|
Name |
Accession |
Description |
Interval |
E-value |
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
38-363 |
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: 668.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 38 FYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITT 117
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 118 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGM 197
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME----------------EIVRAFTHVINQGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 277
Cdd:cd19141 145 AMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 278 YSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLP 357
Cdd:cd19141 225 YSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLP 304
|
....*.
gi 1907154428 358 KLSSSI 363
Cdd:cd19141 305 KLTPNI 310
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
37-376 |
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: 652.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 37 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 116
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 117 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQG 196
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPME----------------ETVRAMTHVINQG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 197 MAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP 276
Cdd:cd19158 145 MAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 277 PYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 356
Cdd:cd19158 225 PYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 304
|
330 340
....*....|....*....|
gi 1907154428 357 PKLSSSIVHEIDSILGNKPY 376
Cdd:cd19158 305 PKLSSSIVHEIDSILGNKPY 324
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
39-375 |
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: 644.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19159 3 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGMA 198
Cdd:cd19159 83 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPME----------------EIVRAMTHVINQGMA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 278
Cdd:cd19159 147 MYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPES 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 279 SRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPK 358
Cdd:cd19159 227 SRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK 306
|
330
....*....|....*..
gi 1907154428 359 LSSSIVHEIDSILGNKP 375
Cdd:cd19159 307 MTSHVVNEIDNILRNKP 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
39-371 |
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: 633.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGMA 198
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME----------------ETVRAMTYVINQGMA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 278
Cdd:TIGR01293 145 MYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPY 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 279 SRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPK 358
Cdd:TIGR01293 225 SRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPK 304
|
330
....*....|...
gi 1907154428 359 LSSSIVHEIDSIL 371
Cdd:TIGR01293 305 LSSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
39-375 |
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: 624.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19160 5 YRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGMA 198
Cdd:cd19160 85 IYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPME----------------EIVRAMTYVINQGMA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 278
Cdd:cd19160 149 MYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 279 SRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPK 358
Cdd:cd19160 229 CRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQ 308
|
330
....*....|....*..
gi 1907154428 359 LSSSIVHEIDSILGNKP 375
Cdd:cd19160 309 LTPQTVMEIDALLGNKP 325
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
39-370 |
0e+00 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 513.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19143 3 YRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQG 196
Cdd:cd19143 83 IFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATP----------------IEETVRAMNDLIDQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 197 MAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP 276
Cdd:cd19143 147 KAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIP 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 277 PYSRASLKGYQWLKDkILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 356
Cdd:cd19143 227 EGSRLALPGYEWLKD-RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVL 305
|
330
....*....|....
gi 1907154428 357 PKLSSSIVHEIDSI 370
Cdd:cd19143 306 PKLTPEVMEKIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
46-363 |
5.39e-165 |
|
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: 463.60 E-value: 5.39e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFWGGKA 125
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 E-TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLE----------------ETVRAMDDLIRQGKILYWGTS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLK 284
Cdd:cd19074 143 EWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 285 gYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAiqVLPKLSSSI 363
Cdd:cd19074 222 -DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
39-375 |
5.61e-165 |
|
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: 464.63 E-value: 5.61e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19142 3 YRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAEtERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGMA 198
Cdd:cd19142 83 IYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPME----------------EVVRAMSYLIDNGLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 278
Cdd:cd19142 146 MYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 279 SRASLKGY-----QWLKDKIlsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 353
Cdd:cd19142 226 TKLSFKSSkykvgSDGNGIH--EETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSL 303
|
330 340
....*....|....*....|..
gi 1907154428 354 QVLPKLSSSIVHEIDSILGNKP 375
Cdd:cd19142 304 QLLPKLNSAVMEELERILDNKP 325
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
39-375 |
7.74e-100 |
|
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: 298.63 E-value: 7.74e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWvTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVI 115
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 116 TTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVIN 194
Cdd:COG0667 80 ATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTP----------------IEETLGALDELVR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWSSMEIMEAYSVARqfNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG 274
Cdd:COG0667 144 EGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 275 --IPPYSRASLKGYQWlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:COG0667 221 atFPEGDRAATNFVQG-------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAA 293
|
330 340
....*....|....*....|...
gi 1907154428 353 IQVlpKLSSSIVHEIDSILGNKP 375
Cdd:COG0667 294 ADL--ELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
39-370 |
1.20e-88 |
|
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: 269.83 E-value: 1.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK 118
Cdd:cd19087 3 YRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWG-GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHVINQGM 197
Cdd:cd19087 79 VFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLE----------------ETLRALDDLVRQGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 277
Cdd:cd19087 143 IRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 278 --YSRASLKGYQwlkDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 355
Cdd:cd19087 222 esGRLVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI 295
|
330
....*....|....*
gi 1907154428 356 lpKLSSSIVHEIDSI 370
Cdd:cd19087 296 --TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
39-370 |
4.08e-80 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 248.30 E-value: 4.08e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTwVTFG---------GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwR 109
Cdd:cd19091 3 YRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 110 RSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRA 188
Cdd:cd19091 79 RDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTP----------------LEETLRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 189 MTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVS 268
Cdd:cd19091 143 LDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 269 GKY--DSGIPPYSRASLKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQL 346
Cdd:cd19091 222 GKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQL 296
|
330 340
....*....|....*....|....
gi 1907154428 347 MENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19091 297 EDNLGAAGL--SLTPEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
39-357 |
8.37e-80 |
|
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: 247.17 E-value: 8.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVY--AAGKAEVVLGNIIKK-KGWRRSSLVI 115
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 116 TTKI---FWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHV 192
Cdd:cd19089 81 STKAgygMWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLE----------------ETMTALADA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYD 272
Cdd:cd19089 143 VRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 273 SGIPPYSRAsLKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19089 221 NGIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAA 296
|
....*
gi 1907154428 353 IQVLP 357
Cdd:cd19089 297 LKNLD 301
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
46-368 |
2.04e-75 |
|
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: 235.50 E-value: 2.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWV---TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IF 120
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 121 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMY 200
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTP----------------IEETAEALEKLKKEGKIRY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 201 WGTSRWSSMEIMEAysvarqFNLIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSG--IPPY 278
Cdd:cd19084 142 IGVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLPYC-RENGIGVLPYGPLAQGLLTGKYKKEptFPPD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 279 -SRASLKGYQwlkdkilSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlp 357
Cdd:cd19084 215 dRRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW-- 285
|
330
....*....|.
gi 1907154428 358 KLSSSIVHEID 368
Cdd:cd19084 286 ELTEEELKEID 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-368 |
2.13e-72 |
|
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: 228.25 E-value: 2.13e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 42 LGKSGLRVSCLGLGTWVtFGGQItDEMAEHLMTLAY-DNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSL 113
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTA-DEETSFALLDAFvDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 114 VITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVI 193
Cdd:cd19081 79 VIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATP----------------LEETLGALNDLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS 273
Cdd:cd19081 142 RQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRS 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 274 GIPPySRASLKGYQWlkDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 353
Cdd:cd19081 222 EADL-PGSTRRGEAA--KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAA 295
|
330
....*....|....*
gi 1907154428 354 QVlpKLSSSIVHEID 368
Cdd:cd19081 296 GL--RLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
50-351 |
4.69e-72 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 224.71 E-value: 4.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTWvTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI-FWGGKAETE 128
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 129 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWSS 208
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTP----------------VEETLEALNELVREGKIRYIGVSNWSA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 209 MEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqw 288
Cdd:cd06660 143 ERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG----------------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 289 lkdkilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIG 351
Cdd:cd06660 200 ------------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
39-354 |
2.12e-70 |
|
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: 223.05 E-value: 2.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKK--KGWRrSSLV 114
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 115 ITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTH 191
Cdd:cd19151 81 ISTKagyTMWPGPY-GDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETP----------------LEETMGALDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 192 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKY 271
Cdd:cd19151 143 IVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 DSGIPPYSRASlKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIG 351
Cdd:cd19151 221 LNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVG 296
|
...
gi 1907154428 352 AIQ 354
Cdd:cd19151 297 ALD 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
39-360 |
5.03e-70 |
|
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: 222.46 E-value: 5.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWvTFGGQ------ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSS 112
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 113 LVITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTH 191
Cdd:cd19079 80 VVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETP----------------IEETLEALHD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 192 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKvEVQLPELFHKIGVGAMTWSPLACGIVSGKY 271
Cdd:cd19079 144 VVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 DSGIP-PYSRASLKGYQWLKdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 350
Cdd:cd19079 223 GDTTErRRSTTDTAKLKYDY---FTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAV 296
|
330
....*....|
gi 1907154428 351 GAIQVlpKLS 360
Cdd:cd19079 297 AALDI--KLS 304
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
49-370 |
9.12e-70 |
|
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: 222.06 E-value: 9.12e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 49 VSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-- 119
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 ---FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPM-EAGDPFSSFKSRTFI-IEETVRAMTHVIN 194
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfGGGYYTEPSEEEDSVsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG 274
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 275 --IPPYSRASL-KGYQwlkdkilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLM 347
Cdd:cd19094 238 aaRPEGGRLNLfPGYM----------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|...
