|
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 ... |
38-347 |
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: 676.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 38 FYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITT 117
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 118 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 197
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKI 277
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 278 LSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSI 347
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
37-360 |
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: 661.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 37 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 116
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 117 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 196
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 197 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 276
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 277 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 356
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 8393646 357 NKPY 360
Cdd:cd19158 321 NKPY 324
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
39-359 |
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: 651.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19159 3 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 198
Cdd:cd19159 83 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKIL 278
Cdd:cd19159 163 YSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 279 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNK 358
Cdd:cd19159 243 SEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNK 322
|
.
gi 8393646 359 P 359
Cdd:cd19159 323 P 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
39-355 |
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: 641.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 198
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKIL 278
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 279 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSIL 355
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
39-359 |
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: 632.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19160 5 YRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 198
Cdd:cd19160 85 IYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKIL 278
Cdd:cd19160 165 YSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 279 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNK 358
Cdd:cd19160 245 SEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNK 324
|
.
gi 8393646 359 P 359
Cdd:cd19160 325 P 325
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
39-354 |
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: 522.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19143 3 YRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 196
Cdd:cd19143 83 IFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 197 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDk 276
Cdd:cd19143 163 EAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKD- 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 277 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSI 354
Cdd:cd19143 242 RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
39-359 |
4.01e-169 |
|
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: 474.65 E-value: 4.01e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 118
Cdd:cd19142 3 YRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAEtERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 198
Cdd:cd19142 83 IYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGY-----QWL 273
Cdd:cd19142 162 FSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSkykvgSDG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 274 KDKIlsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDS 353
Cdd:cd19142 242 NGIH--EETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELER 319
|
....*.
gi 8393646 354 ILGNKP 359
Cdd:cd19142 320 ILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
46-347 |
7.25e-169 |
|
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: 472.85 E-value: 7.25e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFWGGKA 125
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 E-TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQ 204
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 FNLIPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKgYQWLKDKILSEEGRR 284
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393646 285 QQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAiqVLPKLSSSI 347
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
39-359 |
1.92e-103 |
|
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: 307.49 E-value: 1.92e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWvTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVI 115
Cdd:COG0667 3 YRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 116 TTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 194
Cdd:COG0667 80 ATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 195 IMEAYSVARqfNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG--IPPYSRASLKGYQW 272
Cdd:COG0667 160 LRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFVQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 273 lkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:COG0667 237 -------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALD 307
|
....*..
gi 8393646 353 SILGNKP 359
Cdd:COG0667 308 AALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
39-354 |
1.13e-92 |
|
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: 279.84 E-value: 1.13e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK 118
Cdd:cd19087 3 YRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWG-GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 197
Cdd:cd19087 79 VFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP--YSRASLKGYQwlkD 275
Cdd:cd19087 159 AQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPesGRLVERARYQ---A 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 276 KILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19087 235 RYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
39-341 |
5.70e-84 |
|
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: 257.19 E-value: 5.70e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVY--AAGKAEVVLGNIIKK-KGWRRSSLVI 115
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 116 TTKI---FWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 192
Cdd:cd19089 81 STKAgygMWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 193 MEIMEAYSVARQFNlIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRAsLKGYQW 272
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 273 LKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLP 341
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
39-354 |
2.32e-83 |
|
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: 256.00 E-value: 2.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTwVTFG---------GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwR 109
Cdd:cd19091 3 YRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 110 RSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTS 188
Cdd:cd19091 79 RDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 189 RWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPYSRAS 266
Cdd:cd19091 159 NFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 267 LKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSS 346
Cdd:cd19091 238 RTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLTPE 310
|
....*...
gi 8393646 347 IVHEIDSI 354
Cdd:cd19091 311 EIARLDKV 318
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
46-352 |
4.61e-79 |
|
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: 244.36 E-value: 4.61e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWV---TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IF 120
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 121 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAys 200
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 201 varqFNLIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSG--IPPY-SRASLKGYQwlkdki 277
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLPYC-RENGIGVLPYGPLAQGLLTGKYKKEptFPPDdRRSRFPFFR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 278 lSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
42-352 |
4.91e-76 |
|
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: 237.11 E-value: 4.91e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 42 LGKSGLRVSCLGLGTWVtFGGQItDEMAEHLMTLAY-DNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSL 113
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTA-DEETSFALLDAFvDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 114 VITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 193
Cdd:cd19081 79 VIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 194 EIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPySRASLKGYQWl 273
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADL-PGSTRRGEAA- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 274 kDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19081 236 -KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
50-335 |
1.23e-75 |
|
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: 233.18 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTWvTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI-FWGGKAETE 128
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 129 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLI 208
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 209 PPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrqqak 288
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 8393646 289 lkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIG 335
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
39-338 |
2.15e-74 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 233.06 E-value: 2.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKK--KGWRrSSLV 114
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 115 ITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 191
Cdd:cd19151 81 ISTKagyTMWPGPY-GDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 SMEIMEAYSVARQFNlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKGYQ 271
Cdd:cd19151 159 PEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSS 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 272 WLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 338
Cdd:cd19151 236 FLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
39-344 |
6.16e-74 |
|
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: 231.70 E-value: 6.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWvTFGGQ------ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSS 112
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 113 LVITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 191
Cdd:cd19079 80 VVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 SMEIMEAYSVARQFNLIPPICEQAEYHMFQREKvEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGY 270
Cdd:cd19079 160 AWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393646 271 QWLKdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLS 344
Cdd:cd19079 239 KYDY---FTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLS 304
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
52-355 |
2.33e-69 |
|
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: 219.49 E-value: 2.33e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvTFGGQ---ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETE 128
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 129 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlI 208
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 209 PPICEQAEYHMFqREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQAK 288
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG--------ERRRLLKKGTPLNLEA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 289 LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQvlPKLSSSIVHEIDSIL 355
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
39-340 |
1.03e-68 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 218.48 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLVI 115
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 116 TTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 192
Cdd:cd19150 82 STKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 193 MEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYqw 272
Cdd:cd19150 160 ERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 273 LKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 340
Cdd:cd19150 237 LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
49-354 |
5.97e-67 |
|
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: 214.35 E-value: 5.97e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 49 VSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-- 119
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 ---FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTP------------------MEETVRAMTHVIN 178
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 179 QGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG 258
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 259 --IPPYSRASL-KGYQwlkdkilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLM 331
Cdd:cd19094 238 aaRPEGGRLNLfPGYM----------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|...
gi 8393646 332 ENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19094 308 ENIDAFDV--PLSDELLAEIDAV 328
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
31-352 |
1.27e-64 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 209.08 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 31 SPKR--QLQfYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK 106
Cdd:PRK09912 6 NPERygQMQ-YRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLRED 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 107 -GWRRSSLVITTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMA 182
Cdd:PRK09912 85 fAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 183 MYWGTSRWSSMEIMEAYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 262
Cdd:PRK09912 163 LYVGISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 263 SRASLKG--YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 340
Cdd:PRK09912 242 SRMHREGnkVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
330
....*....|..
