|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-317 |
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: 587.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19143 81 TKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLR 240
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 241 --KQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRIEEI 317
Cdd:cd19143 241 drKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-310 |
7.46e-146 |
|
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: 412.37 E-value: 7.46e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVVSTKFFWGLAE 89
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKG--WPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 90 APNQYhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAE 169
Cdd:cd19074 79 GPNDR-GLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 170 RHHLHKPVMEQPQYNLFHRKRVEEEyKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQL---DGYDWLRKQVTDa 246
Cdd:cd19074 158 QFGLIPPVVEQPQYNMLWREIEEEV-IPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAtdeDNRDKKRRLLTD- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 247 gkNNV--VGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEV 310
Cdd:cd19074 236 --ENLekVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGV--KLSPEV 297
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
2-310 |
2.63e-126 |
|
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: 363.69 E-value: 2.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 2 NYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVST 81
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 82 KFFWGlAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEI 161
Cdd:cd19141 81 KIFWG-GKAETE-RGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 162 RAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLRK 241
Cdd:cd19141 159 MEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKE 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 242 QVTDAGKNNVVGKLGEV---ANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEV 310
Cdd:cd19141 239 KILSEEGRRQQAKLKELqiiADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-318 |
1.86e-122 |
|
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: 354.10 E-value: 1.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWvTYGN---QVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSY 77
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGGpwgGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKG--RPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 78 VVSTKFFWGLAEAPNQYHtLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWS 157
Cdd:COG0667 78 VIATKVGRRMGPGPNGRG-LSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 158 ADEIRAAYDIAErhHLHKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDG--VPADSRAqldG 235
Cdd:COG0667 157 AEQLRRALAIAE--GLPPIVAVQNEYSLLDR-SAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRA---A 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 236 YDWLRKQVTDAGKnNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIE 315
Cdd:COG0667 231 TNFVQGYLTERNL-ALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALD 307
|
...
gi 501400857 316 EII 318
Cdd:COG0667 308 AAL 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-320 |
1.16e-119 |
|
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: 347.36 E-value: 1.16e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGlAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19160 83 TKIYWG-GQAETE-RGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLR 240
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 241 KQV-TDAGKNN--VVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRIEEI 317
Cdd:cd19160 241 EKVqSEEGKKQqaKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
...
gi 501400857 318 IGD 320
Cdd:cd19160 321 LGN 323
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-320 |
1.40e-113 |
|
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: 331.62 E-value: 1.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGlAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19159 81 TKLYWG-GKAETE-RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLR 240
Cdd:cd19159 159 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 241 -KQVTDAGK--NNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRIEEI 317
Cdd:cd19159 239 eRIVSEEGRkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 318
|
...
gi 501400857 318 IGD 320
Cdd:cd19159 319 LRN 321
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
3-318 |
1.19e-108 |
|
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved core region of the beta subunit of voltage-gated potassium (Kv) channels in animals. Amino-terminal regions differ substantially, in part by alternative splicing, and are not included in the model. Four beta subunits form a complex with four alpha subunit cytoplasmic (T1) regions, and the structure of the complex is solved. The beta subunit belongs to a family of NAD(P)H-dependent aldo-keto reductases, binds NADPH, and couples voltage-gated channel activity to the redox potential of the cell. Plant beta subunits and their closely related bacterial homologs (in Deinococcus radiudurans, Xylella fastidiosa, etc.) appear more closely related to each other than to animal forms. However, the bacterial species lack convincing counterparts the Kv alpha subunit and the Kv beta homolog may serve as an enzyme. Cutoffs are set for this model such that yeast and plant forms and bacterial close homologs score between trusted and noise cutoffs.
Pssm-ID: 213602 [Multi-domain] Cd Length: 317 Bit Score: 319.19 E-value: 1.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVSTK 82
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 83 FFWGLAEAPNQyhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIR 162
Cdd:TIGR01293 81 IFWGGKAETER--GLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 163 AAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLRKQ 242
Cdd:TIGR01293 159 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 243 V-TDAGKNNV--VGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRIEEII 318
Cdd:TIGR01293 239 IlSEEGRRQQarLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-320 |
5.54e-105 |
|
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: 310.09 E-value: 5.54e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGlAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19158 81 TKIFWG-GKAETE-RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLR 240
Cdd:cd19158 159 IMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 241 KQVTDAGKNNVVGKLGE---VANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRIEEI 317
Cdd:cd19158 239 DKILSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSI 318
|
...
gi 501400857 318 IGD 320
Cdd:cd19158 319 LGN 321
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-317 |
5.15e-98 |
|
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: 291.78 E-value: 5.15e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSwVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawpRVSYVVS 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGR---RDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19087 77 TKVFGPMGDDPND-RGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDG--VPADSRAQLDGYdw 238
Cdd:cd19087 156 IAKAQGIAARRGLLRFVSEQPMYNLLKR-QAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkrPESGRLVERARY-- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 239 lRKQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIEEI 317
Cdd:cd19087 233 -QARYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-320 |
1.01e-92 |
|
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: 278.58 E-value: 1.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPNqyhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19142 81 TKIYWSYGSEER---GLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLR 240
Cdd:cd19142 158 IMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSKYKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 241 KQV---TDAGKNNVVGKLGE---VANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARITPEVKTRI 314
Cdd:cd19142 238 GSDgngIHEETRRASHKLRElslIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEEL 317
|
....*.
gi 501400857 315 EEIIGD 320
Cdd:cd19142 318 ERILDN 323
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-317 |
1.40e-91 |
|
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: 275.65 E-value: 1.40e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSwVTYG---------NQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELa 71
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 72 wpRVSYVVSTKFFWGLAEAPNQYhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYW 151
Cdd:cd19091 79 --RDDVLIATKVRGRMGEGPNDV-GLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 152 GTSEWSADEIRAAYDIAERHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDG--VPADS 229
Cdd:cd19091 156 GVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGqpAPEGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 230 RAQLDGYDWLRkqVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPE 309
Cdd:cd19091 235 RLRRTGFDFPP--VDRERGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLTPE 310
|
....*...
gi 501400857 310 VKTRIEEI 317
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
3-315 |
1.34e-90 |
|
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: 272.92 E-value: 1.34e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWvTYGNQ------VDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVS 76
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 77 YVVSTKFFWGLAEAPNQYHtLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEW 156
Cdd:cd19079 80 VVIATKVYFPMGDGPNGRG-LSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 157 SADEIRAAYDIAERHHLHKPVMEQPQYNLFHRkrvEEEykR----LYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQ 232
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYR---EEE--RemipLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 233 LDGYdWLRKQVTDAGKnNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKT 312
Cdd:cd19079 234 DTAK-LKYDYFTEADK-EIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLSEEEIK 309
|
...
gi 501400857 313 RIE 315
Cdd:cd19079 310 YLE 312
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-315 |
4.01e-84 |
|
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: 255.53 E-value: 4.01e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWV---TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawpRVSYVVSTKFF-- 84
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGR---RDDVVIATKCGlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 WGlaEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19084 78 WD--GGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 ydiaerHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDG---VPADSRA---QLDGYDW 238
Cdd:cd19084 156 ------RKYGPIVSLQPPYSMLERE-IEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSrfpFFRGENF 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 239 LRKQvtdagknNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIE 315
Cdd:cd19084 229 EKNL-------EIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
3-301 |
1.53e-81 |
|
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: 249.48 E-value: 1.53e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAG--GKSEEIMGQALKE-LAWPRVSYVV 79
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPppGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKFFWGLAEAPNQyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSAD 159
Cdd:cd19089 81 STKAGYGMWPGPYG-DGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 160 EIRAAYDIAERHHLhKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWL 239
Cdd:cd19089 160 KARRAIALLRELGV-PLIIHQPRYSLLDRW-AEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAAESKFLT 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 240 RKQVTDAgKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19089 238 EEALTPE-KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALK 298
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-302 |
8.25e-80 |
|
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: 245.20 E-value: 8.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 5 RLGRSGLQVSELSIGSWVtYGNQVDTHAARESLAAARDAGVNFFDNAEVY-------AGGKSEEIMGQALKELAwPRVSY 77
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYsawvpgnAGGESETIIGRWLKSRG-KRDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 78 VVSTKFfwGLAEAPNQYhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWS 157
Cdd:cd19081 79 VIATKV--GFPMGPNGP-GLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 158 ADEIRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQldGYD 237
Cdd:cd19081 156 AWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTR--RGE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501400857 238 WLRKQVTDAGKnNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADV 302
Cdd:cd19081 234 AAKRYLNERGL-RILDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL 297
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-318 |
1.39e-76 |
|
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: 236.44 E-value: 1.39e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSWvTYGNQVDTHAARESLAAAR---DAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVSTKFfWGLAEAPN 92
Cdd:pfam00248 1 IGLGTW-QLGGGWGPISKEEALEALRaalEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 93 QYHTlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIraayDIAERHH 172
Cdd:pfam00248 79 SGGS--KENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQI----EKALTKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 173 LHKPVMEQPQYNLFhRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRaqldgyDWLRKQVTDAGKN-NV 251
Cdd:pfam00248 153 KIPIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG------ERRRLLKKGTPLNlEA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 252 VGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIEEII 318
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF--PLSDEEVARIDELL 290
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
3-296 |
1.60e-74 |
|
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: 231.52 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA--GGKSEEIMGQALKE-LAWPRVSYVV 79
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdLKPYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKFFWGLAEAPNQYHTlNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSAD 159
Cdd:cd19151 82 STKAGYTMWPGPYGDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 160 EIRAAYDIAERhhLHKP-VMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDW 238
Cdd:cd19151 161 EAREAAAILKD--LGTPcLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAAKGSSFL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 239 LRKQVTDAgKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGEN 296
Cdd:cd19151 238 KPEQITEE-KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDA 294
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-298 |
1.43e-72 |
|
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: 223.93 E-value: 1.43e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIGSWvTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVSYVVSTKFFWGLAEAPNQ 93
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGGHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 94 YHtLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHL 173
Cdd:cd06660 79 SR-LSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 174 HKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLltgkyrdgvpadsraqldgydwlrkqvtdagknnvvg 253
Cdd:cd06660 158 PGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGP------------------------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501400857 254 klgevanelgctiGQLAIGWILKNPNVSTVITGASRVEQIGENMK 298
Cdd:cd06660 201 -------------AQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-315 |
1.41e-71 |
|
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: 224.02 E-value: 1.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELSIGSwVTYGNQ----VDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawpRVSYVV 79
Cdd:cd19080 1 RLLGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGN---RDRIVL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKFFWGlAEAPNQYHTLN-RKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSA 158
Cdd:cd19080 77 ATKYTMN-RRPGDPNAGGNhRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 159 DEIRAAYDIAERHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGvpADSRAQLDGYDW 238
Cdd:cd19080 156 WVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVT 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 239 LRKQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIE 315
Cdd:cd19080 233 VGFGKLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
3-301 |
1.05e-68 |
|
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: 216.94 E-value: 1.05e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA--GGKSEEIMGQALKE-LAWPRVSYVV 79
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREdFAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKFFWGLAEAPnqYHTL-NRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSA 158
Cdd:cd19150 82 STKAGYDMWPGP--YGEWgSRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 159 DEIRAAYDIAERhhLHKPVM-EQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQlDGYD 237
Cdd:cd19150 160 ERTREAAAILRE--LGTPLLiHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS-KERS 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501400857 238 WLRKQVTDAGKNNvVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19150 237 LSPKMLTEANLNS-IRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-317 |
7.29e-65 |
|
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: 206.28 E-value: 7.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 13 VSELSIGSWV----TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElawPRVSYVVSTKFFwgla 88
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 eapnqYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIA 168
Cdd:cd19085 74 -----PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 169 erhhlhKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYR---DGVPADSRAQL-----DGYdwlR 240
Cdd:cd19085 149 ------RIDSNQLPYNLLWR-AIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSsaeDFPPGDARTRLfrhfePGA---E 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 241 KQVTDAgknnvVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIEEI 317
Cdd:cd19085 219 EETFEA-----LEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
3-309 |
2.30e-63 |
|
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: 202.83 E-value: 2.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIG----SWVtYGNQvDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElawPRVSYV 78
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgmSAF-YGPA-DEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 79 VSTKFfwGLAEAPNQYHTLN---RKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSE 155
Cdd:cd19076 77 IATKF--GIVRDPGSGFRGVdgrPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 156 WSADEIRAAydiaerHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRdgvpadSRAQLDG 235
Cdd:cd19076 155 ASADTIRRA------HAVHPITAVQSEYSLWTRD-IEDEVLPTCRELGIGFVAYSPLGRGFLTGAIK------SPEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 236 YDWLRKQVTDAGKN-----NVVGKLGEVANELGCTIGQLAIGWIL-KNPNVsTVITGASRVEQIGENMKSADVaaRITPE 309
Cdd:cd19076 222 DDFRRNNPRFQGENfdknlKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDI-VPIPGTKRIKYLEENVGALDV--VLTPE 298
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-299 |
1.18e-62 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 202.53 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA--GGKSEEIMGQALKE-LAWPRVSY 77
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 78 VVSTKFfwGLAEAPNQYHT-LNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEW 156
Cdd:PRK09912 93 IISTKA--GYDMWPGPYGSgGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 157 SADEIRAAYDIAERHHLhkPVM-EQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDG 235
Cdd:PRK09912 171 SPERTQKMVELLREWKI--PLLiHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREG 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 236 --YDWLRKQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKS 299
Cdd:PRK09912 249 nkVRGLTPKMLTEANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-316 |
1.43e-59 |
|
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: 192.83 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIG----SWvTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElawPRVSYVVSTKFFW 85
Cdd:cd19078 1 GLEVSAIGLGcmgmSH-GYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 GLAeaPNQYHTL----NRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEI 161
Cdd:cd19078 77 KID--GGKPGPLgldsRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 162 RaaydiaeRHHLHKPVME-QPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYrdgvpaDSRAQLDGYD--- 237
Cdd:cd19078 155 R-------RAHAVCPVTAvQSEYSMMWR-EPEKEVLPTLEELGIGFVPFSPLGKGFLTGKI------DENTKFDEGDdra 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 238 WLRKQVTDAGKNN--VVGKLGEVANELGCTIGQLAIGWIL-KNPNVsTVITGASRVEQIGENMKSADVaaRITPEVKTRI 314
Cdd:cd19078 221 SLPRFTPEALEANqaLVDLLKEFAEEKGATPAQIALAWLLaKKPWI-VPIPGTTKLSRLEENIGAADI--ELTPEELREI 297
|
..