gi 1907154428 348 ENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19094 308 ENIDAFDV--PLSDELLAEIDAV 328
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
52-371 |
1.53e-65 |
|
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: 209.86 E-value: 1.53e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvTFGGQ---ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETE 128
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 129 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWSS 208
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTP----------------IEETWDALEELKKEGKIRAIGVSNFDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 209 MEIMEAYSVARqfnlIPPICEQAEYHMFqREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqw 288
Cdd:pfam00248 143 EQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG-------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 289 LKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQvlPKLSSSIVHEID 368
Cdd:pfam00248 210 ERRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARID 287
|
...
gi 1907154428 369 SIL 371
Cdd:pfam00248 288 ELL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
39-356 |
1.51e-64 |
|
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: 208.08 E-value: 1.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLVI 115
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 116 TTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTHV 192
Cdd:cd19150 82 STKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLE----------------ETMGALDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYD 272
Cdd:cd19150 144 VRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 273 SGIPPYSRASLKGYqwLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19150 223 NGIPEGSRASKERS--LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGA 297
|
....
gi 1907154428 353 IQVL 356
Cdd:cd19150 298 LDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
31-368 |
2.09e-60 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 198.67 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 31 SPKR--QLQfYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK 106
Cdd:PRK09912 6 NPERygQMQ-YRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLRED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 107 -GWRRSSLVITTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfii 182
Cdd:PRK09912 85 fAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPME--------------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 183 eETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPL 262
Cdd:PRK09912 148 -ETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 263 ACGIVSGKYDSGIPPYSRASLKG--YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGA 340
Cdd:PRK09912 226 AQGLLTGKYLNGIPQDSRMHREGnkVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGA 302
|
330 340
....*....|....*....|....*...
gi 1907154428 341 SNAEQLMENIGAIQVLpKLSSSIVHEID 368
Cdd:PRK09912 303 SRAEQLEENVQALNNL-TFSTEELAQID 329
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-368 |
2.94e-54 |
|
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: 181.26 E-value: 2.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 42 LGKSGLRVSCLGLGTwVTFGGQ----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITT 117
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 118 KIFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQ 195
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTP----------------VEEVMRALDDLVRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 196 GMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGi 275
Cdd:cd19080 143 GKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 276 pPYSRASLKGYQWLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 355
Cdd:cd19080 221 -EEGRAGEAKGVTVGFGKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
330
....*....|...
gi 1907154428 356 lpKLSSSIVHEID 368
Cdd:cd19080 297 --TLSPEQLARLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
49-370 |
3.60e-53 |
|
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: 178.16 E-value: 3.60e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 49 VSCLGLGTWV----TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFwggk 124
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 aetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVP----------------LEETMEALEKLKEEGKIRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlipPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRA 281
Cdd:cd19085 135 NFGPAQLEEALDAGR------IDSNQLPYNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDART 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 282 SLKgyqwlkdkILSEEGRRQQAK--LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKL 359
Cdd:cd19085 208 RLF--------RHFEPGAEEETFeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--EL 277
|
330
....*....|.
gi 1907154428 360 SSSIVHEIDSI 370
Cdd:cd19085 278 SPSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
39-369 |
5.16e-50 |
|
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: 170.53 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWV----TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 114
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 115 ITTK--IFWGGKAETE----------RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiI 182
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP----------------I 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 183 EETVRAMTHVINQGMAMYWGTSRWSSMEIMEaYSVARQFNLIppiceQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPL 262
Cdd:cd19149 142 EETMEALEELKRQGKIRAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 263 ACGIVSGKYDSGippysRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGAS 341
Cdd:cd19149 215 EQGLLTGKITPD-----REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGAR 289
|
330 340
....*....|....*....|....*...
gi 1907154428 342 NAEQLMENIGAIQVlpKLSSSIVHEIDS 369
Cdd:cd19149 290 KPEQAEENAKAGDI--RLSAEDIATMRS 315
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
48-368 |
2.60e-47 |
|
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: 162.78 E-value: 2.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 48 RVSCLGLGTWvTFGGQI----TDEMAEHLMT---LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIf 120
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgyGEYGDEDLQAafdAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 121 wggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMeagdpfssfksrtfiIEETVRAMTHVINQGMAMY 200
Cdd:cd19093 78 ----APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ---------------IEALMDGLADAVEEGLVRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 201 WGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY-DSGIPPYS 279
Cdd:cd19093 139 VGVSNYSADQLRRAHKALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 280 RASLKG-YQWLKDKILseegrrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIQVlpK 358
Cdd:cd19093 218 RRRLFGrKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW--R 283
|
330
....*....|
gi 1907154428 359 LSSSIVHEID 368
Cdd:cd19093 284 LSEEEVAELD 293
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
39-367 |
3.06e-47 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 162.77 E-value: 3.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLG----TWvtFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 114
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 115 ITTKifWG---GKAETERGL--SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAM 189
Cdd:cd19076 77 IATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVP----------------IEETVGAM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 190 THVINQGMAMYWGTSRWSSMEIMEAYSVArqfnlipPICE-QAEYHMFQREKVEVQLP---ELfhkiGVGAMTWSPLACG 265
Cdd:cd19076 139 AELVEEGKVRYIGLSEASADTIRRAHAVH-------PITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 266 IVSGKYDSgippysraslkgyqwlKDKILSEEGRRQQ-----------AKL-KELQAIAERLGCTLPQLAIAWCL-RNEG 332
Cdd:cd19076 208 FLTGAIKS----------------PEDLPEDDFRRNNprfqgenfdknLKLvEKLEAIAAEKGCTPAQLALAWVLaQGDD 271
|
330 340 350
....*....|....*....|....*....|....*
gi 1907154428 333 VSSVlLGASNAEQLMENIGAIQVlpKLSSSIVHEI 367
Cdd:cd19076 272 IVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
40-370 |
1.67e-46 |
|
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: 161.05 E-value: 1.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 40 RNLGKSGLRVSCLGLGTwVTFGGQ-----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLV 114
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 115 ITTK---IFWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiieETVRAMTH 191
Cdd:cd19083 79 IATKgahKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKA----------------EAVGALQE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 192 VINQGMAMYWGTSRWSSMEIMEAySVARQFNLIppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKY 271
Cdd:cd19083 141 LKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKY 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 DSGIppysraSLKGYQWLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMEN 349
Cdd:cd19083 214 TKDT------KFPDNDLRNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDN 287
|
330 340
....*....|....*....|.
gi 1907154428 350 IGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19083 288 LKALDV--TLTEEEIAFIDAL 306
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
52-370 |
1.80e-45 |
|
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: 158.10 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIikkkGWRRSSLVITTKI-FWGGKaeterG 130
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKAnPGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 131 LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSME 210
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTP----------------LEETLAAIDELYKEGKFKEFGLSNYSAWE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 211 IMEAYSVARQFNLIPPICEQAEYHMFQReKVEvqlPELF-----HKIGVGAmtWSPLACGIVSGKYDSG--IPPYSR--A 281
Cdd:cd19075 140 VAEIVEICKENGWVLPTVYQGMYNAITR-QVE---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 282 SLKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVL 356
Cdd:cd19075 214 NNALGKLYRDRYWKPS---YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKG 290
|
330
....*....|....
gi 1907154428 357 PkLSSSIVHEIDSI 370
Cdd:cd19075 291 P-LPEEVVKAIDEA 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
47-352 |
1.07e-44 |
|
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: 154.17 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 47 LRVSCLGLGTWV---TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI--FW 121
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPdpntPMEAGDpfssfksrtfiIEETVRAMTHVINQGMAMYW 201
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNP----PDEVLD-----------NDELFEALEKLKQEGKIRAY 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 202 GtsrWS--SMEIMEAYSVARQFNLIppiceQAEYHMFQREKVEvqlpELFHKI---GVGAMTWSPLACGIVSGKydsgip 276
Cdd:cd19086 143 G---VSvgDPEEALAALRRGGIDVV-----QVIYNLLDQRPEE----ELFPLAeehGVGVIARVPLASGLLTGK------ 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154428 277 pysraslkgyqwlkdkilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19086 205 ------------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-371 |
4.79e-44 |
|
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: 154.37 E-value: 4.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 49 VSCLGLGTWVTFGGQIT-------DEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSsLVITTK--I 119
Cdd:cd19102 1 LTTIGLGTWAIGGGGWGggwgpqdDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAM 199
Cdd:cd19102 78 LWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEP----------------IEEAWGALAELKEEGKVR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 200 YWGTSRWSSMEIMEAYSVARQFNLIPPiceqaeYHMFQREKVEVQLPelF---HKIGVgaMTWSPLACGIVSGKYDsgip 276
Cdd:cd19102 142 AIGVSNFSVDQMKRCQAIHPIASLQPP------YSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 277 PYSRASLKGYQWLK-DKILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 354
Cdd:cd19102 208 PERVASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAAD 287
|
330
....*....|....*..
