|
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 ... |
121-430 |
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: 671.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVITT 200
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 201 KIYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIME 280
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLKDKI 360
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 361 LSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSI 430
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
120-442 |
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: 650.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVIT 199
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIM 279
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 280 EAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLKDK 359
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 360 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEVDSILG 439
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 1721957790 440 NKP 442
Cdd:cd19159 321 NKP 323
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
120-443 |
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: 645.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVIT 199
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIM 279
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 280 EAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLKDK 359
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 360 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEVDSILG 439
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 1721957790 440 NKPY 443
Cdd:cd19158 321 NKPY 324
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
118-442 |
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: 634.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 118 TGMKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLV 197
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 198 ITTKIYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPME 277
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 278 IMEAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLK 357
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 358 DKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEVDSI 437
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
....*
gi 1721957790 438 LGNKP 442
Cdd:cd19160 321 LGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
122-438 |
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: 630.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 122 YRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVITTK 201
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 IYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEA 281
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 282 YSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLKDKIL 361
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 362 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEVDSIL 438
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
120-437 |
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: 514.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVIT 199
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPME 277
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 278 IMEAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLK 357
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 358 DkILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEVDSI 437
Cdd:cd19143 241 D-RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
120-442 |
3.23e-171 |
|
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: 483.12 E-value: 3.23e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVIT 199
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWGGKAEtERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIM 279
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 280 EAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGY-----Q 354
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSkykvgS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 355 WLKDKIlsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLSSSITHEV 434
Cdd:cd19142 240 DGNGIH--EETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEEL 317
|
....*...
gi 1721957790 435 DSILGNKP 442
Cdd:cd19142 318 ERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
129-430 |
1.08e-164 |
|
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: 465.53 E-value: 1.08e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTLVITTKIYWGGKA 208
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 E-TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARQ 287
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 288 FNQIPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKgYQWLKDKILSEEGRR 367
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721957790 368 QQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAiqVLPKLSSSI 430
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
120-442 |
1.52e-104 |
|
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: 313.27 E-value: 1.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWvTFG---GQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTL 196
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKIYW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSP 275
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEAYSVARQFnqIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG--VPAYSRASLKGY 353
Cdd:COG0667 158 EQLRRALAIAEGL--PPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 354 QWlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSITHE 433
Cdd:COG0667 235 QG-------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
....*....
gi 1721957790 434 VDSILGNKP 442
Cdd:COG0667 306 LDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
120-437 |
2.73e-94 |
|
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: 286.78 E-value: 2.73e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTwVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVIT 199
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWG-GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEI 278
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 279 MEAYSVARQFNQIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG--VPAYSRASLKGYQwl 356
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkrPESGRLVERARYQ-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 357 kDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSITHEVDS 436
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDE 307
|
.
gi 1721957790 437 I 437
Cdd:cd19087 308 L 308
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
122-424 |
1.41e-81 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 254.10 E-value: 1.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 122 YRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVY--AAGKAETVLGNIIKK-KGWRRSTLVI 198
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 199 TTKI-Y--WGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSP 275
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEAYSVARQFnQIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRAsLKGYQW 355
Cdd:cd19089 159 AKARRAIALLREL-GVPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 356 LKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLP 424
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
120-422 |
3.13e-81 |
|
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: 253.69 E-value: 3.13e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTwVTFG---------GQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkg 190
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 191 wRRSTLVITTKI-YWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWG 269
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 270 TSRWSPMEIMEAYSVARQFNQIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKY--DSGVPAYSR 347
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 348 ASLKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
129-419 |
8.46e-78 |
|
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: 243.97 E-value: 8.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWV---TFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITTK--IY 203
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYS 283
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 284 VArqfnqiPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIISGKYDSG---VPAYSRASLKGYQwlkdki 360
Cdd:cd19084 158 YG------PIVSLQPPYSMLEREIEEELLPYC-RENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR------ 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 361 lSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGA 282
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
121-421 |
1.36e-75 |
|
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: 238.84 E-value: 1.36e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYA--AGKAETVLGNIIKK--KGWRrSTL 196
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKI--------Y--WGgkaeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAM 266
Cdd:cd19151 80 IISTKAgytmwpgpYgdWG---------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 267 YWGTSRWSPMEIMEAYSVARQFNqIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYS 346
Cdd:cd19151 151 YVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 347 RASlKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQ 421
Cdd:cd19151 229 RAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
121-427 |
1.74e-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: 238.64 E-value: 1.74e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLGTWvTFGGQ------ITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRS 194
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 195 TLVITTKIYW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 273
Cdd:cd19079 79 EVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 274 SPMEIMEAYSVARQFNQIPPICEQAEYHMFQREKvEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGY 353
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 354 qwLKDKILSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLS 427
Cdd:cd19079 238 --LKYDYFTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLS 304
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
133-418 |
3.69e-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: 234.72 E-value: 3.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTWvTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRSTLVITTKI-YWGGKAETE 211
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 212 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARQFNQI 291
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 292 PPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGiisgkydsgvpaysraslkgyqwlkdkilseegrrqqak 371
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1721957790 372 lkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIG 418
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
125-437 |
1.35e-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: 235.96 E-value: 1.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 125 LGKSGLRVSCLGLGTWVtFGGQITDETAEQLMTLAYENGINLFDTAEVYAA-------GKAETVLGNIIKKKGwRRSTLV 197
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 198 ITTKIYWGgKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPME 277
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 278 IMEAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG--VPAYSRASLKGyqw 355
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEadLPGSTRRGEAA--- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 356 lkDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSssiTHEVD 435
Cdd:cd19081 236 --KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLT---DEEVA 305
|
..
gi 1721957790 436 SI 437
Cdd:cd19081 306 RL 307
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
121-423 |
9.06e-68 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 218.48 E-value: 9.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYA--AGKAETVLGNIIKKK-GWRRSTLV 197
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 198 ITTKI---YWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWS 274
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 275 PMEIMEAYSVARQFNqIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYq 354
Cdd:cd19150 159 PERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 355 wLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVL 423
Cdd:cd19150 237 -LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
135-438 |
1.10e-67 |
|
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: 217.56 E-value: 1.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvTFGGQ---ITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVITTKIyWGGKAETE 211
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 212 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARqfnqI 291
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 292 PPICEQAEYHMFqREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRaslkgyqwLKDKILSEEGRRQQAK 371
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG--------ERRRLLKKGTPLNLEA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 372 LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQvlPKLSSSITHEVDSIL 438
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
132-437 |
3.46e-66 |
|
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: 215.12 E-value: 3.46e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 132 VSCLGLGTwVTFGGQITDETAEQLMTLAYENGINLFDTAEVYA-------AGKAETVLGNIIKKKGwRRSTLVITTKI-- 202
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 ---YWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTP------------------MEETVRAMTHVIN 261
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 262 QGMAMYWGTSRWSPMEIMEAYSVARQFNQIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG 341
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 342 --VPAYSRASL-KGYQwlkdkilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLM 414
Cdd:cd19094 238 aaRPEGGRLNLfPGYM----------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|...