gi 501400857 315 EE 316
Cdd:cd19078 298 ED 299
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
19-318 |
2.20e-58 |
|
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: 189.81 E-value: 2.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 19 GSWVTYGNQVDTHAaRESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVsyVVSTK--FFWglAEAPNQYHT 96
Cdd:cd19102 15 GWGGGWGPQDDRDS-IAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLR-DRP--IVATKcgLLW--DEEGRIRRS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 97 LNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAerhhlhkP 176
Cdd:cd19102 89 LKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIH-------P 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 177 VME-QPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKyrdgVPADSRAQLDGYDWLRKQVTDAGKN-----N 250
Cdd:cd19102 162 IASlQPPYSLLRRG-IEAEILPFCAEHGIGVIVYSPMQSGLLTGK----MTPERVASLPADDWRRRSPFFQEPNlarnlA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 251 VVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTRIEEII 318
Cdd:cd19102 237 LVDALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-317 |
2.49e-56 |
|
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: 185.46 E-value: 2.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 13 VSELSIGSwVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA-------GGKSEEIMGQALKELAwPRVSYVVSTK--- 82
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 83 ----FFWGLAEAPNqyhtLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPV------------------EETVWAMS 140
Cdd:cd19094 79 pgegITWPRGGGTR----LDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgggyytepseeedsvsfEEQLEALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 141 DMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPVMEQPQYNLFHRKRVEE--EYKRlYEDIglGLTTWSPLASGLLT 218
Cdd:cd19094 155 ELVKAGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNRNFEEGlaEACH-RENV--GLLAYSPLAGGVLT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 219 GKYRDGVPADSRAQLDGYDWLRKQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMK 298
Cdd:cd19094 232 GKYLDGAARPEGGRLNLFPGYMARYRSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENID 311
|
330
....*....|....*....
gi 501400857 299 SADVAarITPEVKTRIEEI 317
Cdd:cd19094 312 AFDVP--LSDELLAEIDAV 328
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-316 |
6.69e-56 |
|
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: 184.01 E-value: 6.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWV----TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawpRVSYV 78
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---RDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 79 VSTKF----------FWGLAEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKA 148
Cdd:cd19149 78 LATKCglrwdreggsFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 149 LYWGTSEWSADEIRAAYDIAErhhlhkPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKY---RDGV 225
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAGQ------LDIIQEKYSMLDRG-IEKELLPYCKKNNIAFQAYSPLEQGLLTGKItpdREFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 226 PADSRAqldGYDWL----RKQVTDAgknnvVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19149 231 AGDARS---GIPWFspenREKVLAL-----LEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGD 302
|
330
....*....|....*
gi 501400857 302 VaaRITPEVKTRIEE 316
Cdd:cd19149 303 I--RLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-302 |
9.98e-55 |
|
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: 180.69 E-value: 9.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELSIGSWVTYGNQ----VDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVV 79
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGHNlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKE--YNRNEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKffWGLAEAPNQYHTLNR-KYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSA 158
Cdd:cd19083 80 ATK--GAHKFGGDGSVLNNSpEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 159 DEIRAAydiaeRHHLHKPVMeQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYrdgvpaDSRAQLDGYDW 238
Cdd:cd19083 158 EQLKEA-----NKDGYVDVL-QGEYNLLQRE-AEEDILPYCVENNISFIPYFPLASGLLAGKY------TKDTKFPDNDL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 239 lRKQVTD----AGKNNV--VGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADV 302
Cdd:cd19083 225 -RNDKPLfkgeRFSENLdkVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV 293
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-309 |
5.95e-53 |
|
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: 175.49 E-value: 5.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 12 QVSELSIGSW------VTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVSYVVSTKfFW 85
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK-FA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 GLAeapnqyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19093 79 PLP------WRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALMdGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 YDiAERHHLHKPVMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYR-DGVPADSRAQLDG-YDWLRKQ 242
Cdd:cd19093 153 HK-ALKERGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSpENPPPGGRRRLFGrKNLEKVQ 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 243 VtdagknnVVGKLGEVANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENMKSADVaaRITPE 309
Cdd:cd19093 232 P-------LLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW--RLSEE 287
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-299 |
2.66e-52 |
|
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: 172.28 E-value: 2.66e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 11 LQVSELSIGSWV----TYGNqVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElawPRVSYVVSTKFFWG 86
Cdd:cd19086 1 LEVSEIGFGTWGlggdWWGD-VDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFGNR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 87 LAEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIRAAy 165
Cdd:cd19086 77 FDGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVLDNDELFeALEKLKQEGKIRAYGVSVGDPEEALAA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 166 diaerhhLHKPVME--QPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKyrdgvpadsraqldgydwlrkqv 243
Cdd:cd19086 156 -------LRRGGIDvvQVIYNLLDQ-RPEEELFPLAEEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 244 tdagknnvvgklgevanelgctIGQLAIGWILKNPNVSTVITGASRVEQIGENMKS 299
Cdd:cd19086 205 ----------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-315 |
5.50e-52 |
|
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: 172.03 E-value: 5.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQV----DTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVVSTKFFw 85
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSkdysDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKG--FDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 glaeaPNQYHtlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAY 165
Cdd:cd19072 78 -----PDHLK---YDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 166 DIAERhhlHKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVpadsraqldgydwlrkqvtd 245
Cdd:cd19072 150 SYLKK---GPIVANQVEYNLFDR-EEESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL-------------------- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 246 agknnvvgkLGEVANELGCTIGQLAIGWILKNPNVsTVITGASRVEQIGENMKSADVaaRITPEVKTRIE 315
Cdd:cd19072 206 ---------LDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALGW--ELSEEDLQRLD 263
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
19-306 |
1.45e-48 |
|
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: 164.65 E-value: 1.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 19 GSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWprvsYVVSTKFFwglaeaPNQYHTLN 98
Cdd:cd19075 8 MTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGERG----FKIDTKAN------PGVGGGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 99 RKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPVM 178
Cdd:cd19075 78 PENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 179 EQPQYNLFHRKrVEEEY----KRLyediGLGLTTWSPLASGLLTGKYRDG--VPADSR-----AQLDGY-DW-LRKQVTD 245
Cdd:cd19075 158 YQGMYNAITRQ-VETELfpclRKL----GIRFYAYSPLAGGFLTGKYKYSedKAGGGRfdpnnALGKLYrDRyWKPSYFE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501400857 246 AgknnvVGKLGEVANELGCTIGQLAIGWI-----LKNPNVSTVITGASRVEQIGENMK-------SADVAARI 306
Cdd:cd19075 233 A-----LEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAalekgplPEEVVKAI 300
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
25-301 |
1.54e-48 |
|
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: 164.26 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 25 GNQVDTHAARESLAAARDAGVNFFDNAEVYAG----GKSEEIMGQALKELAwPRVSYVVSTK---FFWGLAEAPNqyhtL 97
Cdd:cd19082 11 GTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATKgghPDLEDMSRSR----L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 98 NRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPV 177
Cdd:cd19082 86 SPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 178 MEQPQYNLFHRKR----------VEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRaQLDGYD----WLRKQv 243
Cdd:cd19082 166 ASSPQWSLARPNEppwpgptlvaMDEEMRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSE-LRRVYYseenFERLE- 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 244 tdagknnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19082 244 ----------RAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
4-302 |
1.26e-46 |
|
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: 158.15 E-value: 1.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELsiGSWvtyGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKelAWPRvSYVVSTKF 83
Cdd:cd19088 2 SRLGYGAMRLTGP--GIW---GPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALH--PYPD-DVVIATKG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 84 fwGLAE-APNQYHTLNRK-YLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEI 161
Cdd:cd19088 74 --GLVRtGPGWWGPDGSPeYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 162 RAAYDIAErhhlhkPVMEQPQYNLFHRKrvEEEYKRLYEDIGLGLTTWSPLASGLLTgkyRDGvpadsraqldgydwlrk 241
Cdd:cd19088 152 EEARAIVR------IVSVQNRYNLANRD--DEGVLDYCEAAGIAFIPWFPLGGGDLA---QPG----------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 242 qvtdagknnvvGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADV 302
Cdd:cd19088 204 -----------GLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGL 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-321 |
7.93e-45 |
|
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: 155.29 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELSIGSW---VTYGNQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPNQYHTLNR-KYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSAD 159
Cdd:cd19144 82 TKFGIEKNVETGEYSVDGSpEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 160 EIRAAYDIaerHHL------HKPV---MEQPQYNLFHRKRveeeykrlyeDIGLGLTTWSPLASGLLTGKYRdgvpadSR 230
Cdd:cd19144 162 TLRRAHAV---HPIaavqieYSPFsldIERPEIGVLDTCR----------ELGVAIVAYSPLGRGFLTGAIR------SP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 231 AQLDGYDWLRK----QVTDAGKN-NVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaR 305
Cdd:cd19144 223 DDFEEGDFRRMaprfQAENFPKNlELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--K 300
|
330
....*....|....*.