gi 1907154428 355 VlpKLSSSIVHEIDSIL 371
Cdd:cd19102 288 L--RLTPEELAEIEALL 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
46-371 |
5.87e-44 |
|
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: 154.31 E-value: 5.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTW-VTFG-GQITD--EMAEhLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFW 121
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkeEMIE-LIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 ----GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGM 197
Cdd:cd19078 77 kidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVP----------------IEEVAGTMKELIKEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWSSMEIMEAYSVArqfnliPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI-- 275
Cdd:cd19078 141 IRHWGLSEAGVETIRRAHAVC------PVTAVQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkf 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 276 -PPYSRASLKGYqwlkdkilSEEGRRQQAKLKEL-QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 353
Cdd:cd19078 214 dEGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAA 285
|
330
....*....|....*...
gi 1907154428 354 QVlpKLSSSIVHEIDSIL 371
Cdd:cd19078 286 DI--ELTPEELREIEDAL 301
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
46-354 |
7.34e-43 |
|
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: 150.07 E-value: 7.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTFGGQ----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFw 121
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 ggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYW 201
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIP----------------IEETLRAMEELVEEGKIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 202 GTSRWSSMEIMEAYSVARQfnlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSgippysra 281
Cdd:cd19072 136 GVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS-------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 282 slkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNAEQLMENIGAIQ 354
Cdd:cd19072 204 ------------------------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-370 |
9.75e-39 |
|
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: 140.86 E-value: 9.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGtwvtfGGQI-----TDEMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRS 111
Cdd:cd19104 2 YRRFGRTGLKVSELTFG-----GGGIgglmgRTTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 112 SLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEAGDPFSSFKSrtFIIEETVRAMT 190
Cdd:cd19104 74 GPYITTKV---RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDKPVGGTLSTTDV--LGLGGVADAFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 191 HVINQGMAMYWGTSRWSSMEIME------AYSVARQF-NLIPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLA 263
Cdd:cd19104 149 RLRSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVYyNLLNPSAAEARPRGWSAQDYG-GIIDAAAEHGVGVMGIRVLA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 264 CGIVSGKYDSGIPPYSRAslkgyqwlkDKILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNA 343
Cdd:cd19104 228 AGALTTSLDRGREAPPTS---------DSDVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNR 294
|
330 340
....*....|....*....|....*..
gi 1907154428 344 EQLMENIGAIQVLPkLSSSIVHEIDSI 370
Cdd:cd19104 295 EELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
39-370 |
9.29e-37 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 136.52 E-value: 9.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRS 111
Cdd:PRK10625 3 YHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 112 SLVITTKIfwGGKAET-------ERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFS-SFKSRTFIIE 183
Cdd:PRK10625 81 KLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKLGYSwTDSAPAVSLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 184 ETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLA 263
Cdd:PRK10625 159 ETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 264 CGIVSGKYDSGIPPY-SRASLKgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 342
Cdd:PRK10625 238 FGTLTGKYLNGAKPAgARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATT 311
|
330 340
....*....|....*....|....*...
gi 1907154428 343 AEQLMENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:PRK10625 312 MEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-352 |
6.79e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 132.46 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI--- 119
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 --FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGM 197
Cdd:cd19752 79 prDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTP----------------LEETLEAFNELVKAGK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLacgiV 267
Cdd:cd19752 143 VRAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPL----L 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 268 SGKYDSgippysraslkgyqwlKDKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQ 345
Cdd:cd19752 219 SGAYTR----------------PDRPLPEQYDGPdsDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQ 282
|
....*..
gi 1907154428 346 LMENIGA 352
Cdd:cd19752 283 LEENLAA 289
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
50-352 |
1.57e-35 |
|
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: 131.52 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA----GKAEVVLGNIIKKKGwRRSSLVITTKifwGG-- 123
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 124 ---KAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMY 200
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVP----------------VGEIVDTLNELVRAGKIRA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 201 WGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFqrEKVEVQLP------------ELFHKIGVGAMTWSPLACGIVS 268
Cdd:cd19082 139 FGASNWSTERIAEANAYAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 269 GKYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQAKLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLME 348
Cdd:cd19082 217 KRAAGGAEDDSE--------LRRVYYSEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRD 285
|
....
gi 1907154428 349 NIGA 352
Cdd:cd19082 286 SLAA 289
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
52-354 |
5.87e-35 |
|
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: 129.60 E-value: 5.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGT-WVTFG-GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKIfwGGKAETER 129
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 130 GLSRKHIIEGLKASLERLQLEYVDVVF---ANRPDPNTPMEAGDPFS---SFKSRTFIIE-----ETVRAMTHVINQGma 198
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMihdPERVPWVDILAPGGALEallELKEEGLIKHiglggGPPDLLRRAIETG-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 mywgtsrwssmeimeAYSVARQFNLIPPICEQAEYHMFqrekvevqlpELFHKIGVGAMTWSPLACGIVSGKYDSGIPPy 278
Cdd:cd19090 155 ---------------DFDVVLTANRYTLLDQSAADELL----------PAAARHGVGVINASPLGMGLLAGRPPERVRY- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154428 279 sraslkGYQWLKDkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 354
Cdd:cd19090 209 ------TYRWLSP--------ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
45-370 |
1.09e-34 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 128.25 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPntpmeagDPFssfksrtfiiEETVRAMTHVINQGMAMYWGTS 204
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWPGP-------GPY----------VETWRALEELYEEGLIRAIGVS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREkvevqlPELF-----HKIGVGAmtWSPLACGivsgkydsgippys 279
Cdd:COG0656 129 NFDPEHLEELLAETG----VKPAVNQVELHPYLQQ------RELLafcreHGIVVEA--YSPLGRG-------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 280 raslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENIGAIQVlpKL 359
Cdd:COG0656 183 ------------KLLDDP---------VLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDF--EL 237
|
330
....*....|.
gi 1907154428 360 SSSIVHEIDSI 370
Cdd:COG0656 238 SDEDMAAIDAL 248
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
44-355 |
1.48e-34 |
|
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: 128.83 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 44 KSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK---IF 120
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 121 WGGKAETERG---LSRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEAgdpfssfksrtfiiEETVRAMTHVINQGM 197
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDP--LMDP--------------EEVAEAFDELVKSGK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWSSMeimeaysvarQFNL------IPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGky 271
Cdd:cd19092 145 VRYFGVSNFTPS----------QIELlqsyldQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFG-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 dsgippysraslkgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIG 351
Cdd:cd19092 213 ------------------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVK 268
|
....
gi 1907154428 352 AIQV 355
Cdd:cd19092 269 ALDI 272
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-353 |
7.02e-34 |
|
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: 126.16 E-value: 7.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGlgtwvtFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTK 118
Cdd:cd19105 3 YRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAETerglsRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDpfssfksrtfiieETVRAMTHVINQGMA 198
Cdd:cd19105 75 ASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNE-------------ELLEALEKLKKEGKV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSME--------------IMEAYSVARQFNLIPPICEQAeyHMfqrekvevqlpelfHKIGVGAMtwsplac 264
Cdd:cd19105 137 RFIGFSTHDNMAevlqaaiesgwfdvIMVAYNFLNQPAELEEALAAA--AE--------------KGIGVVAM------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 265 givsgkydsgippysraslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCTLPQLAIAWCLRNEGVSSVLLGASNAE 344
Cdd:cd19105 194 ---------------------------KTLA-GGYLQPALLSVLKA----KGFSLPQAALKWVLSNPRVDTVVPGMRNFA 241
|
....*....
gi 1907154428 345 QLMENIGAI 353
Cdd:cd19105 242 ELEENLAAA 250
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
46-371 |
2.59e-33 |
|
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: 125.88 E-value: 2.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVT----FGGqiTDEmAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK- 118
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGM 197
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVP----------------IEETAEALKELLDEGK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 AMYWGTSRWsSMEIMEAY-SVARQFNLIPPiceqaeYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKY--DSG 274
Cdd:cd19148 141 IRAIGVSNF-SPEQMETFrKVAPLHTVQPP------YNLFEREIEKDVLPYA-RKHNIVTLAYGALCRGLLSGKMtkDTK 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 275 IPPYS-RASLKGYQwlkdkilseEGRRQQ--AKLKELQAIA-ERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 350
Cdd:cd19148 213 FEGDDlRRTDPKFQ---------EPRFSQylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVD 283
|
330 340
....*....|....*....|.
