|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-287 |
0e+00 |
|
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: 625.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19159 37 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19159 117 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19159 197 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19159 277 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
1-275 |
0e+00 |
|
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: 586.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19141 36 VTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19141 116 DIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19141 196 FHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCL 275
|
250 260 270
....*....|....*....|....*....|....*
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 275
Cdd:cd19141 276 KNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-287 |
0e+00 |
|
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: 556.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19160 39 LTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19160 119 DIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19160 199 YHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCL 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19160 279 RSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
1-283 |
0e+00 |
|
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: 527.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:TIGR01293 35 LTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:TIGR01293 115 DIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:TIGR01293 195 YHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCL 274
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 283
Cdd:TIGR01293 275 RNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-288 |
0e+00 |
|
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: 521.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19158 37 MTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19158 117 DVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19158 197 FHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCL 276
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPY 288
Cdd:cd19158 277 RNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-282 |
3.50e-164 |
|
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: 458.60 E-value: 3.50e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLE 78
Cdd:cd19143 37 MKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19143 117 YVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19143 197 PLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKDR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAIAW 275
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 282
Cdd:cd19143 276 CLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-287 |
1.57e-142 |
|
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: 404.15 E-value: 1.57e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAEtERGLSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19142 37 VTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19142 116 DIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPEL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19142 196 YNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIA 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 287
Cdd:cd19142 276 WSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
4-265 |
2.21e-139 |
|
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: 395.04 E-value: 2.21e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKAE-TERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19074 31 AYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGPGpNDRGLSRKHIFESIHASLKRLQLDYVDI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEvQLPELYH 162
Cdd:cd19074 109 YYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE-EVIPLCE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRN 242
Cdd:cd19074 188 KNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRN 266
|
250 260
....*....|....*....|...
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19074 267 PAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
4-287 |
9.25e-87 |
|
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: 262.04 E-value: 9.25e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:COG0667 42 ALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:COG0667 120 YQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcyqWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:COG0667 197 ELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT----NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLL 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 287
Cdd:COG0667 270 AQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
4-282 |
5.09e-77 |
|
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: 237.09 E-value: 5.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19087 39 ALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:cd19087 116 YQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAAR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwlkERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19087 195 AYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVL 268
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 282
Cdd:cd19087 269 SHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
3-267 |
4.44e-70 |
|
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: 219.41 E-value: 4.44e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19091 47 IALDAGINFFDTADVYSEGESEEILGKALKG---RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYID 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELY 161
Cdd:cd19091 124 LYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19091 203 LDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWL 277
|
250 260
....*....|....*....|....*...
gi 1034635487 240 LRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19091 278 LSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
4-280 |
8.01e-69 |
|
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: 215.47 E-value: 8.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19084 34 AIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAysvarqFNMIPPVCEQAEYHLFQREKVEVQLPeLY 161
Cdd:cd19084 111 LYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLP-YC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19084 184 RENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAW 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19084 257 TLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-269 |
7.09e-67 |
|
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: 210.96 E-value: 7.09e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVITTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19089 38 AFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVISTKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQL 157
Cdd:cd19089 116 DYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19089 194 LEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALS 269
|
250 260 270
....*....|....*....|....*....|..
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 269
Cdd:cd19089 270 WVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
4-263 |
7.71e-66 |
|
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: 205.83 E-value: 7.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd06660 26 ALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSRSRLSPEHIRRDLEESLRRLGTDYIDL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYH 162
Cdd:cd06660 105 YYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgctLPQLAVAWCLRN 242
Cdd:cd06660 185 ENGLPLLAYSPLARG-----------------------------------------------------PAQLALAWLLSQ 211
|
250 260
....*....|....*....|.
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLG 263
Cdd:cd06660 212 PFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
6-280 |
9.05e-65 |
|
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: 205.53 E-value: 9.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 6 ESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLE 78
Cdd:cd19081 37 DAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVVIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19081 115 YIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqwlKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAV 236
Cdd:cd19081 195 PLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA-----AKRYLNERGLRI---LDALDEVAAEHGATPAQVAL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034635487 237 AWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19081 267 AWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
4-267 |
3.39e-63 |
|
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: 201.66 E-value: 3.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19079 44 ALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYH 162
Cdd:cd19079 123 YQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKCYQWLKErivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19079 202 EEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKYDYF---TEADKEIVDRVEE---VAKERGVSMAQVALAWLLS 275
|
250 260
....*....|....*....|....*.
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19079 276 KPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-266 |
7.96e-60 |
|
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: 193.00 E-value: 7.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSLVITTKL--------Y--WGgkaeterglSRKHIIEGLK 69
Cdd:cd19151 39 AFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELIISTKAgytmwpgpYgdWG---------SKKYLIASLD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 70 GSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQ 149
Cdd:cd19151 109 QSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 150 REkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGC 229
Cdd:cd19151 188 RW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQ 262
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034635487 230 TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19151 263 KLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
1-282 |
4.20e-59 |
|
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: 191.62 E-value: 4.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHIIEGL 68
Cdd:cd19094 24 LDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvagpgEGITWPRGGGTRLDRENIREAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 69 KGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVA 130
Cdd:cd19094 103 EGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVKAGKIRHIGLSNETPWGVMKFLELA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 131 RQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLkcYQWLKERIVSE 208
Cdd:cd19094 183 EQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldGAARPEGGRLNL--FPGYMARYRSP 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 209 EGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV-LPKmtsHVVNEIDNI 282
Cdd:cd19094 260 QALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDVpLSD---ELLAEIDAV 328
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
4-283 |
4.36e-59 |
|
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: 190.22 E-value: 4.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:pfam00248 27 ALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWPSGGSKENIRKSLEESLKRLGTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqREKVEVQLPELYHK 163
Cdd:pfam00248 106 YLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEELLEYCKK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQNKLKDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:pfam00248 181 NGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNLEALEALEEIAKEHGVSPAQVALRWALS 250
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 283
Cdd:pfam00248 251 KPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
4-268 |
3.91e-57 |
|
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: 186.12 E-value: 3.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQL 77
Cdd:cd19150 39 AFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELIISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 157
Cdd:cd19150 117 DYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyqwlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLA 235
Cdd:cd19150 196 LDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS-------KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMA 268
|
250 260 270
....*....|....*....|....*....|...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:cd19150 269 LAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
4-268 |