gi 1721957790 415 ENIGAIQVlpKLSSSITHEVDSI 437
Cdd:cd19094 308 ENIDAFDV--PLSDELLAEIDAV 328
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
120-423 |
4.64e-64 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 210.23 E-value: 4.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYA--AGKAETVLGNIIKKK-GWRRSTL 196
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKI---YWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 273
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 274 SPMEIMEAYSVARQFnQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKG- 352
Cdd:PRK09912 171 SPERTQKMVELLREW-KIPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGn 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 353 -YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVL 423
Cdd:PRK09912 250 kVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
125-435 |
1.24e-58 |
|
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: 194.75 E-value: 1.24e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 125 LGKSGLRVSCLGLGTwVTFGGQ----ITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITT 200
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 201 KIYWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRwspmei 278
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISD------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 279 MEAYSVAR-----QFNQIPPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGvpAYSRASLKG 352
Cdd:cd19080 153 TPAWVVARantlaELRGWSPFVAlQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 353 YQWLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSITH 432
Cdd:cd19080 230 GVTVGFGKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLA 304
|
...
gi 1721957790 433 EVD 435
Cdd:cd19080 305 RLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
132-437 |
6.29e-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: 187.02 E-value: 6.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 132 VSCLGLGTWV----TFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITTKIYwggk 207
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 aetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVAR- 286
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRi 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 287 QFNQIPpiceqaeYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG---VPAYSRASLKgyqwlkdkILSE 363
Cdd:cd19085 151 DSNQLP-------YNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAedfPPGDARTRLF--------RHFE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721957790 364 EGRRQQAK--LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSITHEVDSI 437
Cdd:cd19085 215 PGAEEETFeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
122-422 |
8.80e-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: 174.38 E-value: 8.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 122 YRNLGKSGLRVSCLGLGTWV----TFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLV 197
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 198 ITTK--IYWGGKAETE----------RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMA 265
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 266 MYWGTSRWSPMEIMEAysvaRQFNQIPPIceQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIISGKYDSGvpay 345
Cdd:cd19149 158 RAIGASNVSVEQIKEY----VKAGQLDII--QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPD---- 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721957790 346 sRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19149 227 -REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
121-422 |
2.14e-50 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 173.17 E-value: 2.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLG----TWvtFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTL 196
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKiyWG---GKAETERGL--SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTS 271
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 272 RWSPMEIMEAYSVArqfnqipPICE-QAEYHMFQREKVEVQLP---ELfhkiGVGAMTWSPLACGIISGKYDSgvpaysr 347
Cdd:cd19076 154 EASADTIRRAHAVH-------PITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 348 aslkgyqwlKDKILSEEGRRQQ-----------AKL-KELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASTTDQLM 414
Cdd:cd19076 216 ---------PEDLPEDDFRRNNprfqgenfdknLKLvEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLE 285
|
....*...
gi 1721957790 415 ENIGAIQV 422
Cdd:cd19076 286 ENVGALDV 293
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
123-422 |
7.58e-48 |
|
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: 166.44 E-value: 7.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 123 RNLGKSGLRVSCLGLGTwVTFGGQ-----ITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTLV 197
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 198 ITTK--IYWGGKaETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSP 275
Cdd:cd19083 79 IATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEAySVARQFNQIppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIISGKYDSGVpaysraSLKGYQW 355
Cdd:cd19083 158 EQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 356 LKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19083 225 RNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV 293
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
130-419 |
9.63e-48 |
|
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: 163.80 E-value: 9.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 130 LRVSCLGLGTWV---TFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITTKI--YW 204
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPmeimeayS 283
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSVGDP-------E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 284 VARQFNQIPPI-CEQAEYHMFQREKVEvqlpELFHKI---GVGAMTWSPLACGIISGKydsgvpaysraslkgyqwlkdk 359
Cdd:cd19086 151 EALAALRRGGIdVVQVIYNLLDQRPEE----ELFPLAeehGVGVIARVPLASGLLTGK---------------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 360 ilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19086 205 --------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
131-419 |
5.89e-47 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 163.55 E-value: 5.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 131 RVSCLGLGTW------VTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRSTLVITTKIyw 204
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 ggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETV-RAMTHVINQGMAMYWGTSRWSPMEIMEAYS 283
Cdd:cd19093 78 ---APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 284 VARQfNQIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKY-DSGVPAYSRASLKG-YQWLKDKIL 361
Cdd:cd19093 155 ALKE-RGVPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGRRRLFGrKNLEKVQPL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721957790 362 seegrrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASTTDQLMENIGA 419
Cdd:cd19093 234 ----------LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
135-421 |
9.48e-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: 163.50 E-value: 9.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIikkkGWRRSTLVITTKIY-WGGKaeterG 213
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 214 LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARQFNQIPP 293
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 294 ICEQAEYHMFQReKVEvqlPELF-----HKIGVGAmtWSPLACGIISGKYDSG--VPAYSR--ASLKGYQWLKDKILSEE 364
Cdd:cd19075 156 TVYQGMYNAITR-QVE---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdPNNALGKLYRDRYWKPS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 365 grrQQAKLKELQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASTTDQLMENIGAIQ 421
Cdd:cd19075 230 ---YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALE 288
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
129-422 |
2.32e-46 |
|
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli aldehyde reductase (AKR13C1) and Thermotoga maritima aldo-keto reductase (AKR13C2). Aldehyde reductase (EC 1.1.1.21), also called aldose reductase, is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides.
