|
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 ... |
25-333 |
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: 671.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 104
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 184
Cdd:cd19141 82 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 185 YSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKIL 264
Cdd:cd19141 162 YSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKIL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 265 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSI 333
Cdd:cd19141 242 SEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
23-346 |
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 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 182
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 262
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 263 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILG 342
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 27436969 343 NKPY 346
Cdd:cd19158 321 NKPY 324
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
23-345 |
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: 650.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 182
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 262
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 263 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILG 342
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 27436969 343 NKP 345
Cdd:cd19159 321 NKP 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
25-341 |
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: 641.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 104
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 184
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 185 YSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKIL 264
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 265 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSIL 341
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
22-345 |
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: 632.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 22 GMIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 101
Cdd:cd19160 2 GMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 102 TTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 181
Cdd:cd19160 82 TTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 182 MEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKD 261
Cdd:cd19160 162 MEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 262 KILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSIL 341
Cdd:cd19160 242 KVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALL 321
|
....
gi 27436969 342 GNKP 345
Cdd:cd19160 322 GNKP 325
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
23-340 |
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 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 180
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 181 IMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLK 260
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 261 DkILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSI 340
Cdd:cd19143 241 D-RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
23-345 |
2.89e-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: 474.26 E-value: 2.89e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWGGKAEtERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 182
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGY-----Q 257
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSkykvgS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 258 WLKDKIlsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEI 337
Cdd:cd19142 240 DGNGIH--EETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEEL 317
|
....*...
gi 27436969 338 DSILGNKP 345
Cdd:cd19142 318 ERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
32-333 |
2.07e-167 |
|
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: 468.22 E-value: 2.07e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFWGGKA 111
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 E-TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQ 190
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 FNLTPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKgYQWLKDKILSEEGRR 270
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436969 271 QQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAiqVLPKLSSSI 333
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
23-345 |
1.05e-105 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 312.50 E-value: 1.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWvTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSL 99
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 100 VITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 178
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 179 MEIMEAYSVARqfNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG--IPPYSRASLKGY 256
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 257 QWlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHE 336
Cdd:COG0667 235 QG-------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
....*....
gi 27436969 337 IDSILGNKP 345
Cdd:COG0667 306 LDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
23-340 |
3.42e-95 |
|
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: 285.62 E-value: 3.42e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVIT 102
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWG-GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 181
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 182 MEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP--YSRASLKGYQwl 259
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPesGRLVERARYQ-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 260 kDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDS 339
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDE 307
|
.
gi 27436969 340 I 340
Cdd:cd19087 308 L 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
23-340 |
1.51e-84 |
|
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: 258.70 E-value: 1.51e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTwVTFG---------GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkg 93
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 94 wRRSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWG 172
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 173 TSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPYSR 250
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 251 ASLKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLS 330
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLT 308
|
330
....*....|
gi 27436969 331 SSIIHEIDSI 340
Cdd:cd19091 309 PEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
25-327 |
2.46e-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: 257.96 E-value: 2.46e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVY--AAGKAEVVLGNIIKK-KGWRRSSLVI 101
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 102 TTKI---FWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 178
Cdd:cd19089 81 STKAgygMWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 179 MEIMEAYSVARQFNlTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRAsLKGYQW 258
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 259 LKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLP 327
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
32-338 |
2.33e-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: 244.74 E-value: 2.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWV---TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IF 106
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 107 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAys 186
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 187 varqFNLTPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSG--IPPY-SRASLKGYQwlkdki 263
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLPYC-RENGIGVLPYGPLAQGLLTGKYKKEptFPPDdRRSRFPFFR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 264 lSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
24-324 |
6.47e-76 |
|
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: 236.15 E-value: 6.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 24 IYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKK--KGWRrSSL 99
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 100 VITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 176
Cdd:cd19151 80 IISTKagyTMWPGPY-GDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 177 SSMEIMEAYSVARQFNlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKGY 256
Cdd:cd19151 158 PPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 257 QWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 324
Cdd:cd19151 235 SFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
36-321 |
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: 232.79 E-value: 1.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTWvTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI-FWGGKAETE 114
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 115 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLT 194
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 195 PPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrqqak 274
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27436969 275 lkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 321
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
25-330 |
7.73e-75 |
|
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: 233.63 E-value: 7.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWvTFGGQ------ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSS 98
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 99 LVITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 177
Cdd:cd19079 80 VVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 178 SMEIMEAYSVARQFNLTPPICEQAEYHMFQREKvEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGY 256
Cdd:cd19079 160 AWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436969 257 QWLKdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLS 330
Cdd:cd19079 239 KYDY---FTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLS 304
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
28-338 |
1.85e-74 |
|
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: 232.49 E-value: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 28 LGKSGLRVSCLGLGTWVtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSLV 100
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 101 ITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 180
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 181 IMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPySRASLKGYQWlk 260
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADL-PGSTRRGEAA-- 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 261 DKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19081 236 KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
38-341 |
2.18e-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: 218.72 E-value: 2.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvTFGGQ---ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETE 114
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 115 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlT 194
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 195 PPICEQAEYHMFqREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQAK 274
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG--------ERRRLLKKGTPLNLEA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 275 LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQvlPKLSSSIIHEIDSIL 341
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
24-326 |
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: 217.71 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 24 IYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLV 100
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 101 ITTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 177
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 178 SMEIMEAYSVARQFNlTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYq 257
Cdd:cd19150 159 PERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 258 wLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVL 326
Cdd:cd19150 237 -LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
35-340 |
1.07e-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: 215.89 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 35 VSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-- 105
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 ---FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTP------------------MEETVRAMTHVIN 164
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 165 QGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG 244
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 245 --IPPYSRASL-KGYQwlkdkilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLM 317
Cdd:cd19094 238 aaRPEGGRLNLfPGYM----------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|...
gi 27436969 318 ENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:cd19094 308 ENIDAFDV--PLSDELLAEIDAV 328
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
23-338 |
5.67e-64 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 206.76 E-value: 5.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSL 99
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 100 VITTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 176
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 177 SSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKG- 255
Cdd:PRK09912 171 SPERTQKMVELLREWKI-PLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGn 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 256 -YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLpKLSSSII 334
Cdd:PRK09912 250 kVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL-TFSTEEL 325
|
....
gi 27436969 335 HEID 338
Cdd:PRK09912 326 AQID 329
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
28-338 |
9.35e-59 |
|
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: 192.05 E-value: 9.35e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 28 LGKSGLRVSCLGLGTwVTFGGQ----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITT 103
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 104 KIFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEI 181
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 182 MEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGipPYSRASLKGYQWLKD 261
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 262 KILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19080 236 GKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
35-340 |
1.05e-56 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 186.25 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 35 VSCLGLGTWV----TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFwggk 110
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 aetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 190
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 fnltpPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKgyqwlkdkILSEE 267
Cdd:cd19085 150 -----IDSNQLPYNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDARTRLF--------RHFEP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 268 GRRQQAK--LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:cd19085 216 GAEEETFeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
25-339 |
3.58e-51 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 172.46 E-value: 3.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWV----TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 100
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 101 ITTK--IFWGGKAETE----------RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMA 168
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 169 MYWGTSRWSSMEIMEAYSVArqfnlTPPICeQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSGKYDSGippy 248
Cdd:cd19149 158 RAIGASNVSVEQIKEYVKAG-----QLDII-QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPD---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 249 sRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlp 327
Cdd:cd19149 227 -REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI-- 303
|
330
....*....|..