6.12e-53 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 176.33 E-value: 6.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLVITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQL 77
Cdd:PRK09912 52 AFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQL 157
Cdd:PRK09912 130 EYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--KCYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLA 235
Cdd:PRK09912 209 LDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegNKVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMA 285
|
250 260 270
....*....|....*....|....*....|...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:PRK09912 286 LSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
5-267 |
6.33e-52 |
|
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: 172.40 E-value: 6.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWG--GKAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLATKYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYH 162
Cdd:cd19080 118 LYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRN 242
Cdd:cd19080 197 ALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGFGKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQK 271
|
250 260
....*....|....*....|....*
gi 1034635487 243 EGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19080 272 PGVVIPIIGARTLEQLKDNLGALDL 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
4-285 |
2.03e-50 |
|
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: 168.15 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19085 32 ALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS-------PDNLTPEDVRKSCERSLKRLGTDYIDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmipPVCEQAEYHLFQREKVEVQLPEL-YH 162
Cdd:cd19085 102 QIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRAIEYEILPFCrEH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 163 KIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVA 237
Cdd:cd19085 176 GIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFEPGaeEETFEALEKLKEIADELGVTMAQLALA 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 285
Cdd:cd19085 246 WVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
4-282 |
1.78e-42 |
|
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: 147.95 E-value: 1.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19083 42 ALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVVIATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELy 161
Cdd:cd19083 119 LYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQWLKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19083 192 VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDLRNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLALAWY 265
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034635487 240 LRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 282
Cdd:cd19083 266 LTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFIDAL 306
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-283 |
7.34e-42 |
|
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: 146.28 E-value: 7.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19102 35 ALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImeaysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPel 160
Cdd:cd19102 112 LYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM-------KRCQAIHPIASlQPPYSLLRRGIEAEILP-- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 Y---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK-ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLA 235
Cdd:cd19102 183 FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19102 257 IAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
4-283 |
9.40e-42 |
|
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: 145.84 E-value: 9.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW----GGKAETERGLSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19078 34 AVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFkidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPE 159
Cdd:cd19078 111 IDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAVC------PVTAVQSEYSMMWREPEKEVLPT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 160 LyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlkerivSEEGRKQQNKLKDL-SPIAERLGCTLPQLA 235
Cdd:cd19078 185 L-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGATPAQIA 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19078 256 LAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDAL 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
3-264 |
9.79e-42 |
|
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: 145.45 E-value: 9.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLywggkAETERGLSRKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19093 34 AALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-----APLPWRLTRRSVVKALKASLERLGLDSIDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELY 161
Cdd:cd19093 108 YQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQNGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIISGKYG--NGVPESSRASLKCYQWLKERIVseegrkqqnkLKDLSPIAERLGCTLPQLAVAWC 239
Cdd:cd19093 187 DELGITLIAYSPLAQGLLTGKYSpeNPPPGGRRRLFGRKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWL 256
|
250 260
....*....|....*....|....*
gi 1034635487 240 LRNEGVssVLLGSSTPEQLIENLGA 264
Cdd:cd19093 257 IAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
4-279 |
1.86e-40 |
|
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: 142.35 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLE 78
Cdd:cd19076 41 ALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP 158
Cdd:cd19076 116 VIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRASLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 235
Cdd:cd19076 190 tcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPEDD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034635487 236 VAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 279
Cdd:cd19076 262 LAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-267 |
7.68e-40 |
|
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: 141.26 E-value: 7.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LYWGGKAETE----------RGLSRKHIIEGLKG 70
Cdd:cd19149 41 AALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVLATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQ 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 71 SLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQR 150
Cdd:cd19149 118 SLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 151 EKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAER 226
Cdd:cd19149 192 GIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefDAGDARSGIPWFS--------PENREKVLALLEkWKPLCEK 262
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034635487 227 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19149 263 YGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
4-266 |
7.61e-39 |
|
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: 137.36 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19072 35 AIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS-------PDHLKYDDVIKAAKESLKRLGTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHK 163
Cdd:cd19072 106 LIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivseegrkqqnkLKDLSPIAERLGCTLPQLAVAWCLRNE 243
Cdd:cd19072 182 NGIAIIAYSPLEKGKLSNAKG--------------------------------SPLLDEIAKKYGKTPAQIALNWLISKP 229
|
250 260
....*....|....*....|...
gi 1034635487 244 GVsSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19072 230 NV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
4-264 |
5.46e-38 |
|
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: 134.14 E-value: 5.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19086 33 ALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRFDGGPERPQDFSPEYIREAVEASLKRLGTDYID 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIMEAYSVArqfnmippvCEQAEYHLFQREKVEVQL 157
Cdd:cd19086 110 LYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALRRGGID---------VVQVIYNLLDQRPEEELF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 158 PELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkerivseegrkqqnklkdlspiaerlgctLPQLAVA 237
Cdd:cd19086 181 PLA-EEHGVGVIARVPLASGLLTGK------------------------------------------------LAQAALR 211
|
250 260
....*....|....*....|....*..
gi 1034635487 238 WCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19086 212 FILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
5-264 |
9.73e-38 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 134.99 E-value: 9.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-----KAETERgLSRKHIIEGLKGSLQRL 75
Cdd:cd19082 27 VELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhpdleDMSRSR-LSPEDIRADLEESLERL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 76 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFqrEKVEV 155
Cdd:cd19082 102 GTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSLA--RPNEP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLKCYQwlkerivSEEGRKQQNKLKDLspi 223
Cdd:cd19082 180 PWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRRVYY-------SEENFERLERAKEL--- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034635487 224 AERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19082 249 AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
5-282 |
6.80e-37 |
|
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: 133.07 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19075 30 LERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----GLSPENVRKQLETSLKRLKVDKVDVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHK 163
Cdd:cd19075 101 YLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITR-QVETELFPCLRK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEegrkqqnkLKDLSPIAERLGCTLPQL 234
Cdd:cd19075 180 LGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA--------LEKVEEAAEKEGISLAEA 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 235 AVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 282
Cdd:cd19075 252 ALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-264 |
1.33e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 118.97 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK-----LYWGGKAETERGLSRKHIIEGLKGSL 72
Cdd:cd19752 27 VAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgagpRDPDGGPESPEGLSAETIEQEIDKSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 73 QRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQR-- 150
Cdd:cd19752 106 RRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPrp 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 151 ---EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRASLKCYqwlkerivseEGRKQQNKLKDLS 221
Cdd:cd19752 186 gadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPLPEQY----------DGPDSDARLAVLE 246
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034635487 222 PIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19752 247 EVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
6-280 |
1.69e-31 |
|
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: 118.12 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 6 ESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFA 85
Cdd:cd19138 40 DLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL-------PSNASRQGTVRACERSLRRLGTDYLDLYLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 86 NRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMippVCEQAEYHLFQReKVEVQLPELYHKIG 165
Cdd:cd19138 110 HWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC---AANQVLYNLGSR-GIEYDLLPWCREHG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 166 VGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGV 245
Cdd:cd19138 185 VPVMAYSPLAQG---GLLRRGLLENP---------------------------TLKEIAARHGATPAQVALAWVLRDGNV 234
|
250 260 270
....*....|....*....|....*....|....*
gi 1034635487 246 SSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19138 235 IAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
2-258 |
2.48e-30 |
|
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: 115.87 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 2 TI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK--LYWGGKAETERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19148 30 TIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLEWDEGGEVVRNSSPARIRKEVEDSLRRLQT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIMEAY-SVARQFNMIPPvceqaeYHLFQREKVEVQ 156
Cdd:cd19148 109 DYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQMETFrKVAPLHTVQPP------YNLFEREIEKDV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LP-ELYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKCYQwlkerivseEGRKQQ-----NKLKDLSpiA 224
Cdd:cd19148 182 LPyARKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPKFQ---------EPRFSQylaavEELDKLA--Q 245
|
250 260 270
....*....|....*....|....*....|....