gi 8393646 341 pKLSSSIVHEID 352
Cdd:PRK09912 319 -TFSTEELAQID 329
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
42-352 |
2.66e-57 |
|
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: 188.58 E-value: 2.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 42 LGKSGLRVSCLGLGTwVTFGGQ----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITT 117
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 118 KIFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 195
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 196 MEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGipPYSRASLKGYQWLKD 275
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 276 KILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19080 236 GKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
49-354 |
4.15e-57 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 187.79 E-value: 4.15e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 49 VSCLGLGTWV----TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFwggk 124
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 aetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 204
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 fnlipPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKgyqwlkdkILSEE 281
Cdd:cd19085 150 -----IDSNQLPYNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDARTRLF--------RHFEP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 282 GRRQQAK--LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19085 216 GAEEETFeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
39-353 |
8.71e-53 |
|
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: 177.08 E-value: 8.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWV----TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 114
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 115 ITTK--IFWGGKAETE----------RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMA 182
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 183 MYWGTSRWSSMEIMEaYSVARQFNLIppiceQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSGKYDSGippy 262
Cdd:cd19149 158 RAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPD---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 263 sRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlp 341
Cdd:cd19149 227 -REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI-- 303
|
330
....*....|..
gi 8393646 342 KLSSSIVHEIDS 353
Cdd:cd19149 304 RLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
40-354 |
1.17e-50 |
|
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: 171.45 E-value: 1.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 40 RNLGKSGLRVSCLGLGTwVTFGGQ-----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLV 114
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 115 ITTK---IFWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 191
Cdd:cd19083 79 IATKgahKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 SMEIMEAySVARQFNLIppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSGIppysraSLKGYQ 271
Cdd:cd19083 157 LEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 272 WLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVH 349
Cdd:cd19083 224 LRNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIA 301
|
....*
gi 8393646 350 EIDSI 354
Cdd:cd19083 302 FIDAL 306
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
39-351 |
3.39e-50 |
|
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: 170.09 E-value: 3.39e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLG----TWvtFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 114
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 115 ITTKifWG---GKAETERGL--SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 189
Cdd:cd19076 77 IATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 190 WSSMEIMEAYSVArqfnlipPICE-QAEYHMFQREKVEVQLP---ELfhkiGVGAMTWSPLACGIVSGKYDSgippysra 265
Cdd:cd19076 155 ASADTIRRAHAVH-------PITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 266 slkgyqwlKDKILSEEGRRQQ-----------AKL-KELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASNAEQLME 332
Cdd:cd19076 216 --------PEDLPEDDFRRNNprfqgenfdknLKLvEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEE 286
|
330
....*....|....*....
gi 8393646 333 NIGAIQVlpKLSSSIVHEI 351
Cdd:cd19076 287 NVGALDV--VLTPEELAEI 303
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
48-352 |
2.53e-49 |
|
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: 167.40 E-value: 2.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 48 RVSCLGLGTWvTFGGQI----TDEMAEHLMT---LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIf 120
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgyGEYGDEDLQAafdAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 121 wggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETV-RAMTHVINQGMAMYWGTSRWSSMEIMEAY 199
Cdd:cd19093 78 ----APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 200 SVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY-DSGIPPYSRASLKG-YQWLKDKI 277
Cdd:cd19093 154 KALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGRRRLFGrKNLEKVQP 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 278 LseegrrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19093 233 L----------LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
52-354 |
3.28e-49 |
|
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: 167.73 E-value: 3.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIikkkGWRRSSLVITTKI-FWGGKaeterG 130
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKAnPGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 131 LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPP 210
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 211 ICEQAEYHMFQReKVEvqlPELF-----HKIGVGAmtWSPLACGIVSGKYDSG--IPPYSR--ASLKGYQWLKDKILSEE 281
Cdd:cd19075 156 TVYQGMYNAITR-QVE---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdPNNALGKLYRDRYWKPS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 282 grrQQAKLKELQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASNAEQLMENIGAIQVLPkLSSSIVHEIDSI 354
Cdd:cd19075 230 ---YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGP-LPEEVVKAIDEA 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
46-355 |
2.69e-47 |
|
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: 162.40 E-value: 2.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTW-VTFG-GQITD--EMAEhLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFW 121
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkeEMIE-LIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 ----GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 197
Cdd:cd19078 77 kidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVArqfnliPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKGYqwlk 274
Cdd:cd19078 157 AHAVC------PVTAVQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 275 dkilSEEGRRQQAKLKEL-QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDS 353
Cdd:cd19078 226 ----TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIED 299
|
..
gi 8393646 354 IL 355
Cdd:cd19078 300 AL 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
49-355 |
4.24e-47 |
|
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: 162.07 E-value: 4.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 49 VSCLGLGTWVTFGGQIT-------DEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSsLVITTK--I 119
Cdd:cd19102 1 LTTIGLGTWAIGGGGWGggwgpqdDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAY 199
Cdd:cd19102 78 LWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 200 SVARQFNLIPPiceqaeYHMFQREKVEVQLPelF---HKIGVgaMTWSPLACGIVSGKYDsgipPYSRASLKGYQWLK-D 275
Cdd:cd19102 158 AIHPIASLQPP------YSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT----PERVASLPADDWRRrS 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 276 KILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19102 224 PFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEAL 301
|
.
gi 8393646 355 L 355
Cdd:cd19102 302 L 302
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
47-336 |
8.96e-47 |
|
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: 159.18 E-value: 8.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 47 LRVSCLGLGTWV---TFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI--FW 121
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEETVRAMTHVINQGMAMYWGtsrWS--SMEIMEA 198
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYG---VSvgDPEEALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 YSVARQFNLIppiceQAEYHMFQREKVEvqlpELFHKI---GVGAMTWSPLACGIVSGKydsgippysraslkgyqwlkd 275
Cdd:cd19086 155 ALRRGGIDVV-----QVIYNLLDQRPEE----ELFPLAeehGVGVIARVPLASGLLTGK--------------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393646 276 kilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19086 205 ---------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
46-338 |
2.76e-46 |
|
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: 158.55 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTFGGQ----ITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFw 121
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 ggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSV 201
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 202 ARQfnlIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSgippysraslkgyqwlkdkilsee 281
Cdd:cd19072 152 LKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS------------------------ 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 282 grrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNAEQLMENIGAIQ 338
Cdd:cd19072 204 --------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
50-336 |
1.09e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 142.09 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI--- 119
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 --FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 197
Cdd:cd19752 79 prDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARQFNLIPPICEQAEYHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLacgiVSGKYDSgippysrasl 267
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPL----LSGAYTR---------- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393646 268 kgyqwlKDKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19752 225 ------PDRPLPEQYDGPdsDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
50-336 |
1.86e-39 |
|
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: 141.54 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA----GKAEVVLGNIIKKKGwRRSSLVITTKifwGG-- 123
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 124 ---KAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYS 200
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 201 VARQFNLIPPICEQAEYHMFqrEKVEVQLP------------ELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslk 268
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSE---- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 269 gyqwLKDKILSEEGRRQQAKLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19082 229 ----LRRVYYSEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
45-354 |
8.65e-38 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 136.34 E-value: 8.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 204
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 fnlIPPICEQAEYHMFQREkvevqlPELF-----HKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILS 279
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELLafcreHGIVVEA--YSPLGRG--------------------------KLLD 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 280 EEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:COG0656 187 DP---------VLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-354 |
1.52e-37 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 137.40 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGtwvtfGGQI-----TDEMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRS 111
Cdd:cd19104 2 YRRFGRTGLKVSELTFG-----GGGIgglmgRTTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 112 SLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF------ANRPDPNTPM---------EETVRAMTHV 176
Cdd:cd19104 74 GPYITTKV---RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQlhnrigDERDKPVGGTlsttdvlglGGVADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 177 INQGMAMYWGTSRWSSMEIME------AYSVARQF-NLIPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACG 249
Cdd:cd19104 151 RSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVYyNLLNPSAAEARPRGWSAQDYG-GIIDAAAEHGVGVMGIRVLAAG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 250 IVSGKYDSGIPPYSRAslkgyqwlkDKILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQ 329
Cdd:cd19104 230 ALTTSLDRGREAPPTS---------DSDVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREE 296
|
330 340
....*....|....*....|....*
gi 8393646 330 LMENIGAIQVLPkLSSSIVHEIDSI 354
Cdd:cd19104 297 LEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
39-354 |
1.76e-37 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 138.06 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRS 111
Cdd:PRK10625 3 YHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 112 SLVITTKIfwGGKAET-------ERGLSRKHIIEGLKASLERLQLEYVD---VVFANRPD--------------PNTPME 167
Cdd:PRK10625 81 KLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPTncfgklgyswtdsaPAVSLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 168 ETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLA 247
Cdd:PRK10625 159 ETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 248 CGIVSGKYDSGIPPY-SRASLKgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 326
Cdd:PRK10625 238 FGTLTGKYLNGAKPAgARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATT 311
|
330 340
....*....|....*....|....*...