gi 27436969 328 KLSSSIIHEIDS 339
Cdd:cd19149 304 RLSAEDIATMRS 315
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
26-340 |
1.47e-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: 170.68 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 26 RNLGKSGLRVSCLGLGTwVTFGGQ-----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLV 100
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 101 ITTK---IFWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 177
Cdd:cd19083 79 IATKgahKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 178 SMEIMEAySVARQFNLTppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSGIppysraSLKGYQ 257
Cdd:cd19083 157 LEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 258 WLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIH 335
Cdd:cd19083 224 LRNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIA 301
|
....*
gi 27436969 336 EIDSI 340
Cdd:cd19083 302 FIDAL 306
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
25-337 |
1.65e-49 |
|
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: 167.78 E-value: 1.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLG----TWvtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 100
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 101 ITTKifWG---GKAETERGL--SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSR 175
Cdd:cd19076 77 IATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 176 WSSMEIMEAYSVArqfnltpPICE-QAEYHMFQREKVEVQLP---ELfhkiGVGAMTWSPLACGIVSGKYDSgippysra 251
Cdd:cd19076 155 ASADTIRRAHAVH-------PITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 252 slkgyqwlKDKILSEEGRRQQ-----------AKL-KELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASNADQLME 318
Cdd:cd19076 216 --------PEDLPEDDFRRNNprfqgenfdknLKLvEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEE 286
|
330
....*....|....*....
gi 27436969 319 NIGAIQVlpKLSSSIIHEI 337
Cdd:cd19076 287 NVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
32-341 |
1.23e-48 |
|
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: 165.48 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTW-VTFG-GQITD--EMAEqLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFW 107
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkeEMIE-LIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 ----GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 183
Cdd:cd19078 77 kidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AYSVarqfnlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKGYqwlk 260
Cdd:cd19078 157 AHAV------CPVTAVQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 261 dkilSEEGRRQQAKLKEL-QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDS 339
Cdd:cd19078 226 ----TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIED 299
|
..
gi 27436969 340 IL 341
Cdd:cd19078 300 AL 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
34-338 |
3.05e-48 |
|
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: 164.32 E-value: 3.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 34 RVSCLGLGTWvTFGGQI----TDEMAEQLMT---LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIf 106
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgyGEYGDEDLQAafdAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 107 wggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETV-RAMTHVINQGMAMYWGTSRWSSMEIMEAY 185
Cdd:cd19093 78 ----APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 186 SVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY-DSGIPPYSRASLKG-YQWLKDKI 263
Cdd:cd19093 154 KALKERGV-PLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGRRRLFGrKNLEKVQP 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 264 LseegrrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19093 233 L----------LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
35-341 |
6.38e-48 |
|
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: 163.61 E-value: 6.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 35 VSCLGLGTWVTFGGQI---------TDEMAeqLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSsLVITTK- 104
Cdd:cd19102 1 LTTIGLGTWAIGGGGWgggwgpqddRDSIA--AIRAALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 183
Cdd:cd19102 76 gLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AYSVARQFNLTPPiceqaeYHMFQREKVEVQLPelF---HKIGVgaMTWSPLACGIVSGKYDsgipPYSRASLKGYQWLK 260
Cdd:cd19102 156 CQAIHPIASLQPP------YSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT----PERVASLPADDWRR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 261 -DKILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIE 299
|
...
gi 27436969 339 SIL 341
Cdd:cd19102 300 ALL 302
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
38-340 |
7.95e-47 |
|
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: 160.80 E-value: 7.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIikkkGWRRSSLVITTKI-FWGGKaeterG 116
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKAnPGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 117 LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPP 196
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 197 ICEQAEYHMFQReKVEvqlPELF-----HKIGVGAmtWSPLACGIVSGKYDSG--IPPYSR--ASLKGYQWLKDKILSEE 267
Cdd:cd19075 156 TVYQGMYNAITR-QVE---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdPNNALGKLYRDRYWKPS 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 268 grrQQAKLKELQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASNADQLMENIGAIQVLPkLSSSIIHEIDSI 340
Cdd:cd19075 230 ---YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGP-LPEEVVKAIDEA 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
33-322 |
1.01e-46 |
|
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: 158.79 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 33 LRVSCLGLGTWV---TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI--FW 107
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeiMEAYS 186
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVS-------VGDPE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 187 VARQFNLTPPI-CEQAEYHMFQREKVEvqlpELFHKI---GVGAMTWSPLACGIVSGKydsgippysraslkgyqwlkdk 262
Cdd:cd19086 151 EALAALRRGGIdVVQVIYNLLDQRPEE----ELFPLAeehGVGVIARVPLASGLLTGK---------------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 263 ilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19086 205 --------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
32-324 |
2.85e-45 |
|
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: 155.85 E-value: 2.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVTFGGQ----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFw 107
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 ggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSV 187
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 188 ARQfnlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSgippysraslkgyqwlkdkilsee 267
Cdd:cd19072 152 LKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS------------------------ 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 268 grrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNADQLMENIGAIQ 324
Cdd:cd19072 204 --------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
36-322 |
1.03e-40 |
|
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: 144.62 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA----GKAEVVLGNIIKKKGwRRSSLVITTKifwGG-- 109
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 110 ---KAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYS 186
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 187 VARQFNLTPPICEQAEYHMFqrEKVEVQLP------------ELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslk 254
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSE---- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 255 gyqwLKDKILSEEGRRQQAKLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19082 229 ----LRRVYYSEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
36-322 |
4.28e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 142.86 E-value: 4.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI--- 105
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 --FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 183
Cdd:cd19752 79 prDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AYSVARQFNLTPPICEQAEYHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLacgiVSGKYDSgippysrasl 253
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPL----LSGAYTR---------- 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436969 254 kgyqwlKDKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19752 225 ------PDRPLPEQYDGPdsDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
23-340 |
7.71e-39 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 141.14 E-value: 7.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwR 95
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 96 RSSLVITTKIfwGGKAET-------ERGLSRKHIIEGLKASLERLQLEYVD---VVFANRPD--------------PNTP 151
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPTncfgklgyswtdsaPAVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 152 MEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSP 231
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 232 LACGIVSGKYDSGIPPY-SRASLKgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGA 310
Cdd:PRK10625 236 LAFGTLTGKYLNGAKPAgARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|
gi 27436969 311 SNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:PRK10625 310 TTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
23-323 |
2.12e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 137.33 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGlgtwvtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVIT 102
Cdd:cd19105 1 MPYRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKIFWGGKAETerglsRKHIIEGLKASLERLQLEYVDVVF---ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 179
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 180 E--IMEA-----YSVAR-QFNltppiceqaeyHMFQREKVEVQLPELfHKIGVG--AMtwsplacgivsgkydsgippys 249
Cdd:cd19105 148 AevLQAAiesgwFDVIMvAYN-----------FLNQPAELEEALAAA-AEKGIGvvAM---------------------- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436969 250 raslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 323
Cdd:cd19105 194 ------------KTLA-GGYLQPALLSVLKA----KGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-340 |
3.07e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 138.94 E-value: 3.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGtwvtfGGQI-----TDEMAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRS 97
Cdd:cd19104 2 YRRFGRTGLKVSELTFG-----GGGIgglmgRTTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 98 SLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF------ANRPDPNTPM---------EETVRAMTHV 162
Cdd:cd19104 74 GPYITTKV---RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQlhnrigDERDKPVGGTlsttdvlglGGVADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 163 INQGMAMYWGTSRWSSMEIME------AYSVARQF-NL--------TPPICEQAEYHmfqrekvevQLPELFHKIGVGAM 227
Cdd:cd19104 151 RSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVYyNLlnpsaaeaRPRGWSAQDYG---------GIIDAAAEHGVGVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 228 TWSPLACGIVSGKYDSGIPPYSRAslkgyqwlkDKILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVL 307
Cdd:cd19104 222 GIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVSTVL 288
|
330 340 350
....*....|....*....|....*....|...