gi 501400857 306 ITPEVKTRIEEIIGDA 321
Cdd:cd19144 301 LTEEEEKEIREIAEEA 316
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-309 |
4.04e-44 |
|
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: 152.97 E-value: 4.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELSIGSW---VTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawPRVSYVVS 80
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKDG--PREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19145 81 TKFGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAydiaerHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGK---YRDGVPADSRAQLDgyd 237
Cdd:cd19145 161 IRRA------HAVHPITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKaklEELLENSDVRKSHP--- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501400857 238 wlRKQVTDAGKNNVV-GKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSadVAARITPE 309
Cdd:cd19145 231 --RFQGENLEKNKVLyERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGA--LSVKLTKE 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
9-302 |
5.96e-44 |
|
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: 151.94 E-value: 5.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVSTKFFWGLA 88
Cdd:cd19092 2 EGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGIRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 EAPN----QYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19092 82 DDPRpgriKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIELL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 ydiaeRHHLHKP-VMEQPQYNLFHRKRVEE---EYKRLYediGLGLTTWSPLASGLLTGkyrdgvPADSRAQldgydwlr 240
Cdd:cd19092 162 -----QSYLDQPlVTNQIELSLLHTEAIDDgtlDYCQLL---DITPMAWSPLGGGRLFG------GFDERFQ-------- 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 241 kqvtdagknNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADV 302
Cdd:cd19092 220 ---------RLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-317 |
2.52e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 143.56 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 2 NYRRLGRSGLQVSELSIGS------WVTyGNQVDTHAAresLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawpRV 75
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGggigglMGR-TTREEQIAA---VRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 76 SYVVSTKFFWGLAEAPNQYHTLNRKyllnaIDASLKRLQLDYVDLVFCH------RPDPNTPVEETVW---------AMS 140
Cdd:cd19104 74 GPYITTKVRLDPDDLGDIGGQIERS-----VEKSLKRLKRDSVDLLQLHnrigdeRDKPVGGTLSTTDvlglggvadAFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 141 DMITRGKALYWGTSEWsaDEIRAAYDIAERHHLHkpvMEQPQYNL--------FHRKRVEEEYKRLYEDI---GLGLTTW 209
Cdd:cd19104 149 RLRSEGKIRFIGITGL--GNPPAIRELLDSGKFD---AVQVYYNLlnpsaaeaRPRGWSAQDYGGIIDAAaehGVGVMGI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 210 SPLASGLLTGKYRDGVPADSRAQLDGYDWLRKQVtdagknnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASR 289
Cdd:cd19104 224 RVLAAGALTTSLDRGREAPPTSDSDVAIDFRRAA----------AFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKN 293
|
330 340
....*....|....*....|....*...
gi 501400857 290 VEQIGENMKSADvAARITPEVKTRIEEI 317
Cdd:cd19104 294 REELEEAVAAEA-AGPLPAENLARLEAL 320
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-293 |
8.45e-39 |
|
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: 138.98 E-value: 8.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQ---VDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVSYVVSTKFfwG 86
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMwggTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKV--G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 87 LAEAPNQYHTLN--RKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19148 78 LEWDEGGEVVRNssPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 YDIAERHHLhkpvmeQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRdgvpADSraQLDGYDwLRK--- 241
Cdd:cd19148 158 RKVAPLHTV------QPPYNLFERE-IEKDVLPYARKHNIVTLAYGALCRGLLSGKMT----KDT--KFEGDD-LRRtdp 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 242 --------QVTDAgknnvVGKLGEVANE-LGCTIGQLAIGWILKNPNVSTVITGASRVEQI 293
Cdd:cd19148 224 kfqeprfsQYLAA-----VEELDKLAQErYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-301 |
1.76e-38 |
|
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: 137.85 E-value: 1.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIGSwVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA-------GGKSEEIMGQALKELAwPRVSYVVSTKFFWG 86
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 87 L---AEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRA 163
Cdd:cd19752 79 PrdpDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 164 AYDIAERHHLHKPVMEQPQYNLFHRKR---------VEEEYKRLYEDIG-LGLTTWSPLASGLLTgkyRDGVPAdsRAQL 233
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPRPgadfgvqriVTDELLDYASSRPdLTLLAYSPLLSGAYT---RPDRPL--PEQY 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 234 DGYDWLRKqvtdagknnvVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19752 234 DGPDSDAR----------LAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-300 |
2.25e-38 |
|
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: 136.56 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWVTYGNQVDThaaresLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawPRVSYVVS 80
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLPRESPEL------LRRALDLGINYFDTAEGYGNGNSEEIIGEALKGL--RRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEAPnqyhtlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTP---VEETVWAMSDMITRGKALYWGTSEWS 157
Cdd:cd19105 73 TKASPRLDKKD-------KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEErllNEELLEALEKLKKEGKVRFIGFSTHD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 158 ADE--IRAA-----YDIAerhhlhkpvmeQPQYNLFHRKRVEEE-----YKRlyediGLGLTTWSPLASGLLtgkyrdgv 225
Cdd:cd19105 146 NMAevLQAAiesgwFDVI-----------MVAYNFLNQPAELEEalaaaAEK-----GIGVVAMKTLAGGYL-------- 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501400857 226 padsraqldgYDWLRKqvtdagknnvvgklgeVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSA 300
Cdd:cd19105 202 ----------QPALLS----------------VLKAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-301 |
3.30e-37 |
|
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: 134.60 E-value: 3.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIG--SWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawPRVSYV 78
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGasPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGI--PRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 79 VSTKFfwGLAEA-PNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCH----RPDPNTPVEETVWAMSDMITRGKALYWGT 153
Cdd:cd19163 79 LATKV--GRYGLdPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHdiefAPSLDQILNETLPALQKLKEEGKVRFIGI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 154 SewsadeiraAYDIaerhHLHKPVMEQPQ-----------YNLFHRKRveEEYKRLYEDIGLGLTTWSPLASGLLTGKyr 222
Cdd:cd19163 157 T---------GYPL----DVLKEVLERSPvkidtvlsychYTLNDTSL--LELLPFFKEKGVGVINASPLSMGLLTER-- 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 223 dGVPADSRAQldgydwlrKQVTDAGKnnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19163 220 -GPPDWHPAS--------PEIKEACA-----KAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAE 284
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
25-302 |
1.50e-34 |
|
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: 127.74 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 25 GNQVDTHAARESLAAARDAGVNFFDNAEVYAGGK---SEEIMGQALKelAWPRVS--YVVSTKFfwGLAEAPNQYHTlNR 99
Cdd:cd19077 19 PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDphaNLKLLARFFR--KYPEYAdkVVLSVKG--GLDPDTLRPDG-SP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 100 KYLLNAIDASLKRL-QLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIaerhhlHKPVM 178
Cdd:cd19077 94 EAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAV------HPIAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 179 EQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKY---RDGVPADSRAQLDGYDwlrkqvTDAGKNN--VVG 253
Cdd:cd19077 168 VEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIkslADIPEGDFRRHLDRFN------GENFEKNlkLVD 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 501400857 254 KLGEVANELGCTIGQLAIGWILKNPNVSTV-ITGASRVEQIGENMKSADV 302
Cdd:cd19077 242 ALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV 291
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-309 |
3.24e-33 |
|
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: 123.06 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQVDTHA----ARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVVSTKFfw 85
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDYSrdeeMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKV-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 glaeapnqYHT-LNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19137 77 --------WPTnLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 ydiaeRHHLHKP-VMEQPQYNLFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKyrdgvpadsraqldgydwlrkqv 243
Cdd:cd19137 149 -----ISKSQTPiVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN----------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 244 tdagknnvvGKLGEVANELGCTIGQLAIGWILKNPNVSTvITGASRVEQIGENMKSADVaaRITPE 309
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNVVA-IPKAGRVEHLKENLKATEI--KLSEE 254
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-309 |
1.92e-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: 121.20 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvTYGNQVDTHAA-RESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElawPRVSYVVSTKFFwgl 87
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQeIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 88 aeaPnqyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDpNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDI 167
Cdd:cd19138 80 ---P---SNASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 168 AERHHLhkpVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGlltGKYRDGVPADSraqldgydwlrkqvtdag 247
Cdd:cd19138 153 PGGGNC---AANQVLYNLGSRG-IEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENP------------------ 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 248 knnvvgKLGEVANELGCTIGQLAIGWILKNPNVsTVITGASRVEQIGENMKSADVAarITPE 309
Cdd:cd19138 208 ------TLKEIAARHGATPAQVALAWVLRDGNV-IAIPKSGSPEHARENAAAADLE--LTEE 260
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-299 |
2.51e-32 |
|
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: 120.42 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIGSWVTYGNQ--VDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKELawPRVSYVVSTKFfWGLAEAP 91
Cdd:cd19095 1 SVLGLGTSGIGRVWgvPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALAGL--RRDDLFIATKV-GTHGEGG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 92 NQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSewsadeiraAYDIAERH 171
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS---------GDGEELEA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 172 HLHKPVME--QPQYNLFHRKrvEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAQLDGYDWLRKQVTDAgkn 249
Cdd:cd19095 147 AIASGVFDvvQLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRRVRRRPLYADYARRPEFAAEIGGATWA--- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 501400857 250 nvvgklgevanelgctigQLAIGWILKNPNVSTVITGASRVEQIGENMKS 299
Cdd:cd19095 222 ------------------QAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-317 |
2.53e-32 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 123.04 E-value: 2.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSwVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYA-------GGKSEEIMGQALKELAwP 73
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPvpprpetQGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 74 RVSYVVSTKFFwGLAEA------PNQyhTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPD-----------------PNT 130
Cdd:PRK10625 79 REKLIIASKVS-GPSRNndkgirPNQ--ALDRKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtdsaPAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 131 PVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWS 210
Cdd:PRK10625 156 SLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 211 PLASGLLTGKYRDGV-PADSRAQLdgydWLR-KQVTDAGKNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGAS 288
Cdd:PRK10625 235 CLAFGTLTGKYLNGAkPAGARNTL----FSRfTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGAT 310
|
330 340
....*....|....*....|....*....