gi 8393646 327 AEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:PRK10625 312 MEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-337 |
1.14e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 133.09 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGlgtwvtFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTK 118
Cdd:cd19105 3 YRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAETerglsRKHIIEGLKASLERLQLEYVDVVF---ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME- 194
Cdd:cd19105 75 ASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNMAe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 195 -------------IMEAYSVARQFNLIPPICEQAeyHMfqrekvevqlpelfHKIGVGAMtwsplacgivsgkydsgipp 261
Cdd:cd19105 150 vlqaaiesgwfdvIMVAYNFLNQPAELEEALAAA--AE--------------KGIGVVAM-------------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8393646 262 ysraslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 337
Cdd:cd19105 194 --------------KTLA-GGYLQPALLSVLKA----KGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
46-339 |
1.63e-36 |
|
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: 133.08 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvTFGGQIT-----DEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIF 120
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 121 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYS 200
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 201 VARQfnliPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwlkdkilse 280
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN-------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 281 egrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLgASNAEQLMENIGAIQV 339
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
50-336 |
2.04e-36 |
|
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: 132.36 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTWVTFG--GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKkkGWRRSSLVITTKI--FWGGkA 125
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 ETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSrwSSMEIMEAYSVARQF 205
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS--GDGEELEAAIASGVF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 206 NLIppiceQAEYHMFQREKVEVqLPELfHKIGVGAMTWSPLAcgivsgkydSGIPPYSRASLKGYQWLKDKilseegrrq 285
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPLYADYARR--------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 8393646 286 qaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19095 209 ------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
46-355 |
2.24e-36 |
|
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: 133.59 E-value: 2.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVT----FGGqiTDEmAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK- 118
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWsSMEIME 197
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNF-SPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AY-SVARQFNLIPPiceqaeYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKY--DSGIPPYS-RASLKGYQwl 273
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPYA-RKHNIVTLAYGALCRGLLSGKMtkDTKFEGDDlRRTDPKFQ-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 274 kdkilseEGRRQQ--AKLKELQAIA-ERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHE 350
Cdd:cd19148 227 -------EPRFSQylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGW--SLNDEDMKE 297
|
....*
gi 8393646 351 IDSIL 355
Cdd:cd19148 298 IDAIL 302
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
44-339 |
3.77e-36 |
|
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: 132.68 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 44 KSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK---IF 120
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 121 WGGKAETERG---LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMeime 197
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 aysvarQFNL------IPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGkydsgippysraslkgyq 271
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDGTLDYCQLLDITPMAWSPLGGGRLFG------------------ 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 272 wlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 339
Cdd:cd19092 213 --------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
45-352 |
1.21e-35 |
|
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: 130.83 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWvtFGGQITDEMAEHLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIfWG 122
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV-LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 GKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDpNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVA 202
Cdd:cd19138 81 SNA------SRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 203 RQFNLippICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilsEEG 282
Cdd:cd19138 154 GGGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG------------------------------GLL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 283 RRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVlLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19138 200 RRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
52-338 |
1.65e-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: 130.75 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGT-WVTFG-GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKIfwGGKAETER 129
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 130 GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEET-----VRAMTHVINQGMAMYWGTSRWSSMEIMEA-----Y 199
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPDLLRRAietgdF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 200 SVARQFNLIPPICEQAEYHMFqrekvevqlpELFHKIGVGAMTWSPLACGIVSGKYDSGIPPysraslkGYQWLKDkils 279
Cdd:cd19090 157 DVVLTANRYTLLDQSAADELL----------PAAARHGVGVINASPLGMGLLAGRPPERVRY-------TYRWLSP---- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 280 eegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQ 338
Cdd:cd19090 216 ----ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
41-313 |
3.50e-34 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 127.96 E-value: 3.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 41 NLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK-- 118
Cdd:COG4989 5 KLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMe 194
Cdd:COG4989 85 IRLPSEARDNRVkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPS- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 195 imeaysvarQFNLI------PPICEQAEYHMFQREKVE------VQLpelfHKIGVgaMTWSPLAcgivSGKYDSGippy 262
Cdd:COG4989 164 ---------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLA----GGRLFGG---- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 8393646 263 sraslkgyqwlkdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLR 313
Cdd:COG4989 221 ---------------FDEQFPRLRAALDE---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
40-354 |
3.75e-33 |
|
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: 125.63 E-value: 3.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 40 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVIT 116
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 117 TKifWGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 191
Cdd:cd19144 82 TK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 SMEIMEAYSVArqfnlipPICE-QAEYHMF--QREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS----------- 257
Cdd:cd19144 160 AETLRRAHAVH-------PIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpddfeegdfrr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 258 GIPPYSRASLKGYQWLKDKIlseegrrqqaklkelQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 337
Cdd:cd19144 233 MAPRFQAENFPKNLELVDKI---------------KAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|....*..
gi 8393646 338 QVlpKLSSSIVHEIDSI 354
Cdd:cd19144 298 KV--KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
40-351 |
3.53e-32 |
|
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: 122.54 E-value: 3.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 40 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVIT 116
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 117 TKI---FWGGKAETERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 193
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 194 EIMEAYSVArqfnlipPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGK-----------YDSGIPP 261
Cdd:cd19145 160 TIRRAHAVH-------PITAvQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKakleellensdVRKSHPR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 262 YSRASLKgyqwlKDKILSEegrrqqaklkELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASNAEQLMENIGAIQVl 340
Cdd:cd19145 232 FQGENLE-----KNKVLYE----------RVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV- 294
|
330
....*....|.