gi 27436969 308 LGASNADQLMENIGAIQVLPkLSSSIIHEIDSI 340
Cdd:cd19104 289 VGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
31-338 |
2.32e-37 |
|
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: 135.07 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWvtFGGQITDEMAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIfWG 108
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV-LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 GKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDpNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVA 188
Cdd:cd19138 81 SNA------SRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 189 RQFNLTppiCEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilsEEG 268
Cdd:cd19138 154 GGGNCA---ANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG------------------------------GLL 199
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 269 RRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVlLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19138 200 RRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
31-340 |
2.90e-37 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 134.41 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 110
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 AeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 190
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 fnlTPPICEQAEYHMFQREkvevqlPELF-----HKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILS 265
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELLafcreHGIVVEA--YSPLGRG--------------------------KLLD 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 266 EEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:COG0656 187 DP---------VLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
32-325 |
7.33e-37 |
|
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: 133.46 E-value: 7.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvTFGGQIT-----DEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIF 106
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 107 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYS 186
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 187 VARqfnlTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwlkdkilse 266
Cdd:cd19137 151 KSQ----TPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN-------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 267 egrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLgASNADQLMENIGAIQV 325
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
32-341 |
1.10e-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: 134.36 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVT----FGGqiTDEmAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK- 104
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWsSMEIME 183
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNF-SPEQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AY-SVARQFNLTPPiceqaeYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKY--DSGIPPYS-RASLKGYQwl 259
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPYA-RKHNIVTLAYGALCRGLLSGKMtkDTKFEGDDlRRTDPKFQ-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 260 kdkilseEGRRQQ--AKLKELQAIA-ERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHE 336
Cdd:cd19148 227 -------EPRFSQylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGW--SLNDEDMKE 297
|
....*
gi 27436969 337 IDSIL 341
Cdd:cd19148 298 IDAIL 302
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
30-325 |
8.39e-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: 131.52 E-value: 8.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 30 KSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK---IF 106
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 107 WGGKAETERG---LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeime 183
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVS--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 aysvarqfNLTPpiceqAEYHMFQRekvevqlpELFHKIGVGAMTWSPLACGIVsgkyDSGIPPYSRasLKGYQWL---- 259
Cdd:cd19092 152 --------NFTP-----SQIELLQS--------YLDQPLVTNQIELSLLHTEAI----DDGTLDYCQ--LLDITPMawsp 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 260 --KDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 325
Cdd:cd19092 205 lgGGRLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
38-324 |
3.90e-35 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 129.60 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGT-WVTFG-GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKIfwGGKAETER 115
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 116 GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEET-----VRAMTHVINQGMAMYWGTSRWSSMEIMEA-----Y 185
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPDLLRRAietgdF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 186 SVARQFNltppiceqaEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSGKYDSGIPPysraslkGYQWLKDkils 265
Cdd:cd19090 157 DVVLTAN---------RYTLLDQSAADELLP-AAARHGVGVINASPLGMGLLAGRPPERVRY-------TYRWLSP---- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 266 eegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 324
Cdd:cd19090 216 ----ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
36-322 |
5.05e-35 |
|
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: 128.51 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTWVTFG--GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKkkGWRRSSLVITTKI--FWGGkA 111
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 ETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRwSSMEIMEAYSvarqf 191
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIA----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 192 nlTPPI-CEQAEYHMFQREKVEVqLPELfHKIGVGAMTWSPLAcgivsgkydSGIPPYSRASLKGYQWLKDKilseegrr 270
Cdd:cd19095 150 --SGVFdVVQLPYNVLDREEEEL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPLYADYARR-------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27436969 271 qqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19095 209 -------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
23-299 |
8.56e-35 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 129.12 E-value: 8.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TK--IFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 176
Cdd:COG4989 81 TKcgIRLPSEARDNRVkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 177 SSMeimeaysvarQFNL------TPPICEQAEYHMFQREKVE------VQLpelfHKIGVgaMTWSPLAcgivSGKYDSG 244
Cdd:COG4989 161 TPS----------QFELlqsaldQPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLA----GGRLFGG 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 245 ippysraslkgyqwlkdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLR 299
Cdd:COG4989 221 -------------------FDEQFPRLRAALDE---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
26-340 |
1.43e-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: 126.40 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 26 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVIT 102
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKifWGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 177
Cdd:cd19144 82 TK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 178 SMEIMEAYSVArqfnltpPICE-QAEYHMF--QREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS----------- 243
Cdd:cd19144 160 AETLRRAHAVH-------PIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpddfeegdfrr 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 244 GIPPYSRASLKGYQWLKDKIlseegrrqqaklkelQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 323
Cdd:cd19144 233 MAPRFQAENFPKNLELVDKI---------------KAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGAL 297
|
330
....*....|....*..
gi 27436969 324 QVlpKLSSSIIHEIDSI 340
Cdd:cd19144 298 KV--KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
26-337 |
9.97e-33 |
|
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: 123.70 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 26 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVIT 102
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 103 TKI---FWGGKAETERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 179
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 180 EIMEAYSVArqfnltpPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGK-----------YDSGIPP 247
Cdd:cd19145 160 TIRRAHAVH-------PITAvQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKakleellensdVRKSHPR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 248 YSRASLKgyqwlKDKILSEegrrqqaklkELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASNADQLMENIGAIQVl 326
Cdd:cd19145 232 FQGENLE-----KNKVLYE----------RVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV- 294
|
330
....*....|.