Pssm-ID: 381304 [Multi-domain] Cd Length: 301 Bit Score: 162.40 E-value: 2.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTW-VTFG-GQITD-ETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITTK---- 201
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKfgfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 IYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEA 281
Cdd:cd19078 78 IDGGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 282 YSVArqfnqiPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGV---PAYSRASLKGYqwlkd 358
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF----- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 359 kilSEEGRRQQAKLKEL-QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI 287
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
132-438 |
1.29e-45 |
|
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: 160.53 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 132 VSCLGLGTWV-----TFGGQITDETAEQLMTL--AYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTLVITT-KIY 203
Cdd:cd19102 1 LTTIGLGTWAiggggWGGGWGPQDDRDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDRPIVATKcGLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRwspmeimeaYS 283
Cdd:cd19102 79 WDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSN---------FS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 284 VA--RQFNQIPPICE-QAEYHMFQREKVEVQLPelF---HKIGVgaMTWSPLACGIISGKYDSGvpaySRASLKGYQWLK 357
Cdd:cd19102 150 VDqmKRCQAIHPIASlQPPYSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMTPE----RVASLPADDWRR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 358 -DKILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSITHEVD 435
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIE 299
|
...
gi 1721957790 436 SIL 438
Cdd:cd19102 300 ALL 302
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
129-421 |
1.18e-44 |
|
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: 156.62 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTFGGQ----ITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIkkKGWRRSTLVITTKIYw 204
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 ggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSV 284
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 285 ARqfnQIPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSgvpaysraslkgyqwlkdkilsee 364
Cdd:cd19072 152 LK---KGPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS------------------------ 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 365 grrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASTTDQLMENIGAIQ 421
Cdd:cd19072 204 --------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
133-419 |
1.63e-41 |
|
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: 149.24 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTwVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAA----GKAETVLGNIIKKKGwRRSTLVITTKiywGG-- 206
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 207 ---KAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEA-- 281
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEAna 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 282 ----------------YSVARQFNQIPP----ICEQAEYHMFQREKvevQLPelfhkigvgAMTWSPLACGIISGKYDSG 341
Cdd:cd19082 155 yakahglpgfaasspqWSLARPNEPPWPgptlVAMDEEMRAWHEEN---QLP---------VFAYSSQARGFFSKRAAGG 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721957790 342 VPAYSRaslkgyqwLKDKILSEEGRRQQAKLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19082 223 AEDDSE--------LRRVYYSEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
120-437 |
1.74e-40 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 148.08 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTwVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAA-------GKAETVLGNIIKKKGwR 192
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 193 RSTLVITTKIywGGKAET-------ERGLSRKHIIEGLKASLERLQLEYVD---VVFANRPD--------------PNTP 248
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPTncfgklgyswtdsaPAVS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 249 MEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARQfNQIPPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWS 327
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEK-HDLPRIVTiQNPYSLLNRS-FEVGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 328 PLACGIISGKYDSGV-PAYSRASLKgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLG 406
Cdd:PRK10625 235 CLAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|.
gi 1721957790 407 ASTTDQLMENIGAIQVlpKLSSSITHEVDSI 437
Cdd:PRK10625 309 ATTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
133-419 |
2.35e-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: 145.94 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTwVTFGGQITDETAEQLMTLAYENGINLFDTAEVYA-------AGKAETVLGNIIKKKGwRRSTLVITTKIYWG 205
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVGAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 -----GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIME 280
Cdd:cd19752 79 prdpdGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AYSVARQFNQIPPICEQAEYHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLACGiisgkydsgvpAYSRAsl 350
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPLLSG-----------AYTRP-- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 351 kgyqwlkDKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19752 226 -------DRPLPEQYDGPdsDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
120-420 |
2.21e-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: 139.64 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGlgtwvtFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIkkKGWRRSTLVIT 199
Cdd:cd19105 1 MPYRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKIYWGGKAETerglsRKHIIEGLKASLERLQLEYVDVVF---ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPM 276
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 277 E--------------IMEAYSVARQFNQIPPICEQAeyHMfqrekvevqlpelfHKIGVGAMtwsplacgiisgkydsgv 342
Cdd:cd19105 148 AevlqaaiesgwfdvIMVAYNFLNQPAELEEALAAA--AE--------------KGIGVVAM------------------ 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1721957790 343 paysraslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAI 420
Cdd:cd19105 194 ----------------KTLA-GGYLQPALLSVLKA----KGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
128-419 |
4.36e-38 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 139.03 E-value: 4.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGK 207
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 AeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARq 287
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 288 fnqIPPICEQAEYHMFQREkvevqlPELF-----HKIGVGAmtWSPLACGiisgkydsgvpaysraslkgyqwlkdKILS 362
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELLafcreHGIVVEA--YSPLGRG--------------------------KLLD 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 363 EEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASTTDQLMENIGA 419
Cdd:COG0656 187 DP---------VLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
129-438 |
8.24e-37 |
|
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: 136.67 E-value: 8.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVT----FGGqiTDEtAEQLMTL--AYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRSTLVITTK- 201
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 -IYWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPmEIME 280
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AysvarqFNQIPPI-CEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIISGKYDsgvpaysraslKGYQWLKDK 359
Cdd:cd19148 156 T------FRKVAPLhTVQPPYNLFEREIEKDVLPYA-RKHNIVTLAYGALCRGLLSGKMT-----------KDTKFEGDD 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 360 ILSEEGRRQQAKLK-------ELQAIA-ERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSIT 431
Cdd:cd19148 218 LRRTDPKFQEPRFSqylaaveELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGW--SLNDEDM 295
|
....*..