gi 8393646 341 pKLSSSIVHEI 351
Cdd:cd19145 295 -KLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
45-352 |
1.02e-31 |
|
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: 121.19 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLG----TWVtfGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEV---VLGNIIKKKGWRRSSLVITT 117
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 118 KifwGGKAET--ERGLSRKHIIEGLKASLERL-QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 194
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 195 IMEAYSVArqfnliPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPY-SRASLkgyq 271
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGdFRRHL---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 272 wlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV-LLGASNAEQLMENIGAIQVlpKLSSSIVHE 350
Cdd:cd19077 226 ---DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKE 300
|
..
gi 8393646 351 ID 352
Cdd:cd19077 301 IN 302
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
52-352 |
8.15e-30 |
|
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: 114.68 E-value: 8.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergL 131
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPI 211
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 212 CEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkydsgippysraslkgyqwlkdkilseegRRQQAKL 289
Cdd:cd19073 145 VNQVEFHPFlyQAELLEYCRE---NDIVITA--YSPLA-----------------------------------RGEVLRD 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393646 290 KELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19073 185 PVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAIFDW--ELTSEDVAKID 243
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
39-337 |
5.11e-29 |
|
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: 113.80 E-value: 5.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVI 115
Cdd:cd19163 3 YRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 116 TTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVV------FAnrPDPNTPMEETVRAMTHVINQGMAMYWGTS 188
Cdd:cd19163 80 ATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIGIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 189 RWsSMEIMeAYSVARQFNLIPPICEQAEYHMFQREKVEvqLPELFHKIGVGAMTWSPLACGIVSgkyDSGIPPYSRASlk 268
Cdd:cd19163 158 GY-PLDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERGPPDWHPAS-- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 269 gyQWLKDKIlseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAI 337
Cdd:cd19163 229 --PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
46-354 |
5.80e-29 |
|
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: 112.74 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWGGka 125
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 etergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 205
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 206 nlIPPICEQAEYHMF--QRekvevQLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseegr 283
Cdd:cd19140 148 --APLFTNQVEYHPYldQR-----KLLDAAREHGIALTAYSPLARGEV---------------------LKDPV------ 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8393646 284 rqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19140 194 --------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
49-336 |
2.87e-27 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 108.07 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 49 VSCLGLGTWVTFGGQITDEMAEH---LMTL--AYDNGINLFDTAEVYAAGKAEvvlgNIIKK--KGWRrSSLVITTKIFW 121
Cdd:cd19088 1 VSRLGYGAMRLTGPGIWGPPADReeaIAVLrrALELGVNFIDTADSYGPDVNE----RLIAEalHPYP-DDVVIATKGGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 --GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAY 199
Cdd:cd19088 76 vrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 200 SVARqfnlIppICEQAEYHMFQREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkils 279
Cdd:cd19088 156 AIVR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG-------------------------------- 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 280 eeGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19088 196 --GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-342 |
1.04e-26 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 106.84 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTwVTFG---------GQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKgwrrSSLVITTKIfwg 122
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRP-DPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeimeAYSV 201
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS---------VYSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 202 arqfnlippicEQAEYhMFQREKVE-VQLPelfhkigVGAMTWSPLACGIVSGKYDSGIPPYSRaS--LKGYQWLKDKIL 278
Cdd:cd19097 144 -----------EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR-SvfLQGLLLMEPDKL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393646 279 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPK 342
Cdd:cd19097 204 PAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
52-352 |
1.28e-26 |
|
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: 106.03 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 131
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWP-------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKHIIEGLKASLERLQLEYVDVV-----FANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 205
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEGGSKeARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 206 nlIPPICEQAEYHMF--QREkvevqLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGR 283
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKE-----LVEFCKEHGIVVQAYSPLG---------------------------------RGR 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 284 RQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEID 352
Cdd:cd19071 187 RPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
46-355 |
2.50e-26 |
|
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: 107.12 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGT------WVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI 119
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 FWGGK-AETER------GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 192
Cdd:cd19146 87 TTGYRrGGPIKiksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 193 MEIMEAYSVARQFNLIPPICEQAEYHM----FQREKVEVQLPElfhkiGVGAMTWSPLAcgivSGKYDSGIPPYSRASLK 268
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 269 GYQWLKdkilSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIV 348
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEI 308
|
....*..
gi 8393646 349 HEIDSIL 355
Cdd:cd19146 309 QEIEDAY 315
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
39-334 |
7.43e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 103.75 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWvtfGGQITD-EMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITT 117
Cdd:COG1453 3 YRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 118 KIfwggkaeTERGLSRKHIIEGLKASLERLQLEYVDV----------VFANRPDPNTPMEETVRAmthvINQGMAMYWGt 187
Cdd:COG1453 75 KL-------PPWVRDPEDMRKDLEESLKRLQTDYIDLylihglnteeDLEKVLKPGGALEALEKA----KAEGKIRHIG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 188 srWSS-------MEIMEAY---SVARQFNLippiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkyds 257
Cdd:COG1453 143 --FSThgsleviKEAIDTGdfdFVQLQYNY-----------LDQDNQAGEEALEAAAEKGIGVIIMKPLKGG-------- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 258 gippysraslkgyqwlkdkilseegrrqqaKLKELQAIAERLGC---TLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 334
Cdd:COG1453 202 ------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
39-334 |
1.01e-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: 100.63 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTK 118
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IfwggkaeTERglSRKHIIEGLKASLERLQLEYVDVVF----ANRPDPNTPMEEtvramthvinqgmamywgtsrwssME 194
Cdd:cd19100 74 T-------GAR--DYEGAKRDLERSLKRLGTDYIDLYQlhavDTEEDLDQVFGP------------------------GG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 195 IMEAYSVARQFNLIppiceqaeyhmfqrekvevqlpelfHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRAslkgyqwlk 274
Cdd:cd19100 121 ALEALLEAKEEGKI-------------------------RFIGISGHSPEVLLRALETGEFDVVLFPINPA--------- 166
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 275 dkilseeGRRQQAKLKELQAIAERLG------------------CTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENI 334
Cdd:cd19100 167 -------GDHIDSFREELLPLAREKGvgviamkvlaggrllsgdPLDPEQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
38-347 |
1.53e-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: 101.46 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 38 FYRNLGKSGLRVSCLGLGTwVTFGGQITDEM----AEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSL 113
Cdd:cd19153 1 FGETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 114 VITTKIFWGGKAETErgLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRW 190
Cdd:cd19153 80 TVATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 191 sSMEIMEaySVARQFNLIPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsGIPPYSRAS--L 267
Cdd:cd19153 158 -PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPWHPASgeL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 268 KGYQWLKDKILSEEGRrqqaklkelqaiaerlgcTLPQLAIAWCLRNE-GVSSVLLGASNAEQLMENIGAIQVLPKLSSS 346
Cdd:cd19153 232 RHYAAAADAVCASVEA------------------SLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASLGAA 293
|
.