gi 27436969 327 pKLSSSIIHEI 337
Cdd:cd19145 295 -KLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
31-338 |
7.17e-32 |
|
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: 7.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLG----TWVtfGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEV---VLGNIIKKKGWRRSSLVITT 103
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 104 KifwGGKAET--ERGLSRKHIIEGLKASLERL-QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME 180
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 181 IMEAYSVArqfnltPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPY-SRASLkgyq 257
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGdFRRHL---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 258 wlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV-LLGASNADQLMENIGAIQVlpKLSSSIIHE 336
Cdd:cd19077 226 ---DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKE 300
|
..
gi 27436969 337 ID 338
Cdd:cd19077 301 IN 302
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
38-322 |
1.50e-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: 116.22 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergL 117
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPI 197
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 198 CEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkydsgippysraslkgyqwlkdkilseegRRQQAKL 275
Cdd:cd19073 145 VNQVEFHPFlyQAELLEYCRE---NDIVITA--YSPLA-----------------------------------RGEVLRD 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27436969 276 KELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENIGA 322
Cdd:cd19073 185 PVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
23-323 |
3.64e-30 |
|
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: 116.50 E-value: 3.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSL 99
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 100 VITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVV------FAnrPDPNTPMEETVRAMTHVINQGMAMYWG 172
Cdd:cd19163 78 YLATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 173 TS-------RwssmEIMEAYSVARQFNLTppiceQAEYHMFQREKVEvqLPELFHKIGVGAMTWSPLACGIVSgkyDSGI 245
Cdd:cd19163 156 ITgypldvlK----EVLERSPVKIDTVLS-----YCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERGP 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 246 PPYSRASlkgyQWLKDKIlseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 323
Cdd:cd19163 222 PDWHPAS----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
32-340 |
2.05e-28 |
|
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: 110.81 E-value: 2.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGka 111
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 etergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqf 191
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELS--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 192 nlTPPI-CEQAEYHMF--QRekvevQLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseeg 268
Cdd:cd19140 147 --EAPLfTNQVEYHPYldQR-----KLLDAAREHGIALTAYSPLARGEV---------------------LKDPV----- 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436969 269 rrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:cd19140 194 ---------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
35-322 |
1.61e-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: 108.46 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 35 VSCLGLGTW-----VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEvvlgNIIKK--KGWRrSSLVITTKIFW 107
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNE----RLIAEalHPYP-DDVVIATKGGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 --GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAY 185
Cdd:cd19088 76 vrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 186 SVARqfnltppI-CEQAEYHMFQREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkil 264
Cdd:cd19088 156 AIVR-------IvSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG------------------------------- 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 265 seeGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19088 196 ---GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
23-320 |
1.62e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.68 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 23 MIYRNLGKSGLRVSCLGLGTWvtfGGQITD-EMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVI 101
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 102 TTKIfwggkaeTERGLSRKHIIEGLKASLERLQLEYVDV----------VFANRPDPNTPMEETVRAmthvINQGMAMYW 171
Cdd:COG1453 73 ATKL-------PPWVRDPEDMRKDLEESLKRLQTDYIDLylihglnteeDLEKVLKPGGALEALEKA----KAEGKIRHI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 172 GtsrWSS-------MEIMEAY---SVARQFNLtppiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgky 241
Cdd:COG1453 142 G---FSThgsleviKEAIDTGdfdFVQLQYNY-----------LDQDNQAGEEALEAAAEKGIGVIIMKPLKGG------ 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 242 dsgippysraslkgyqwlkdkilseegrrqqaKLKELQAIAERLGC---TLPQLAIAWCLRNEGVSSVLLGASNADQLME 318
Cdd:COG1453 202 --------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDE 249
|
..
gi 27436969 319 NI 320
Cdd:COG1453 250 NL 251
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
32-341 |
2.40e-27 |
|
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: 109.82 E-value: 2.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGT------WVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI 105
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 FWGGK-AETER------GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSS 178
Cdd:cd19146 87 TTGYRrGGPIKiksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 179 MEIMEAYSVARQFNLTPPICEQAEYHM----FQREKVEVQLPElfhkiGVGAMTWSPLAcgivSGKYDSGIPPYSRASLK 254
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 255 GYQWLKdkilSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSII 334
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEI 308
|
....*..
gi 27436969 335 HEIDSIL 341
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-328 |
1.93e-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: 105.69 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTwVTFG---------GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKgwrrSSLVITTKIfwg 108
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRP-DPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeimeAYSV 187
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS---------VYSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 188 arqfnltppicEQAEYhMFQREKVE-VQLPelfhkigVGAMTWSPLACGIVSGKYDSGIPPYSRaS--LKGYQWLKDKIL 264
Cdd:cd19097 144 -----------EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR-SvfLQGLLLMEPDKL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436969 265 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPK 328
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 ... |
38-338 |
3.04e-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: 104.87 E-value: 3.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 117
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWP-------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SRKHIIEGLKASLERLQLEYVDVV-----FANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 191
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEGGSKeARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 192 nlTPPICEQAEYHMF--QREkvevqLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGR 269
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKE-----LVEFCKEHGIVVQAYSPLG---------------------------------RGR 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 270 RQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 338
Cdd:cd19071 187 RPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
25-320 |
1.04e-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: 100.25 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTWVTfgGQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTK 104
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 IfwggkaeTERglSRKHIIEGLKASLERLQLEYVDVVF----ANRPDPNTPMEE--------------TVRAM---TH-- 161
Cdd:cd19100 74 T-------GAR--DYEGAKRDLERSLKRLGTDYIDLYQlhavDTEEDLDQVFGPggalealleakeegKIRFIgisGHsp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 162 -VINQGMAMYWgtsrwssMEIMeaysvarQFNLTPpiceqAEYHMfqREKVEVQLPEL-FHKIGVGAMtwSPLACGivsg 239
Cdd:cd19100 145 eVLLRALETGE-------FDVV-------LFPINP-----AGDHI--DSFREELLPLArEKGVGVIAM--KVLAGG---- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 240 kydsgippysraslkgyQWLKDKILSeegrrqqaklkelqaiaerlgctlPQLAIAWCLRNEGVSSVLLGASNADQLMEN 319
Cdd:cd19100 198 -----------------RLLSGDPLD------------------------PEQALRYALSLPPVDVVIVGMDSPEELDEN 236
|
.
