 110
Cdd:cd19126 23 DETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKLWNDDQRA---------RRTEDAFQESL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 111 KRLDTPYVDIVFAHrYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGICDRlslhKPVVEQPQYNMMVRDR 190
Cdd:cd19126 91 DRLGLDYVDLYLIH-WPGKDKFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHADV----VPAVNQVEFHPYLTQK 165
|
170 180
....*....|....*....|....*.
gi 124399033 191 FEWEYesVFASGYGSTIWSPLYQGLL 216
Cdd:cd19126 166 ELRGY--CKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-211 |
3.52e-06 |
|
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: 48.03 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWVNSDDKDtqdRNTKIIQKAWELGINFFDTAEIYGdgkAEIHLGHALKT-----LNVQRQDIVISTKI 83
Cdd:cd19124 1 SGQTMPVIGMGTASDPPSPE---DIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlgLVKSRDELFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 84 YGGDgndfpnskyLSRKHLIEGLRNSLKRLDTPYVDIVFAH--------RYDYQTP--------LEETCRAFDWIIRHGL 147
Cdd:cd19124 75 WCSD---------AHPDLVLPALKKSLRNLQLEYVDLYLIHwpvslkpgKFSFPIEeedflpfdIKGVWEAMEECQRLGL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124399033 148 AHYWGTSEWTAQQIHqaigicDRLSLHK--PVVEQPQYNMMVRDRFEWEYESvfASGYGSTIWSPL 211
Cdd:cd19124 146 TKAIGVSNFSCKKLQ------ELLSFATipPAVNQVEMNPAWQQKKLREFCK--ANGIHVTAYSPL 203
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
8-302 |
4.51e-06 |
|
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: 47.51 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 8 ATGLKVSAISYGNWVNSDDKDTqdrnTKIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTLNVQRQDIVISTKIYGGD 87
Cdd:cd19156 4 ANGVEMPRLGLGVWRVQDGAEA----ENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKLWNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 88 gndfpnSKYLSRkhlIEGLRNSLKRLDTPYVDIVFAHrYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWTAQQIHQAIGI 167
Cdd:cd19156 77 ------QGYEST---LAAFEESLEKLGLDYVDLYLIH-WPVKGKFKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 168 CDRlslhKPVVEQ----PQYNMMVRDRFEWEYESVFasgygsTIWSPLYQGlltgkynddiladgrfnnsdniyvkhfyq 243
Cdd:cd19156 147 CKV----APMVNQielhPLLTQEPLRKFCKEKNIAV------EAWSPLGQG----------------------------- 187
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 124399033 244 QILGDPEkrtkiqnqlkqLGEVAKELGVTQAQLSLAWALKNKDVStaITSATRPEQLEE 302
Cdd:cd19156 188 KLLSNPV-----------LKAIGKKYGKSAAQVIIRWDIQHGIIT--IPKSVHEERIQE 233
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-167 |
5.10e-06 |
|
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: 47.49 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvNSDDKDTQDRNTkiIQKAWELGINFFDTAEIYGdgkAEIHLGHALKTL----NVQRQDIVISTKIY 84
Cdd:cd19119 8 TGASIPALGLGTA-SPHEDRAEVKEA--VEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgSIKREELFITTKVW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 85 ggdgndfPnskyLSRKHLIEGLRNSLKRLDTPYVDIVFAHrydYQTPL----EETCRAFDWIIRHGLAHYWGTSEW--TA 158
Cdd:cd19119 82 -------P----TFYDEVERSLDESLKALGLDYVDLLLVH---WPVCFekdsDDSGKPFTPVNDDGKTRYAASGDHitTY 147
|
170
....*....|....*..
gi 124399033 159 QQIHQ--------AIGI 167
Cdd:cd19119 148 KQLEKiyldgrakAIGV 164
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
8-302 |
7.05e-06 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 47.00 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 8 ATGLKVSAISYGNWVNSDDKDTQDrntkIIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGD 87
Cdd:cd19157 5 NNGVKMPWLGLGVFKVEEGSEVVN----AVKTALKNGYRSIDTAAIYGN---EEGVGKGIKESGIPREELFITSKVWNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 88 gndfpnskyLSRKHLIEGLRNSLKRLDTPYVDIVFAHrYDYQTPLEETCRAFDWIIRHGLAHYWGTSEWtaqQIHQAIGI 167
Cdd:cd19157 78 ---------QGYDSTLKAFEASLERLGLDYLDLYLIH-WPVKGKYKETWKALEKLYKDGRVRAIGVSNF---QVHHLEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 168 CDRLSLhKPVVEQPQYNmmvrDRFEWEYESVFASGYGSTI--WSPLYQGlltgkynddiladgrfnnsdniyvkhfyqQI 245
Cdd:cd19157 145 LADAEI-VPMVNQVEFH----PRLTQKELRDYCKKQGIQLeaWSPLMQG-----------------------------QL 190
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124399033 246 LGDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALKNkDVSTaITSATRPEQLEE 302
Cdd:cd19157 191 LDNP-----------VLKEIAEKYNKSVAQVILRWDLQN-GVVT-IPKSIKEHRIIE 234
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-168 |
2.32e-05 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 45.59 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTqdrntKIIQKAWELGINFFDTAEIYGDGKAeihLGHALKTL----NVQRQDIVISTKIYG 85
Cdd:cd19155 9 GEKMPVVGLGTWQSSPEEIE-----TAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKKWidsgKVKREELFIVTKLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 GdGNdfpnskylsRKHLIEG-LRNSLKRLDTPYVDIVFAH---------------------RYDYQTPLEETCRAFDWII 143