gi 1907154428 351 GAIQVlpKLSSSIVHEIDSIL 371
Cdd:cd19148 284 EVFGW--SLNDEDMKEIDAIL 302
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
46-355 |
1.09e-32 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 123.06 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvTFGGQIT-----DEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIF 120
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 121 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMeagdpfssfksrtfiiEETVRAMTHVINQGMAMY 200
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPL----------------EETLSAMAEGVRQGLIRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 201 WGTSRWSSMEIMEAYSVARQfnliPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysr 280
Cdd:cd19137 135 IGVSNFNRRLLEEAISKSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN---------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907154428 281 aslkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLgASNAEQLMENIGAIQV 355
Cdd:cd19137 201 -------------------------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
50-352 |
1.56e-32 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 122.73 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTWVTFG--GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKI--FWGGkA 125
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRAL--AGLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 ETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmeagdpfssfksrtfIIEETVRAMTHVINQGMAMYWGTSr 205
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDE----------------LTGEVLETLEDLKAAGKVRYIGVS- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 206 wSSMEIMEAYSVARQFNLIppiceQAEYHMFQREKVEVqLPELfHKIGVGAMTWSPLAcgivsgkydSGIPPYSRASLKG 285
Cdd:cd19095 139 -GDGEELEAAIASGVFDVV-----QLPYNVLDREEEEL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154428 286 YQWLKDKilseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19095 202 YADYARR---------------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
45-368 |
1.64e-32 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 122.74 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWvtFGGQITDEMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIfWG 122
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV-LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 GKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRPdpntpmeAGDPFssfksrtfiiEETVRAMTHVINQGMAMYWG 202
Cdd:cd19138 81 SNA------SRQGTVRACERSLRRLGTDYLDLYLLHWR-------GGVPL----------AETVAAMEELKKEGKIRAWG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 203 TSRWSSMEIMEAYSVARQFNLippICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysras 282
Cdd:cd19138 138 VSNFDTDDMEELWAVPGGGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG----------------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 283 lkgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVlLGASNAEQLMENIGAIQVlpKLSSS 362
Cdd:cd19138 197 -------------GLLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEE 260
|
....*.
gi 1907154428 363 IVHEID 368
Cdd:cd19138 261 DLAELD 266
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
41-329 |
1.48e-31 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 121.03 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 41 NLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK-- 118
Cdd:COG4989 5 KLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEAgdpfssfksrtfiiEETVRAMTHVIN 194
Cdd:COG4989 85 IRLPSEARDNRVkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDP--LMDP--------------EEVAEAFDELKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWSSMeimeaysvarQFNLI------PPICEQAEYHMFQREKVE------VQLpelfHKIGVgaMTWSPL 262
Cdd:COG4989 149 SGKVRHFGVSNFTPS----------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154428 263 AcgivSGKYDSGippysraslkgyqwlkdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLR 329
Cdd:COG4989 213 A----GGRLFGG-------------------FDEQFPRLRAALDE---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
40-370 |
6.56e-30 |
|
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: 117.16 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 40 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVIT 116
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 117 TKifWGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTH 191
Cdd:cd19144 82 TK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTP----------------IEKTVAAMAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 192 VINQGMAMYWGTSRWSSMEIMEAYSVArqfnlipPICE-QAEYHMF--QREKVEVQLPELFHKIGVGAMTWSPLACGIVS 268
Cdd:cd19144 144 LVQEGKIKHIGLSECSAETLRRAHAVH-------PIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 269 GKYDS-----------GIPPYSRASLKGYQWLKDKIlseegrrqqaklkelQAIAERLGCTLPQLAIAWCLRNEGVSSVL 337
Cdd:cd19144 217 GAIRSpddfeegdfrrMAPRFQAENFPKNLELVDKI---------------KAIAKKKNVTAGQLTLAWLLAQGDDIIPI 281
|
330 340 350
....*....|....*....|....*....|...
gi 1907154428 338 LGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19144 282 PGTTKLKRLEENLGALKV--KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
40-367 |
4.04e-29 |
|
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: 114.84 E-value: 4.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 40 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVIT 116
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAL--KDGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 117 TKI---FWGGKAETERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVI 193
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVP----------------IEITMGELKKLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGTSRWSSMEIMEAYSVArqfnlipPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGK-- 270
Cdd:cd19145 144 EEGKIKYIGLSEASADTIRRAHAVH-------PITAvQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKak 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 271 ---------YDSGIPPYSRASLKgyqwlKDKILSEegrrqqaklkELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGA 340
Cdd:cd19145 216 leellensdVRKSHPRFQGENLE-----KNKVLYE----------RVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGT 279
|
330 340
....*....|....*....|....*..
gi 1907154428 341 SNAEQLMENIGAIQVlpKLSSSIVHEI 367
Cdd:cd19145 280 TKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
45-368 |
6.87e-29 |
|
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: 113.87 E-value: 6.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLG----TWVtfGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEV---VLGNIIKKKGWRRSSLVITT 117
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 118 KifwGGKAET--ERGLSRKHIIEGLKASLERL-QLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVIN 194
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVP----------------IEETIKALKELVK 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWSSMEIMEAYSVArqfnliPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--D 272
Cdd:cd19077 140 EGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIksL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 273 SGIPPY-SRASLkgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV-LLGASNAEQLMENI 350
Cdd:cd19077 214 ADIPEGdFRRHL-------DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENL 286
|
330
....*....|....*...
gi 1907154428 351 GAIQVlpKLSSSIVHEID 368
Cdd:cd19077 287 KAANV--ELTDEELKEIN 302
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
39-353 |
3.58e-28 |
|
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: 111.87 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVI 115
Cdd:cd19163 3 YRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 116 TTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANrpDpntpMEAGDPFSSfksrtfIIEETVRAMTHVIN 194
Cdd:cd19163 80 ATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVH--D----IEFAPSLDQ------ILNETLPALQKLKE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWsSMEIMeAYSVARQFNLIPPICEQAEYHMFQREKVEvqLPELFHKIGVGAMTWSPLACGIVSgkyDSG 274
Cdd:cd19163 148 EGKVRFIGITGY-PLDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERG 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 275 IPPYSRASlkgyQWLKDKIlseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 353
Cdd:cd19163 221 PPDWHPAS----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
52-368 |
5.15e-26 |
|
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: 104.66 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergL 131
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEI 211
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVP----------------LEETLGALKELKEAGKVKSIGVSNFTIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 212 MEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkydsgippysraslkgyqwl 289
Cdd:cd19073 133 EEALDISP----LPIAVNQVEFHPFlyQAELLEYCRE---NDIVITA--YSPLA-------------------------- 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 290 kdkilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 368
Cdd:cd19073 178 ---------RGEVLRDPVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAIFDW--ELTSEDVAKID 243
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
52-368 |
1.56e-25 |
|
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: 103.72 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 131
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWP-------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFssfksrtfiiEETVRAMTHVINQGMAMYWGTSRWSSMEI 211
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSKEAR----------LETWRALEELVDEGLVRSIGVSNFNVEHL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 212 MEAYSVARqfnlIPPICEQAEYHMF--QREkvevqLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwl 289
Cdd:cd19071 139 EELLAAAR----IKPAVNQIELHPYlqQKE-----LVEFCKEHGIVVQAYSPLG-------------------------- 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 290 kdkilseEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 368
Cdd:cd19071 184 -------RGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
46-370 |
3.83e-25 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 102.72 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWGGka 125
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 etergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSR 205
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVP----------------LAETLGALNEAQEAGLARHIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 206 WSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QRekvevQLPELFHKIGVGAMTWSPLACGIVsgkydsgippysrasl 283
Cdd:cd19140 134 FTVALLREAVELSE----APLFTNQVEYHPYldQR-----KLLDAAREHGIALTAYSPLARGEV---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 284 kgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSI 363
Cdd:cd19140 189 -----LKDPV--------------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEE 246
|
....*..
gi 1907154428 364 VHEIDSI 370
Cdd:cd19140 247 MARIAAL 253
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-358 |
8.97e-25 |
|
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: 101.84 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTwVTFG---------GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKgwrrSSLVITTKIfwg 122
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmeagdpfSSFKSRTFIIEetvrAMTHVINQGMAMYWG 202
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPD-----------DLLKHGGKLVE----ALLELKKEGLIRKIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 203 TSrwssmeimeAYSVarqfnlippicEQAEYhMFQREKVE-VQLPelfhkigVGAMTWSPLACGIVSGKYDSGIPPYSRa 281
Cdd:cd19097 138 VS---------VYSP-----------EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR- 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 282 S--LKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPK 358
Cdd:cd19097 189 SvfLQGLLLMEPDKLPAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
39-350 |
1.52e-24 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.36 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWvtfGGQITD-EMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITT 117
Cdd:COG1453 3 YRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 118 KIfwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVF----ANRPDPNTPMEAGDPFssfksrtfiieETVRAMthvI 193
Cdd:COG1453 75 KL-------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLihglNTEEDLEKVLKPGGAL-----------EALEKA---K 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGtsrWSS-------MEIMEAY---SVARQFNLippiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSPLA 263
Cdd:COG1453 134 AEGKIRHIG---FSThgsleviKEAIDTGdfdFVQLQYNY-----------LDQDNQAGEEALEAAAEKGIGVIIMKPLK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 264 CGivsgkydsgippysraslkgyqwlkdkilseegrrqqaKLKELQAIAERLGC---TLPQLAIAWCLRNEGVSSVLLGA 340
Cdd:COG1453 200 GG--------------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGM 241
|
330
....*....|
gi 1907154428 341 SNAEQLMENI 350
Cdd:COG1453 242 STPEQLDENL 251
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
39-371 |
1.94e-24 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 102.16 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 115
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 116 TTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmeagdpfssFKSRTFIIEETVRAMTHVINQ 195
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIE-------------FGSLDQIVNETIPALQKLKES 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 196 GMAMYWGTSRwSSMEIMEaYSVARqfnlIPP-----ICEQAEYHMFQREKVEVqLPELFHKiGVGAMTWSPLACGIVSgk 270
Cdd:PLN02587 144 GKVRFIGITG-LPLAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT-- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 271 yDSGIPPYSRASLKgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 350
Cdd:PLN02587 214 -ENGPPEWHPAPPE----LK------SACAAAATHCKEK------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENV 276
|
330 340
....*....|....*....|...