gi 27436969 320 I 320
Cdd:cd19100 237 L 237
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
38-322 |
1.23e-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: 101.67 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTwVTFG--GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI-------FWG 108
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 GKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDP--NTPMEETVRAMTHVINQGM--AMYWGTSRWSsmeim 182
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWA----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARQFNLTPpICEQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVsgkyDSGIPPYSRASlkgYQWLKDK 262
Cdd:cd19162 155 ALLRAARRADVDV-VMVAGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAGDRYD---YRPATPE 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 263 ILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19162 226 VL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
26-333 |
2.01e-24 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 101.07 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 26 RNLGKSGLRVSCLGLGTwVTFGGQITDEM----AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 101
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 102 TTKIFWGGKAETErgLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRWsS 178
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 179 MEIMEaySVARQFNLTPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsGIPPYSRAS--LKG 255
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPWHPASgeLRH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 256 YQWLKDKILSEEGRrqqaklkelqaiaerlgcTLPQLAIAWCLRNE-GVSSVLLGASNADQLMENIGAIQVLPKLSSSI 333
Cdd:cd19153 234 YAAAADAVCASVEA------------------SLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASLGAAI 294
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
25-341 |
1.80e-23 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 98.70 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 25 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 101
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 102 TTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRwSS 178
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITG-LP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 179 MEIMEaYSVARqfnlTPP-----ICEQAEYHMFQREKVEVqLPELFHKiGVGAMTWSPLACGIVSgkyDSGIPPYSRASL 253
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 254 KgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLS--S 331
Cdd:PLN02587 226 E----LK------SACAAAATHCKEK------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGidE 289
|
330
....*....|
gi 27436969 332 SIIHEIDSIL 341
Cdd:PLN02587 290 ELLSEVEAIL 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
33-320 |
6.71e-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: 94.31 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 33 LRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGN----IIKKKGWRRSSLVITTKifwG 108
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 G----------------KAETERGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRP----------DPN 149
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 150 TPMEETVRAMTHVINQGMAMYWGTSRWSsmeIMEAYSVARQFNLTPPICEQAE-----YHMFqreKVeVQLPelFHKIGV 224
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWD---GFRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP--LNLLEP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 225 GAMT----WSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLAIAWCLRN 300
Cdd:cd19099 229 EALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRALQFARST 295
|
330 340
....*....|....*....|
gi 27436969 301 EGVSSVLLGASNADQLMENI 320
Cdd:cd19099 296 PGVDSALVGMRRPEHVDENL 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
36-322 |
8.04e-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: 93.01 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGgkae 112
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 113 teRGLSRKHIIEGLKASLERLQLEYVDvVFA----NRPD------PNTPMEETVRAMThvinQGMAMYWGTSRWSSMEIM 182
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKK----EGLIRHIGFSFHDSPELL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARQFNltppICeQAEYHMFQREKVEVQ-LPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkd 261
Cdd:cd19096 148 KEILDSYDFD----FV-QLQYNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGG-------------------------- 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436969 262 kilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 322
Cdd:cd19096 197 --------GLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
38-325 |
1.34e-21 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 93.44 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTwVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIFWGGKAETE 114
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 115 RGLSRKHII--------------EGLKA----SLERLQLEYVDVVFANRPDPNTPMEET-----------VRAMTHVINQ 165
Cdd:cd19152 80 VEPTFEPGFwnplpfdavfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 166 GMAMYW--GTSRWSSME----------IMeaysVARQFNLTppicEQAEYHMFqrekvevqLPELF-HKIGVgamtwspl 232
Cdd:cd19152 160 GVIKAIglGVNDWEVILrileeadldwVM----LAGRYTLL----DHSAAREL--------LPECEkRGVKV-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 233 acgIVSGKYDSGIppysrasLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 312
Cdd:cd19152 216 ---VNAGPFNSGF-------LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASS 285
|
330
....*....|...
gi 27436969 313 ADQLMENIGAIQV 325
Cdd:cd19152 286 PERVEENVALLAT 298
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
30-340 |
8.03e-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: 85.54 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 30 KSGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITT 103
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 104 KIFWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPM------------EETVRAMTHVIN 164
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMengmsihdavdvEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 165 QGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsGKYDSG 244
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------GSPGRA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 245 IPPYSRASLKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQ 324
Cdd:cd19154 217 NFTKSTGVSPAPNLLQDPI--------------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENFNIFD 280
|
330
....*....|....*.
gi 27436969 325 VlpKLSSSIIHEIDSI 340
Cdd:cd19154 281 F--SLSEEDMATLEEI 294
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-298 |
6.99e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.77 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 40 LGTW----------VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGG 109
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 110 kaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---NTPmeetvramtHVI---NQGMAMYWGTSRWSSMEIME 183
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADverWTP---------ELIpllKSGKVKHVGVSNHNLAEIKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGYQWLKDK 262
Cdd:cd19103 153 ANEILAKAGV-SLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSGRAETYNPLLPQ 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 27436969 263 IlseegRRQQAKLKElqaIAERLGCTLPQLAIAWCL 298
Cdd:cd19103 232 L-----EELTAVMAE---IGAKHGASIAQVAIAWAI 259
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
37-320 |
1.30e-17 |
|
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: 81.80 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 37 CLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVY----AAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAE 112
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 113 TERglsrkhIIEGLKASLERLQLEYVDVVFANRP---DPNT----------------PMEETVRAMTHVINQGMAMYWGT 173
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 174 SRWSSMEIMEAYSVARqfnlTPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgivsGKYDSGippysras 252
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG-------- 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 253 lkgyqwlKDKILSEegrrqqaklKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASNADQLMENI 320
Cdd:cd19128 207 -------NLTFLND---------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
36-328 |
1.61e-17 |
|
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium luteolum PLD (EC1.1.1.107) is a founding member of aldo-keto reductase family 15 member A1 (AKR15A1). It catalyzes irreversible oxidation of pyridoxal.
Pssm-ID: 381387 [Multi-domain] Cd Length: 310 Bit Score: 81.99 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 36 SCLGLGTwVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIfwgGK-- 110
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 --AETERGL-----------------SRKHIIEGLKASLERLQLEYVDVVF---------ANRPDPN---TPMEETVRAM 159
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 160 THVINQGM--AMYWGTSRWSSM-EIMeaysvaRQFNLTppiCE--QAEYHMFQREKVEVQLPELfHKIGVGAmtwsplac 234
Cdd:cd19161 155 EELKKAGVikAFGLGVNEVQIClEAL------DEADLD---CFllAGRYSLLDQSAEEEFLPRC-EQRGTSL-------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 235 gIVSGKYDSGIPPYSRASLKGYQWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAD 314
Cdd:cd19161 217 -VIGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPA 289
|
330
....*....|....*
gi 27436969 315 QLMENIGAIQ-VLPK 328
Cdd:cd19161 290 QLRQNVEAFQtDIPE 304
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
34-341 |
1.96e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 81.49 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 34 RVSCLGLGTWVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGW---RRSSLVITTKIFW 107
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GGKAETergLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNtpMEETVRAMTHVINQGMAMYWG-----TSRWSsm 179
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqfhWWDYSDPG--YLDAAKHLAELQEEGKIRHLGltnfdTERLR-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 180 EIMEAysvarqfnLTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY----DSGIPPYSRASLKG 255
Cdd:cd19101 152 EILDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvpEPTGPALETRSLQK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 256 YQWLKDKILSEEGrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIH 335
Cdd:cd19101 223 YKLMIDEWGGWDL--FQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLDDEDRA 298
|
....*.