gi 1721957790 432 HEVDSIL 438
Cdd:cd19148 296 KEIDAIL 302
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
127-422 |
9.21e-37 |
|
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: 136.15 E-value: 9.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 127 KSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVITTK---IY 203
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 WGGKAETERG---LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEI-- 278
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIel 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 279 ----MEAYSVARQfNQIPPICEQA------EYHMfqrekvevqlpelFHKIGVgaMTWSPLACGIISGkydsgvpaysra 348
Cdd:cd19092 161 lqsyLDQPLVTNQ-IELSLLHTEAiddgtlDYCQ-------------LLDITP--MAWSPLGGGRLFG------------ 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 349 slkgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19092 213 --------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
120-396 |
2.05e-36 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 135.66 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVIT 199
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TK--IYWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 273
Cdd:COG4989 81 TKcgIRLPSEARDNRVkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 274 SPMEI------MEAYSVARQFnQIPPICEQA------EYHmfQREKVEVqlpelfhkigvgaMTWSPLACGIISGKYDsg 341
Cdd:COG4989 161 TPSQFellqsaLDQPLVTNQI-ELSLLHTDAfddgtlDYC--QLNGITP-------------MAWSPLAGGRLFGGFD-- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 342 vpaysraslkgyqwlkdkilsEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLR 396
Cdd:COG4989 223 ---------------------EQFPRLRAALDE---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
128-422 |
8.76e-36 |
|
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: 133.14 E-value: 8.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvtFGGQITDETAEQLMTL--AYENGINLFDTAEVYAAGKAETVLGNIIKKkgwRRSTLVITTKIYwg 205
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 gkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVA 285
Cdd:cd19138 80 -----PSNASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 286 rqfNQIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGiisgkydsgvpaysraslkgyqwlkdkilsEEG 365
Cdd:cd19138 154 ---GGGNCAANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG------------------------------GLL 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 366 RRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVlLGASTTDQLMENIGAIQV 422
Cdd:cd19138 200 RRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL 255
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
129-422 |
9.69e-36 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 132.69 E-value: 9.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvTFGGQIT-----DETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgWRRSTLVITTKIY 203
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYS 283
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 284 VARQfnqiPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKydsgvpaysraslkgyqwlkdkilse 363
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN-------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 364 egrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLgASTTDQLMENIGAIQV 422
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
121-421 |
1.24e-35 |
|
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: 133.93 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 121 KYRNLGKSGLRVSCLGLGtwvtfGGQI-----TDETAEQLMTL--AYENGINLFDTAEVYAAGKAETVLGNIIKKKgwrR 193
Cdd:cd19104 1 KYRRFGRTGLKVSELTFG-----GGGIgglmgRTTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 194 STLVITTKIywgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF------ANRPDPNTPM---------EETVRAMTH 258
Cdd:cd19104 73 AGPYITTKV---RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQlhnrigDERDKPVGGTlsttdvlglGGVADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 259 VINQGMAMYWGTSRWSPMEIME------AYSVARQF---------NQIPPICEQAEYHmfqrekvevQLPELFHKIGVGA 323
Cdd:cd19104 150 LRSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVYynllnpsaaEARPRGWSAQDYG---------GIIDAAAEHGVGV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 324 MTWSPLACGIISGKYDSGVPAYSRAslkgyqwlkDKILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSV 403
Cdd:cd19104 221 MGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVSTV 287
|
330
....*....|....*...
gi 1721957790 404 LLGASTTDQLMENIGAIQ 421
Cdd:cd19104 288 LVGVKNREELEEAVAAEA 305
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
135-421 |
1.42e-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: 132.68 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGT-WVTFG-GQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIkkKGWRRSTLVITTKIywGGKAETER 212
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 213 GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEET-----VRAMTHVINQGMAMYWGTSRWSPMEIMEA-----Y 282
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPDLLRRAietgdF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 283 SVARQFNQIPPICEQAEYHMFqrekvevqlpELFHKIGVGAMTWSPLACGIISGKYDSGVPAysraslkGYQWLKDkils 362
Cdd:cd19090 157 DVVLTANRYTLLDQSAADELL----------PAAARHGVGVINASPLGMGLLAGRPPERVRY-------TYRWLSP---- 215
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 363 eegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQ 421
Cdd:cd19090 216 ----ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
133-419 |
5.19e-33 |
|
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: 125.04 E-value: 5.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTWVTFG--GQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKkkGWRRSTLVITTKI--YWGGkA 208
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 ETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRwSPMEIMEAYSVARqF 288
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 289 NQIppiceQAEYHMFQREKVEVqLPELfHKIGVGAMTWSPLAcgiisgkydSGVPAYSRASLKGYQWLKDKilseegrrq 368
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPLYADYARR--------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 369 qaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19095 209 ------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
128-437 |
8.28e-33 |
|
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: 125.81 E-value: 8.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLG----TWVtfGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAE---TVLGNIIKKKGWRRSTLVITT 200
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHanlKLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 201 KiywGGKAET--ERGLSRKHIIEGLKASLERL-QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPME 277
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 278 IMEAYSVArqfnqiPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKGYQWLK 357
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 358 DKILseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV-LLGASTTDQLMENIGAIQVlpKLSSsitHEVDS 436
Cdd:cd19077 230 GENF----EKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTD---EELKE 300
|
.
gi 1721957790 437 I 437
Cdd:cd19077 301 I 301
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
120-420 |
4.58e-32 |
|
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: 123.82 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTwVTFG---GQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIkkKGWRRSTL 196
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKI--YwGGKAETERGLSRKHIIEGLKASLERLQLEYVDVV------FAnrPDPNTPMEETVRAMTHVINQGMAMYW 268
Cdd:cd19163 78 YLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 269 GTSRWsPMEIMeAYSVARQFNQIPPICEQAEYHMFQREKVEvqLPELFHKIGVGAMTWSPLACGIISgkyDSGVPAYSRA 348
Cdd:cd19163 155 GITGY-PLDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERGPPDWHPA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 349 SlkgyQWLKDKIlseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAI 420
Cdd:cd19163 228 S----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
123-427 |
5.97e-32 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 123.70 E-value: 5.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 123 RNLGKSGLRVSCLGLGTW---VTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTLVIT 199
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 200 TKI---YWGGKAETERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPM 276
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 277 EIMEAYSVArqfnqipPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIISGK-----------YDSGVPA 344
Cdd:cd19145 160 TIRRAHAVH-------PITAvQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKakleellensdVRKSHPR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 345 YSRASLKgyqwlKDKILSEegrrqqaklkELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASTTDQLMENIGAIQVl 423
Cdd:cd19145 232 FQGENLE-----KNKVLYE----------RVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV- 294
|
....