gi 1907154428 351 GAIQVLPKLS--SSIVHEIDSIL 371
Cdd:PLN02587 277 AAATELETSGidEELLSEVEAIL 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
38-363 |
3.25e-24 |
|
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: 101.07 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 38 FYRNLGKSGLRVSCLGLGTwVTFGGQITDEM----AEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSL 113
Cdd:cd19153 1 FGETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 114 VITTKIFWGGKAETErgLSRKHIIEGLKASLERLQLEYVDVVFANrpdpntPMEAGDPFSsfksrtfIIEETVRAMTHVI 193
Cdd:cd19153 80 TVATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLH------DIEFVDYDT-------LVDEALPALRTLK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGTSRWsSMEIMEaySVARQFNLIPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKyd 272
Cdd:cd19153 145 DEGVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 273 sGIPPYSRAS--LKGYQWLKDKILSEEGRrqqaklkelqaiaerlgcTLPQLAIAWCLRNE-GVSSVLLGASNAEQLMEN 349
Cdd:cd19153 220 -GPPPWHPASgeLRHYAAAADAVCASVEA------------------SLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSM 280
|
330
....*....|....
gi 1907154428 350 IGAIQVLPKLSSSI 363
Cdd:cd19153 281 LAAVDAVASLGAAI 294
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
49-352 |
4.18e-24 |
|
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: 99.60 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 49 VSCLGLGTWVTFGGQITDEMAEH---LMTL--AYDNGINLFDTAEVYAAGKAEvvlgNIIKK--KGWRrSSLVITTKIFW 121
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADReeaIAVLrrALELGVNFIDTADSYGPDVNE----RLIAEalHPYP-DDVVIATKGGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 --GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHVINQGMAM 199
Cdd:cd19088 76 vrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVP----------------FEEQLGALAELQDEGLIR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 200 YWGTSRWSSMEIMEAYSVARqfnlIppICEQAEYHMFQREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippys 279
Cdd:cd19088 140 HIGLSNVTVAQIEEARAIVR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG---------------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 280 raslkgyqwlkdkilseeGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19088 196 ------------------GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-156 |
7.52e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 98.71 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 39 YRNLGKSGLRVSCLGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTK 118
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 1907154428 119 IfwggkaeTERglSRKHIIEGLKASLERLQLEYVDVVF 156
Cdd:cd19100 74 T-------GAR--DYEGAKRDLERSLKRLGTDYIDLYQ 102
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
46-371 |
2.51e-23 |
|
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: 99.04 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGT------WVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI 119
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 FWGGK-AETER------GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMTHV 192
Cdd:cd19146 87 TTGYRrGGPIKiksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTS----------------IPELMQSLNHL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHM----FQREKVEVQLPElfhkiGVGAMTWSPLAcgivS 268
Cdd:cd19146 151 VAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----Q 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 269 GKYDSGIPPYSRASLKGYQWLKdkilSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLME 348
Cdd:cd19146 222 GQFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKG 294
|
330 340
....*....|....*....|...
gi 1907154428 349 NIGAIQVlpKLSSSIVHEIDSIL 371
Cdd:cd19146 295 NIEALGI--SLSDEEIQEIEDAY 315
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
52-352 |
5.71e-22 |
|
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: 94.73 E-value: 5.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTwVTFG--GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI-------FWG 122
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 GKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNtPMEAgdpfssfksrtfiIEETVRAMTHVINQGM--A 198
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRH-LLQA-------------LTDAFPALEELRAEGVvgA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSsmeimEAYSVARQFNLiPPICEQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVsgkyDSGIPPY 278
Cdd:cd19162 146 IGVGVTDWA-----ALLRAARRADV-DVVMVAGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAG 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154428 279 SRASlkgYQWLKDKILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 352
Cdd:cd19162 215 DRYD---YRPATPEVL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-350 |
6.19e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 95.08 E-value: 6.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 47 LRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGN----IIKKKGWRRSSLVITTKifwG 122
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 G----------------KAETERGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRPDPNTPMEAGDPFS 173
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPEEQLLELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 174 SfksrtfIIEETVRAMTHVINQGMAMYWGTSRWSsmeIMEAYSVARQFNLIPPICEQAE-----YHMFqreKVeVQLPel 248
Cdd:cd19099 158 D------RLEEAFEALEEAVAEGKIRYYGISTWD---GFRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP-- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 249 FHKIGVGAMT----WSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLAI 324
Cdd:cd19099 223 LNLLEPEALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRAL 289
|
330 340
....*....|....*....|....*.
gi 1907154428 325 AWCLRNEGVSSVLLGASNAEQLMENI 350
Cdd:cd19099 290 QFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
52-355 |
1.27e-21 |
|
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: 93.83 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTwVTFGG---QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIFWGGKAETE 128
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 129 RGLSRKHII--------------EGLKA----SLERLQLEYVDVVFANRPDPNTpmeAGDPFSSFKSRTfiIEETVRAMT 190
Cdd:cd19152 80 VEPTFEPGFwnplpfdavfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDL---AGAESDEHFAQA--IKGAFRALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 191 HVINQGMAMYW--GTSRWSSME----------IMeaysVARQFNLIppicEQAEYHMFqrekvevqLPELF-HKIGVgam 257
Cdd:cd19152 155 ELREEGVIKAIglGVNDWEVILrileeadldwVM----LAGRYTLL----DHSAAREL--------LPECEkRGVKV--- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 258 twsplacgIVSGKYDSGIppysrasLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVL 337
Cdd:cd19152 216 --------VNAGPFNSGF-------LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVA 280
|
330
....*....|....*...
gi 1907154428 338 LGASNAEQLMENIGAIQV 355
Cdd:cd19152 281 PGASSPERVEENVALLAT 298
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
50-352 |
3.82e-21 |
|
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: 91.47 E-value: 3.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGgkae 126
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 127 teRGLSRKHIIEGLKASLERLQLEYVDvVFA----NRPDPNTPMEAGDpfssfksrtfIIEETVRAMT-----HVinqGM 197
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEWLEKARKGG----------LLEFLEKAKKeglirHI---GF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 198 amywgtsrwSS-------MEIMEAYSVArqFNLIPpiceqaeYHMFQREKVEVQ-LPELFHKIGVGAMTWSPLACGivsg 269
Cdd:cd19096 139 ---------SFhdspellKEILDSYDFD--FVQLQ-------YNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGG---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 270 kydsgippysraslkgyqwlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMEN 349
Cdd:cd19096 197 ------------------------------GLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDEN 246
|
...
gi 1907154428 350 IGA 352
Cdd:cd19096 247 IAA 249
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
51-350 |
1.76e-20 |
|
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: 90.27 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 51 CLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVY----AAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAE 126
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 127 TERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSfKSRTFI----IEETVRAMTHVINQGMAMYWG 202
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPLAFDMDTDGDPRDD-NQIQSLskkpLEDTWRAMEQCVDEKLTKNIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 203 TSRWSSMEIMEAYSVARqfnlIPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgivsGKYDSGippysra 281
Cdd:cd19128 147 VSNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG------- 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 282 slkgyqwlKDKILSEegrrqqaklKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASNAEQLMENI 350
Cdd:cd19128 207 --------NLTFLND---------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
44-370 |
1.24e-19 |
|
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: 88.24 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 44 KSGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITT 117
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 118 KIFWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPMEAG-DPFSSFKsrtfiIEETVRAM 189
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMENGmSIHDAVD-----VEDVWRGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 190 THVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsG 269
Cdd:cd19154 145 EKVYDEGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------G 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 270 KYDSGIPPYSRASLKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMEN 349
Cdd:cd19154 212 SPGRANFTKSTGVSPAPNLLQDPI--------------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKEN 275
|
330 340
....*....|....*....|.
gi 1907154428 350 IGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19154 276 FNIFDF--SLSEEDMATLEEI 294
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
50-358 |
4.43e-17 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 80.83 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 50 SCLGLGTwVTFGG---QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIfwgGK-- 124
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 --AETERGL-----------------SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmeAGDPFSSFKSRTFiIEET 185
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYT---HGDRKERHHFAQL-MSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 186 VRAMTHVINQGM--AMYWGTSRWSSM-EIMEAYSVarQFNLIppiceQAEYHMFQREKVEVQLPELfHKIGVGAmtwspl 262
Cdd:cd19161 151 FKALEELKKAGVikAFGLGVNEVQIClEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 263 acgIVSGKYDSGIPPYSRASLKGYQWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 342
Cdd:cd19161 217 ---VIGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARN 287
|
330
....*....|....*..