gi 27436969 336 EIDSIL 341
Cdd:cd19101 299 AIDAVL 304
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
38-320 |
6.63e-17 |
|
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: 79.34 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 117
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 srkhiiEGLKASLERLQLEYVDVVFANRPdpnTPME----ETVRAMTHVINQGMAMYWGTSRWSS---MEIMEAYSVArq 190
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 fnltpPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyqwLKDKILSEeg 268
Cdd:cd19131 153 -----PVVNQIELHprFQQRE-----LRAFHAKHGIQTESWSPLGQGGL---------------------LSDPVIGE-- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27436969 269 rrqqaklkelqaIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 320
Cdd:cd19131 200 ------------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
39-346 |
2.32e-16 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 78.04 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 39 GLGTWVTFGGQIT-DEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKaetergl 117
Cdd:cd19120 10 GTGTAWYKSGDDDiQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 srkHIIEGLKASLERLQLEYVDVVFANRP----DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnl 193
Cdd:cd19120 80 ---DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 194 TPPICEQAEYHMFqrekVEVQLPEL--FH-KIGVGAMTWSPLAcgivsgkydsgipPYSRaslkgyqwlkdkilseegRR 270
Cdd:cd19120 153 IKPAVNQIEFHPY----LYPQQPALleYCrEHGIVVSAYSPLS-------------PLTR------------------DA 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436969 271 QQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIqvLPKLSSSIIHEIDSILGNKPY 346
Cdd:cd19120 198 GGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
30-320 |
4.45e-16 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 77.39 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 30 KSGLRVSCLGLGTWVTFGGQITDEMAEQLmTLAYDNginlFDTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIfW 107
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKTAI-KEGYRH----IDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GGKAETERglsrkhIIEGLKASLERLQLEYVDVVF----------ANRPDP----NTPMEETVRAMTHVINQGMAMYWGT 173
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYLihwpvrlkkgAHMPEPeevlPPDIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 174 SRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsgkydsGIPpysrasl 253
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSP------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 254 kGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNADQLMENI 320
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 ... |
32-320 |
5.68e-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: 76.46 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGK 110
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSvarq 190
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLIL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 FNLTPPICEQAEYHMFqREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGRR 270
Cdd:cd19133 145 HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA---------------------------------EGRN 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27436969 271 QQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNADQLMENI 320
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; ... |
38-340 |
5.99e-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: 76.24 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 117
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTP 195
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 196 PICEQAEYhmFQREKVEVQLPElfHKIGVGAmtWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqakl 275
Cdd:cd19139 149 NQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLAYGKV---------------------LDDPV------------ 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 276 keLQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
Cdd:cd19139 190 --LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
32-237 |
1.60e-15 |
|
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: 75.17 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVTFGGqitDEMAEQLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKA 111
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG---DETERAVQT-ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 ETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 191
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27436969 192 nlTPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGIV 237
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
38-320 |
2.23e-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: 74.89 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkAETERGL 117
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SRKhiIEGLKASLERLQLEYVDVVFANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAysvarqFNLT-- 194
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENL------IDLTff 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 195 PPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrQQ 272
Cdd:cd19134 153 TPAVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG-----------------------------------RL 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 27436969 273 AKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 320
Cdd:cd19134 193 LDNPAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
32-346 |
2.31e-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: 75.23 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVTfggqITDEMAEQLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKI 105
Cdd:cd19111 1 GFPMPVIGLGTYQS----PPEEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 fwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVFAN-------------RPDPNTPMEETVRAMTHVINQGMAMYWG 172
Cdd:cd19111 71 -------PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 173 TSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkyDSGIPPYSR 250
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPLG--------SPGRANQSL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 251 ASLKgYQWLKD-KILseegrrqqaklkelqAIAERLGCTLPQLAIAWCL-RNEGvssVLLGASNADQLMENIGAIQVlpK 328
Cdd:cd19111 207 WPDQ-PDLLEDpTVL---------------AIAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--E 265
|
330
....*....|....*...
gi 27436969 329 LSSSIIHEIDSILGNKPY 346
Cdd:cd19111 266 LTEEHFKKLKTLDRNMKY 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
31-303 |
3.97e-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: 74.28 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWvTFGGQITDEMAEQLMtlayDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 110
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTP-------MEETVRAMTHVINQGMAMYWGTSRWSS---ME 180
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIehlEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 181 IMEAYSVarqfnltPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlK 260
Cdd:cd19135 154 LLEDCSV-------VPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLA--------------------------K 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 27436969 261 DKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 303
Cdd:cd19135 198 GKALEEP---------TVTELAKKYQKTPAQILIRWSIQNGVV 231
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
31-338 |
5.38e-15 |
|
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: 74.86 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLG------TWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK 104
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 IFW--------GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 176
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 177 SSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSgiPPYSRASLKGY 256
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGKFQS--KKAVEERKKNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 257 QWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSII 334
Cdd:cd19147 238 EGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEI 315
|
....
gi 27436969 335 HEID 338
Cdd:cd19147 316 EYLE 319
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
38-340 |
8.09e-15 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 73.98 E-value: 8.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWVTFGGQitdemAEQLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETEr 115
Cdd:cd19123 15 LGLGTWKSKPGE-----VGQAVKQALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 116 glsrkHIIEGLKASLERLQLEYVD-------VVF---ANRPDPNT--------PMEETVRAMTHVINQGMAMYWGTSRWS 177
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 178 SMEIMEAYSVARqfnlTPPICEQAEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgivsgkydSGIPPYSRASL 253
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPLG---------SGDRPAAMKAE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 254 KGYQWLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENIGAIQVlpKLSSS 332
Cdd:cd19123 222 GEPVLLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDAS 282
|
....*...