Cdd:cd19155 81 G-GN---------RREKVEKfLLKSLEKLQLDYVDLYLIHfpvgslskeddsgkldptgehKQDYTTDLLDIWKAMEAQV 150
|
170 180
....*....|....*....|....*
gi 124399033 144 RHGLAHYWGTSEWTAQQIHQAIGIC 168
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNA 175
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
24-311 |
3.47e-05 |
|
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: 45.03 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 24 SDDKDT---QDRNTKIIQKAWELGINFFDTAEIYGdgKAEIHLGHALKTLNVQRQDIVISTK---IYGGDGN---DFPNS 94
Cdd:cd19098 25 GSGRSVeamRAHTHAVLDAAWAAGVRYFDAARSYG--RAEEFLGSWLRSRNIAPDAVFVGSKwgyTYTADWQvdaAVHEV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 95 KYLSRKHLIEGLRNSLKRLDtPYVDIVFAHRYDYQTP-LEET--------CRAFDWIIrhGLAhYWGTSEwtAQQIHQAI 165
Cdd:cd19098 103 KDHSLARLLKQWEETRSLLG-KHLDLYQIHSATLESGvLEDAdvlaalaeLKAEGVKI--GLS-LSGPQQ--AETLRRAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 166 GIcdRLSLHKP--VVeQPQYNMMVRDRFEwEYESVFASGYGSTIwsplyqglltgkynDDILADGRfnnsdniyvkhfyq 243
Cdd:cd19098 177 EI--EIDGARLfdSV-QATWNLLEQSAGE-ALEEAHEAGMGVIV--------------KEALANGR-------------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124399033 244 qiLGDPEKRTKIQNQLKQLGEVAKELGVTQAQLSLAWALKNKDVSTAITSATRPEQLEETVKSVQVVK 311
Cdd:cd19098 225 --LTDRNPSPELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSL 290
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-141 |
4.43e-05 |
|
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: 44.44 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvNSDDKDTQdrntKIIQKAWELGINFFDTAEIYGDgkaEIHLGHALK---TLNVQRQDIVISTKIYg 85
Cdd:cd19121 8 TGASIPAVGLGTW-QAKAGEVK----AAVAHALKIGYRHIDGALCYQN---EDEVGEGIKeaiAGGVKREDLFVTTKLW- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124399033 86 gdgndfpnSKYLSRkhLIEGLRNSLKRLDTPYVDIVFAH---------RYDYQTPLEETCRAFDW 141
Cdd:cd19121 79 --------STYHRR--VELCLDRSLKSLGLDYVDLYLVHwpvllnpngNHDLFPTLPDGSRDLDW 133
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-180 |
5.91e-05 |
|
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: 44.36 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 9 TGLKVSAISYGNWvnsddKDTQDRNTKIIQKAWELGINFFDTAEIYGDGKaEIHLG--HALKTLNVQRQDIVISTKIYgg 86
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKLW-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 87 dgNDFPNSKYLSRkhlieGLRNSLKRLDTPYVDIVFAH------------------------RYDY-QTPLEETCRAFDW 141
Cdd:cd19113 79 --NNFHDPKNVET-----ALNKTLSDLKLDYVDLFLIHfpiafkfvpieekyppgfycgdgdNFVYeDVPILDTWKALEK 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 124399033 142 IIRHGLAHYWGTSEWTAQQIHQAIgicdRLSLHKPVVEQ 180
Cdd:cd19113 152 LVDAGKIKSIGVSNFPGALILDLL----RGATIKPAVLQ 186
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-302 |
4.45e-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: 41.24 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVNSDDKDTQDrntkiIQKAWELGINFFDTAEIYGDgkaEIHLGHALKTLNVQRQDIVISTKIYGGD-G 88
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADA-----VATALADGYRLIDTAAAYGN---EREVGEGIRRSGVDRSDIFVTTKLWISDyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 89 NDfpnskylsrkHLIEGLRNSLKRLDTPYVDIVFAHrydYQTPLE-----ETCRAFDWIIRHGLAHYWGTSEWTAQQIHQ 163
Cdd:cd19127 78 YD----------KALRGFDASLRRLGLDYVDLYLLH---WPVPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPEHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 164 AIGICD------RLSLHkPVVEQPQynMMVRDRfeweyesvfASGYGSTIWSPLyqglltgkynDDILADGRFNNSDNIY 237
Cdd:cd19127 145 LIDATTvvpavnQVELH-PYFSQKD--LRAFHR---------RLGIVTQAWSPI----------GGVMRYGASGPTGPGD 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124399033 238 VkhfyqqiLGDPekrtkiqnqlkQLGEVAKELGVTQAQLSLAWALKNkDVStAITSATRPEQLEE 302
Cdd:cd19127 203 V-------LQDP-----------TITGLAEKYGKTPAQIVLRWHLQN-GVS-AIPKSVHPERIAE 247
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-180 |
6.64e-04 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 40.90 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 10 GLKVSAISYGNWVnSDDKDTQDrntkIIQKAWELGINFFDTAEIYgdgKAEIHLGHALKTL----NVQRQDIVISTKIYg 85
Cdd:cd19129 3 SGAIPALGFGTLI-PDPSATRN----AVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKLW- 73
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124399033 86 gdgndfpNSKYlsRKHLIE-GLRNSLKRLDTPYVDIVFAHR--------------------YDYQTPLEETCRAFDWIIR 144
Cdd:cd19129 74 -------NTNH--RPERVKpAFEASLKRLQLDYLDLYLIHTpfafqpgdeqdprdangnviYDDGVTLLDTWRAMERLVD 144
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170 180 190
....*....|....*....|....*....|....*.
gi 124399033 145 HGLAHYWGTSEWTAQQIhQAIGICDRLslhKPVVEQ 180
Cdd:cd19129 145 EGRCKAIGLSDVSLEKL-REIFEAARI---KPAVVQ 176
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