gi 501400857 289 RVEQIGENMKSADVAarITPEVKTRIEEI 317
Cdd:PRK10625 311 TMEQLKTNIESLHLT--LSEEVLAEIEAV 337
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-300 |
4.12e-32 |
|
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: 120.74 E-value: 4.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIG-SWVTYG-NQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKElaWPRVSYVVSTKFfwGLAEAP 91
Cdd:cd19090 1 SALGLGtAGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALAE--LPREPLVLSTKV--GRLPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 92 NQYHTlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEET-----VWAMSDMITRGKALYWGTSEWSADEIRAA-- 164
Cdd:cd19090 75 TADYS--ADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPDLLRRAie 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 ---YDIAERHHlhkpvmeqpQYNLFHRKRVEEEYKrLYEDIGLGLTTWSPLASGLLTGKYRDGVPadsraqlDGYDWLRK 241
Cdd:cd19090 153 tgdFDVVLTAN---------RYTLLDQSAADELLP-AAARHGVGVINASPLGMGLLAGRPPERVR-------YTYRWLSP 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 242 QVTDAGKnnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSA 300
Cdd:cd19090 216 ELLDRAK-----RLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAA 269
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-317 |
7.84e-32 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 121.85 E-value: 7.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLGRSGLQVSELSIGSWvtYGNQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKElawPRVSYVVS 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM--RLPRKDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFfwglaeaPNQYHTLN--RKYLlnaiDASLKRLQLDYVDLVFCHRPDPNTPVEETV------WAMSDMITRGKALYWG 152
Cdd:COG1453 74 TKL-------PPWVRDPEdmRKDL----EESLKRLQTDYIDLYLIHGLNTEEDLEKVLkpggalEALEKAKAEGKIRHIG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 153 -TSEWSADEIRAA---YDIAerhhlhkpvMEQPQYN-LFHRKRVEEE-YKRLYEDiGLGLTTWSPLASGLLTgkyrdgvp 226
Cdd:COG1453 143 fSTHGSLEVIKEAidtGDFD---------FVQLQYNyLDQDNQAGEEaLEAAAEK-GIGVIIMKPLKGGRLA-------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 227 adsraqldgydwlrkqvtdagknnvvgKLGEVANELGC---TIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVA 303
Cdd:COG1453 205 ---------------------------NPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNL 257
|
330
....*....|....
gi 501400857 304 ARITPEVKTRIEEI 317
Cdd:COG1453 258 EPLTEEELAILERL 271
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
3-318 |
1.66e-31 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 119.88 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSwVTYGN---QVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVV 79
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGSvfgPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 80 STKFfwglaeapNQYHT---LNRKYLLNAIDASLKRLQLDYVDLVFCHR---PDPNTPVEETVWAMSDMITRGKALYWGT 153
Cdd:PLN02587 80 STKC--------GRYGEgfdFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 154 SEWSADEIRAAYDIAERHHLhKPVMEQPQYNLfHRKRVEEEYKRLyEDIGLGLTTWSPLASGLLTGKyrdGVPADSRAQl 233
Cdd:PLN02587 152 TGLPLAIFTYVLDRVPPGTV-DVILSYCHYSL-NDSSLEDLLPYL-KSKGVGVISASPLAMGLLTEN---GPPEWHPAP- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 234 dgydwlrKQVTDAGKnnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAAR--ITPEVK 311
Cdd:PLN02587 225 -------PELKSACA-----AAATHCKEKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgIDEELL 292
|
....*..
gi 501400857 312 TRIEEII 318
Cdd:PLN02587 293 SEVEAIL 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
9-318 |
3.17e-31 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 119.45 E-value: 3.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIG-SWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVSYVVSTKFFWGL 87
Cdd:cd19146 12 SPLCLGAMSFGeAWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKYTTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 88 AEAPN-----QYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIR 162
Cdd:cd19146 91 RRGGPikiksNYQGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 163 AAYDIAERHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASglltGKYRDGVPADSRAQLDGYDWLRKQ 242
Cdd:cd19146 171 KANAYARAHGLTQFVVYQGHWSAAFRD-FERDILPMCEAEGMALAPWGVLGQ----GQFRTEEEFKRRGRSGRKGGPQTE 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 243 vtdagKNNVVG-KLGEVANELGCTIGQLAIGWIL-KNPNVSTVItGASRVEQIGENMKSADVAarITPEVKTRIEEII 318
Cdd:cd19146 246 -----KERKVSeKLEKVAEEKGTAITSVALAYVMhKAPYVFPIV-GGRKVEHLKGNIEALGIS--LSDEEIQEIEDAY 315
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-318 |
2.03e-30 |
|
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: 116.93 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 5 RLGRSGLQVSelsiGSWvtyGNQVDTHAARESLAAARDAGVNFFDNAEVYAGgkSEEIMGQALKELAWPRVSY---VVST 81
Cdd:cd19101 4 RVINGMWQLS----GGH---GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRRERDAAddvQIHT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 82 KFFwglaeAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTP-VEETVWAMSDMITRGKALYWGTSEWSADE 160
Cdd:cd19101 75 KWV-----PDPGELTMTRAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IRAAYDiaerhHLHKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRdGVPADSRAQLDGYDwLR 240
Cdd:cd19101 150 LREILD-----AGVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYL-GVPEPTGPALETRS-LQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 241 K--QVTDAGKN-----NVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVaaRITPEVKTR 313
Cdd:cd19101 222 KykLMIDEWGGwdlfqELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLDDEDRAA 299
|
....*
gi 501400857 314 IEEII 318
Cdd:cd19101 300 IDAVL 304
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-317 |
1.65e-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: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfwgla 88
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 eaPNQYHTlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNtPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIA 168
Cdd:COG0656 68 --WNDNHG--YDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 169 ErhhlHKPVMEQPQYNLFHRkrvEEEYKRLYEDIGLGLTTWSPLASGlltgkyrdGVPADSraqldgydwlrkqvtdagk 248
Cdd:COG0656 143 G----VKPAVNQVELHPYLQ---QRELLAFCREHGIVVEAYSPLGRG--------KLLDDP------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 249 nnvvgKLGEVANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENMKSADVaaRITPEVKTRIEEI 317
Cdd:COG0656 189 -----VLAEIAEKHGKTPAQVVLRWHLQRGVV--VIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
23-301 |
4.50e-27 |
|
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: 106.49 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 23 TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVVSTKFFWGLAEAPNQYhtlnRKYL 102
Cdd:cd19096 13 SDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPWSVKSAEDF----RRIL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 103 lnaiDASLKRLQLDYVDLVFCH---RPD------PNTPVEETVWAMSDmitrGKALYWG-TSEWSADEIRAAydIAERhh 172
Cdd:cd19096 87 ----EESLKRLGVDYIDFYLLHglnSPEwlekarKGGLLEFLEKAKKE----GLIRHIGfSFHDSPELLKEI--LDSY-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 173 lhkpVME--QPQYNLFHRKRVeeEYKRLYE---DIGLGLTTWSPLASGLLTgkyrdGVPADSRAQLDGYDwlrkqvtdag 247
Cdd:cd19096 155 ----DFDfvQLQYNYLDQENQ--AGRPGIEyaaKKGMGVIIMEPLKGGGLA-----NNPPEALAILCGAP---------- 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501400857 248 knnvvgklgevanelgCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19096 214 ----------------LSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-298 |
2.65e-26 |
|
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: 105.86 E-value: 2.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 11 LQVSELSIGSWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAW----PRVSYVVSTK---- 82
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELIEkggiKRDEVVIVTKagyi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 83 FFWGL--------------------AEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRP----------DPNTPV 132
Cdd:cd19099 81 PGDGDeplrplkyleeklgrglidvADSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFYDRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 133 EETVWAMSDMITRGKALYWGTSEWSADEIRAAYD---------------IAERHHLHkpVMEQPqYNLFH------RKRV 191
Cdd:cd19099 161 EEAFEALEEAVAEGKIRYYGISTWDGFRAPPALPghlsleklvaaaeevGGDNHHFK--VIQLP-LNLLEpealteKNTV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 192 EEEYKRLYE---DIGLGLTTWSPLASGLLTGkyrdGVPADSRAQLDGYDwlrkqvtdagknnvvgklgevanelgcTIGQ 268
Cdd:cd19099 238 KGEALSLLEaakELGLGVIASRPLNQGQLLG----ELRLADLLALPGGA---------------------------TLAQ 286
|
330 340 350
....*....|....*....|....*....|
gi 501400857 269 LAIGWILKNPNVSTVITGASRVEQIGENMK 298
Cdd:cd19099 287 RALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
8-317 |
6.27e-25 |
|
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: 100.80 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 8 RSGLQVSELSIGSWVTYGNQvdthaARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWgl 87
Cdd:cd19140 3 VNGVRIPALGLGTYPLTGEE-----CTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKV-W-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 88 aeaPNQYHTLNrkyLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAaydi 167
Cdd:cd19140 72 ---PDNYSPDD---FLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLRE---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 168 AERHHLHKPVMEQPQYNLFHRKRVEEEYKRlyeDIGLGLTTWSPLASGlltgkyrdGVPADSRaqldgydwlrkqvtdag 247
Cdd:cd19140 142 AVELSEAPLFTNQVEYHPYLDQRKLLDAAR---EHGIALTAYSPLARG--------EVLKDPV----------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 248 knnvvgkLGEVANELGCTIGQLAIGWILKNPNVStVITGASRVEQIGENMKSADVAarITPEVKTRIEEI 317
Cdd:cd19140 194 -------LQEIGRKHGKTPAQVALRWLLQQEGVA-AIPKATNPERLEENLDIFDFT--LSDEEMARIAAL 253
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-298 |
6.54e-24 |
|
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: 97.55 E-value: 6.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 3 YRRLGRSGLQVSELSIGSWVTygNQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKElawPRVSYVVSTK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 83 FfwglaeapnqyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW------AMSDMITRGKALYWG-TSE 155
Cdd:cd19100 74 T-----------GARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaleALLEAKEEGKIRFIGiSGH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 156 WSAdeirAAYDIAERHHLHkpVMeQPQYNLFHRKRVEEEyKRLYEDI---GLGLTTWSPLASGLLTGKyrdgvPADSRAQ 232
Cdd:cd19100 143 SPE----VLLRALETGEFD--VV-LFPINPAGDHIDSFR-EELLPLArekGVGVIAMKVLAGGRLLSG-----DPLDPEQ 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 233 ldgydwlrkqvtdagknnvvgklgevanelgctigqlAIGWILKNPNVSTVITGASRVEQIGENMK 298
Cdd:cd19100 210 -------------------------------------ALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
32-314 |
1.50e-23 |
|
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: 97.81 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 32 AARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKelAWPRVSYVVSTKFFWGLAEAPNQYHTLNRKYL-------LN 104
Cdd:cd19162 20 EAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVGRLLEPGAAGRPAGADRRFdfsadgiRR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 105 AIDASLKRLQLDYVDLVFCHRPDP--NTPVEETVWAMSDMITRG--KALYWGTSEWsadeiRAAYDIAERHHLhKPVMEQ 180
Cdd:cd19162 98 SIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGvvGAIGVGVTDW-----AALLRAARRADV-DVVMVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 181 PQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLLTGKYRDGVPADSRAqldgydwLRKQVTDAgknnvVGKLGEVAN 260
Cdd:cd19162 172 GRYTLLDR-RAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYDYRP-------ATPEVLAR-----ARRLAAVCR 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501400857 261 ELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMksADVAARITPEVKTRI 314
Cdd:cd19162 239 RYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNL--ALLRTPIPAEFWAEL 290
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
16-302 |
1.52e-22 |
|
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: 95.48 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSW----------VTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKElaWPRVSYVVSTKFFW 85
Cdd:cd19103 7 IALGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 GLA-EAPNQyhtlnrkyLLNAIDASLKRLQLDYVDLVFCHRPdpnTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19103 85 QIAgQSADP--------VADMLEGSLARLGTDYIDIYWIHNP---ADVERWTPELIPLLKSGKVKHVGVSNHNLAEIKRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 YDIAERHHLH-KPVmeQPQYNLFHRKrveeeykrlYEDIGL-------GLTTWS--PLASGLLTGKY--RDGVPADSrAQ 232
Cdd:cd19103 154 NEILAKAGVSlSAV--QNHYSLLYRS---------SEEAGIldyckenGITFFAymVLEQGALSGKYdtKHPLPEGS-GR 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 233 LDGYDWLRKQVTdagknNVVGKLGEVANELGCTIGQLAIGW-ILKNpnvSTVITGASRVEQIGENMKSADV 302