gi 1721957790 424 pKLS 427
Cdd:cd19145 295 -KLT 297
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
120-437 |
1.37e-31 |
|
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: 123.32 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTW---VTFGGQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKKGWRRSTL 196
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 197 VITTKiyWGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTS 271
Cdd:cd19144 79 FLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 272 RWSPMEIMEAYSVArqfnqipPICE-QAEYHMF--QREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDS-------- 340
Cdd:cd19144 157 ECSAETLRRAHAVH-------PIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpddfeegd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 341 ---GVPAYSRASLKGYQWLKDKIlseegrrqqaklkelQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENI 417
Cdd:cd19144 230 frrMAPRFQAENFPKNLELVDKI---------------KAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENL 294
|
330 340
....*....|....*....|
gi 1721957790 418 GAIQVlpKLSSSITHEVDSI 437
Cdd:cd19144 295 GALKV--KLTEEEEKEIREI 312
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
135-419 |
1.79e-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: 118.14 E-value: 1.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIYWGGkaetergL 214
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArqfnQIPPI 294
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDIS----PLPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 295 CEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgiisgkydsgvpaysraslkgyqwlkdkilseegRRQQAKL 372
Cdd:cd19073 145 VNQVEFHPFlyQAELLEYCRE---NDIVITA--YSPLA-----------------------------------RGEVLRD 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1721957790 373 KELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASTTDQLMENIGA 419
Cdd:cd19073 185 PVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
129-417 |
5.62e-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: 111.20 E-value: 5.62e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIYWGGka 208
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 etergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArqf 288
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELS--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 289 nQIPPICEQAEYHMF--QRekvevQLPELFHKIGVGAMTWSPLACGiisgkydsgvpaysraslkgyqwlkdKILSEEgr 366
Cdd:cd19140 147 -EAPLFTNQVEYHPYldQR-----KLLDAAREHGIALTAYSPLARG--------------------------EVLKDP-- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 367 rqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASTTDQLMENI 417
Cdd:cd19140 193 -------VLQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
135-425 |
3.40e-27 |
|
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: 109.54 E-value: 3.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTwVTFG---------GQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKKgwrrSTLVITTKIywg 205
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRP-DPNTPMEETVRAMTHVINQGMAMYWGTSrwspmeimeAYSV 284
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS---------VYSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 285 arqfnqippicEQAEYhMFQREKVE-VQLPelfhkigVGAMTWSPLACGIISGKYDSGVPAYSRaS--LKGYQWLKDKIL 361
Cdd:cd19097 144 -----------EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR-SvfLQGLLLMEPDKL 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 362 SEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPK 425
Cdd:cd19097 204 PAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
132-419 |
3.50e-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: 109.23 E-value: 3.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 132 VSCLGLGTW-----VTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRStLVITTKIYW-- 204
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALH--PYPDD-VVIATKGGLvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAysv 284
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 285 arqfNQIPPI-CEQAEYHMFQREKVEVQlpELFHKIGVGAMTWSPLAcgiisgkydsgvpaysraslkgyqwlkdkilse 363
Cdd:cd19088 155 ----RAIVRIvSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG--------------------------------- 195
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721957790 364 eGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19088 196 -GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
120-417 |
1.14e-26 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 120 MKYRNLGKSGLRVSCLGLGTWvtfGGQITD-ETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKkgwRRSTLVI 198
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 199 TTKIYWGGKaeterglSRKHIIEGLKASLERLQLEYVDVVfanrpdpntpmeetvraMTHVINQGMAMYWGTSRWSPMEI 278
Cdd:COG1453 73 ATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLY-----------------LIHGLNTEEDLEKVLKPGGALEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 279 MEAysvARQ----------FNQIPPICEQA------EYHMFQ------REKVEVQLPELFHKIGVGAMTWSPLACGIISg 336
Cdd:COG1453 129 LEK---AKAegkirhigfsTHGSLEVIKEAidtgdfDFVQLQynyldqDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 337 kydsgvpaysraslkgyqwlkdkilseegrrqqAKLKELQAIAERlGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMEN 416
Cdd:COG1453 205 ---------------------------------NPPEKLVELLCP-PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDEN 250
|
.
gi 1721957790 417 I 417
Cdd:COG1453 251 L 251
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
122-438 |
9.46e-26 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 106.79 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 122 YRNLGKSGLRVSCLGLGTwVTFG---GQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVI 198
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 199 TTKIywgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRwSP 275
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITG-LP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEaYSVARqfnqIPP-----ICEQAEYHMFQREKVEVqLPELFHKiGVGAMTWSPLACGIISgkyDSGVPAYSRASL 350
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 351 KgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVLPKLS--S 428
Cdd:PLN02587 226 E----LK------SACAAAATHCKEK------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGidE 289
|
330
....*....|
gi 1721957790 429 SITHEVDSIL 438
Cdd:PLN02587 290 ELLSEVEAIL 299
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
135-417 |
1.32e-25 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 104.87 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGgkaeteRGL 214
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SRKHIIEGLKASLERLQLEYVDVV-----FANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARqf 288
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEGGSKeARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 289 nqIPPICEQAEYHMF--QREkvevqLPELFHKIGVGAMTWSPLAcgiisgkydsgvpaysraslkgyqwlkdkilseEGR 366
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKE-----LVEFCKEHGIVVQAYSPLG---------------------------------RGR 186
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 367 RQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASTTDQLMENI 417
Cdd:cd19071 187 RPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
129-438 |
1.79e-25 |
|
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: 105.97 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGT------WVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRSTLVITTKI 202
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 ---YWGGKAETER----GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSP 275
Cdd:cd19146 87 ttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEAYSVARQFNQIPPICEQAEYHM----FQREKVEVQLPElfhkiGVGAMTWSPLAcgiiSGKYDSGVPAYSRASLK 351
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 352 GYQWLKdkilSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQVlpKLSSSIT 431
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEI 308
|
....*..
gi 1721957790 432 HEVDSIL 438
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
123-430 |
1.90e-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: 102.61 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 123 RNLGKSGLRVSCLGLGTwVTFGGQITDET----AEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGWRRSTLVI 198
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 199 TTKIYWGGKAETErgLSRKHIIEGLKASLERLQLEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRWsP 275
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEaySVARQFNQIPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKydsGVPAYSRAS--LKG 352
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPWHPASgeLRH 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 353 YQWLKDKILSEEGRrqqaklkelqaiaerlgcTLPQLAIAWCLRNE-GVSSVLLGASTTDQLMENIGAIQVLPKLSSSI 430
Cdd:cd19153 234 YAAAADAVCASVEA------------------SLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASLGAAI 294
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
122-417 |
2.62e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 100.63 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 122 YRNLGKSGLRVSCLGLGTWVTfgGQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKkgwRRSTLVITTK 201
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 IYwggkaetERglSRKHIIEGLKASLERLQLEYVDVVF----ANRPDPNTPMEE--------------TVRAM---TH-- 258
Cdd:cd19100 74 TG-------AR--DYEGAKRDLERSLKRLGTDYIDLYQlhavDTEEDLDQVFGPggalealleakeegKIRFIgisGHsp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 259 -VINQGMAMYWgtsrwspME-IMEAYSVarqfnqippiceqAEYHMfqREKVEVQLPEL-FHKIGVGAMtwSPLACGiis 335
Cdd:cd19100 145 eVLLRALETGE-------FDvVLFPINP-------------AGDHI--DSFREELLPLArEKGVGVIAM--KVLAGG--- 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 336 gkydsgvpaysraslkgyQWLKDKILSeegrrqqaklkelqaiaerlgctlPQLAIAWCLRNEGVSSVLLGASTTDQLME 415
Cdd:cd19100 198 ------------------RLLSGDPLD------------------------PEQALRYALSLPPVDVVIVGMDSPEELDE 235
|
..