gi 1034635487 225 ERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 258
Cdd:cd19148 246 ERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
4-267 |
4.91e-30 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 114.20 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19137 35 AIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW-------PTNLRYDDLLRSLQNSLRRLDTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmiPPVCEQAEYHLFQREKVEVQLPELYHK 163
Cdd:cd19137 106 LIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT----PIVCNQVKYNLEDRDPERDGLLEYCQK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 164 IGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNE 243
Cdd:cd19137 182 NGITVVAYSPLRRGLE---------------------KTNRTLEE--------------IAKNYGKTIAQIALAWLIQKP 226
|
250 260
....*....|....*....|....
gi 1034635487 244 GVSSVLLgSSTPEQLIENLGAIQV 267
Cdd:cd19137 227 NVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
4-264 |
2.09e-29 |
|
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: 111.94 E-value: 2.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19095 29 ALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-GRDRKDFSPAAIRASIERSLRRLGTDYID 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqFNMIppvceQAEYHLFQREKVEVqLPELY 161
Cdd:cd19095 104 LLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-FDVV-----QLPYNVLDREEEEL-LPLAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 -HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrkqqnklkdLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19095 176 eAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR---------------PEFAAEIGGATWAQAALRFVL 229
|
250 260
....*....|....*....|....
gi 1034635487 241 RNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19095 230 SHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
4-272 |
2.82e-29 |
|
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: 112.65 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQL 77
Cdd:cd19092 33 ALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRLGDDPRPGRIKhydTSKEHILASVEGSLKRLGT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNM------IPPVCEQAEYHLFQRE 151
Cdd:cd19092 113 DYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS----------QIELlqsyldQPLVTNQIELSLLHTE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessraslkcyqwlkeRIVSEEGRKQQNKLKDLSPIAERL 227
Cdd:cd19092 183 AIDDgtldYCQLLDITP----MAWSPLGGG--------------------------RLFGGFDERFQRLRAALEELAEEY 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034635487 228 GCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 272
Cdd:cd19092 233 GVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
4-264 |
8.90e-29 |
|
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: 8.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:COG0656 27 ALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDNH------GYDDTLAAFEESLERLGLDYLDLY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREkvevqlPEL--Y 161
Cdd:COG0656 97 LIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ------RELlaF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCL 240
Cdd:COG0656 166 CReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE--------------IAEKHGKTPAQVVLRWHL 210
|
250 260
....*....|....*....|....
gi 1034635487 241 RNeGVsSVLLGSSTPEQLIENLGA 264
Cdd:COG0656 211 QR-GV-VVIPKSVTPERIRENLDA 232
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
4-284 |
1.46e-28 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 111.87 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLVITTKLywGGKAET-------ERGLSRKHIIEGLK 69
Cdd:PRK10625 39 AVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SREKLIIASKV--SGPSRNndkgirpNQALDRKNIREALH 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 70 GSLQRLQLEYVD---VVFANRP-----------DSNTP---MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 132
Cdd:PRK10625 116 DSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavsLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 133 FNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGR 211
Cdd:PRK10625 196 HDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGE 268
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034635487 212 KQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILR 284
Cdd:PRK10625 269 QTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-265 |
9.64e-28 |
|
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: 107.67 E-value: 9.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19105 34 ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 F---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME--IMEA-----YSVArqfnMIPpvceqaeY-HLFQREK 152
Cdd:cd19105 107 QlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNMAevLQAAiesgwFDVI----MVA-------YnFLNQPAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 153 VEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessraslkcyqwlkerivSEEGRKQQNKLKDLSpiaerlgctL 231
Cdd:cd19105 176 LEEALAAAAeKGIGVVAMK--TLAGGY----------------------------LQPALLSVLKAKGFS---------L 216
|
250 260 270
....*....|....*....|....*....|....
gi 1034635487 232 PQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19105 217 PQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
1-280 |
1.16e-27 |
|
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: 108.48 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITTKlywGGKAET--ERGLSRKHIIEGLKGSLQRL 75
Cdd:cd19077 31 MKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSVK---GGLDPDtlRPDGSPEAVRKSIENILRAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 76 -QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVE 154
Cdd:cd19077 108 gGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREIEE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 234
Cdd:cd19077 182 NGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL----DRFNGENFEKNLKLVDALQELAEKKGCTPAQL 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034635487 235 AVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19077 258 ALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
4-266 |
1.75e-27 |
|
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: 107.64 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19090 29 ALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV--GRLPEDTADYSADRVRRSVEESLERLGRDRIDLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQFNMIPPVCeqaEYHLFQREKVEVQLP 158
Cdd:cd19090 103 MIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGDFDVVLTAN---RYTLLDQSAADELLP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrkQQNKLKDLSPIAERLGCTLPQLAVAW 238
Cdd:cd19090 179 AAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE--------LLDRAKRLYELCDEHGVPLPALALRF 242
|
250 260
....*....|....*....|....*...
gi 1034635487 239 CLRNEGVSSVLLGSSTPEQLIENLGAIQ 266
Cdd:cd19090 243 LLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-279 |
1.18e-26 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 105.98 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYV 80
Cdd:cd19145 42 AFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLATKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPEL 160
Cdd:cd19145 119 DLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQWLKeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL 240
Cdd:cd19145 192 CRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSHP-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVL 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034635487 241 -RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 279
Cdd:cd19145 268 hQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
4-287 |
1.27e-26 |
|
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: 106.37 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQRLQLE 78
Cdd:cd19144 43 AFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQ 156
Cdd:cd19144 119 YIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRASLKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQL 234
Cdd:cd19144 193 VLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDDFEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQL 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1034635487 235 AVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKP 287
Cdd:cd19144 267 TLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEEEKEIREIAEEAE 317
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
4-264 |
4.66e-26 |
|
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: 103.45 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW--GGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19088 33 ALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRID 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIppVCEQAEYHLFQREKVEVQlpELY 161
Cdd:cd19088 110 LYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR----I--VSVQNRYNLANRDDEGVL--DYC 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivseegrkqqnklkDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:cd19088 182 EAAGIAFIPWFPLG--------GGDLAQPGG--------------------------LLAEVAARLGATPAQVALAWLLA 227
|
250 260
....*....|....*....|...