Cdd:cd19103 222 AETYNPLLPQLE-----ELTAVMAEIGAKHGASIAQVAIAWaIAKG---TTPIIGVTKPHHVEDAARAASI 284
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-315 |
4.10e-22 |
|
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: 93.10 E-value: 4.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 15 ELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFFwglaeapnqY 94
Cdd:cd19073 3 ALGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVW---------R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 95 HTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERhhlh 174
Cdd:cd19073 66 DHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 175 KPVMEQPQYNLFHRKRveeEYKRLYEDIGLGLTTWSPLASGlltgkyrdGVPADSRAQldgydwlrkqvtdagknnvvgk 254
Cdd:cd19073 142 PIAVNQVEFHPFLYQA---ELLEYCRENDIVITAYSPLARG--------EVLRDPVIQ---------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 255 lgEVANELGCTIGQLAIGWIL-KNpnvSTVITGASRVEQIGENMKSADVAarITPEVKTRIE 315
Cdd:cd19073 189 --EIAEKYDKTPAQVALRWLVqKG---IVVIPKASSEDHLKENLAIFDWE--LTSEDVAKID 243
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-301 |
5.47e-22 |
|
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: 92.98 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIGSW---VTYG-----NQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKELAWPRVSyvvsTKFfw 85
Cdd:cd19097 1 SKLALGTAqfgLDYGianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRLDKFKII----TKL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 glaEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19097 73 ---PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPDDLLKHGGKLVeALLELKKEGLIRKIGVSVYSPEELEKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 165 YDIaerhhlHKPVMEQPQYNLFHRKRVEEEY-KRLYEDiGLGLTTWSPLASGLLTGKyRDGVPADSRaqldgyDWlrkqv 243
Cdd:cd19097 150 LES------FKIDIIQLPFNILDQRFLKSGLlAKLKKK-GIEIHARSVFLQGLLLME-PDKLPAKFA------PA----- 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 244 tdagkNNVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAD 301
Cdd:cd19097 211 -----KPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-304 |
1.48e-21 |
|
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: 92.60 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSELSIGSWV---TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAWPRVSYVVS 80
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAAlggVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 81 TKFFWGLAEApnqyHTLNRKYLLNAIDASLKRLQLDYVDLVFCHR---PDPNTPVEETVWAMSDMITRGKALYWGTSEWS 157
Cdd:cd19153 83 TKVGRYRDSE----FDYSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 158 ADEIRaayDIAERHHLHKP--VMEQPQYNLfHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTGK-YRDGVPADSRaqld 234
Cdd:cd19153 159 LDTLT---RATRRCSPGSLdaVLSYCHLTL-QDARLESDAPGLVRGAGPHVINASPLSMGLLTSQgPPPWHPASGE---- 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 235 gydwLRKQVTDAGKnnvvgklgeVANELGCTIGQLAIGWILKNPN-VSTVITGASRVEQIGENMKSADVAA 304
Cdd:cd19153 231 ----LRHYAAAADA---------VCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAAVDAVA 288
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-309 |
1.61e-19 |
|
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: 87.19 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIG-SWVTYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELAwPRVSYVVSTKFF--- 84
Cdd:cd19147 11 SPLILGAMSIGdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKFTtdy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 --WGLAE-APNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRGKALYWGTSEWSADEI 161
Cdd:cd19147 90 kaYEVGKgKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 162 RAAYDIAERHHLHKPVMEQPQYNLFHRKrVEEEYKRLYEDIGLGLTTWSPLASGLLTGK------------YRDGVPADS 229
Cdd:cd19147 170 SAANYYATAHGKTPFSVYQGRWNVLNRD-FERDIIPMARHFGMALAPWDVLGGGKFQSKkaveerkkngegLRSFVGGTE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 230 RAQLDgydwlrKQVTDAgknnvvgkLGEVANELGC-TIGQLAIGWIL-KNPNVSTVItGASRVEQIGENMKSADVaaRIT 307
Cdd:cd19147 249 QTPEE------VKISEA--------LEKVAEEHGTeSVTAIALAYVRsKAPNVFPLV-GGRKIEHLKDNIEALSI--KLT 311
|
..
gi 501400857 308 PE 309
Cdd:cd19147 312 PE 313
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
33-309 |
2.70e-19 |
|
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: 86.51 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 33 ARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawPRVSYVVSTKFFW---GLAEAPNQYHTLNRKYL------- 102
Cdd:cd19152 22 AKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALREL--GREDYVISTKVGRllvPLQEVEPTFEPGFWNPLpfdavfd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 103 ------LNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVWAMSDMITRG-KALywgTSEWSADEIRAA------YDIAE 169
Cdd:cd19152 100 ysydgiLRSIEDSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIKGAfRAL---EELREEGVIKAIglgvndWEVIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 170 RHHLHKP---VMEQPQYNLFHrkrvEEEYKRLY---EDIGLGLTTWSPLASGLLTG----KYRDGVPADSraqlDGYDWL 239
Cdd:cd19152 177 RILEEADldwVMLAGRYTLLD----HSAARELLpecEKRGVKVVNAGPFNSGFLAGgdnfDYYEYGPAPP----ELIARR 248
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 240 RkqvtdagknnvvgKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSAdvAARITPE 309
Cdd:cd19152 249 D-------------RIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL--ATEIPAA 303
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
21-301 |
1.32e-18 |
|
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: 83.30 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 21 WVTYG-NQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfwglaeaPNQYHTlnR 99
Cdd:cd19071 3 LIGLGtYKLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-------WPTDHG--Y 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 100 KYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEET-----VW-AMSDMITRGKALYWGTSEWSADEIRAAYDIAErhhl 173
Cdd:cd19071 71 ERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKearleTWrALEELVDEGLVRSIGVSNFNVEHLEELLAAAR---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 174 HKPVMEQPQYNLFHRKRVEEEYKRLYediGLGLTTWSPLASGlltgkyRDGVPADSRaqldgydwlrkqvtdagknnvvg 253
Cdd:cd19071 147 IKPAVNQIELHPYLQQKELVEFCKEH---GIVVQAYSPLGRG------RRPLLDDPV----------------------- 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501400857 254 kLGEVANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENMKSAD 301
Cdd:cd19071 195 -LKEIAKKYGKTPAQVLLRWALQRGVV--VIPKSSNPERIKENLDVFD 239
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-304 |
1.07e-17 |
|
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: 81.99 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 14 SELSIGSwVTYGN---QVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKELawPRVSYVVSTKFFWGLAEA 90
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREK--PRDEFVLSTKVGRLLKPA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 91 -------PNQYHT---LNRKY------LLNAIDASLKRLQLDYVDLVFCHRPDPNTPVE--ETVW----------AMSDM 142
Cdd:cd19161 78 regsvpdPNGFVDplpFEIVYdysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDrkERHHfaqlmsggfkALEEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 143 ITRG--KALYWGTSEWsaDEIRAAYDIAErhhlHKPVMEQPQYNLFHRkRVEEEYKRLYEDIGLGLTTWSPLASGLL-TG 219
Cdd:cd19161 158 KKAGviKAFGLGVNEV--QICLEALDEAD----LDCFLLAGRYSLLDQ-SAEEEFLPRCEQRGTSLVIGGVFNSGILaTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 220 KyrdgvpaDSRAQLDgYdwlrkqvTDAGKN--NVVGKLGEVANELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENM 297
Cdd:cd19161 231 T-------KSGAKFN-Y-------GDAPAEiiSRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNV 295
|
....*..
gi 501400857 298 KSADVAA 304
Cdd:cd19161 296 EAFQTDI 302
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-214 |
2.16e-14 |
|
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: 72.44 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKff 84
Cdd:cd19154 8 NGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAELleegVVKREDLFITTK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 wglaeAPNQYHTlnRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVE------------------ETVWA-MSDMITR 145
Cdd:cd19154 78 -----LWTHEHA--PEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEgesgtmengmsihdavdvEDVWRgMEKVYDE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 146 GKALYWGTSEWSADEIRAAYDIAERhhlhKPVMEQPQYNLFHRkrvEEEYKRLYEDIGLGLTTWSPLAS 214
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDNARV----KPHNNQVECHLYFP---QKELVEFCKKHNISVTSYATLGS 212
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
10-302 |
1.33e-13 |
|
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: 69.32 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWglae 89
Cdd:cd19131 7 GNTIPQLGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-W---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 90 apNQYHTLNRKylLNAIDASLKRLQLDYVDLVFCHRPDP--NTPVEetVW-AMSDMITRGKALYWGTSEWSADEIRAAYD 166
Cdd:cd19131 74 --NSDQGYDST--LRAFDESLRKLGLDYVDLYLIHWPVPaqDKYVE--TWkALIELKKEGRVKSIGVSNFTIEHLQRLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 167 ------IAERHHLHkPVMEQPQYNLFHRKRveeeykrlyediGLGLTTWSPLASGlltgkyrdGVPADSRaqldgydwlr 240
Cdd:cd19131 148 etgvvpVVNQIELH-PRFQQRELRAFHAKH------------GIQTESWSPLGQG--------GLLSDPV---------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 241 kqvtdagknnvvgkLGEVANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENMKSADV 302
Cdd:cd19131 197 --------------IGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENFDVFDF 242
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
11-299 |
4.61e-13 |
|
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: 68.46 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 11 LQVSELSIGSwVTYGNQVDTH----AARESLAAARDAGVNFFDNAEVYagGKSEEIMGQALKELA--WPRVSYVVSTKff 84
Cdd:cd19164 11 AGLPPLIFGA-ATFSYQYTTDpesiPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKALRdeFPRDTYFIITK-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 wgLAEAPNQYHTLNRKYLLNAIDASLKRLQLDYVDLVFCHrpDPN-TPVEETVWAMSDMIT---RGKALYWGTSEWSADE 160
Cdd:cd19164 86 --VGRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGISGYPLPV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 161 IrAAYDIAERHHLHKP---VMEQPQYNLfHRKRVEEEYKRLYEDIGLG-LTTWSPLASGLLTgkyRDGVPadsraqldgy 236
Cdd:cd19164 162 L-LRLAELARTTAGRPldaVLSYCHYTL-QNTTLLAYIPKFLAAAGVKvVLNASPLSMGLLR---SQGPP---------- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 237 DW------LRkqvtdagknNVVGKLGEVANELGCTIGQLAIGWILK--NPNVSTVItGASRVEQIGENMKS 299
Cdd:cd19164 227 EWhpaspeLR---------AAAAKAAEYCQAKGTDLADVALRYALRewGGEGPTVV-GCSNVDELEEAVEA 287
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-217 |
1.12e-12 |
|
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: 66.69 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYgnqvDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWglae 89
Cdd:cd19126 6 GTRMPWLGLGVFQTP----DGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-W---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 90 apNQYHTLNRKylLNAIDASLKRLQLDYVDLVFCHRPDPNTpVEETVWAMSDMITRGKALYWGTS---EWSADEIRAAYD 166
Cdd:cd19126 74 --NDDQRARRT--EDAFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSnfqEHHLEELLAHAD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 501400857 167 IAerhhlhkPVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLL 217
Cdd:cd19126 149 VV-------PAVNQVE---FHPYLTQKELRGYCKSKGIVVEAWSPLGQGGL 189
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
26-224 |
1.53e-12 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 66.49 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 26 NQVDTHAArESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFFWGLAEAPNqyhtlnrkyllnA 105
Cdd:cd19120 21 DDIQRDLV-DSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIKDPRE------------A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 106 IDASLKRLQLDYVDLVFCHRP---DPNTPVEETVWA-MSDMITRGKALYWGTSEWSADEIRAAYDIAerhhLHKPVMEQP 181
Cdd:cd19120 85 LRKSLAKLGVDYVDLYLIHSPffaKEGGPTLAEAWAeLEALKDAGLVRSIGVSNFRIEDLEELLDTA----KIKPAVNQI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 501400857 182 QYNLFhrkrVEEEYKRLYE---DIGLGLTTWSPLASgllTGKYRDG 224
Cdd:cd19120 161 EFHPY----LYPQQPALLEycrEHGIVVSAYSPLSP---LTRDAGG 199
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
33-215 |
2.21e-12 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 66.06 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 33 ARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWglaeaPNQYHTLNRKYllnAIDASLKR 112
Cdd:cd19133 25 CERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSGIPREELFITTKL-W-----IQDAGYEKAKK---AFERSLKR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 113 LQLDYVDLVFCHRPDPNtpVEETVWAMSDMITRGKALYWGTSEWSADEIRaayDIAERHHLhKPVMEQPQYNLFHRKRVE 192
Cdd:cd19133 93 LGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLV---DLILHNEV-KPAVNQIETHPFNQQIEA 166
|
170 180
....*....|....*....|...