gi 8393646 347 I 347
Cdd:cd19153 294 I 294
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
52-336 |
2.97e-24 |
|
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: 100.90 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTwVTFG--GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI-------FWG 122
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 GKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDP--NTPMEETVRAMTHVINQGM--AMYWGTSRWSsmeim 196
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWA----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 197 EAYSVARQFNLiPPICEQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVsgkyDSGIPPYSRASlkgYQWLKDK 276
Cdd:cd19162 155 ALLRAARRADV-DVVMVAGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAGDRYD---YRPATPE 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 277 ILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19162 226 VL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
39-355 |
1.21e-23 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 99.47 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 39 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 115
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 116 TTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRwSS 192
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITG-LP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 193 MEIMEaYSVARqfnlIPP-----ICEQAEYHMFQREKVEVqLPELFHKiGVGAMTWSPLACGIVSgkyDSGIPPYSRASL 267
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 268 KgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLS--S 345
Cdd:PLN02587 226 E----LK------SACAAAATHCKEK------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGidE 289
|
330
....*....|
gi 8393646 346 SIVHEIDSIL 355
Cdd:PLN02587 290 ELLSEVEAIL 299
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
50-336 |
1.88e-22 |
|
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: 94.94 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTW---VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGgkae 126
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 127 teRGLSRKHIIEGLKASLERLQLEYVDvVFA----NRPD------PNTPMEETVRAMT-----HVinqGMamywgtsrwS 191
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF---------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 S-------MEIMEAYSVArqFNLIPpiceqaeYHMFQREKVEVQ-LPELFHKIGVGAMTWSPLACGivsgkydsgippys 263
Cdd:cd19096 140 FhdspellKEILDSYDFD--FVQLQ-------YNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGG-------------- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393646 264 raslkgyqwlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 336
Cdd:cd19096 197 --------------------GLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
52-339 |
4.36e-22 |
|
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: 94.98 E-value: 4.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTwVTFGG---QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIFWGGKAETE 128
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 129 RGLSRKHII--------------EGLKA----SLERLQLEYVDVVFANRPDPNTPMEET-----------VRAMTHVINQ 179
Cdd:cd19152 80 VEPTFEPGFwnplpfdavfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 180 GMAMYW--GTSRWSSME----------IMeaysVARQFNLIppicEQAEYHMFqrekvevqLPELF-HKIGVgamtwspl 246
Cdd:cd19152 160 GVIKAIglGVNDWEVILrileeadldwVM----LAGRYTLL----DHSAAREL--------LPECEkRGVKV-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 247 acgIVSGKYDSGIppysrasLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 326
Cdd:cd19152 216 ---VNAGPFNSGF-------LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASS 285
|
330
....*....|...
gi 8393646 327 AEQLMENIGAIQV 339
Cdd:cd19152 286 PERVEENVALLAT 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
47-334 |
5.50e-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: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 47 LRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGN----IIKKKGWRRSSLVITTKifwG 122
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 G----------------KAETERGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRP----------DPN 163
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 164 TPMEETVRAMTHVINQGMAMYWGTSRWSsmeIMEAYSVARQFNLIPPICEQAE-----YHMFqreKVeVQLPelFHKIGV 238
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWD---GFRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP--LNLLEP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 239 GAMT----WSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLAIAWCLRN 314
Cdd:cd19099 229 EALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRALQFARST 295
|
330 340
....*....|....*....|
gi 8393646 315 EGVSSVLLGASNAEQLMENI 334
Cdd:cd19099 296 PGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
44-354 |
6.22e-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: 85.93 E-value: 6.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 44 KSGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITT 117
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 118 KIFWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPM------------EETVRAMTHVIN 178
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMengmsihdavdvEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 179 QGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsGKYDSG 258
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------GSPGRA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 259 IPPYSRASLKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENIGAIQ 338
Cdd:cd19154 217 NFTKSTGVSPAPNLLQDPI--------------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENFNIFD 280
|
330
....*....|....*.
gi 8393646 339 VlpKLSSSIVHEIDSI 354
Cdd:cd19154 281 F--SLSEEDMATLEEI 294
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
48-355 |
1.17e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 85.34 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 48 RVSCLGLGTWVTFGG--------QITDEMAEHlmtlaYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGW---RRSSLVIT 116
Cdd:cd19101 1 TISRVINGMWQLSGGhggirdedAAVRAMAAY-----VDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 117 TKIFWGGKAETergLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNtpMEETVRAMTHVINQGMAMYWG-----TS 188
Cdd:cd19101 74 TKWVPDPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqfhWWDYSDPG--YLDAAKHLAELQEEGKIRHLGltnfdTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 189 RWSsmEIMEAysvarqfnLIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY----DSGIPPYSR 264
Cdd:cd19101 149 RLR--EILDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvpEPTGPALET 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 265 ASLKGYQWLKDKILSEEGrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLS 344
Cdd:cd19101 218 RSLQKYKLMIDEWGGWDL--FQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLD 293
|
330
....*....|.
gi 8393646 345 SSIVHEIDSIL 355
Cdd:cd19101 294 DEDRAAIDAVL 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
51-334 |
1.86e-18 |
|
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: 84.11 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 51 CLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVY----AAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAE 126
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 127 TERglsrkhIIEGLKASLERLQLEYVDVVFANRP---DPNT----------------PMEETVRAMTHVINQGMAMYWGT 187
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 188 SRWSSMEIMEAYSVARqfnlIPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgivsGKYDSGippysras 266
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG-------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 267 lkgyqwlKDKILSEegrrqqaklKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASNAEQLMENI 334
Cdd:cd19128 207 -------NLTFLND---------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
54-312 |
1.42e-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: 82.00 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 54 LGTW----------VTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGG 123
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 124 kaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---NTPmeetvramtHVI---NQGMAMYWGTSRWSSMEIME 197
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADverWTP---------ELIpllKSGKVKHVGVSNHNLAEIKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARQFNlIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGYQWLKDK 276
Cdd:cd19103 153 ANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSGRAETYNPLLPQ 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 8393646 277 IlseegRRQQAKLKElqaIAERLGCTLPQLAIAWCL 312
Cdd:cd19103 232 L-----EELTAVMAE---IGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
53-360 |
4.37e-17 |
|
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: 80.35 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 53 GLGTWVTFGGQIT-DEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKaetergl 131
Cdd:cd19120 10 GTGTAWYKSGDDDiQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 srkHIIEGLKASLERLQLEYVDVVFANRP----DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnl 207
Cdd:cd19120 80 ---DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 208 IPPICEQAEYHMFqrekVEVQLPEL--FH-KIGVGAMTWSPLAcgivsgkydsgipPYSRaslkgyqwlkdkilseegRR 284
Cdd:cd19120 153 IKPAVNQIEFHPY----LYPQQPALleYCrEHGIVVSAYSPLS-------------PLTR------------------DA 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8393646 285 QQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIqvLPKLSSSIVHEIDSILGNKPY 360
Cdd:cd19120 198 GGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
50-342 |
5.65e-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: 80.45 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 50 SCLGLGTwVTFGG---QITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIfwgGK-- 124
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 --AETERGL-----------------SRKHIIEGLKASLERLQLEYVDVVF---------ANRPDPN---TPMEETVRAM 173
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 174 THVINQGM--AMYWGTSRWSSM-EIMEAYSVarQFNLIppiceQAEYHMFQREKVEVQLPELfHKIGVGAmtwsplacgI 250
Cdd:cd19161 155 EELKKAGVikAFGLGVNEVQIClEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 251 VSGKYDSGIPPYSRASLKGYQWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQL 330
Cdd:cd19161 218 IGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
330
....*....|...