gi 1721957790 416 NI 417
Cdd:cd19100 236 NL 237
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
135-419 |
6.35e-24 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 100.90 E-value: 6.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTwVTFG--GQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKkkGWRRSTLVITTKI-------YWG 205
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 GKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDP--NTPMEETVRAMTHVINQGM--AMYWGTSRWSpmeim 279
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWA----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 280 EAYSVARQFnQIPPICEQAEYHMFQREKVEVQLPELFHKiGVGAmtwsplacgIISGKYDSGVPAYSRA--SLKGYQWLK 357
Cdd:cd19162 155 ALLRAARRA-DVDVVMVAGRYTLLDRRAATELLPLCAAK-GVAV---------VAAGVFNSGILATDDPagDRYDYRPAT 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 358 DKILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19162 224 PEVL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
133-419 |
5.67e-23 |
|
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: 97.63 E-value: 5.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTW---VTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgWRRSTLVITTKIYWGgkae 209
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 210 teRGLSRKHIIEGLKASLERLQLEYVDvVFA----NRPD------PNTPMEETVRAMT-----HVinqGMamywgTSRWS 274
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 275 P---MEIMEAYSVArqFNQIPpiceqaeYHMFQREKVEVQ-LPELFHKIGVGAMTWSPLACGIISgkydsgvpaysrasl 350
Cdd:cd19096 144 PellKEILDSYDFD--FVQLQ-------YNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA--------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 351 kgyqwlkdkilseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGA 419
Cdd:cd19096 200 -------------------NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
130-417 |
7.44e-21 |
|
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: 92.77 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 130 LRVSCLGLGTWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGN----IIKKKGWRRSTLVITTKiywG 205
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 G----------------KAETERGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRP----------DPN 246
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 247 TPMEETVRAMTHVINQGMAMYWGTSRWSPmeiMEAYSVARQFNQIPPICEQAE-----YHMFqreKVeVQLPelFHKIGV 321
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWDG---FRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP--LNLLEP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 322 GAMT----WSPLACGIISGKYDSGVPAYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLAIAWCLRN 397
Cdd:cd19099 229 EALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRALQFARST 295
|
330 340
....*....|....*....|
gi 1721957790 398 EGVSSVLLGASTTDQLMENI 417
Cdd:cd19099 296 PGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
135-422 |
1.37e-20 |
|
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: 91.90 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTwVTFGG---QITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwrRSTLVITTKIYWGGKAETE 211
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 212 RGLSRKHII--------------EGLKA----SLERLQLEYVDVVFANRPDPNTPMEET-----------VRAMTHVINQ 262
Cdd:cd19152 80 VEPTFEPGFwnplpfdavfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 263 GMAMYW--GTSRWSPME----------IMeaysVARQFNqippICEQAEYHMFqrekvevqLPELF-HKIGVgamtwspl 329
Cdd:cd19152 160 GVIKAIglGVNDWEVILrileeadldwVM----LAGRYT----LLDHSAAREL--------LPECEkRGVKV-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 330 acgIISGKYDSGVpaysrasLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGAST 409
Cdd:cd19152 216 ---VNAGPFNSGF-------LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASS 285
|
330
....*....|...
gi 1721957790 410 TDQLMENIGAIQV 422
Cdd:cd19152 286 PERVEENVALLAT 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
137-395 |
1.40e-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: 85.85 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 137 LGTW----------VTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKkgWRRSTLVITTKIYWGG 206
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 207 kaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---NTPmeetvramtHVI---NQGMAMYWGTSRWSPMEIME 280
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADverWTP---------ELIpllKSGKVKHVGVSNHNLAEIKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AYSVARQFNqIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIISGKYDSG--VPAYSrASLKGYQWLKD 358
Cdd:cd19103 153 ANEILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKhpLPEGS-GRAETYNPLLP 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 1721957790 359 KIlseegRRQQAKLKElqaIAERLGCTLPQLAIAWCL 395
Cdd:cd19103 231 QL-----EELTAVMAE---IGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
135-417 |
1.97e-18 |
|
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: 84.73 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGKAETERGL 214
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 srkhiiEGLKASLERLQLEYVDVVFANRPdpnTPME----ETVRAMTHVINQGMAMYWGTSRWSP---MEIMEAYSVARQ 287
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 288 FNQIP--PICEQAEYHMFQREkvevqlpelfHKIGVGAmtWSPLACGiisgkydsgvpaysraslkgyqwlkdKILSEeg 365
Cdd:cd19131 155 VNQIElhPRFQQRELRAFHAK----------HGIQTES--WSPLGQG--------------------------GLLSD-- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 366 rrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASTTDQLMENI 417
Cdd:cd19131 195 -------PVIGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
127-417 |
6.02e-18 |
|
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: 84.00 E-value: 6.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 127 KSGLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKkgW------RRSTLVITT 200
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 201 KIYWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPM------------EETVRAMTHVIN 261
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddeGESGTMengmsihdavdvEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 262 QGMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacGIISGKYDSG 341
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL--GSPGRANFTK 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1721957790 342 VPAYSraslKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASTTDQLMENI 417
Cdd:cd19154 221 STGVS----PAPNLLQDPI--------------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
129-334 |
8.04e-18 |
|
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: 82.87 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTFGGqitDETAEQLMTlAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGKA 208
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG---DETERAVQT-ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 ETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARqf 288
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1721957790 289 nqIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGII 334
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
129-393 |
8.17e-18 |
|
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: 82.62 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITD-ETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGK 207
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAY---GNEEAVGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSvarq 287
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLIL---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 288 FNQIPPICEQAEYHMFqREKVEVQlpELFHKIGVGAMTWSPLAcgiisgkydsgvpaysraslkgyqwlkdkilseEGRR 367
Cdd:cd19133 145 HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA---------------------------------EGRN 188
|
250 260
....*....|....*....|....*.
gi 1721957790 368 QQAKLKELQAIAERLGCTLPQLAIAW 393
Cdd:cd19133 189 NLFENPVLTEIAEKYGKSVAQVILRW 214
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
133-425 |
4.35e-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: 81.60 E-value: 4.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 133 SCLGLGTwVTFGG---QITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwrRSTLVITTKIywgGK-- 207
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 --AETERGL-----------------SRKHIIEGLKASLERLQLEYVDVVF---------ANRPDPN---TPMEETVRAM 256
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 257 THVINQGM--AMYWGTSRWSPM-EIMEAYsvarqfnQIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtwsplacgI 333
Cdd:cd19161 155 EELKKAGVikAFGLGVNEVQIClEALDEA-------DLDCFLLAGRYSLLDQSAEEEFLPRC-EQRGTSL---------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 334 ISGKYDSGVPAYSRASLKGYQWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQL 413
Cdd:cd19161 218 IGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
330
....*....|...