gi 501400857 193 EEYKRLYediGLGLTTWSPLASG 215
Cdd:cd19133 167 VEFLKKY---GVQIEAWGPFAEG 186
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
15-215 |
3.54e-12 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 65.48 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 15 ELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWglaeapNQY 94
Cdd:PRK11565 17 QLGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-W------NDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 95 HTLNRKyllnAIDASLKRLQLDYVDLVFCHRPDPntPVEETVWAMSDMIT---RGKALYWGTSEWSADEIRAAYD----- 166
Cdd:PRK11565 82 HKRPRE----ALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIHHLQRLIDetgvt 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 501400857 167 -IAERHHLHkPVMEQPQ---YNLFHRKRVEeeykrlyediglgltTWSPLASG 215
Cdd:PRK11565 156 pVINQIELH-PLMQQRQlhaWNATHKIQTE---------------SWSPLAQG 192
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-215 |
7.47e-12 |
|
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: 64.33 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSW-VTYGNQVdthaaRESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWgla 88
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEV-----VNAVKTALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-W--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 EAPNQYHTLnrkylLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEetVW-AMSDMITRGKALYWGTSEWsadeiraaydi 167
Cdd:cd19157 75 NADQGYDST-----LKAFEASLERLGLDYLDLYLIHWPVKGKYKE--TWkALEKLYKDGRVRAIGVSNF----------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 168 aERHHLH--------KPVMEQPQYnlfHRKRVEEEYKRLYEDIGLGLTTWSPLASG 215
Cdd:cd19157 137 -QVHHLEdlladaeiVPMVNQVEF---HPRLTQKELRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-273 |
1.13e-11 |
|
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: 63.83 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYAggkSEEIMGQALKELAWPRVSYVVSTKFfwglae 89
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 90 aPNQYHtlNRKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIraayDIA 168
Cdd:cd19132 70 -PGRHH--GYEEALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYVEAWqALIEAREEGLVRSIGVSNFLPEHL----DRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 169 ERHHLHKPVMEQ----PQYNLFHRKRVEEEYKRLYEdiglgltTWSPL--ASGLLTGkyrdgvpadsraqldgydwlrkq 242
Cdd:cd19132 143 IDETGVTPAVNQielhPYFPQAEQRAYHREHGIVTQ-------SWSPLgrGSGLLDE----------------------- 192
|
250 260 270
....*....|....*....|....*....|.
gi 501400857 243 vtdagknnvvGKLGEVANELGCTIGQLAIGW 273
Cdd:cd19132 193 ----------PVIKAIAEKHGKTPAQVVLRW 213
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
37-307 |
1.47e-10 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 61.21 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 37 LAAARDAGVNFFDNAEVYagGKSEEIMGQALKELAWPRVSYVVSTKffWG---LAE-----APNQY--HTLNRkyLLNAI 106
Cdd:cd19098 41 LDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytyTADwqvdaAVHEVkdHSLAR--LLKQW 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 107 DASLKRLQlDYVDLVFCHRPDPNTPV---EETVWAMSDMITRGKALYWGTS-EWSADEIRAAYDIA-ERHHLHKPVmeQP 181
Cdd:cd19098 115 EETRSLLG-KHLDLYQIHSATLESGVledADVLAALAELKAEGVKIGLSLSgPQQAETLRRALEIEiDGARLFDSV--QA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 182 QYNLFHRKRVE--EEYKrlyeDIGLGLTTWSPLASGLLTGKyrdgvpadsraqldgydwlrkqVTDAGKNNVVGKLGEVA 259
Cdd:cd19098 192 TWNLLEQSAGEalEEAH----EAGMGVIVKEALANGRLTDR----------------------NPSPELAPLMAVLKAVA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 501400857 260 NELGCTIGQLAIGWILKNPNVSTVITGASRVEQIGENMKSADVAARIT 307
Cdd:cd19098 246 DRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLE 293
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-214 |
1.14e-09 |
|
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: 58.28 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKffw 85
Cdd:cd19111 1 GFPMPVIGLGTY-----QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKWWlkngKLKREEVFITTK--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 86 glaeAPNQYHTlnRKYLLNAIDASLKRLQLDYVDLVFCH-------------RPDPNTPVEETVWAMSDMITRGKALYWG 152
Cdd:cd19111 70 ----LPPVYLE--FKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 501400857 153 TSEWSADEIRAAYDIAerhhLHKPVMEQPQYNLFHRKRveeEYKRLYEDIGLGLTTWSPLAS 214
Cdd:cd19111 144 LSNFNPRQINKILAYA----KVKPSNLQLECHAYLQQR---ELRKFCNKKNIVVTAYAPLGS 198
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-131 |
1.43e-09 |
|
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: 57.89 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVdthaaRESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWgla 88
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPNEV-----AKAVEAALKAGYRHIDTAAIY---GNEEEVGQGIKDSGVPREEIFITTKL-W--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 501400857 89 eapNQYHtlnrKYLLNAIDASLKRLQLDYVDLVFCHRPDPNTP 131
Cdd:cd19117 78 ---CTWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDP 113
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
1-302 |
1.66e-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: 57.81 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 1 MNYRRLgRSGLQVSELSIGSWVTYGNQVdthaaRESLAAARDAGVNFFDNAEVYagGKSEEImGQAL----KELAWPRVS 76
Cdd:cd19123 1 MKTLPL-SNGDLIPALGLGTWKSKPGEV-----GQAVKQALEAGYRHIDCAAIY--GNEAEI-GAALaevfKEGKVKRED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 77 YVVSTKFfWGLAEAPNQyhtlnrkyLLNAIDASLKRLQLDYVDLVFCHRP------------------DPNTPVEETVWA 138
Cdd:cd19123 72 LWITSKL-WNNSHAPED--------VLPALEKTLADLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 139 MSDMITRGKALYWGTSEWSADEIRAAYDIAErhhlHKPVMEQPQYNLFHRKRVEEEYKRlyeDIGLGLTTWSPLASgllt 218
Cdd:cd19123 143 MEELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQVELHPYLQQPELLAFCR---DNGIHLTAYSPLGS---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 219 gkyrdGVPADSRAQLDGYDWLRKQVtdagknnvvgkLGEVANELGCTIGQLAIGWILKNpNVSTVITGASRvEQIGENMK 298
Cdd:cd19123 212 -----GDRPAAMKAEGEPVLLEDPV-----------INKIAEKHGASPAQVLIAWAIQR-GTVVIPKSVNP-ERIQQNLE 273
|
....
gi 501400857 299 SADV 302
Cdd:cd19123 274 AAEV 277
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
9-301 |
1.84e-09 |
|
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: 57.81 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVdthaaRESLAAARDAGVNFFDNAEVYaGGKSEeiMGQALKELAWPRVsyVVSTKFFWGLA 88
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEV-----GAAVKIALKAGYRHLDLAKVY-QNQHE--VGQALKELLKEEP--GVKREDLFITS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 EAPNQYHTlnRKYLLNAIDASLKRLQLDYVDLVFCHRP---------DPNTPVE---------------ETVWAMSDMIT 144
Cdd:cd19118 73 KLWNNSHR--PEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlNPLTAVPtnggevdldlsvslvDTWKAMVELKK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 145 RGKALYWGTSEWSADEIRAAYDIA---------ERHhlhkPVMEQPQYNLFHRKRveeeykrlyediGLGLTTWSPLAsg 215
Cdd:cd19118 151 TGKVKSIGVSNFSIDHLQAIIEETgvvpavnqiEAH----PLLLQDELVDYCKSK------------NIHITAYSPLG-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 216 lltgkyrdgvpadsraqldgydwlrkqvtdagkNNVVGK--------LGEVANELGCTIGQLAIGWILKNPNvsTVITGA 287
Cdd:cd19118 213 ---------------------------------NNLAGLpllvqhpeVKAIAAKLGKTPAQVLIAWGIQRGH--SVIPKS 257
|
330
....*....|....
gi 501400857 288 SRVEQIGENMKSAD 301
Cdd:cd19118 258 VTPSRIRSNFEQVE 271
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
29-185 |
2.15e-09 |
|
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: 57.47 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 29 DTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKFfWglaeapNQYHTLNRkyLLN 104
Cdd:cd19129 17 DPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagKIRREDLFVTTKL-W------NTNHRPER--VKP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 105 AIDASLKRLQLDYVDLVFCHRP--------------------DPNTPVEETVWAMSDMITRGKALYWGTSEWSADEIRAA 164
Cdd:cd19129 85 AFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREI 164
|
170 180
....*....|....*....|....*...