gi 8393646 331 MENIGAIQ-VLPK 342
Cdd:cd19161 292 RQNVEAFQtDIPE 304
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
44-334 |
7.86e-17 |
|
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: 79.70 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 44 KSGLRVSCLGLGTWVTFGGqitdeMAEHLMTLAYDNGINLFDTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIfW 121
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPG-----VVGNAVKTAIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GGKAETERglsrkhIIEGLKASLERLQLEYVDVVF----------ANRPDP----NTPMEETVRAMTHVINQGMAMYWGT 187
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYLihwpvrlkkgAHMPEPeevlPPDIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 188 SRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsgkydsGIPpysrasl 267
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSP------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 268 kGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNAEQLMENI 334
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 ... |
46-334 |
1.05e-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: 78.77 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITD-EMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSvarq 204
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLIL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 FNLIPPICEQAEYHMFqREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGRR 284
Cdd:cd19133 145 HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA---------------------------------EGRN 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 8393646 285 QQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 334
Cdd:cd19133 189 NLFENPVLTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
52-354 |
1.76e-16 |
|
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: 78.16 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 131
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIP 209
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 210 PICEQAEYhmFQREKVEVQLPElfHKIGVGAmtWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqakl 289
Cdd:cd19139 149 NQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLAYGKV---------------------LDDPV------------ 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 290 keLQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:cd19139 190 --LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
52-334 |
2.56e-16 |
|
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: 77.80 E-value: 2.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 131
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 srkhiiEGLKASLERLQLEYVDVVFANRPdpnTPME----ETVRAMTHVINQGMAMYWGTSRWSS---MEIMEAYSVArq 204
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 fnlipPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyqwLKDKILSEeg 282
Cdd:cd19131 153 -----PVVNQIELHprFQQRE-----LRAFHAKHGIQTESWSPLGQGGL---------------------LSDPVIGE-- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 8393646 283 rrqqaklkelqaIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENI 334
Cdd:cd19131 200 ------------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
46-251 |
5.56e-16 |
|
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: 76.71 E-value: 5.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTFGGqitDEMAEHLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKA 125
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG---DETERAVQT-ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 ETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 205
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 8393646 206 nlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGIV 251
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
45-317 |
1.15e-15 |
|
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: 76.21 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWvtFGGQITDEMAEHLMTlayDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19135 9 NGVEMPILGLGTS--HSGGYSHEAVVYALK---ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTP-------MEETVRAMTHVINQGMAMYWGTSRWSSMEIME 197
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlKDKI 277
Cdd:cd19135 154 LLEDCS----VVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLA--------------------------KGKA 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 8393646 278 LSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 317
Cdd:cd19135 201 LEEP---------TVTELAKKYQKTPAQILIRWSIQNGVV 231
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
46-360 |
1.37e-15 |
|
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: 76.00 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTfggqITDEMAEHLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKI 119
Cdd:cd19111 1 GFPMPVIGLGTYQS----PPEEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 fwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVFAN-------------RPDPNTPMEETVRAMTHVINQGMAMYWG 186
Cdd:cd19111 71 -------PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 187 TSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkyDSGIPPYSR 264
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPLG--------SPGRANQSL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 265 ASLKgYQWLKD-KILseegrrqqaklkelqAIAERLGCTLPQLAIAWCL-RNEGvssVLLGASNAEQLMENIGAIQVlpK 342
Cdd:cd19111 207 WPDQ-PDLLEDpTVL---------------AIAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--E 265
|
330
....*....|....*...
gi 8393646 343 LSSSIVHEIDSILGNKPY 360
Cdd:cd19111 266 LTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
52-334 |
1.61e-15 |
|
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: 75.66 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkAETERGL 131
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKhiIEGLKASLERLQLEYVDVVFANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnLIPP 210
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 211 ICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrQQAK 288
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG-----------------------------------RLLD 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 8393646 289 LKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENI 334
Cdd:cd19134 195 NPAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
52-354 |
1.82e-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: 75.91 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETEr 129
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 130 glsrkHIIEGLKASLERLQLEYVD-------VVF---ANRPDPNT--------PMEETVRAMTHVINQGMAMYWGTSRWS 191
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 192 SMEIMEAYSVARqfnlIPPICEQAEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgivsgkydSGIPPYSRASL 267
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPLG---------SGDRPAAMKAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 268 KGYQWLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNAEQLMENIGAIQVlpKLSSS 346
Cdd:cd19123 222 GEPVLLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDAS 282
|
....*...
gi 8393646 347 IVHEIDSI 354
Cdd:cd19123 283 DMATIAAL 290
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
46-334 |
6.22e-15 |
|
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: 73.84 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggka 125
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 eteRGlsRKH----IIEGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRWSSM---EIME 197
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEhldRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVARQFNLIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPLAcgivsgkydsgippysraslKGYQWLKD 275
Cdd:cd19132 145 ETGVTPAVNQIElhPYFPQAEQRAYHREH------------GIVTQSWSPLG--------------------RGSGLLDE 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 276 KIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENI 334
Cdd:cd19132 193 PV--------------IKAIAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
45-352 |
5.18e-14 |
|
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: 72.16 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLG------TWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK 118
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IFW--------GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 190
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 191 SSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSgiPPYSRASLKGY 270
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGKFQS--KKAVEERKKNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 271 QWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIV 348
Cdd:cd19147 238 EGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEI 315
|
....