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19088 228 RSPVMLPIPGTSSVEHLEENLAA 250
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
4-272 |
1.30e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 102.92 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQL 77
Cdd:COG4989 40 ALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeimeaysvarQFNMI------PPVCEQAEYHLFQRE 151
Cdd:COG4989 120 DYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPS----------QFELLqsaldqPLVTNQIELSLLHTD 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVE------VQLpelyHKIGVgaMTWSPLACGIISGKYgngvpessraslkcyqwlkerivSEEGRKQQNKLKDlspIAE 225
Cdd:COG4989 190 AFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF-----------------------DEQFPRLRAALDE---LAE 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1034635487 226 RLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 272
Cdd:COG4989 238 KYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDI--ELT 282
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
4-264 |
9.99e-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: 95.12 E-value: 9.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWGGKAETER--GLSRKHIIEGLKGSLQR 74
Cdd:cd19162 28 AWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAGRPAGADRrfDFSADGIRRSIEASLER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 75 LQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeimeAYSVARQFN----MIPpvceqAEYH 146
Cdd:cd19162 106 LGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA-----LLRAARRADvdvvMVA-----GRYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 147 LFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQWLKERIVSeegRKQQnklkdLSPIAER 226
Cdd:cd19162 176 LLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRPATPEVLA---RARR-----LAAVCRR 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034635487 227 LGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19162 240 YGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-282 |
1.87e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 95.02 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRSSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19104 41 ALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FA-NRPDSNTP--------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL- 147
Cdd:cd19104 115 QLhNRIGDERDkpvggtlsttdvlgLGGVADAFERLRSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLl 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 148 -----FQREKVEV-----QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnkl 217
Cdd:cd19104 190 npsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA---- 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034635487 218 KDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPkMTSHVVNEIDNI 282
Cdd:cd19104 257 AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
5-283 |
4.14e-22 |
|
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: 94.03 E-value: 4.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL---YWGGKAETER----GLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19146 45 YEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKYttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQT 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKV 153
Cdd:cd19146 124 SYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDIL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 154 EVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLKCYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQ 233
Cdd:cd19146 204 PMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITS 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNIL 283
Cdd:cd19146 268 VALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEIQEIEDAY 315
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
4-262 |
1.99e-20 |
|
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: 87.92 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19071 23 ALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDHGYERVREALEESLKDLGLDYLDLY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 -----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEv 155
Cdd:cd19071 93 lihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELHPYlqQKELVE- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseegrkqqnklKDLSPIAERLGCTLPQL 234
Cdd:cd19071 168 -----FcKEHGIVVQAYSPLGRG-------------RRPLLDD--------------------PVLKEIAKKYGKTPAQV 209
|
250 260
....*....|....*....|....*...
gi 1034635487 235 AVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19071 210 LLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
4-264 |
3.77e-20 |
|
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: 86.94 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19073 23 ALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------LRPEDLKKSVDRSLEKLGTDYVDLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVEVQLPely 161
Cdd:cd19073 93 LIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHpfLYQAELLEYCRE--- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19073 166 NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------------IAEKYDKTPAQVALRWLVQ 208
|
250 260
....*....|....*....|...
gi 1034635487 242 nEGVsSVLLGSSTPEQLIENLGA 264
Cdd:cd19073 209 -KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-270 |
1.84e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 85.66 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19097 35 ALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL---PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSvARQFNMIppvceQAEYHLF-QREKVEVQLPELy 161
Cdd:cd19097 106 LLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFKIDII-----QLPFNILdQRFLKSGLLAKL- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCYQWlkerivseegrkqQNKLKDLSPIAERLGCTLPQLAVAWCLR 241
Cdd:cd19097 179 KKKGIEIHARSVFLQGLL-------LMEPDKLPAKFAPA-------------KPLLKKLHELAKKLGLSPLELALGFVLS 238
|
250 260
....*....|....*....|....*....
gi 1034635487 242 NEGVSSVLLGSSTPEQLIENLGAIQVLPK 270
Cdd:cd19097 239 LPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
4-264 |
1.11e-18 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 83.38 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkaeteRGLSRKHIIEGLKGSLQRLQLEYVDvV 83
Cdd:cd19096 30 AIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW------SVKSAEDFRRILEESLKRLGVDYID-F 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FA----NRPD------SNTPMEEIVRAMT-----HVinqGMamywgTSRWSA---MEIMEAYsvarQFNMIppvceQAEY 145
Cdd:cd19096 101 YLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDSPellKEILDSY----DFDFV-----QLQY 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 146 HLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessraslkcyqwlkerivseegrkqqNKLKDLSPIA 224
Cdd:cd19096 164 NYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA----------------------------------NNPPEALAIL 209
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034635487 225 ERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19096 210 CGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
4-262 |
1.11e-18 |
|
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: 83.08 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19140 30 ALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-------YSPDDFLASVEESLRKLRTDYVDLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQRekvevQLPELY 161
Cdd:cd19140 100 LLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHpyLDQR-----KLLDAA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19140 171 REHGIALTAYSPLARG---------------------EVLKDPVLQE--------------IGRKHGKTPAQVALRWLLQ 215
|
250 260
....*....|....*....|.