gi 1721957790 414 MENIGAIQ-VLPK 425
Cdd:cd19161 292 RQNVEAFQtDIPE 304
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
134-417 |
5.05e-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: 81.03 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 134 CLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVY----AAGKAetvLGNIIKKKGWRRSTLVITTKIyWGGKAE 209
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 210 TERglsrkhIIEGLKASLERLQLEYVDVVFANRP---DPNT----------------PMEETVRAMTHVINQGMAMYWGT 270
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 271 SRWSPMEIMEAYSVARqfnqIPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgiisGKYDSGVPAYsras 349
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDGNLTF---- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 350 lkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASTTDQLMENI 417
Cdd:cd19128 211 ------LND--------------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
136-395 |
1.29e-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: 79.58 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 136 GLGTWVTFGGQIT-DETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIYWGGKaetergl 214
Cdd:cd19120 10 GTGTAWYKSGDDDiQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 srkHIIEGLKASLERLQLEYVDVVFANRP----DPNTPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVARqfnq 290
Cdd:cd19120 80 ---DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 291 IPPICEQAEYHMFqrekVEVQLPEL--FH-KIGVGAMTWSPLAcgiisgkydsgvPAYSRAslkgyqwlkdkilseegrr 367
Cdd:cd19120 153 IKPAVNQIEFHPY----LYPQQPALleYCrEHGIVVSAYSPLS------------PLTRDA------------------- 197
|
250 260
....*....|....*....|....*...
gi 1721957790 368 QQAKLKELQAIAERLGCTLPQLAIAWCL 395
Cdd:cd19120 198 GGPLDPVLEKIAEKYGVTPAQVLLRWAL 225
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
129-393 |
1.99e-16 |
|
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: 78.85 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYAAgkaETVLGNIIKKKGWRRSTLVITTKIywggka 208
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 eteRGlsRKH----IIEGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRWSPM---EIME 280
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFLPEhldRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AYSVARQFNQIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPLAcgiisgkydsgvpaysraslKGYQWLKD 358
Cdd:cd19132 145 ETGVTPAVNQIElhPYFPQAEQRAYHREH------------GIVTQSWSPLG--------------------RGSGLLDE 192
|
250 260 270
....*....|....*....|....*....|....*
gi 1721957790 359 KIlseegrrqqaklkeLQAIAERLGCTLPQLAIAW 393
Cdd:cd19132 193 PV--------------IKAIAEKHGKTPAQVVLRW 213
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
131-416 |
5.22e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 78.41 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 131 RVSCLGLGTWVTFGG---QITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKKGWRRST---LVITTKIYW 204
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRERDAaddVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 GGKAETergLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNtpMEETVRAMTHVINQGMAMYWG-----TSRWSpm 276
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqfhWWDYSDPG--YLDAAKHLAELQEEGKIRHLGltnfdTERLR-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 277 EIMEAysvarqfnQIPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIISGKYdSGVPAYSRASLKGYQWL 356
Cdd:cd19101 152 EILDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGPALETRSLQ 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1721957790 357 KDKILSEEG---RRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMEN 416
Cdd:cd19101 222 KYKLMIDEWggwDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDN 284
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
128-400 |
6.70e-16 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 77.36 E-value: 6.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvTFGGQITDETAEQLMtlayENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGK 207
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNTP-------MEETVRAMTHVINQGMAMYWGTSRWSPMEIME 280
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 aysvARQFNQIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgiisgkydsgvpaysraslkgyqwlKDKI 360
Cdd:cd19135 154 ----LLEDCSVVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLA--------------------------KGKA 200
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1721957790 361 LSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 400
Cdd:cd19135 201 LEEP---------TVTELAKKYQKTPAQILIRWSIQNGVV 231
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
128-433 |
1.96e-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: 76.79 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLG------TWVTFGGQITDETAEQLMTLAYENGINLFDTAEVYAAGKAETVLGNIIKKKGwRRSTLVITTK 201
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 IYW--------GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 273
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 274 SPMEIMEAYSVARQFNQIPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgiiSGKYDSGVPAYSRAslKGY 353
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGKFQSKKAVEERK--KNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 354 QWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAiqvlpkLSSSIT 431
Cdd:cd19147 238 EGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEA------LSIKLT 311
|
..
gi 1721957790 432 HE 433
Cdd:cd19147 312 PE 313
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
129-308 |
4.03e-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: 75.61 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKkgW------RRSTLVITTKI 202
Cdd:cd19111 1 GFPMPVIGLGTY-----QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 YwggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFAN-------------RPDPNTPMEETVRAMTHVINQGMAMYWG 269
Cdd:cd19111 71 P-------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721957790 270 TSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMF--QREKV 308
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELR 180
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
135-332 |
5.58e-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: 74.51 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYAagkAETVLGNIIKKKGWRRSTLVITTKIywggkAETERGL 214
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SRKhiIEGLKASLERLQLEYVDVVFANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArqfnQIPP 293
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1721957790 294 ICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACG 332
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG 190
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
135-422 |
2.86e-14 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 72.39 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIYWggkaeteRGL 214
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSV----ARQF 288
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVvgagAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 289 NQIppiceqaEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGiisgkydsgvpaysraslkgyqwlkdKILSEEgrr 367
Cdd:cd19139 149 NQI-------ELSpYLQNRKLVAHCKQ--HGIHVTS--YMTLAYG--------------------------KVLDDP--- 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 368 qqaklkELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19139 189 ------VLAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
127-417 |
6.50e-14 |
|
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: 71.99 E-value: 6.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 127 KSGLRVSCLGLGTWVTFGGQITD--ETAeqlMTLAYENginlFDTAEVYaagKAETVLGNIIKKKG----WRRSTLVITT 200
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNavKTA---IKEGYRH----IDCAAIY---GNEKEIGKALKKLFedgvVKREDLFITS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 201 KIyWGGKAETERglsrkhIIEGLKASLERLQLEYVDVVF----------ANRPDP----NTPMEETVRAMTHVINQGMAM 266
Cdd:cd19125 76 KL-WCTDHAPED------VPPALEKTLKDLQLDYLDLYLihwpvrlkkgAHMPEPeevlPPDIPSTWKAMEKLVDSGKVR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 267 YWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgiisgkydsGVPays 346
Cdd:cd19125 149 AIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSP--- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 347 raslkGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASTTDQLMENI 417
Cdd:cd19125 208 -----GTTWVKKNVLKDP---------IVTKVAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