gi 8393646 349 HEID 352
Cdd:cd19147 316 EYLE 319
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
52-334 |
6.45e-14 |
|
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: 71.54 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfgGQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAEter 129
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYG-NEAEVgeAIREKIAEGVVKREDLFITTKL-WNSYHE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 130 glsRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPME---------ETVRAMTHVINQGMAMYWGTSRWSSM 193
Cdd:cd19116 85 ---REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 194 EIMEAYSVARqfnlIPPICEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacGIVSGKYDSGIPPYsraslkgyqw 272
Cdd:cd19116 162 QINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPR---------- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393646 273 LKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 334
Cdd:cd19116 222 LDDPT--------------LVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
52-336 |
8.79e-14 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 70.44 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIfWggkaeTERgL 131
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWS------SMEIMEAYSVAR 203
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 204 QfnlippiceQAEYHMF-QREKVEVQLPElfHKIGVGA-MTwspLACGIVsgkydsgippysraslkgyqwLKDKIlsee 281
Cdd:PRK11172 151 N---------QIELSPYlQNRKVVAFAKE--HGIHVTSyMT---LAYGKV---------------------LKDPV---- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 282 grrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNAEQLMENIGA 336
Cdd:PRK11172 192 ----------IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
52-334 |
1.10e-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: 70.35 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEmaEHLMTL---AYDNGINLFDTAEVYaagKAEVVLGNIIK----KKGWRRSSLVITTKIfwgGK 124
Cdd:cd19136 4 LGLGTF-----RLRGE--EEVRQAvdaALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKL---AP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AETERGLSRkhiiEGLKASLERLQLEYVDVVFANRP-----DPNTPME-----ETVRAMTHVINQGMAMYWGTSRW--SS 192
Cdd:cd19136 71 KDQGYEKAR----AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYtvRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 193 MEIMEAYSvarqfnLIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgy 270
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG--------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393646 271 qwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQLMENI 334
Cdd:cd19136 195 ---DLRLLEDP---------TVLAIAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
46-354 |
2.52e-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: 69.86 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTKI 119
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 FWGGkaeterglSRKHIIEG-LKASLERLQLEYVDVVFANRP---------------------DPNTPMEETVRAMTHVI 177
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 178 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIVSGKYD 256
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 257 SGIPPYSRASLkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNAEQLMENiga 336
Cdd:cd19155 224 TGSPSGSSPDL-----LQD--------------PVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKEN--- 279
|
330
....*....|....*....
gi 8393646 337 IQVLP-KLSSSIVHEIDSI 354
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 |
3.52e-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: 3.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 44 KSGLRVSCLGLGTwvtFGGQITDEMAE----HLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKK--KGWRRSSLVITT 117
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 8393646 118 KIfwGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF 156
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
52-249 |
3.71e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.95 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKaetergl 131
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 sRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEETVRAMTHVIN---QGMAMYWGTSRWSS---MEIMEAYSVArqf 205
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 8393646 206 nlipPICEQAEYH--MFQRekvEVQLPELFHKIGVGAmtWSPLACG 249
Cdd:PRK11565 156 ----PVINQIELHplMQQR---QLHAWNATHKIQTES--WSPLAQG 192
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
45-334 |
4.88e-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: 68.45 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGqitDEMAEHLMTLAYDNGINLFDTAEVY----AAGKA--EVVLGNIIKKkgwrRSSLVITTK 118
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS---PEDIKAAVLEAIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 119 IfWGGKAEterglsRKHIIEGLKASLERLQLEYVDV------------VFANRPDPNTP----MEETVRAMTHVINQGMA 182
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLylihwpvslkpgKFSFPIEEEDFlpfdIKGVWEAMEECQRLGLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 183 MYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH-MFQREKvevqLPELFHKIGVGAMTWSPLACgivsgkydsgipp 261
Cdd:cd19124 147 KAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGA------------- 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8393646 262 ysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNAEQLMENI 334
Cdd:cd19124 206 ------PGTKWGSNAVMESD---------VLKEIAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
46-334 |
6.65e-13 |
|
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: 68.20 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWG--G 123
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVAT-----ALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 124 KAETERGLsrkhiieglKASLERLQLEYVDVVFANRPDPNTpMEETV---RAMTHVINQGMAMYWGTSRWSS---MEIME 197
Cdd:cd19127 78 YDKALRGF---------DASLRRLGLDYVDLYLLHWPVPND-FDRTIqayKALEKLLAEGRVRAIGVSNFTPehlERLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 198 AYSVArqfnlipPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcGIVsgKYDSGIPPySRASLkgyqwLKDKI 277
Cdd:cd19127 148 ATTVV-------PAVNQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPT-GPGDV-----LQDPT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 8393646 278 LSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNeGVSSVlLGASNAEQLMENI 334
Cdd:cd19127 209 ITG--------------LAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
46-335 |
4.44e-12 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 65.49 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTW-VTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 204
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 fnlIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEg 282
Cdd:cd19157 150 ---IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG--------------------------QLLDNP- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 8393646 283 rrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIG 335
Cdd:cd19157 195 --------VLKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
45-310 |
4.77e-12 |
|
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: 65.87 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQItdemaEHLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKK-----KGWRRSSLVITTKI 119
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 120 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDV--------------VFANRPDPN-----TPMEETVRAMTHVINQG 180
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDGTirydsTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 181 MAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgivsgkydsGIP 260
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 8393646 261 pySRAslkgyqWLK--DKILSEEGRrqqaklkeLQAIAERLGCTLPQLAIAW 310
Cdd:cd19106 210 --DRP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
45-334 |
4.81e-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: 65.97 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQITDemaehLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWg 122
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKE-----LILNAIKIGYRHFDCAADYK-NEKEVgeALAEAFKTGLVKREDLFITTKL-W- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 gkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP-----------------------DPNTPMEETVRAMTHVINQ 179
Cdd:cd19112 79 ---NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 180 GMAMYWGTSRWSS--MEIMEAYSvarqfnLIPPICEQAEYH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIVSGKYD 256
Cdd:cd19112 152 GLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8393646 257 SGIPPysraslkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNAEQLMENI 334
Cdd:cd19112 222 GSVSP-----------LDDPVLKD--------------LAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
46-333 |
8.29e-11 |
|
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: 61.76 E-value: 8.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITD-EMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 124
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 204
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 205 fnlIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEgr 283
Cdd:cd19156 149 ---VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG--------------------------KLLSNP-- 193
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 8393646 284 rqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMEN 333
Cdd:cd19156 194 -------VLKAIGKKYGKSAAQVIIRWDIQHGII--TIPKSVHEERIQEN 234
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
45-354 |
9.49e-10 |
|
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: 59.05 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGgk 124
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 125 aeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNTP---------------------MEETVRAMTHVINQGMAM 183
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 184 YWGTSRWSSMEIMEAysVARQFNLIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYs 263
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------STNAPLL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 264 raslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNAEQLMENIGAIQvlpkL 343
Cdd:cd19117 219 ------------------------KEPVIIKIAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 8393646 344 SSSIVHEIDSI 354
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
60-341 |
2.98e-09 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 57.47 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 60 FGGQITDEMAEHLMTL-AYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhI 136
Cdd:cd19129 11 FGTLIPDPSATRNAVKaALEAGFRHFDCAERYR-NEAEVgeAMQEVFKAGKIRREDLFVTTKL-WNTNHRPER------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 137 IEGLKASLERLQLEYVDVV-----FANRP---------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 196
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 197 EAYSVARqfnlIPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwLKDK 276
Cdd:cd19129 163 EIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LEDP 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8393646 277 ILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGvsSVLLGASNAEQLMENIGaIQVLP 341
Cdd:cd19129 218 VIT--------------AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLP 265
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
45-193 |
2.58e-08 |
|
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: 54.81 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQ-ITDEMAEHlmtlAYDNGINLFDTAEVYAA----GKAevvLGNIIKKKGWRRSSLVITTKI 119
Cdd:cd19119 8 TGASIPALGLGTASPHEDRaEVKEAVEA----AIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKV 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 120 ---FWggkaeterglsrKHIIEGLKASLERLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSSM 193
Cdd:cd19119 81 wptFY------------DEVERSLDESLKALGLDYVDLLLVHWPVCfEKDSDDSGKPFTPVNDDGKTRYAASGDHITT 146
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
65-339 |
5.39e-08 |
|
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: 53.89 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 65 TDEMAEH---LMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKifWG----------GKAETERGL 131
Cdd:cd19098 30 VEAMRAHthaVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SRKHIIEGLKASLERLQlEYVDV-----------VFANrpdpntpmEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA-- 198
Cdd:cd19098 106 SLARLLKQWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQQAETLRRal 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 199 ---YSVARQFNlippiCEQAEYHMFQREKVEvQLpELFHKIGVGAMTWSPLACGIVSGKYDSGippysraslkgyqwlkd 275
Cdd:cd19098 177 eieIDGARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDRNPSP----------------- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8393646 276 kilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQV 339
Cdd:cd19098 233 --------ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
45-333 |
1.32e-07 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 52.41 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaAGKAEV--VLGNIIKKK-GWRRSSLVITTKIfW 121
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKI-----ALKAGYRHLDLAKVY-QNQHEVgqALKELLKEEpGVKREDLFITSKL-W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GGKAETErglsrkHIIEGLKASLERLQLEYVD-------VVFA--NRPDPNTPME---------------ETVRAMTHVI 177
Cdd:cd19118 76 NNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKptGDLNPLTAVPtnggevdldlsvslvDTWKAMVELK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 178 NQGMAMYWGTSRWSS---MEIMEAYSVArqfnlipPICEQAEYH--MFQREKVEvqlpelFHK---IGVGAmtWSPLacg 249
Cdd:cd19118 150 KTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 250 ivsGKYDSGIPPysraslkgyqwlkdkILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNAEQ 329
Cdd:cd19118 212 ---GNNLAGLPL---------------LVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTPSR 262
|
....