gi 27436969 333 IIHEIDSI 340
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 ... |
32-320 |
1.48e-14 |
|
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: 72.69 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggka 111
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 eteRGlsRKH----IIEGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEA 184
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFlpEHLDRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 185 ----YSVARQFNLTPPIcEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPLAcgivsgkydsgippysraslKGYQWLK 260
Cdd:cd19132 145 etgvTPAVNQIELHPYF-PQAEQRAYHREH------------GIVTQSWSPLG--------------------RGSGLLD 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 261 DKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENI 320
Cdd:cd19132 192 EPV--------------IKAIAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
30-142 |
8.80e-14 |
|
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: 70.77 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 30 KSGLRVSCLGLGTwvtFGGQITDEMAE----QLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKK--KGWRRSSLVITT 103
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 27436969 104 KIfwGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF 142
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
38-320 |
1.21e-13 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 69.97 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIK----KKGWRRSSLVITTKIfwgGKAE 112
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKL---APKD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 113 TERGLSRkhiiEGLKASLERLQLEYVDVVFANRP-----DPNTPME-----ETVRAMTHVINQGMAMYWGTSRW--SSME 180
Cdd:cd19136 73 QGYEKAR----AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYtvRHLE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 181 IMEAYSvarqfnLTPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqw 258
Cdd:cd19136 149 ELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG----------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436969 259 lKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENI 320
Cdd:cd19136 195 -DLRLLEDP---------TVLAIAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
38-320 |
1.29e-13 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 70.39 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfgGQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAEter 115
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYG-NEAEVgeAIREKIAEGVVKREDLFITTKL-WNSYHE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 116 glsRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPME---------ETVRAMTHVINQGMAMYWGTSRWSSM 179
Cdd:cd19116 85 ---REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 180 EIMEAYSVARqfnlTPPICEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacGIVSGKYDSGIPPYsraslkgyqw 258
Cdd:cd19116 162 QINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPR---------- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436969 259 LKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNADQLMENI 320
Cdd:cd19116 222 LDDPT--------------LVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
38-322 |
2.43e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 69.28 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIfWggkaeTERgL 117
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTp 195
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 196 piCEQAEYHMF-QREKVEVQLPElfHKIGVGA-MTwspLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqa 273
Cdd:PRK11172 150 --TNQIELSPYlQNRKVVAFAKE--HGIHVTSyMT---LAYGKV---------------------LKDPV---------- 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27436969 274 klkeLQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNADQLMENIGA 322
Cdd:PRK11172 192 ----IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
32-320 |
3.82e-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: 68.59 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWG--G 109
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 110 KAETERGLsrkhiieglKASLERLQLEYVDVVFANRPDPNTpMEETV---RAMTHVINQGMAMYWGTSRWSS---MEIME 183
Cdd:cd19127 78 YDKALRGF---------DASLRRLGLDYVDLYLLHWPVPND-FDRTIqayKALEKLLAEGRVRAIGVSNFTPehlERLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 184 AYSVArqfnltpPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcGIVsgKYDSGIPPySRASLkgyqwLKDKI 263
Cdd:cd19127 148 ATTVV-------PAVNQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPT-GPGDV-----LQDPT 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 264 LSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNeGVSSVlLGASNADQLMENI 320
Cdd:cd19127 209 ITG--------------LAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
38-235 |
4.25e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.56 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKaetergl 117
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 sRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEETVRAMTHVIN---QGMAMYWGTSRWSS---MEIMEAYSVArqf 191
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27436969 192 nltpPICEQAEYH--MFQRekvEVQLPELFHKIGVGAmtWSPLACG 235
Cdd:PRK11565 156 ----PVINQIELHplMQQR---QLHAWNATHKIQTES--WSPLAQG 192
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
32-319 |
2.13e-12 |
|
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: 66.78 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTKI 105
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 FWGGkaeterglSRKHIIEG-LKASLERLQLEYVDVVFANRP---------------------DPNTPMEETVRAMTHVI 163
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 164 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIVSGKYD 242
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 243 SGIPPYSRASLkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNADQLMEN 319
Cdd:cd19155 224 TGSPSGSSPDL-----LQD--------------PVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKEN 279
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
31-306 |
8.85e-12 |
|
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: 64.60 E-value: 8.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGqitDEMAEQLMTLAYDNGINLFDTAEVY----AAGKA--EVVLGNIIKKkgwrRSSLVITTK 104
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS---PEDIKAAVLEAIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 105 IfWGGKAEterglsRKHIIEGLKASLERLQLEYVDV------------VFANRPDPNTP----MEETVRAMTHVINQGMA 168
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLylihwpvslkpgKFSFPIEEEDFlpfdIKGVWEAMEECQRLGLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 169 MYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKvevqLPELFHKIGVGAMTWSPLACgivsgkydsgipp 247
Cdd:cd19124 147 KAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGA------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 248 ysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVSSV 306
Cdd:cd19124 206 ------PGTKWGSNAVMESD---------VLKEIAAAKGKTVAQVSLRW-VYEQGVSLV 248
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
31-296 |
1.28e-11 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 64.71 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGQItdemaEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKK-----KGWRRSSLVITTKI 105
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 106 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDV--------------VFANRPDPN-----TPMEETVRAMTHVINQG 166
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDGTirydsTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 167 MAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgivsgkydsGIP 246
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27436969 247 pySRAslkgyqWLK--DKILSEEGRrqqaklkeLQAIAERLGCTLPQLAIAW 296
Cdd:cd19106 210 --DRP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
32-321 |
7.37e-11 |
|
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: 62.02 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTW-VTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 110
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 AETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 190
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 fnlTPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEg 268
Cdd:cd19157 150 ---IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG--------------------------QLLDNP- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27436969 269 rrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIG 321
Cdd:cd19157 195 --------VLKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
31-320 |
8.20e-11 |
|
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: 62.12 E-value: 8.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGQITDemaeqLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWg 108
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKE-----LILNAIKIGYRHFDCAADYK-NEKEVgeALAEAFKTGLVKREDLFITTKL-W- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 gkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP-----------------------DPNTPMEETVRAMTHVINQ 165
Cdd:cd19112 79 ---NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 166 GMAMYWGTSRWSS--MEIMEAYSVARqfnltpPICEQAEYH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIVSGKYD 242
Cdd:cd19112 152 GLVRSIGISNYDIflTRDCLAYSKIK------PAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436969 243 SGIPPysraslkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENI 320
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 ... |
32-300 |
1.13e-09 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 58.30 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 110
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARq 190
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 191 fnlTPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEgr 269
Cdd:cd19156 149 ---VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG--------------------------KLLSNP-- 193
|
250 260 270
....*....|....*....|....*....|.