gi 501400857 165 YDIAERhhlhKPVMEQ-------PQYNL 185
Cdd:cd19129 165 FEAARI----KPAVVQveshpylPEWEL 188
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
9-298 |
3.20e-09 |
|
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: 56.97 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYagGKSEEImGQALKEL----AWPRVSYVVSTKFf 84
Cdd:cd19125 7 TGAKIPAVGLGTW-----QADPGVVGNAVKTAIKEGYRHIDCAAIY--GNEKEI-GKALKKLfedgVVKREDLFITSKL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 WGLAEAPNQYHTlnrkyllnAIDASLKRLQLDYVDLVFCHRP--------------DPNTPVEETVWAMSDMITRGKALY 150
Cdd:cd19125 78 WCTDHAPEDVPP--------ALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpepeeVLPPDIPSTWKAMEKLVDSGKVRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 151 WGTSEWS---------ADEIRAAYDIAERHhlhkPVMEQPQYNLFHRKRveeeykrlyediGLGLTTWSPLASGlltgky 221
Cdd:cd19125 150 IGVSNFSvkkledllaVARVPPAVNQVECH----PGWQQDKLHEFCKSK------------GIHLSAYSPLGSP------ 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501400857 222 rdgvpadsraqldGYDWLRKQVTdagKNNVVGKlgeVANELGCTIGQLAIGWILKNPNvsTVITGASRVEQIGENMK 298
Cdd:cd19125 208 -------------GTTWVKKNVL---KDPIVTK---VAEKLGKTPAQVALRWGLQRGT--SVLPKSTNEERIKENID 263
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
4-321 |
4.69e-09 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 56.52 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 4 RRLGRSGLQVSelsiGSWVtYGNQVDTHAARESLAAARDAGVNFFDNAEVYAGGKSEEIMGQALKelawP-RVSYVVSTK 82
Cdd:PRK10376 18 NRLGYGAMQLA----GPGV-FGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALH----PyPDDLTIVTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 83 F--------FWGLAEAPNQyhtlnrkyLLNAIDASLKRLQLDYVDLV------FCHRPDPNtPVEETVWAMSDMITRGKA 148
Cdd:PRK10376 89 VgarrgedgSWLPAFSPAE--------LRRAVHDNLRNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 149 LYWGTSEWSADEIRAAYDIAErhhlhkPVMEQPQYNLFHRKRvEEEYKRLYEDiGLG------LTTWSPLASGLLTgkyr 222
Cdd:PRK10376 160 RHIGLSNVTPTQVAEARKIAE------IVCVQNHYNLAHRAD-DALIDALARD-GIAyvpffpLGGFTPLQSSTLS---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 223 dgvpadsraqldgydwlrkqvtdagknnvvgklgEVANELGCTIGQLAIGWILK-NPNVsTVITGASRVEQIGENMKSAD 301
Cdd:PRK10376 228 ----------------------------------DVAASLGATPMQVALAWLLQrSPNI-LLIPGTSSVAHLRENLAAAE 272
|
330 340
....*....|....*....|
gi 501400857 302 VaaRITPEVKTRIEEIIGDA 321
Cdd:PRK10376 273 L--VLSEEVLAELDGIAREA 290
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
16-309 |
8.05e-09 |
|
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: 55.61 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYAggkSEEIMGQALKEL----AWPRVSYVVSTKFfWglaeaP 91
Cdd:cd19128 4 LGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdgGVKREDLFITSKL-W-----P 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 92 NQYHTLNRKYllnAIDASLKRLQLDYVDLVFCHRP---DPNT----------------PVEETVWAMSDMITRGKALYWG 152
Cdd:cd19128 70 TMHQPENVKE---QLLITLQDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 153 TSEWSADEIRAAYDIAERhhlhKPVMEQPQYNLFHRkrvEEEYKRLYEDIGLGLTTWSPLAsglltGKYRDGVPAdsraq 232
Cdd:cd19128 147 VSNYSTKLLTDLLNYCKI----KPFMNQIECHPYFQ---NDKLIKFCIENNIHVTAYRPLG-----GSYGDGNLT----- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 233 LDGYDWLRkqvtdagknnvvgklgEVANELGCTIGQLAIGWILKN-PNVSTVITGASRVEQIGENMKSADVaaRITPE 309
Cdd:cd19128 210 FLNDSELK----------------ALATKYNTTPPQVIIAWHLQKwPKNYSVIPKSANKSRCQQNFDINDL--ALTKE 269
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-317 |
1.01e-08 |
|
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: 55.22 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWvtygnQV-DTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKffwgLA 88
Cdd:cd19156 6 GVEMPRLGLGVW-----RVqDGAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTK----LW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 89 EAPNQYHTLnrkylLNAIDASLKRLQLDYVDLVFCHRPDPNTPVEEtvW-AMSDMITRGKALYWGTSEWSADEIRAAYDI 167
Cdd:cd19156 74 NSDQGYEST-----LAAFEESLEKLGLDYVDLYLIHWPVKGKFKDT--WkAFEKLYKEKKVRAIGVSNFHEHHLEELLKS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 168 AERhhlhKPVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLTgkyrdgvpadsraqldgydwlrkqvtdag 247
Cdd:cd19156 147 CKV----APMVNQIE---LHPLLTQEPLRKFCKEKNIAVEAWSPLGQGKLL----------------------------- 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 248 KNNVVGKLGEVANElgcTIGQLAIGWILKNPNVstVITGASRVEQIGENMKSADVaaRITPEVKTRIEEI 317
Cdd:cd19156 191 SNPVLKAIGKKYGK---SAAQVIIRWDIQHGII--TIPKSVHEERIQENFDVFDF--ELTAEEIRQIDGL 253
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
33-314 |
1.22e-08 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 54.95 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 33 ARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKFfwglaeAPNqYHTLNRKYllNAIDA 108
Cdd:cd19136 17 VRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDLlpkyGLSREDIFITSKL------APK-DQGYEKAR--AACLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 109 SLKRLQLDYVDLVFCHRP-----DPNTPVE-----ETVWAMSDMITRGKALYWGTSEWSA---DEIRAAYDIaerhhlhK 175
Cdd:cd19136 85 SLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVrhlEELLKYCEV-------P 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 176 PVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLtgkyrdgvpadsraqldgydwlrKQVTDAgknnvvgKL 255
Cdd:cd19136 158 PAVNQVE---FHPHLVQKELLKFCKDHGIHLQAYSSLGSGDL-----------------------RLLEDP-------TV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 501400857 256 GEVANELGCTIGQLAIGWILKNpNVStVITGASRVEQIGENMKSADVAarITPEVKTRI 314
Cdd:cd19136 205 LAIAKKYGRTPAQVLLRWALQQ-GIG-VIPKSTNPERIAENIKVFDFE--LSEEDMAEL 259
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
10-297 |
1.51e-08 |
|
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: 54.86 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSigswvtygnqvDTHAAReSLAAARDAGVNFFDNAEVYAggkSEEIMGQALKELAWPRVSYVVSTKFFwglae 89
Cdd:cd19134 15 GLGVGELS-----------DDEAER-SVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 90 APNQYHTLNRKyllnAIDASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIRAAYDIA 168
Cdd:cd19134 75 TPDQGFTASQA----ACRASLERLGLDYVDLYLIHWPAGREGKYVDSWgGLMKLREEGLARSIGVSNFTAEHLENLIDLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 169 erhhLHKPVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLASGLLtgkyrdgvpadsraqLDgydwlrkqvtdagk 248
Cdd:cd19134 151 ----FFTPAVNQIE---LHPLLNQAELRKVNAQHGIVTQAYSPLGVGRL---------------LD-------------- 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 501400857 249 NNVVGKLgevANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENM 297
Cdd:cd19134 195 NPAVTAI---AAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-131 |
2.32e-08 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 54.46 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAW---PRVSYVVSTKFfW 85
Cdd:cd19121 8 TGASIPAVGLGTW-----QAKAGEVKAAVAHALKIGYRHIDGALCY---QNEDEVGEGIKEAIAggvKREDLFVTTKL-W 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 501400857 86 glaeapNQYHTLNRKyllnAIDASLKRLQLDYVDLVFCHRPDPNTP 131
Cdd:cd19121 79 ------STYHRRVEL----CLDRSLKSLGLDYVDLYLVHWPVLLNP 114
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
34-317 |
3.65e-08 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 53.51 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 34 RESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFFWglaeapnqyHTLNRKYLLNAIDASLKRL 113
Cdd:cd19139 17 IDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI---------DNLSKDKLLPSLEESLEKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 114 QLDYVDLVFCHRPDPN--TPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPVMEQPQYnLFHRKRV 191
Cdd:cd19139 85 RTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY-LQNRKLV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 192 EEEYKRlyediGLGLTTWSPLASGLLTgkyRDGVpadsraqldgydwlrkqvtdagknnvvgkLGEVANELGCTIGQLAI 271
Cdd:cd19139 164 AHCKQH-----GIHVTSYMTLAYGKVL---DDPV-----------------------------LAAIAERHGATPAQIAL 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 501400857 272 GWILKNPNVstVITGASRVEQIGENMKSADVaaRITPEVKTRIEEI 317
Cdd:cd19139 207 AWAMARGYA--VIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
8-298 |
4.28e-08 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 53.48 E-value: 4.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 8 RSGLQVSELSIGSWvTYGNQvdTHAAreSLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFFwgl 87
Cdd:cd19135 8 SNGVEMPILGLGTS-HSGGY--SHEA--VVYALKECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKLW--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 88 aeaPNQYHTLNRKyllNAIDASLKRLQLDYVDLVFCHRPDPNTPV-------EETVWAMSDMITRGKALYWGTSEWSA-- 158
Cdd:cd19135 77 ---PSDYGYESTK---QAFEASLKRLGVDYLDLYLLHWPDCPSSGknvketrAETWRALEELYDEGLCRAIGVSNFLIeh 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 159 -DEIRAAYDIAerhhlhkPVMEQPQYNLFHRkrvEEEYKRLYEDIGLGLTTWSPLASGLLTGKyrdgvPAdsraqldgyd 237
Cdd:cd19135 151 lEQLLEDCSVV-------PHVNQVEFHPFQN---PVELIEYCRDNNIVFEGYCPLAKGKALEE-----PT---------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 501400857 238 wlrkqvtdagknnvvgkLGEVANELGCTIGQLAIGWILKNpNVSTvITGASRVEQIGENMK 298
Cdd:cd19135 206 -----------------VTELAKKYQKTPAQILIRWSIQN-GVVT-IPKSTKEERIKENCQ 247
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
23-317 |
1.14e-07 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 52.27 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 23 TYGNQVDTHAARESLAAARDAGVNFFDNAEVYAggkSEEIMGQALKE-----LAWPRVSYVVSTKFfWgLAEApnqyhtl 97
Cdd:cd19124 12 TASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEalrlgLVKSRDELFVTSKL-W-CSDA------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 98 NRKYLLNAIDASLKRLQLDYVDLVFCHRP---DP---NTPVE---------ETVW-AMSDMITRGKALYWGTSEWSADEI 161
Cdd:cd19124 80 HPDLVLPALKKSLRNLQLEYVDLYLIHWPvslKPgkfSFPIEeedflpfdiKGVWeAMEECQRLGLTKAIGVSNFSCKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 162 RAAYDIAERhhlhKPVMEQPQYNLFHRKRVEEEYKRlyeDIGLGLTTWSPLASGlltgkyrdgvpadsraqldGYDWLRK 241
Cdd:cd19124 160 QELLSFATI----PPAVNQVEMNPAWQQKKLREFCK---ANGIHVTAYSPLGAP-------------------GTKWGSN 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501400857 242 QVTDAgknnvvGKLGEVANELGCTIGQLAIGWILKNpNVSTVITGASRvEQIGENMKSADVAarITPEVKTRIEEI 317
Cdd:cd19124 214 AVMES------DVLKEIAAAKGKTVAQVSLRWVYEQ-GVSLVVKSFNK-ERMKQNLDIFDWE--LTEEDLEKISEI 279
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
16-126 |
3.27e-07 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 50.74 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSWVTYGNQVDTHAARESLaaarDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKFfWglaeap 91