gi 1907154428 343 AEQLMENIGAIQ-VLPK 358
Cdd:cd19161 288 PAQLRQNVEAFQtDIPE 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
54-328 |
7.19e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 80.07 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 54 LGTW----------VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGG 123
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 124 kaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---NTPmEAGDPFSSFKSRtfiieetvramtHVinqgmamy 200
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADverWTP-ELIPLLKSGKVK------------HV-------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 201 wGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYS 279
Cdd:cd19103 141 -GVSNHNLAEIKRANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEG 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907154428 280 RASLKGYQWLKDKIlseegRRQQAKLKElqaIAERLGCTLPQLAIAWCL 328
Cdd:cd19103 219 SGRAETYNPLLPQL-----EELTAVMAE---IGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
53-376 |
2.34e-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: 78.43 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 53 GLGTWVTFGGQIT-DEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKaetergl 131
Cdd:cd19120 10 GTGTAWYKSGDDDiQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 srkHIIEGLKASLERLQLEYVDVVFANrpdpntpmeagDPFSSfKSRTFIIEETVRAMTHVINQGMAMYWGTSRWSSMEI 211
Cdd:cd19120 80 ---DPREALRKSLAKLGVDYVDLYLIH-----------SPFFA-KEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 212 MEAYSVARqfnlIPPICEQAEYHMFqrekVEVQLPEL--FH-KIGVGAMTWSPLAcgivsgkydsgipPYSRaslkgyqw 288
Cdd:cd19120 145 EELLDTAK----IKPAVNQIEFHPY----LYPQQPALleYCrEHGIVVSAYSPLS-------------PLTR-------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 289 lkdkilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIqvLPKLSSSIVHEID 368
Cdd:cd19120 196 ----------DAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEID 261
|
....*...
gi 1907154428 369 SILGNKPY 376
Cdd:cd19120 262 KAGKQKHF 269
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
44-350 |
2.63e-16 |
|
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: 78.54 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 44 KSGLRVSCLGLGTWVTFGGqitdeMAEHLMTLAYDNGINLFDTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIfW 121
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPG-----VVGNAVKTAIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GGKAETERglsrkhIIEGLKASLERLQLEYVD---VVFANRPDPNTPMEAGDPFSSFKsrtfiIEETVRAMTHVINQGMA 198
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDlylIHWPVRLKKGAHMPEPEEVLPPD-----IPSTWKAMEKLVDSGKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsgkydsGIPpy 278
Cdd:cd19125 148 RAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSP-- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907154428 279 sraslkGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNAEQLMENI 350
Cdd:cd19125 208 ------GTTWVKKNVLKDP---------IVTKVAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
46-350 |
3.02e-16 |
|
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: 77.61 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITD-EMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPdpntpmeAGDPFSSFKsrtfIIEETVRAmthvinqGMAMYWGTS 204
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQP-------FGDVYGAWR----AMEELYKE-------GKIRAIGVS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSvarqFNLIPPICEQAEYHMFqREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslk 284
Cdd:cd19133 133 NFYPDRLVDLIL----HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA--------------------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154428 285 gyqwlkdkilseEGRRQQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 350
Cdd:cd19133 185 ------------EGRNNLFENPVLTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
45-333 |
4.22e-16 |
|
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: 77.36 E-value: 4.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWvtFGGQITDEMAEHLMTlayDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19135 9 NGVEMPILGLGTS--HSGGYSHEAVVYALK---ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPntpmeagdPFSSFKSRTfIIEETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDC--------PSSGKNVKE-TRAETWRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslk 284
Cdd:cd19135 145 NFLIEHLEQLLEDCS----VVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLA--------------------- 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1907154428 285 gyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 333
Cdd:cd19135 197 -----KGKALEEP---------TVTELAKKYQKTPAQILIRWSIQNGVV 231
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-371 |
6.89e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 77.63 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 48 RVSCLGLGTWVTFGG--------QITDEMAEHlmtlaYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGW---RRSSLVIT 116
Cdd:cd19101 1 TISRVINGMWQLSGGhggirdedAAVRAMAAY-----VDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 117 TKIFWGGKAETergLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNtpmeagdpfssfksrtFIieETVRAMTHVI 193
Cdd:cd19101 74 TKWVPDPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqfhWWDYSDPG----------------YL--DAAKHLAELQ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWG-----TSRWSsmEIMEAysvarqfnLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVS 268
Cdd:cd19101 133 EEGKIRHLGltnfdTERLR--EILDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 269 GKY----DSGIPPYSRASLKGYQWLKDKILSEEGrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAE 344
Cdd:cd19101 202 EKYlgvpEPTGPALETRSLQKYKLMIDEWGGWDL--FQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSE 279
|
330 340
....*....|....*....|....*..
gi 1907154428 345 QLMENIGAIQVlpKLSSSIVHEIDSIL 371
Cdd:cd19101 280 HIDDNVRAFSF--RLDDEDRAAIDAVL 304
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
52-370 |
3.97e-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: 75.14 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETEr 129
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 130 glsrkHIIEGLKASLERLQLEYVDVVF-----ANRPDPNTPmEAGDPFSSFKSRTfiIEETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDLYLmhwpvALKKGVGFP-ESGEDLLSLSPIP--LEDTWRAMEELVDKGLCRHIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgivsgkydSGIPPYSR 280
Cdd:cd19123 159 NFSVKKLEDLLATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPLG---------SGDRPAAM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 281 ASLKGYQWLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNAEQLMENIGAIQVlpKL 359
Cdd:cd19123 219 KAEGEPVLLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--EL 279
|
330
....*....|.
gi 1907154428 360 SSSIVHEIDSI 370
Cdd:cd19123 280 DASDMATIAAL 290
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
52-350 |
1.55e-14 |
|
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: 72.79 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 131
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 srkhiiEGLKASLERLQLEYVDVVFANRPDPntpmeAGDPFSsfksrtfiieETVRAMTHVINQGMAMYWGTSRWSS--- 208
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWPVP-----AQDKYV----------ETWKALIELKKEGRVKSIGVSNFTIehl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 209 MEIMEAYSVArqfnlipPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgy 286
Cdd:cd19131 143 QRLIDETGVV-------PVVNQIELHprFQQRE-----LRAFHAKHGIQTESWSPLGQGGL------------------- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154428 287 qwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENI 350
Cdd:cd19131 192 --LSDPVIGE--------------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
46-267 |
2.13e-14 |
|
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: 72.47 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTFGGqitDEMAEHLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKA 125
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG---DETERAVQT-ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 ETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpmeagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSR 205
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-----------------FIDTWKALEKLYASGKVKAIGVSN 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 206 WSSMEIMEAYSVARqfnlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGIV 267
Cdd:cd19126 135 FQEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
46-376 |
4.16e-14 |
|
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: 72.15 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTfggqITDEMAEHLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKI 119
Cdd:cd19111 1 GFPMPVIGLGTYQS----PPEEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 fwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSFKSRTfiiEETVRAMTHVINQGMAM 199
Cdd:cd19111 71 -------PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGERELASSDV---TSVWRAMEALVSEGKVK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 200 YWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkyDSGIPP 277
Cdd:cd19111 141 SIGLSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPLG--------SPGRAN 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 278 YSRASLKgYQWLKD-KILseegrrqqaklkelqAIAERLGCTLPQLAIAWCL-RNEGvssVLLGASNAEQLMENIGAIQV 355
Cdd:cd19111 204 QSLWPDQ-PDLLEDpTVL---------------AIAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF 264
|
330 340
....*....|....*....|.