gi 27436969 270 rqqaklkELQAIAERLGCTLPQLAIAWCLRN 300
Cdd:cd19156 194 -------VLKAIGKKYGKSAAQVIIRWDIQH 217
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
46-337 |
3.36e-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: 57.08 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 46 FGGQITDEMAEQLMTL-AYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhI 122
Cdd:cd19129 11 FGTLIPDPSATRNAVKaALEAGFRHFDCAERYR-NEAEVgeAMQEVFKAGKIRREDLFVTTKL-WNTNHRPER------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 123 IEGLKASLERLQLEYVDVV-----FANRP---------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 182
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 183 EAYSVARqfnlTPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwLKDK 262
Cdd:cd19129 163 EIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LEDP 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436969 263 ILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGvsSVLLGASNADQLMENIGaIQVLPKLSSSIIHEI 337
Cdd:cd19129 218 VIT--------------AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
31-179 |
6.46e-09 |
|
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: 56.35 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGQitdEMAEQLMTLAYDNGINLFDTAEVYAA----GKAevvLGNIIKKKGWRRSSLVITTKI- 105
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436969 106 --FWggkaeterglsrKHIIEGLKASLERLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSSM 179
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWPVCfEKDSDDSGKPFTPVNDDGKTRYAASGDHITT 146
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
31-340 |
1.50e-08 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 55.20 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGgk 110
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 111 aeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNTP---------------------MEETVRAMTHVINQGMAM 169
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 170 YWGTSRWSSMEIMEAysVARQFNLTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYs 249
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------STNAPLL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 250 raslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENIGAIQvlpkL 329
Cdd:cd19117 219 ------------------------KEPVIIKIAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 27436969 330 SSSIIHEIDSI 340
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
31-319 |
1.13e-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: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaAGKAEV--VLGNIIKKK-GWRRSSLVITTKIfW 107
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKI-----ALKAGYRHLDLAKVY-QNQHEVgqALKELLKEEpGVKREDLFITSKL-W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GGKAETErglsrkHIIEGLKASLERLQLEYVD-------VVFA--NRPDPNTPME---------------ETVRAMTHVI 163
Cdd:cd19118 76 NNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKptGDLNPLTAVPtnggevdldlsvslvDTWKAMVELK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 164 NQGMAMYWGTSRWSS---MEIMEAYSVArqfnltpPICEQAEYH--MFQREKVEvqlpelFHK---IGVGAmtWSPLacg 235
Cdd:cd19118 150 KTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 236 ivsGKYDSGIPPysraslkgyqwlkdkILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQ 315
Cdd:cd19118 212 ---GNNLAGLPL---------------LVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTPSR 262
|
....
gi 27436969 316 LMEN 319
Cdd:cd19118 263 IRSN 266
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-325 |
1.49e-07 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 52.35 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 13 LSLRQTGSPGMIyrNLGksglRVSCLGlgtwvtfGGQITDEMAEQ---LMTLAYDNGINLFDTAEVYaaGKAEVVLGNII 89
Cdd:cd19098 5 LGLAALGRPGYI--NLG----HAADLG-------SGRSVEAMRAHthaVLDAAWAAGVRYFDAARSY--GRAEEFLGSWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 90 KKKGWRRSSLVITTKifWG----------GKAETERGLSRKHIIEGLKASLERLQlEYVDV-----------VFANrpdp 148
Cdd:cd19098 70 RSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLKQWEETRSLLG-KHLDLyqihsatlesgVLED---- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 149 ntpmEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA-----YSVARQFNltppiCEQAEYHMFQREKVEvQLpELFHKIG 223
Cdd:cd19098 143 ----ADVLAALAELKAEGVKIGLSLSGPQQAETLRRaleieIDGARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAG 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 224 VGAMTWSPLACGIVSGKYDSGippysraslkgyqwlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGV 303
Cdd:cd19098 212 MGVIVKEALANGRLTDRNPSP-------------------------ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFV 266
|
330 340
....*....|....*....|..
gi 27436969 304 SSVLLGASNADQLMENIGAIQV 325
Cdd:cd19098 267 DVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
32-320 |
6.58e-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: 50.25 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK---KGW-RRSSLVITTKIfW 107
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GGKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRP------DP-------------------NTPMEETVRAMTHV 162
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 163 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgivsgKY 241
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 242 DSGIPPYSRASLKGYQwlkdkILSEEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMEN 319
Cdd:cd19114 199 GIQITAYSSFGNAVYT-----KVTKHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTN 271
|
.
gi 27436969 320 I 320
Cdd:cd19114 272 L 272
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
31-232 |
1.05e-06 |
|
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: 49.45 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYAaGKAEVVLGniIKK---KGWRRSSLVITTKIfW 107
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCYQ-NEDEVGEG--IKEaiaGGVKREDLFVTTKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 108 GgkaetergLSRKHIIEGLKASLERLQLEYVDV----------------VFANRPD------PNTPMEETVRAMTHVINQ 165
Cdd:cd19121 79 S--------TYHRRVELCLDRSLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDgsrdldWDWNHVDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436969 166 GMAMYWGTSRWSSM---EIMEAYSV---ARQFNLTpPICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPL 232
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVvpaVNQVENH-PYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
62-340 |
1.37e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.20 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 62 AYDNGINLFDTAEVYAAGkaevVLGNIIkkkgwR------RSSLVITTKIfwgGKAETERG-----LSRKHIIEGLKASL 130
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 131 ERLQLEYVDVV------FANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltPPICEQAEYH 204
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 205 MFQREkvEVQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkGYQWLKDKILSeegrrqqaklkelqAIAER 284
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPLG---------------------GFTPLQSSTLS--------------DVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 285 LGCTLPQLAIAWCLRNEgvSSVLL--GASNADQLMENIGAIQVlpKLSSSIIHEIDSI 340
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, ... |
34-232 |
3.88e-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: 44.95 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 34 RVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIfWGgka 111
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKL-WC--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 112 eterGLSRKHIIE-GLKASLERLQLEYVDVVFANRP------DPNTPMEE-------------TVRAMTHVINQGMAMYW 171
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436969 172 GTSRWSSmEIMEaySVARQFNL-TPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 232
Cdd:cd19110 149 GVSNFNH-EQLE--RLLNKPGLrVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
38-235 |
9.89e-05 |
|
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: 43.36 E-value: 9.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 117
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 118 SrkhiieGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEAYSVarqfnlT 194
Cdd:cd19130 84 A------AFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG------V 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27436969 195 PPICEQAEYHMF--QREKVEVQlpelfHKIGVGAMTWSPLACG 235
Cdd:cd19130 152 VPAVNQIELHPAyqQRTIRDWA-----QAHDVKIEAWSPLGQG 189
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
31-204 |
3.27e-04 |
|
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: 42.05 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 31 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKaEVVLG--NIIKKKGWRRSSLVITTKIfWG 108
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 109 GKAEterglsRKHIIEGLKASLERLQLEYVDVVF-----ANRPDP--------------------NTPMEETVRAMTHVI 163
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLihfpiAFKFVPieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27436969 164 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH 204
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHH 190
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
32-232 |
3.92e-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: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 32 GLRVSCLGLGTWVTFGGQITDEMAeqlmtLAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIFwgg 109
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 110 KAETERGLSRkhiiEGLKASLERLQLEYVDVVFANRPD-------------------PNTPMEETVRAMTHVINQGMAMY 170
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436969 171 WGTSRWSSMEImeaysvARQFNlTP-----PICEQAEYHMF-QREKvevqLPELFHKIGVGAMTWSPL 232
Cdd:cd19107 148 IGVSNFNHLQI------ERILN-KPglkykPAVNQIECHPYlTQEK----LIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
38-154 |
5.93e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 41.06 E-value: 5.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436969 38 LGLGTWVTfgGQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 113
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 27436969 114 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPDPNTPMEE 154
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEE 122
|
|
| |