gi 1034635487 242 NEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19140 216 QEGV-AAIPKATNPERLEENL 235
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
4-265 |
4.46e-17 |
|
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: 79.52 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19163 42 ALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYID 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VV------FAnrPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMeAYSVARQFNMIPPVCEQAEYHLFQREKVEv 155
Cdd:cd19163 119 IIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIGITGYP-LDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASlkcyQWLKERIvseegrkqqnklKDLSPIAERLGCTLPQLA 235
Cdd:cd19163 194 -LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPAS----PEIKEAC------------AKAAAYCKSRGVDISKLA 253
|
250 260 270
....*....|....*....|....*....|
gi 1034635487 236 VAWCLRNEGVSSVLLGSSTPEQLIENLGAI 265
Cdd:cd19163 254 LQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
4-262 |
1.59e-16 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 78.71 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKaeterglSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:COG1453 38 AIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FanrpdsntpmeeIvramtHVINQGMAMYWGTSRWSAMEIMEAysvARQ----------FNMIPPVCEQA-E-------- 144
Cdd:COG1453 106 L------------I-----HGLNTEEDLEKVLKPGGALEALEK---AKAegkirhigfsTHGSLEVIKEAiDtgdfdfvq 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 145 ---YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnKLKDLS 221
Cdd:COG1453 166 lqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG--------------------------------------RLANPP 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1034635487 222 PIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 262
Cdd:COG1453 208 EKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
1-262 |
3.05e-16 |
|
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: 77.07 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYWGGkaetergLSRKHIIEGLKGSLQR 74
Cdd:cd19154 31 VRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITTKLWTHE-------HAPEDVEEALRESLKK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 75 LQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnm 135
Cdd:cd19154 99 LQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR---- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 IPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCYQWlkerivseegrKQQN 215
Cdd:cd19154 175 VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------GSPGRANFTKSTGVS-----------PAPN 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034635487 216 KLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19154 230 LLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
1-288 |
4.68e-16 |
|
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: 76.12 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterglsrkHIIEGLKGSLQRLQLEYV 80
Cdd:cd19120 31 VKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK----------DPREALRKSLAKLGVDYV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 DVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFqrekVEVQ 156
Cdd:cd19120 98 DLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPY----LYPQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRKQQNKLKDlspIAERLGCTLPQL 234
Cdd:cd19120 170 QPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGPLDPVLEK---IAEKYGVTPAQV 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 235 AVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 288
Cdd:cd19120 220 LLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-262 |
5.02e-16 |
|
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: 76.97 E-value: 5.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywGG----------------KAETERGLSRKH 63
Cdd:cd19099 30 ALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---AGyipgdgdeplrplkylEEKLGRGLIDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 64 IIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 120
Cdd:cd19099 107 DSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFYDRLEEAFEALEEAVAEGKIRYYGISTWDG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 121 meiMEAYSVARQFNMIPPVCE---------------QAEYHLFQREKVEVQ---------LPELYHKIGVGAMTWSPLAc 176
Cdd:cd19099 187 ---FRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEKntvkgealsLLEAAKELGLGVIASRPLN- 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 177 giiSGKYGNGVPESSRAslkcyqwlkerivseegrkqqnklkdlspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPE 256
Cdd:cd19099 263 ---QGQLLGELRLADLL------------------------------ALPGGATLAQRALQFARSTPGVDSALVGMRRPE 309
|
....*.
gi 1034635487 257 QLIENL 262
Cdd:cd19099 310 HVDENL 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-240 |
7.29e-16 |
|
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: 76.22 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGGkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19103 41 AMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI-----AGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPEL 160
Cdd:cd19103 114 WIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIVSEEGRKQQnkLKDLSP----IAERLGCTLPQL 234
Cdd:cd19103 187 CKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAETYNPLLPQ--LEELTAvmaeIGAKHGASIAQV 253
|
....*.
gi 1034635487 235 AVAWCL 240
Cdd:cd19103 254 AIAWAI 259
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
4-267 |
2.46e-15 |
|
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: 74.57 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETERGLSRKHIIEGLKG------------- 70
Cdd:cd19152 29 AWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQEVEPTFEPGFWNPLPfdavfdysydgil 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 71 -----SLQRLQLEYVDVVFANRPDSNTP-----------MEEIVRAMTHVINQGMAMYW--GTSRWS-AMEIME-----A 126
Cdd:cd19152 107 rsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREEGVIKAIglGVNDWEvILRILEeadldW 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 127 YSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgIISGKYGNGVpessRASLKCYQWLKERIV 206
Cdd:cd19152 187 VMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VNAGPFNSGF----LAGGDNFDYYEYGPA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635487 207 SEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19152 241 PPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
5-264 |
2.85e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 74.55 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYWGGKAETergLSRKHIIEGLKGSLQRLQLEYVD 81
Cdd:cd19101 33 VDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVPDPGELT---MTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 82 VV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEIMEAysvarqfnMIPPVCEQAEYHLFQReKVEV 155
Cdd:cd19101 108 LVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EILDA--------GVPIVSNQVQYSLLDR-RPEN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCYQwlkeRIVSEEG--RKQQNKLKDLSPIAERLG 228
Cdd:cd19101 177 GMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKYK----LMIDEWGgwDLFQELLRTLKAIADKHG 251
|
250 260 270
....*....|....*....|....*....|....*.
gi 1034635487 229 CTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 264
Cdd:cd19101 252 VSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-268 |
2.94e-15 |
|
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: 74.49 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19153 42 AFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWsAMEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPE 159
Cdd:cd19153 120 YLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 160 LYHKIGVGAMTWSPLACGIISGKygnGVPE----------SSRASLKcyqWLKERIVSeegrkqqnklkdlspiaerlgc 229
Cdd:cd19153 197 LVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgelrhYAAAADA---VCASVEAS---------------------- 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034635487 230 tLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQVL 268
Cdd:cd19153 249 -LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAV 287
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
3-288 |
7.32e-15 |
|
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: 73.21 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYV 80
Cdd:cd19123 33 QALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE------DVLPALEKTLADLQLDYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 81 D-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 142
Cdd:cd19123 105 DlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 143 AEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQWLKERIVSEegrkqqnklkdlsp 222
Cdd:cd19123 181 VELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPVLLEDPVINK-------------- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034635487 223 IAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 288
Cdd:cd19123 235 IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMATIAALDRHHRY 296
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
4-262 |
2.97e-14 |
|
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: 71.07 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19133 32 AIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQDAGYEK------AKKAFERSLKRLGLDYLDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAYSvarqFNMIPPVCEQAEYHLFQREKVEVqlp 158
Cdd:cd19133 102 LIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLIL----HNEVKPAVNQIETHPFNQQIEAV--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQ--QNKLkdLSPIAERLGCTLPQLAV 236
Cdd:cd19133 168 EFLKKYGVQIEAWGPFA---------------------------------EGRNNlfENPV--LTEIAEKYGKSVAQVIL 212
|
250 260
....*....|....*....|....*.
gi 1034635487 237 AWcLRNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19133 213 RW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
4-283 |
3.38e-14 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 71.35 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PLN02587 40 AFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDIL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaMEIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEV 155
Cdd:PLN02587 117 HCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP-LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 qLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASLKcyqwLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQ 233
Cdd:PLN02587 191 -LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE----LKSacAAAATHCKEK--------------GKNISK 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--MTSHVVNEIDNIL 283
Cdd:PLN02587 248 LALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgIDEELLSEVEAIL 299
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
3-262 |
2.20e-13 |
|
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: 68.70 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLE 78
Cdd:cd19128 22 NAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQPEN------VKEQLLITLQDLQLE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19128 92 YLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCK----IKPF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRASLKCyqwlkerivseegrkqqnklK 218
Cdd:cd19128 168 MNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTFLND--------------------S 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034635487 219 DLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 262
Cdd:cd19128 215 ELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
4-262 |
5.47e-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: 67.40 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 83
Cdd:cd19131 32 ALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL------RAFDESLRKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvev 155
Cdd:cd19131 102 LIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-------PVVNQIELHpRFQQR---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 156 QLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLA 235
Cdd:cd19131 168 ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--------------IAEKHGKTPAQVV 212
|
250 260
....*....|....*....|....*..