gi 1907154428 356 lpKLSSSIVHEIDSILGNKPY 376
Cdd:cd19111 265 --ELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
52-370 |
7.09e-14 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 70.85 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 131
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAgdpfssfksrtfiiEETVRAMTHVINQGMAMYWGTSRWSSMEI 211
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNDEVPV--------------EEYIGALAEAKEQGLTRHIGVSNFTIALL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 212 MEAYSVARQFNLIPPICEQAEYhmFQREKVEVQLPElfHKIGVGAmtWSPLACGIVsgkydsgippysraslkgyqwLKD 291
Cdd:cd19139 135 DEAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLAYGKV---------------------LDD 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 292 KIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:cd19139 188 PV--------------LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
52-350 |
9.06e-14 |
|
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: 70.66 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkAETERGL 131
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 SRKhiIEGLKASLERLQLEYVDVVFANRPDPNTpmeaGDPFSSFksrtfiieetvRAMTHVINQGMAMYWGTSRWSSMEI 211
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGRE----GKYVDSW-----------GGLMKLREEGLARSIGVSNFTAEHL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 212 MEAYSVArqfnLIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwl 289
Cdd:cd19134 144 ENLIDLT----FFTPAVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG------------------------ 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154428 290 kdkilseegrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENI 350
Cdd:cd19134 191 -----------RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
52-350 |
1.58e-13 |
|
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: 69.97 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEmaEHLMTL---AYDNGINLFDTAEVYaagKAEVVLGNIIK----KKGWRRSSLVITTKIfwgGK 124
Cdd:cd19136 4 LGLGTF-----RLRGE--EEVRQAvdaALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKL---AP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AETERGLSRkhiiEGLKASLERLQLEYVDVVFANRPDPntpmeAGDPFSSFKSRTFIIeETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19136 71 KDQGYEKAR----AACLGSLERLGTDYLDLYLIHWPGV-----QGLKPSDPRNAELRR-ESWRALEDLYKEGKLRAIGVS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RW--SSMEIMEAYSvarqfnLIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysr 280
Cdd:cd19136 141 NYtvRHLEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG--------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 281 aslkgyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENI 350
Cdd:cd19136 195 ---------DLRLLEDP---------TVLAIAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
46-350 |
1.91e-13 |
|
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: 69.61 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggka 125
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 eteRGlsRKH----IIEGLKASLERLQLEYVDVVFANRPDPntpmeagdpfssfkSRTFIIeETVRAMTHVINQGMAMYW 201
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNP--------------SRDLYV-EAWQALIEAREEGLVRSI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 202 GTSRWSSM---EIMEAYSVARQFNLIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPLAcgivsgkydsgip 276
Cdd:cd19132 130 GVSNFLPEhldRLIDETGVTPAVNQIElhPYFPQAEQRAYHREH------------GIVTQSWSPLG------------- 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154428 277 pysraslKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENI 350
Cdd:cd19132 185 -------RGSGLLDEPV--------------IKAIAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
52-350 |
3.62e-13 |
|
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: 69.23 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfgGQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAEter 129
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYG-NEAEVgeAIREKIAEGVVKREDLFITTKL-WNSYHE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 130 glsRKHIIEGLKASLERLQLEYVDVVFAnrpdpNTPM---EAGDPFSSFKSRTFIIE--ETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19116 85 ---REQVEPALRESLKRLGLDYVDLYLI-----HWPVafkENNDSESNGDGSLSDIDylETWRGMEDLVKLGLTRSIGVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacGIVSGKYDSGIPPYsrasl 283
Cdd:cd19116 157 NFNSEQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPR----- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154428 284 kgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 350
Cdd:cd19116 222 -----LDDPT--------------LVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
46-370 |
3.76e-13 |
|
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: 69.48 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTKI 119
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 FWGGkaeterglSRKHIIEG-LKASLERLQLEYVDVVFANRPdPNTPMEAGDPFSSFKSRTFIIEETV------RAMTHV 192
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFP-VGSLSKEDDSGKLDPTGEHKQDYTTdlldiwKAMEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIVSGKY 271
Cdd:cd19155 150 VDQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 DSGIPPYSRASLkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNAEQLMENig 351
Cdd:cd19155 223 GTGSPSGSSPDL-----LQD--------------PVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKEN-- 279
|
330 340
....*....|....*....|
gi 1907154428 352 aIQVLP-KLSSSIVHEIDSI 370
Cdd:cd19155 280 -FQVFDfELTEADMAKLSSL 298
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
44-156 |
3.93e-13 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 69.23 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 44 KSGLRVSCLGLGTwvtFGGQITDEMAE----HLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKK--KGWRRSSLVITT 117
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1907154428 118 KIfwGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF 156
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
45-350 |
4.28e-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: 68.83 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGqitDEMAEHLMTLAYDNGINLFDTAEVY----AAGKA--EVVLGNIIKKkgwrRSSLVITTK 118
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS---PEDIKAAVLEAIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IfWGGKAEterglsRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSFKSRTFIIEETVRAMTHVINQGMA 198
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPGKFSFPIEEEDFLPFDIKGVWEAMEECQRLGLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 199 MYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH-MFQREKvevqLPELFHKIGVGAMTWSPLACgivsgkydsgipp 277
Cdd:cd19124 147 KAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGA------------- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 278 ysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 350
Cdd:cd19124 206 ------PGTKWGSNAVMESD---------VLKEIAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
45-370 |
7.91e-12 |
|
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: 65.21 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGgk 124
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 aeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSFKSRTFIIEE-----TVRAMTHVINQGMAM 199
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPDwdfikTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 200 YWGTSRWSSMEIMEAysVARQFNLIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYs 279
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------STNAPLL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 280 raslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENIGAIQvlpkL 359
Cdd:cd19117 219 ------------------------KEPVIIKIAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 1907154428 360 SSSIVHEIDSI 370
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
45-350 |
9.26e-12 |
|
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: 65.20 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQITDemaehLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWg 122
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKE-----LILNAIKIGYRHFDCAADYK-NEKEVgeALAEAFKTGLVKREDLFITTKL-W- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 gkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSFKSR-------TFIIEETVRAMTHVINQ 195
Cdd:cd19112 79 ---NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPVATKHTGVGTTGSALGEDgvldidvTISLETTWHAMEKLVSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 196 GMAMYWGTSRWSS--MEIMEAYSvarqfnLIPPICEQAEYH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIVSGKYD 272
Cdd:cd19112 152 GLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 273 SGIPPysraslkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNAEQLMENI 350
Cdd:cd19112 222 GSVSP-----------LDDPVLKD--------------LAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
45-326 |
2.58e-11 |
|
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: 63.94 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQItdemaEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKK-----KGWRRSSLVITTKI 119
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 120 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRPdpnTPMEAGD-PFSSFKSRTFIIE-----ETVRAMTHVI 193
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLYLIHWP---YAFERGDnPFPKNPDGTIRYDsthykETWKAMEKLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgivsgkyds 273
Cdd:cd19106 145 DKGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL----------- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907154428 274 GIPpySRAslkgyqWLK--DKILSEEGRrqqaklkeLQAIAERLGCTLPQLAIAW 326
Cdd:cd19106 207 GSP--DRP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
45-368 |
2.98e-11 |
|
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: 63.69 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLG------TWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK 118
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 119 IFW--------GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmeagdpfssfksrtfiIEETVRAMT 190
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTS----------------IEEVMDSLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 191 HVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGK 270
Cdd:cd19147 149 ILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 271 YDSgiPPYSRASLKGYQWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNAEQLME 348
Cdd:cd19147 224 FQS--KKAVEERKKNGEGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKD 301
|
330 340
....*....|....*....|
gi 1907154428 349 NIGAIQVlpKLSSSIVHEID 368
Cdd:cd19147 302 NIEALSI--KLTPEEIEYLE 319
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
46-350 |
3.22e-11 |
|
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: 63.19 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWG--G 123
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVAT-----ALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 124 KAETERGLsrkhiieglKASLERLQLEYVDVVFANRPdpnTPMEAGDPFSSFKSRTFIIEE-TVRAMthvinqgmamywG 202
Cdd:cd19127 78 YDKALRGF---------DASLRRLGLDYVDLYLLHWP---VPNDFDRTIQAYKALEKLLAEgRVRAI------------G 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 203 TSRWSS---MEIMEAYSVArqfnlipPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcGIVsgKYDSGIPPyS 279
Cdd:cd19127 134 VSNFTPehlERLIDATTVV-------PAVNQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPT-G 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154428 280 RASLkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNeGVSSVlLGASNAEQLMENI 350
Cdd:cd19127 200 PGDV-----LQDPTITG--------------LAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
52-265 |
4.69e-11 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 62.78 E-value: 4.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKaetergl 131
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 sRKHIIEGLKASLERLQLEYVDVVFANRPDPNtpmeagdpfssfksrtfiIEETVRAMTHVIN---QGMAMYWGTSRWSS 208
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVPA------------------IDHYVEAWKGMIElqkEGLIKSIGVCNFQI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907154428 209 ---MEIMEAYSVArqfnlipPICEQAEYH--MFQRekvEVQLPELFHKIGVGAmtWSPLACG 265
Cdd:PRK11565 143 hhlQRLIDETGVT-------PVINQIELHplMQQR---QLHAWNATHKIQTES--WSPLAQG 192
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
52-352 |
1.07e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 61.58 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIfWggkaeTERgL 131
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEagdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWS---- 207
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNDEVS--------------VEEFMQALLEAKKQGLTREIGISNFTialm 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 208 --SMEIMEAYSVARQfnlippiceQAEYHMF-QREKVEVQLPElfHKIGVGA-MTwspLACGIVsgkydsgippysrasl 283
Cdd:PRK11172 137 kqAIAAVGAENIATN---------QIELSPYlQNRKVVAFAKE--HGIHVTSyMT---LAYGKV---------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 284 kgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNAEQLMENIGA 352
Cdd:PRK11172 187 -----LKDPV--------------IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
46-351 |
2.03e-10 |
|
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: 60.87 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTW-VTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNtpmeagdpfsSFKsrtfiieETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWPVKG----------KYK-------ETWKALEKLYKDGRVRAIGVS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysras 282
Cdd:cd19157 135 NFQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG----------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 283 lkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIG 351
Cdd:cd19157 189 ---------QLLDNP---------VLKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
60-357 |
1.74e-09 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 58.24 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 60 FGGQITDEMAEHLMTL-AYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhI 136
Cdd:cd19129 11 FGTLIPDPSATRNAVKaALEAGFRHFDCAERYR-NEAEVgeAMQEVFKAGKIRREDLFVTTKL-WNTNHRPER------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 137 IEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSF------KSRTFIieETVRAMTHVINQGMAMYWGTSRWSSME 210
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGDEQDPRDANgnviydDGVTLL--DTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 211 IMEAYSVARqfnlIPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwLK 290
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LE 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154428 291 DKILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGvsSVLLGASNAEQLMENIGaIQVLP 357
Cdd:cd19129 216 DPVIT--------------AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLP 265
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
46-349 |
2.01e-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: 57.91 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITD-EMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 125 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPdpntpmeAGDPFssfksrtfiiEETVRAMTHVINQGMAMYWGTS 204
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWP-------VKGKF----------KDTWKAFEKLYKEKKVRAIGVS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 205 RWSSMEIMEAYSVARqfnlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGivsgkydsgippysrasl 283
Cdd:cd19156 134 NFHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG------------------ 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154428 284 kgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMEN 349
Cdd:cd19156 188 --------KLLSNP---------VLKAIGKKYGKSAAQVIIRWDIQHGII--TIPKSVHEERIQEN 234
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
45-262 |
4.03e-09 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 57.16 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEVVLGniIKK---KGWRRSSLVITTKIfW 121
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCYQ-NEDEVGEG--IKEaiaGGVKREDLFVTTKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GgkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSSFK--SRTFIIE----ETVRAMTHVINQ 195
Cdd:cd19121 79 S--------TYHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLPdgSRDLDWDwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907154428 196 GMAMYWGTSRWSSM---EIMEAYSVARQFNLIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPL 262
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
45-349 |
4.39e-09 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 57.04 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaAGKAEV--VLGNIIKKK-GWRRSSLVITTKIfW 121
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKI-----ALKAGYRHLDLAKVY-QNQHEVgqALKELLKEEpGVKREDLFITSKL-W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GGKAETErglsrkHIIEGLKASLERLQLEYVD-------VVFANRPDPN-TPMEAGDPFSSFKSRTFIIEETVRAMTHVI 193
Cdd:cd19118 76 NNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKPTGDLNpLTAVPTNGGEVDLDLSVSLVDTWKAMVELK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 194 NQGMAMYWGTSRWSS---MEIMEAYSVArqfnlipPICEQAEYH--MFQREKVEvqlpelFHK---IGVGAmtWSPLacg 265
Cdd:cd19118 150 KTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 266 ivsGKYDSGIPPysraslkgyqwlkdkILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQ 345
Cdd:cd19118 212 ---GNNLAGLPL---------------LVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTPSR 262
|
....