gi 8393646 330 LMEN 333
Cdd:cd19118 263 IRSN 266
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
46-334 |
2.18e-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: 51.79 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK---KGW-RRSSLVITTKIfW 121
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GGKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRP------DP-------------------NTPMEETVRAMTHV 176
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 177 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgivsgKY 255
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 256 DSGIPPYSRASLKGYQwlkdkILSEEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMEN 333
Cdd:cd19114 199 GIQITAYSSFGNAVYT-----KVTKHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTN 271
|
.
gi 8393646 334 I 334
Cdd:cd19114 272 L 272
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
45-246 |
2.87e-07 |
|
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: 51.38 E-value: 2.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYAaGKAEVVLGniIKK---KGWRRSSLVITTKIfW 121
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCYQ-NEDEVGEG--IKEaiaGGVKREDLFVTTKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GgkaetergLSRKHIIEGLKASLERLQLEYVDV----------------VFANRPD------PNTPMEETVRAMTHVINQ 179
Cdd:cd19121 79 S--------TYHRRVELCLDRSLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDgsrdldWDWNHVDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393646 180 GMAMYWGTSRWSSM---EIMEAYSVARQFNLIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPL 246
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
45-339 |
3.43e-07 |
|
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: 51.08 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQITDEMAehlMTLAYDNGINLFDTAEVYAaGKAEV---VLGNIIKKKGWRRSSLVITTKIfW 121
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYL-NEDEVgdaVRDFLKENPSVKREDLFICTKV-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 122 GGKAETErglsrkHIIEGLKASLERLQLEYVDV------VFANRPDPNTPM-----------------EETVRAMTHVIN 178
Cdd:cd19122 80 NHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 179 QGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACgivsgkyDSG 258
Cdd:cd19122 154 SGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------QNQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 259 IPpysraslkgyqwlkdkilsEEGRRQQAKlKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNAEQLMENIGAIQ 338
Cdd:cd19122 220 VP-------------------STGERVSEN-PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 8393646 339 V 339
Cdd:cd19122 278 L 278
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
76-354 |
1.32e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.20 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 76 AYDNGINLFDTAEVYAAGkaevVLGNIIkkkgwR------RSSLVITTKIfwgGKAETERG-----LSRKHIIEGLKASL 144
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 145 ERLQLEYVDVV------FANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnliPPICEQAEYH 218
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 219 MFQREkvEVQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkGYQWLKDKILSeegrrqqaklkelqAIAER 298
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPLG---------------------GFTPLQSSTLS--------------DVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 8393646 299 LGCTLPQLAIAWCLRNEgvSSVLL--GASNAEQLMENIGAIQVlpKLSSSIVHEIDSI 354
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
48-246 |
1.85e-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: 46.11 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 48 RVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIfWGgka 125
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKL-WC--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 126 eterGLSRKHIIE-GLKASLERLQLEYVDVVFANRP------DPNTPMEE-------------TVRAMTHVINQGMAMYW 185
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8393646 186 GTSRWSSmEIMEaySVARQFNL-IPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 246
Cdd:cd19110 149 GVSNFNH-EQLE--RLLNKPGLrVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
45-218 |
5.15e-05 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 44.74 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKaEVVLG--NIIKKKGWRRSSLVITTKIfWG 122
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 123 GKAEterglsRKHIIEGLKASLERLQLEYVDVVF-----ANRPDP--------------------NTPMEETVRAMTHVI 177
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLihfpiAFKFVPieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 8393646 178 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH 218
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHH 190
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
52-249 |
3.91e-04 |
|
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: 41.43 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWvtfggQITDEMAEHLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 131
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 132 SrkhiieGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEAYSVarqfnlI 208
Cdd:cd19130 84 A------AFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG------V 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 8393646 209 PPICEQAEYHMF--QREKVEVQlpelfHKIGVGAMTWSPLACG 249
Cdd:cd19130 152 VPAVNQIELHPAyqQRTIRDWA-----QAHDVKIEAWSPLGQG 189
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
45-218 |
4.82e-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: 41.64 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 45 SGLRVSCLGLGTWVTFGGQITDEMAEhlmtlAYDNGINLFDTAEVYA----AGKAevvLGNIIKKKGWRRSSLVITTKIf 120
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYN-----AIKAGYRLFDGACDYGneveAGQG---VARAIKEGIVKREDLFIVSKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 121 WGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP------DP------------------NTPMEETVRAMTHV 176
Cdd:cd19115 80 WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvDPavryppgwfydgkkvefsNAPIQETWTAMEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 8393646 177 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlIPPICEQAEYH 218
Cdd:cd19115 154 VDKGLARSIGVSNFSAQLLMDLLRYAR----IRPATLQIEHH 191
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
46-195 |
4.99e-04 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 41.63 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 46 GLRVSCLGLGTWVTFGGQITDEMAehlmtLAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIFwgg 123
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 124 KAETERGLSRkhiiEGLKASLERLQLEYVDVVFANRPD-------------------PNTPMEETVRAMTHVINQGMAMY 184
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKA 147
|
170
....*....|.
gi 8393646 185 WGTSRWSSMEI 195
Cdd:cd19107 148 IGVSNFNHLQI 158
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
52-168 |
1.31e-03 |
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AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 40.29 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8393646 52 LGLGTWVTfgGQITDEMAEHLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 127
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
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90 100 110 120
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gi 8393646 128 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPDPNTPMEE 168
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEE 122
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