gi 1034635487 236 VAWCLRNEGVssVLLGSSTPEQLIENL 262
Cdd:cd19131 213 IRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
6-261 |
5.57e-13 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 67.35 E-value: 5.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 6 ESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVVFA 85
Cdd:cd19135 37 ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSDYGYES------TKQAFEASLKRLGVDYLDLYLL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 86 NRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEaysvARQFNMIPPVCEQAEYHLFQREKvevQLP 158
Cdd:cd19135 107 HWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ----LLEDCSVVPHVNQVEFHPFQNPV---ELI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 159 ELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAW 238
Cdd:cd19135 180 EYCRDNNIVFEGYCPLAKG---------------------KALEEPTVTE--------------LAKKYQKTPAQILIRW 224
|
250 260
....*....|....*....|...
gi 1034635487 239 CLRNEGVssVLLGSSTPEQLIEN 261
Cdd:cd19135 225 SIQNGVV--TIPKSTKEERIKEN 245
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
4-262 |
9.26e-13 |
|
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: 66.91 E-value: 9.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLE 78
Cdd:cd19124 29 AIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL-WCSDAH------PDLVLPALKKSLRNLQLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQ 142
Cdd:cd19124 99 YVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 143 AEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPESsraslkcyQWLKErivseegrkqqnklkdl 220
Cdd:cd19124 175 VEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVMES--------DVLKE----------------- 223
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034635487 221 spIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19124 224 --IAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
4-285 |
1.71e-12 |
|
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: 66.15 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEterglsRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19116 34 AIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE------REQVEPALRESLKRLGLDY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQA 143
Cdd:cd19116 104 VDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN----IKPAVNQI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 144 EYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLkcyqwlkerivsEEGRKQQNKLKDlsp 222
Cdd:cd19116 180 EVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRGQTN------------PPPRLDDPTLVA--- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 223 IAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 285
Cdd:cd19116 230 IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKEN---IDIFDfQLTPEEVAALNSFNTN 288
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
4-288 |
1.93e-12 |
|
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: 65.98 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKLYwggkaetERGLSRKHIIEGLKGSLQRLQL 77
Cdd:cd19111 26 ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKLP-------PVYLEFKDTEKSLEKSLENLKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAE 144
Cdd:cd19111 94 PYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK----VKPSNLQLE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 145 YHLF--QREKVEVQLPelyHKIGVGAmtWSPLacgiisgkygnGVPesSRASLkcYQWLKERIVSEEgrkqQNKLKdlsp 222
Cdd:cd19111 170 CHAYlqQRELRKFCNK---KNIVVTA--YAPL-----------GSP--GRANQ--SLWPDQPDLLED----PTVLA---- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034635487 223 IAERLGCTLPQLAVAWCL-RNEGvssVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRNKPY 288
Cdd:cd19111 222 IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--ELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
4-270 |
3.83e-12 |
|
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: 65.42 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK----AETERGL-----------------SRK 62
Cdd:cd19161 29 AWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRllkpAREGSVPdpngfvdplpfeivydySYD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 63 HIIEGLKGSLQRLQLEYVDVVF---------ANRPDSN---TPMEEIVRAMTHVINQGM--AMYWGTSRWSAM-EIMEAY 127
Cdd:cd19161 104 GIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKALEELKKAGVikAFGLGVNEVQIClEALDEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 128 SVarQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgIISGKYGNGVPESSRASLKCYQWlkeRIVS 207
Cdd:cd19161 184 DL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------VIGGVFNSGILATGTKSGAKFNY---GDAP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034635487 208 EEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ-VLPK 270
Cdd:cd19161 244 AE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQtDIPE 304
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
4-267 |
7.19e-12 |
|
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: 63.91 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19139 23 ALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNLSKDKLLPSLEESLEKLRTDYVDLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYhlFQREKVEVQLPEly 161
Cdd:cd19139 93 LIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAmtWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQQNKLkdLSPIAERLGCTLPQLAVAWCLr 241
Cdd:cd19139 169 HGIHVTS--YMTLA---------------------------------YGKVLDDPV--LAAIAERHGATPAQIALAWAM- 210
|
250 260
....*....|....*....|....*.
gi 1034635487 242 NEGVsSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19139 211 ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
13-262 |
1.16e-11 |
|
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: 63.90 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 13 DTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FA 85
Cdd:cd19125 42 DCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-WCTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 86 NRPDSNTP---------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQ 156
Cdd:cd19125 114 LKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---K 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAV 236
Cdd:cd19125 187 LHEFCKSKGIHLSAYSPL-----------GSPGTTWVKKNV---LKDPIVTK--------------VAEKLGKTPAQVAL 238
|
250 260
....*....|....*....|....*.
gi 1034635487 237 AWCLRnEGvSSVLLGSSTPEQLIENL 262
Cdd:cd19125 239 RWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
4-262 |
7.34e-11 |
|
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: 61.11 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGKAETErglsrkhiiEGLKGSLQRLQL 77
Cdd:cd19136 24 ALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGYEKAR---------AACLGSLERLGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SAMEIMEAYSvarqfnMIPPVCEQAEY 145
Cdd:cd19136 92 DYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRHLEELLKYC------EVPPAVNQVEF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 146 H--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCYQWLKERIVSEegrkqqnklkdlspI 223
Cdd:cd19136 166 HphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DLRLLEDPTVLA--------------I 207
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034635487 224 AERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 262
Cdd:cd19136 208 AKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
4-262 |
9.75e-11 |
|
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: 61.03 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkAETERGLSRKhiIEGLKGSLQRLQLEYVDVV 83
Cdd:cd19134 33 ALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGFTAS--QAACRASLERLGLDYVDLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPPVCEQAEYH--LFQREkvevqLPEL 160
Cdd:cd19134 103 LIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTPAVNQIELHplLNQAE-----LRKV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 161 YHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnklkdlspIAERLGCTLPQLAVAWCL 240
Cdd:cd19134 174 NAQHGIVTQAYSPLGVGRLLDN-----PAVTA------------------------------IAAAHGRTPAQVLLRWSL 218
|
250 260
....*....|....*....|..