gi 1907154428 346 LMEN 349
Cdd:cd19118 263 IRSN 266
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
45-355 |
7.62e-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: 53.39 E-value: 7.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQITDEMAehlMTLAYDNGINLFDTAEVYAaGKAEV---VLGNIIKKKGWRRSSLVITTKIfW 121
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYL-NEDEVgdaVRDFLKENPSVKREDLFICTKV-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GGKAETErglsrkHIIEGLKASLERLQLEYVDV------VFANRPDPNTPMEAGD-PFSSFKSRTFIIEETVRAMTHVIN 194
Cdd:cd19122 80 NHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKLGPDgKYVILKDLTENPEPTWRAMEEIYE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 195 QGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACgivsgkyDSG 274
Cdd:cd19122 154 SGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------QNQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 275 IPpysraslkgyqwlkdkilsEEGRRQQAKlKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIQ 354
Cdd:cd19122 220 VP-------------------STGERVSEN-PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 1907154428 355 V 355
Cdd:cd19122 278 L 278
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
65-355 |
2.22e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 51.96 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 65 TDEMAEH---LMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKifWG------GKAETERGLSRKH 135
Cdd:cd19098 30 VEAMRAHthaVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadWQVDAAVHEVKDH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 136 iieglkaSLERLQLEYvdvvfanrpdPNTPMEAGDPFS-------SFKSRTFIIEETVRAMTHVINQGMAMYWGTSRWSS 208
Cdd:cd19098 106 -------SLARLLKQW----------EETRSLLGKHLDlyqihsaTLESGVLEDADVLAALAELKAEGVKIGLSLSGPQQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 209 MEIMEA-----YSVARQFNlippiCEQAEYHMFQREKVEvQLpELFHKIGVGAMTWSPLACGIVSGKYDSGippysrasl 283
Cdd:cd19098 169 AETLRRaleieIDGARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDRNPSP--------- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907154428 284 kgyqwlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 355
Cdd:cd19098 233 ----------------ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
45-160 |
3.06e-07 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 51.34 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQ-ITDEMAEHlmtlAYDNGINLFDTAEVYAA----GKAevvLGNIIKKKGWRRSSLVITTKI 119
Cdd:cd19119 8 TGASIPALGLGTASPHEDRaEVKEAVEA----AIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1907154428 120 ---FWggkaeterglsrKHIIEGLKASLERLQLEYVDVVFANRP 160
Cdd:cd19119 81 wptFY------------DEVERSLDESLKALGLDYVDLLLVHWP 112
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
46-350 |
4.98e-07 |
|
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: 51.02 E-value: 4.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK---KGW-RRSSLVITTKIfW 121
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 122 GGKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRP------DPNTPMEAGDPFSSFKSRTF---IIEETVRAMTHV 192
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPAENYPFLWKDKELKKFPLeqsPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgivsgKY 271
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 272 DSGIPPYSRASLKGYQwlkdkILSEEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMEN 349
Cdd:cd19114 199 GIQITAYSSFGNAVYT-----KVTKHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTN 271
|
.
gi 1907154428 350 I 350
Cdd:cd19114 272 L 272
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
45-234 |
8.28e-06 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 47.06 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKaEVVLG--NIIKKKGWRRSSLVITTKIfWG 122
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 123 GKAEterglsRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEAGDP--FSSFKSRTFIIE-----ETVRAMTHVI 193
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAFkfVPIEEKYPpgFYCGDGDNFVYEdvpilDTWKALEKLV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907154428 194 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH 234
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHH 190
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
76-370 |
2.42e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 45.73 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 76 AYDNGINLFDTAEVYAAGkaevVLGNIIkkkgwR------RSSLVITTKIfwgGKAETERG-----LSRKHIIEGLKASL 144
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 145 ERLQLEYVDVV-FANRPDPNTPMEAGdpfssfksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnl 223
Cdd:PRK10376 117 RNLGLDVLDVVnLRLMGDGHGPAEGS------------IEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 224 iPPICEQAEYHMFQREkvEVQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkGYQWLKDKILSeegrrqqa 303
Cdd:PRK10376 180 -EIVCVQNHYNLAHRA--DDALIDALARDGIAYVPFFPLG---------------------GFTPLQSSTLS-------- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154428 304 klkelqAIAERLGCTLPQLAIAWCLRNEgvSSVLL--GASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 370
Cdd:PRK10376 228 ------DVAASLGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
48-262 |
2.50e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 45.72 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 48 RVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIfWGgka 125
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKL-WC--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 126 eterGLSRKHIIE-GLKASLERLQLEYVDVVFANRPDPNTPMEAGDPFSS----FKSRTFIIeETVRAMTHVINQGMAMY 200
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLPLDRsgmvIPSDTDFL-DTWEAMEDLVIEGLVKN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154428 201 WGTSRWSSmEIMEaySVARQFNL-IPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 262
Cdd:cd19110 148 IGVSNFNH-EQLE--RLLNKPGLrVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
46-211 |
3.86e-05 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 45.10 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 46 GLRVSCLGLGTWVTFGGQITDEMAehlmtLAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIFwgg 123
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 124 KAETERGLSRkhiiEGLKASLERLQLEYVDVVFANRPdpnTPMEAGDPFSSFKSRTFIIE------ETVRAMTHVINQGM 197
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWP---TGFKPGKELFPLDESGNVIPsdttflDTWEAMEELVDEGL 144
|
170
....*....|....
gi 1907154428 198 AMYWGTSRWSSMEI 211
Cdd:cd19107 145 VKAIGVSNFNHLQI 158
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
52-236 |
6.99e-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: 41.06 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 127
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 128 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPdpnTPMEAGDPFSSFKSRTFIIEETV------RAMTHVINQGMAMYW 201
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVDLYLIHFP---VALKPGEELFPKDENGKLIFDTVdlcatwEAMEKCKDAGLAKSI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1907154428 202 GTSRWSSmeimeaysvaRQFNLI---P-----PICEQAEYHMF 236
Cdd:cd19108 159 GVSNFNR----------RQLEMIlnkPglkykPVCNQVECHPY 191
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
45-234 |
7.55e-04 |
|
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: 41.25 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYA----AGKAevvLGNIIKKKGWRRSSLVITTKIf 120
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYN-----AIKAGYRLFDGACDYGneveAGQG---VARAIKEGIVKREDLFIVSKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 121 WGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP------DPNT--PMEAGDPFSSFKSRTFIIEETVRAMTHV 192
Cdd:cd19115 80 WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvDPAVryPPGWFYDGKKVEFSNAPIQETWTAMEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1907154428 193 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH 234
Cdd:cd19115 154 VDKGLARSIGVSNFSAQLLMDLLRYAR----IRPATLQIEHH 191
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
52-162 |
2.23e-03 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 39.51 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154428 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 131
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPA 83
|
90 100 110
....*....|....*....|....*....|.
gi 1907154428 132 SrkhiieGLKASLERLQLEYVDVVFANRPDP 162
Cdd:cd19130 84 A------AFAESLAKLGLDQVDLYLVHWPTP 108
|
|
| |