Cdd:cd19116 14 IALGTWKLKDDEGVRQAVKHAI----EAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-W------ 79
|
90 100 110
....*....|....*....|....*....|....*
gi 501400857 92 NQYHtlNRKYLLNAIDASLKRLQLDYVDLVFCHRP 126
Cdd:cd19116 80 NSYH--EREQVEPALRESLKRLGLDYVDLYLIHWP 112
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-307 |
4.12e-07 |
|
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: 50.48 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQvdthaARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFF---WG 86
Cdd:cd19127 6 GVEMPALGLGVFQTPPEE-----TADAVATALADGYRLIDTAAAY---GNEREVGEGIRRSGVDRSDIFVTTKLWisdYG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 87 LAEApnqyhtlnrkylLNAIDASLKRLQLDYVDLVFCHRPDPNTpVEETV--W-AMSDMITRGKALYWGTSEWSADEIRA 163
Cdd:cd19127 78 YDKA------------LRGFDASLRRLGLDYVDLYLLHWPVPND-FDRTIqaYkALEKLLAEGRVRAIGVSNFTPEHLER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 164 AYDIAE------RHHLHkPVMEQPQYNLFHRKrveeeykrlyedigLGLTT--WSPLAsGLLTgkYRDGVPADSRAQLDG 235
Cdd:cd19127 145 LIDATTvvpavnQVELH-PYFSQKDLRAFHRR--------------LGIVTqaWSPIG-GVMR--YGASGPTGPGDVLQD 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501400857 236 YdwlrkqvtdagknnvvgKLGEVANELGCTIGQLAIGWILKNPNVStvITGASRVEQIGENMK------SADVAARIT 307
Cdd:cd19127 207 P-----------------TITGLAEKYGKTPAQIVLRWHLQNGVSA--IPKSVHPERIAENIDifdfalSAEDMAAID 265
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
32-314 |
5.48e-07 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 50.02 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 32 AARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKELAWPRVSYVVSTKFfWglaeapnqYHTLNRKYLLNAIDASLK 111
Cdd:PRK11172 17 VVIDSVKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKI-W--------IDNLAKDKLIPSLKESLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 112 RLQLDYVDLVFCHRPDPN--TPVEETVWAMSDMITRGKALYWGTSEWSADEIRAAYDIAERHHLHKPVMEQPQYnLFHRK 189
Cdd:PRK11172 85 KLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIATNQIELSPY-LQNRK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 190 RVEeeykrLYEDIGLGLTTWSPLASGlltgkyrdgvpadsraqldgydwlrKQVTDAgknnvvgKLGEVANELGCTIGQL 269
Cdd:PRK11172 164 VVA-----FAKEHGIHVTSYMTLAYG-------------------------KVLKDP-------VIARIAAKHNATPAQV 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 501400857 270 AIGWILKNPnvSTVITGASRVEQIGENMKSADVaaRITPEVKTRI 314
Cdd:PRK11172 207 ILAWAMQLG--YSVIPSSTKRENLASNLLAQDL--QLDAEDMAAI 247
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-214 |
7.37e-07 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 50.08 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVdthaaRESLAAARDAGVNFFDNAEVYagGKSEEImGQALKE-----LAWPRVSYVVSTKF 83
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVY--GNEQEV-GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 84 fWGLAEAPNQyhtlnrkyLLNAIDASLKRLQLDYVDLVFCHRP------------DPN-------TPVEETVWAMSDMIT 144
Cdd:cd19106 75 -WNTKHHPED--------VEPALRKTLKDLQLDYLDLYLIHWPyafergdnpfpkNPDgtirydsTHYKETWKAMEKLVD 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 145 RGKALYWGTSEWSADEIRAAYDIAErhhlHKPVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLAS 214
Cdd:cd19106 146 KGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVE---CHPYLAQNELIAHCKARGLVVTAYSPLGS 208
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
27-219 |
1.43e-06 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 48.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 27 QVDTHAARESLAAARDAGVNFFDNAEVYAggkSEEIMGQALKELAWPRVSYVVSTKFFwglaeapNQYHTLNRkyLLNAI 106
Cdd:cd19130 19 KVPPADTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGIPRDELFVTTKLW-------NDRHDGDE--PAAAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 107 DASLKRLQLDYVDLVFCHRPDPNTPVEETVW-AMSDMITRGKALYWGTSEWSADEIraayDIAERHHLHKPVMEQPQYNL 185
Cdd:cd19130 87 AESLAKLGLDQVDLYLVHWPTPAAGNYVHTWeAMIELRAAGRTRSIGVSNFLPPHL----ERIVAATGVVPAVNQIELHP 162
|
170 180 190
....*....|....*....|....*....|....
gi 501400857 186 FHRKRVEEEYKRLYediGLGLTTWSPLASGLLTG 219
Cdd:cd19130 163 AYQQRTIRDWAQAH---DVKIEAWSPLGQGKLLG 193
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-182 |
4.65e-06 |
|
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: 47.44 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYAGGKS-EEIMGQALKELAWPRVSYVVSTKFfWgl 87
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEKEvGEGVNRAIDEGLVKREELFLTSKL-W-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 88 aeapNQYHtlNRKYLLNAIDASLKRLQLDYVDLVFCHRP-------------------------DPNTPVEETVWAMSDM 142
Cdd:cd19113 79 ----NNFH--DPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdgdnfvYEDVPILDTWKALEKL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 501400857 143 ITRGKALYWGTSEWSA----DEIRAA----YDIAERHHlhkPVMEQPQ 182
Cdd:cd19113 153 VDAGKIKSIGVSNFPGalilDLLRGAtikpAVLQIEHH---PYLQQPK 197
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-215 |
6.95e-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: 46.72 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVDThaaRESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKFf 84
Cdd:cd19119 8 TGASIPALGLGTASPHEDRAEV---KEAVEAAIKEGYRHIDTAYAY---ETEDFVGEAIKRAiddgSIKREELFITTKV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 85 WglaeaPNQYHTLNRkyllnAIDASLKRLQLDYVDLVFCHRP-----------DPNTPVEE---TVWAMS-DMIT----- 144
Cdd:cd19119 81 W-----PTFYDEVER-----SLDESLKALGLDYVDLLLVHWPvcfekdsddsgKPFTPVNDdgkTRYAASgDHITtykql 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 145 -----RGKALYWGTSEWSADEIRAAYDIAE--------RHHLHKPVMEQPQYNLFHrkrveeeykrlyediGLGLTTWSP 211
Cdd:cd19119 151 ekiylDGRAKAIGVSNYSIVYLERLIKECKvvpavnqvELHPHLPQMDLRDFCFKH---------------GILVTAYSP 215
|
....
gi 501400857 212 LASG 215
Cdd:cd19119 216 LGSH 219
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
9-303 |
1.22e-05 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 46.08 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWVTYGNQVDTHAAresLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL-----AWPRVSYVVSTKF 83
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFY---LNEDEVGDAVRDFlkenpSVKREDLFICTKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 84 FWGLAEAPNqyhtlnrkyLLNAIDASLKRLQLDYVDLVFCHRP------DPNTPV-----------------EETVWAMS 140
Cdd:cd19122 79 WNHLHEPED---------VKWSIDNSLKNLKLDYIDLFLVHWPiaaeknDQRSPKlgpdgkyvilkdltenpEPTWRAME 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 141 DMITRGKALYWGTSEWSADEIRAAYDIAERhhlhKPVMEQPQYNLFhrkRVEEEYKRLYEDIGLGLTTWSPLASglltgk 220
Cdd:cd19122 150 EIYESGKAKAIGVSNWTIPGLKKLLSFAKV----KPHVNQIEIHPF---LPNEELVDYCFSNDILPEAYSPLGS------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 221 yrdgvpadsraqldgydwlRKQVTDAG-KNNVVGKLGEVANELGCTIGQLAIGWILKNPNVstVITGASRVEQIGENMKS 299
Cdd:cd19122 217 -------------------QNQVPSTGeRVSENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKS 275
|
....
gi 501400857 300 ADVA 303
Cdd:cd19122 276 IELS 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-141 |
2.73e-05 |
|
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: 45.17 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 9 SGLQVSELSIGSWvtygnQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKElAW-----PRVSYVVSTKF 83
Cdd:cd19112 7 SGHKMPVIGLGVW-----RMEPGEIKELILNAIKIGYRHFDCAADY---KNEKEVGEALAE-AFktglvKREDLFITTKL 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 84 fWglaeapNQYHtlnrKYLLNAIDASLKRLQLDYVDLVFCHRPDP--NTPVEETVWAMSD 141
Cdd:cd19112 78 -W------NSDH----GHVIEACKDSLKKLQLDYLDLYLVHFPVAtkHTGVGTTGSALGE 126
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
16-214 |
1.44e-04 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 42.79 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSWVTYGNQVdthaaRESLAAARDAGVNFFDNAEVYaggKSEEIMGQA----LKELAWPRVSYVVSTKFFwglaeap 91
Cdd:cd19107 7 LGLGTWKSPPGQV-----TEAVKVAIDAGYRHIDCAYVY---QNENEVGEAiqekIKEQVVKREDLFIVSKLW------- 71
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 92 NQYHtlNRKYLLNAIDASLKRLQLDYVDLVFCHRPD-------------------PNTPVEETVWAMSDMITRGKALYWG 152
Cdd:cd19107 72 CTFH--EKGLVKGACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKAIG 149
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170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501400857 153 TSEWSADEIRAaydIAERHHL-HKPVMEQPQynlFHRKRVEEEYKRLYEDIGLGLTTWSPLAS 214
Cdd:cd19107 150 VSNFNHLQIER---ILNKPGLkYKPAVNQIE---CHPYLTQEKLIQYCQSKGIVVTAYSPLGS 206
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| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
16-161 |
6.80e-04 |
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AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 40.71 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 16 LSIGSWVTYGNQVdTHAARESLaaarDAGVNFFDNAEVYAGgKSEEIMG--QALKELAWPRVSYVVSTKFfwglaeapnq 93
Cdd:cd19110 7 VGLGTWKASPGEV-TEAVKVAI----DAGYRHFDCAYLYHN-ESEVGAGirEKIKEGVVRREDLFIVSKL---------- 70
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 94 YHTLNRKYLL-NAIDASLKRLQLDYVDLVFCHRP------DPNTPVEET------------VW-AMSDMITRGKALYWGT 153
Cdd:cd19110 71 WCTCHKKSLVkTACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRSgmvipsdtdfldTWeAMEDLVIEGLVKNIGV 150
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....*...
gi 501400857 154 SEWSADEI 161
Cdd:cd19110 151 SNFNHEQL 158
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| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
23-134 |
1.24e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 39.91 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 23 TYG-NQVDTHAARESLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKFfWGlaeapnqyhTL 97
Cdd:cd19108 18 TYApEEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WC---------TF 84
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90 100 110
....*....|....*....|....*....|....*...
gi 501400857 98 NRKYLLN-AIDASLKRLQLDYVDLVFCHRPDPNTPVEE 134
Cdd:cd19108 85 HRPELVRpALEKSLKKLQLDYVDLYLIHFPVALKPGEE 122
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| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
10-126 |
2.64e-03 |
|
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: 39.05 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501400857 10 GLQVSELSIGSWVTYGNQVDThaareSLAAARDAGVNFFDNAEVYaggKSEEIMGQALKEL----AWPRVSYVVSTKffw 85
Cdd:cd19155 9 GEKMPVVGLGTWQSSPEEIET-----AVDTALEAGYRHIDTAYVY---RNEAAIGNVLKKWidsgKVKREELFIVTK--- 77
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90 100 110 120
....*....|....*....|....*....|....*....|.
gi 501400857 86 gLAEAPNQYHTLnRKYLLnaidASLKRLQLDYVDLVFCHRP 126
Cdd:cd19155 78 -LPPGGNRREKV-EKFLL----KSLEKLQLDYVDLYLIHFP 112
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