gi 1034635487 241 RNEGVssVLLGSSTPEQLIENL 262
Cdd:cd19134 219 QLGNV--VISRSSNPERIASNL 238
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
2-84 |
1.11e-10 |
|
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: 61.14 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 2 TIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITTKLywGGKAETERGLSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19164 41 RRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIITKV--GRYGPDDFDYSPEWIRASVERSLRRLHTDY 116
|
....*
gi 1034635487 80 VDVVF 84
Cdd:cd19164 117 LDLVY 121
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
4-184 |
1.13e-10 |
|
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: 60.53 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQLEYVDVV 83
Cdd:cd19126 32 ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQRARRTED------AFQESLDRLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEVQLPElyH 162
Cdd:cd19126 102 LIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRGYCKS--K 174
|
170 180 190
....*....|....*....|....*....|.
gi 1034635487 163 KIGVGAmtWSPLACGI---------ISGKYG 184
Cdd:cd19126 175 GIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
4-264 |
1.25e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 60.81 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgLSRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PRK11172 25 ALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-LAKDKLIPSLKESLQKLRTDYVDLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS------AMEIMEAYSVARQfnmippvceQAEYH-LFQREKVE 154
Cdd:PRK11172 95 LIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIATN---------QIELSpYLQNRKVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPElyHKIGVGA-MTwspLAcgiisgkYGngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQ 233
Cdd:PRK11172 166 AFAKE--HGIHVTSyMT---LA-------YG--------------KVLKDPVIAR--------------IAAKHNATPAQ 205
|
250 260 270
....*....|....*....|....*....|.
gi 1034635487 234 LAVAWCLRnEGvSSVLLGSSTPEQLIENLGA 264
Cdd:PRK11172 206 VILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-262 |
1.51e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 60.19 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTKLYWGGKAETERGLSRkhiieglkgSLQRLQLEYVDVV 83
Cdd:cd19100 36 ALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKTGARDYEGAKRDLER---------SLKRLGTDYIDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 F----ANRPDSNTPMEE--IVRAMTHVINQGMAMYWGTS--RWSAM-EIMEAYsvarQFNMIPPVCEQAEYHlfQREKVE 154
Cdd:cd19100 102 QlhavDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISghSPEVLlRALETG----EFDVVLFPINPAGDH--IDSFRE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 155 VQLPELY-HKIGVGAMtwSPLACGiisgkygngvpessraslkcyQWLKERIVSeegrkqqnklkdlspiaerlgctlPQ 233
Cdd:cd19100 176 ELLPLAReKGVGVIAM--KVLAGG---------------------RLLSGDPLD------------------------PE 208
|
250 260
....*....|....*....|....*....
gi 1034635487 234 LAVAWCLRNEGVSSVLLGSSTPEQLIENL 262
Cdd:cd19100 209 QALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
5-280 |
3.16e-10 |
|
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: 59.84 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 5 YESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLYW--------GGKAETERGLSRKHIIEGLKGSLQRLQ 76
Cdd:cd19147 44 YEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKFTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 77 LEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQ 156
Cdd:cd19147 123 TDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 157 LPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwLKERIVSEEGRK------QQNKL-----KDLSPIAE 225
Cdd:cd19147 203 IPMARH-FGMALAPWDVL---------GGGKFQSKKA-------VEERKKNGEGLRsfvggtEQTPEevkisEALEKVAE 265
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034635487 226 RLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 280
Cdd:cd19147 266 EHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEIEYLE 319
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
4-279 |
4.16e-10 |
|
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: 59.39 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEY 79
Cdd:cd19129 28 ALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER------VKPAFEASLKRLQLDY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19129 98 LDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR----IKPA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLACGIisgkygngvpessraslkcyqwlkerivseegrkQQNKLKD 219
Cdd:cd19129 174 VVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGM----------------------------------EPKLLED 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 220 --LSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGaIQVLPKMTSHVVNEI 279
Cdd:cd19129 217 pvITAIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
2-262 |
4.42e-10 |
|
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: 58.96 E-value: 4.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 2 TIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--GKAETERGLSRkhiieglkgSLQRLQLEY 79
Cdd:cd19127 29 ATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyGYDKALRGFDA---------SLRRLGLDY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVarqfnmIPPVcEQAEYHLFQRE 151
Cdd:cd19127 97 VDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERLIDATTV------VPAV-NQVELHPYFSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlkerivseegrkqqnklkdLSPIAERLGCTL 231
Cdd:cd19127 167 K---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT--------------------ITGLAEKYGKTP 220
|
250 260 270
....*....|....*....|....*....|.
gi 1034635487 232 PQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 262
Cdd:cd19127 221 AQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
4-262 |
6.22e-10 |
|
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: 59.08 E-value: 6.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKLYWGGkaeterglSRKHIIEG-LKGSLQRLQ 76
Cdd:cd19155 34 ALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKLPPGG--------NRREKVEKfLLKSLEKLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 77 LEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnm 135
Cdd:cd19155 101 LDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 IPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYGNGVPESSRASLkcyqwLKERIVSEegrkqq 214
Cdd:cd19155 177 IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPGTGSPSGSSPDL-----LQDPVVKA------ 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034635487 215 nklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19155 243 --------IAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
4-262 |
2.21e-09 |
|
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: 57.50 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLYwggkaETERGlsrkHIIEGLKGSLQRLQLEY 79
Cdd:cd19112 33 AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW-----NSDHG----HVIEACKDSLKKLQLDY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVVFANRP-----------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA--MEIMEAYSvarqfn 134
Cdd:cd19112 101 LDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIflTRDCLAYS------ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 135 MIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGIISGKYGNGVpessraslkcyqwlkerivseegrkq 213
Cdd:cd19112 175 KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWFGSV-------------------------- 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 214 qNKLKD--LSPIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENL 262
Cdd:cd19112 225 -SPLDDpvLKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
1-262 |
2.82e-09 |
|
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: 56.51 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 1 MTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggkaeteRGlsRKH----IIEGLKGSLQRLQ 76
Cdd:cd19132 26 VVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL---------PG--RHHgyeeALRTIEESLYRLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 77 LEYVDVVFANRPD-SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM---EIMEAYSVArqfnmipPVCEQAEYH-LFQRE 151
Cdd:cd19132 92 LDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLIDETGVT-------PAVNQIELHpYFPQA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 152 KVEVqlpelYHK-IGVGAMTWSPLacgiisGKyGNGVpessraslkcyqwLKERIVSEegrkqqnklkdlspIAERLGCT 230
Cdd:cd19132 165 EQRA-----YHReHGIVTQSWSPL------GR-GSGL-------------LDEPVIKA--------------IAEKHGKT 205
|
250 260 270
....*....|....*....|....*....|..
gi 1034635487 231 LPQLAVAWCLRnEGVsSVLLGSSTPEQLIENL 262
Cdd:cd19132 206 PAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
4-187 |
3.06e-09 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 56.62 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaeterglsRKHIIEGLKGSLQRLQLEYVDVV 83
Cdd:PRK11565 37 ALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD--------HKRPREALEESLKKLQLDYVDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH-LFQREkvEVQ 156
Cdd:PRK11565 105 LMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT-------PVINQIELHpLMQQR--QLH 173
|
170 180 190
....*....|....*....|....*....|.
gi 1034635487 157 LPELYHKIGVGAmtWSPLACGiisgkyGNGV 187
Cdd:PRK11565 174 AWNATHKIQTES--WSPLAQG------GKGV 196
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
4-184 |
6.41e-09 |
|
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: 55.60 E-value: 6.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLSrkhiieGLKGSLQRLQLEYVDVV 83
Cdd:cd19156 32 AIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSDQGYESTLA------AFEESLEKLGLDYVDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKVEVQLPElyH 162
Cdd:cd19156 102 LIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--K 174
|
170 180 190
....*....|....*....|....*....|.
gi 1034635487 163 KIGVGAmtWSPLACG---------IISGKYG 184
Cdd:cd19156 175 NIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
37-267 |
2.26e-08 |
|
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: 54.17 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 37 RRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV------VFANRPDSNTPM---------------- 94
Cdd:cd19122 68 KREDLFICTKV-WNHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdlten 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 95 -EEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSP 173
Cdd:cd19122 141 pEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 174 LACGiisgkygNGVPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSS 253
Cdd:cd19122 214 LGSQ-------NQVPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSS 264
|
250
....*....|....
gi 1034635487 254 TPEQLIENLGAIQV 267
Cdd:cd19122 265 TPSRIESNFKSIEL 278
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
4-285 |
8.89e-08 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 52.39 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAaGKAEVilGSIIKK-----KGWRRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQLE 78
Cdd:cd19106 29 ALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL-WNTKHHPE------DVEPALRKTLKDLQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 139
Cdd:cd19106 99 YLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 140 CEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVPEssRAslkcyqWLK--ERIVSEEGRkqqnkl 217
Cdd:cd19106 175 VLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSPD--RP------WAKpdEPVLLEEPK------ 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635487 218 kdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVNEIDNILRN 285
Cdd:cd19106 227 --VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQVFDfTLSPEEMKQLDALNRN 288
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
4-263 |
1.85e-07 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 51.24 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGLsrkhiiEGLKGSLQRLQLEYVDVV 83
Cdd:cd19157 33 ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQGYDSTL------KAFEASLERLGLDYLDLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 84 FANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREkvevqLPELY 161
Cdd:cd19157 103 LIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 162 HKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLR 241
Cdd:cd19157 173 KKQGIQLEAWSPLMQG---------------------QLLDNPVLKE--------------IAEKYNKSVAQVILRWDLQ 217
|
250 260
....*....|....*....|..
gi 1034635487 242 NEGVssVLLGSSTPEQLIENLG 263
Cdd:cd19157 218 NGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
3-282 |
8.35e-07 |
|
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: 49.42 E-value: 8.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgkaeTERglsrKHIIEGLKGSLQRLQLEYVDV 82
Cdd:cd19117 35 AALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC----TWH----RRVEEALDQSLKKLGLDYVDL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 83 VFANRP-------DSNTPMEEIVRA--------------MTHVINQGMAMYWGTSRWSAMEIMEAysVARQFNMIPPVCE 141
Cdd:cd19117 103 YLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVKAIGVSNFSIKNLEKL--LASPSAKIVPAVN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 142 QAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpeSSRASLkcyqwLKERIVSEegrkqqnklkdls 221
Cdd:cd19117 181 QIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------STNAPL-----LKEPVIIK------------- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034635487 222 pIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGAIQvlpkMTSHVVNEIDNI 282
Cdd:cd19117 226 -IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----LSDEEFKEIDEL 279
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
4-282 |
1.17e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.81 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 72
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 73 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 146
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 147 LFQREkvEVQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwlkerivseegrkqqnklkdLSPIAER 226
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPL---------GGFTPLQSST--------------------------LSDVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034635487 227 LGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 282
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
4-267 |
2.05e-06 |
|
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: 48.49 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHIIEGLKGSLQ 73
Cdd:cd19098 44 AWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLKQWEETRS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 74 RLQlEYVDV-----------VFANrpdsntpmEEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYSVARQFNm 135
Cdd:cd19098 120 LLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EIDGARLFD- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 136 ippvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSEEGRKqqn 215
Cdd:cd19098 188 ----SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSPELAP--- 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034635487 216 KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 267
Cdd:cd19098 237 LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
4-154 |
3.73e-05 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 44.33 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYA----AGK--AEVILGSIIKkkgwrRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRLQL 77
Cdd:cd19115 35 AIKAGYRLFDGACDYGneveAGQgvARAIKEGIVK-----REDLFIVSKL-WNTFHDGE------RVEPICRKQLADWGI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 78 EYVDVVFANRP------------------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 133
Cdd:cd19115 103 DYFDLFLIHFPialkyvdpavryppgwfydgkkveFSNAPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMDLLRYAR-- 180
|
170 180
....*....|....*....|...
gi 1034635487 134 nmIPPVCEQAEYH--LFQREKVE 154
Cdd:cd19115 181 --IRPATLQIEHHpyLTQPRLVK 201
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
3-148 |
1.04e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 42.99 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 3 IAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAETErgLSRKhiieGLKGSLQRLQLE 78
Cdd:cd19108 35 LAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRPE--LVRP----ALEKSLKKLQLD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 79 YVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------IMEAYSVA----RQFNMI---P----- 137
Cdd:cd19108 105 YVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdagLAKSIGVSnfnrRQLEMIlnkPglkyk 180
|
170
....*....|.
gi 1034635487 138 PVCEQAEYHLF 148
Cdd:cd19108 181 PVCNQVECHPY 191
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
4-152 |
1.20e-03 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 39.85 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 4 AYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyWGGKAeterglSRKHIIEGLKGSLQRLQLEY 79
Cdd:cd19114 26 AIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-WNNFH------GKDHVREAFDRQLKDYGLDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034635487 80 VDVVFANRPDS-------------------------NTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 134
Cdd:cd19114 96 IDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYAK--- 172
|
170
....*....|....*....
gi 1034635487 135 mIPPVCEQAEYHLF-QREK 152
Cdd:cd19114 173 -IKPAVLQIEHHPYlQQKR 190
|
|
| |