135-332 |
7.55e-14 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 71.64 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGKaetergl 214
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 sRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEETVRAMTHVIN---QGMAMYWGTSRWSP---MEIMEAYSVARQF 288
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVTPVI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1721957790 289 NQIP--PICEQAEYHMFQREkvevqlpelfHKIGVGAmtWSPLACG 332
Cdd:PRK11565 159 NQIElhPLMQQRQLHAWNAT----------HKIQTES--WSPLAQG 192
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
135-419 |
1.18e-13 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 70.82 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWggkaeTERgL 214
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SRKHIIEGLKASLERLQLEYVDVVFANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWS------PMEIMEAYSVAR 286
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 287 qfNQIppicEQAEYhmFQREKVEVQLPElfHKIGVGA-MTWsplacgiisgkydsgvpAYSRAslkgyqwLKDKIlseeg 365
Cdd:PRK11172 151 --NQI----ELSPY--LQNRKVVAFAKE--HGIHVTSyMTL-----------------AYGKV-------LKDPV----- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 366 rrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASTTDQLMENIGA 419
Cdd:PRK11172 192 ---------IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
129-403 |
3.03e-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: 69.74 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTfggqITDETAeQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIYWG--G 206
Cdd:cd19127 6 GVEMPALGLGVFQT----PPEETA-DAVATALADGYRLIDTAAAY---GNEREVGEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 207 KAETERGLsrkhiieglKASLERLQLEYVDVVFANRPDPNTpMEETV---RAMTHVINQGMAMYWGTSRWSP---MEIME 280
Cdd:cd19127 78 YDKALRGF---------DASLRRLGLDYVDLYLLHWPVPND-FDRTIqayKALEKLLAEGRVRAIGVSNFTPehlERLID 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 281 AYSVARQFNQIppiceqaEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcGIIsgKYDSGVPaysraslkgyqwlkdki 360
Cdd:cd19127 148 ATTVVPAVNQV-------ELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGP----------------- 197
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1721957790 361 lseEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVSSV 403
Cdd:cd19127 198 ---TGPGDVLQDPTITGLAEKYGKTPAQIVLRWHLQN-GVSAI 236
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
135-417 |
3.35e-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: 69.20 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITD-ETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIK----KKGWRRSTLVITTKI--YWGGK 207
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 AETErglsrkhiiEGLKASLERLQLEYVDVVFANRP-----DPNTPME-----ETVRAMTHVINQGMAMYWGTSRWSP-- 275
Cdd:cd19136 76 EKAR---------AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYTVrh 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 276 MEIMEAYSvarqfnQIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGiisgkydsgvpaysraslkgy 353
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG--------------------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 354 qwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASTTDQLMENI 417
Cdd:cd19136 195 ---DLRLLEDP---------TVLAIAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
127-239 |
3.42e-13 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 70.00 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 127 KSGLRVSCLGLGTwvtFGGQITDE----TAEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKK--KGWRRSTLVITT 200
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDpesiPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1721957790 201 KIywGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF 239
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
135-400 |
6.06e-13 |
|
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: 68.98 E-value: 6.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvTFGGQITDETAEQLMTLAYENginlFDTAEVYA----AGKAetvLGNIIKKKGWRRSTLVITTKIyWGGKAET 210
Cdd:cd19123 15 LGLGTW-KSKPGEVGQAVKQALEAGYRH----IDCAAIYGneaeIGAA---LAEVFKEGKVKREDLWITSKL-WNNSHAP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 211 ErglsrkHIIEGLKASLERLQLEYVD-------VVF---ANRPDPNT--------PMEETVRAMTHVINQGMAMYWGTSR 272
Cdd:cd19123 86 E------DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 273 WSPMEIMEAYSVARqfnqIPPICEQAEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgiiSGKYDSGVPAYSRA 348
Cdd:cd19123 160 FSVKKLEDLLATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPLG----SGDRPAAMKAEGEP 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1721957790 349 SLkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNEGV 400
Cdd:cd19123 225 VL-----LEDPVINK--------------IAEKHGASPAQVLIAWAIqRGTVV 258
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
128-403 |
1.14e-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: 68.06 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGqiTDETAEQLMTlAYENGINLFDTAEVY----AAGKA--ETVLGNIIKKkgwrRSTLVITTK 201
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS--PEDIKAAVLE-AIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 202 IyWGGKAEterglsRKHIIEGLKASLERLQLEYVDV------------VFANRPDPNTP----MEETVRAMTHVINQGMA 265
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLylihwpvslkpgKFSFPIEEEDFlpfdIKGVWEAMEECQRLGLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 266 MYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYH-MFQREKvevqLPELFHKIGVGAMTWSPLACgiisgkydsgvpa 344
Cdd:cd19124 147 KAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGA------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1721957790 345 ysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVSSV 403
Cdd:cd19124 206 ------PGTKWGSNAVMESD---------VLKEIAAAKGKTVAQVSLRW-VYEQGVSLV 248
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
135-417 |
2.57e-12 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 67.31 E-value: 2.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfgGQITDETAEQLMTLAYENGINLFDTAEVY----AAGKAetvLGNIIKKKGWRRSTLVITTKIyWGGKAEt 210
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYgneaEVGEA---IREKIAEGVVKREDLFITTKL-WNSYHE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 211 erglsRKHIIEGLKASLERLQLEYVDVVFANRP-------DPNTPME---------ETVRAMTHVINQGMAMYWGTSRWS 274
Cdd:cd19116 85 -----REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 275 PMEIMEAYSVArqfnQIPPICEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacgiisgkydsGVPAYSRaslkgy 353
Cdd:cd19116 160 SEQINRLLSNC----NIKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRG------ 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1721957790 354 QWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASTTDQLMENI 417
Cdd:cd19116 215 QTNPPPRLDDP---------TLVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
129-400 |
5.22e-12 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 65.88 E-value: 5.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTFGGQITDETAEQlmtlAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGKA 208
Cdd:cd19157 7 GVKMPWLGLGVFKVEEGSEVVNAVKT----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 ETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArqf 288
Cdd:cd19157 79 GYDSTL------KAFEASLERLGLDYLDLYLIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADA--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 289 nQIPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGiisgkydsgvpaysraslkgyqwlkdKILSEEgr 366
Cdd:cd19157 149 -EIVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG--------------------------QLLDNP-- 194
|
250 260 270
....*....|....*....|....*....|....
gi 1721957790 367 rqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 400
Cdd:cd19157 195 -------VLKEIAEKYNKSVAQVILRWDLQNGVV 221
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
128-417 |
1.37e-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: 65.20 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQITDetaeqLMTLAYENGINLFDTAEVYaagKAETVLGNIIK---KKGW-RRSTLVITTKIY 203
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKE-----LILNAIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 wggkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP-----------------------DPNTPMEETVRAMTHVI 260
Cdd:cd19112 79 -----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 261 NQGMAMYWGTSRWsPMEIME---AYSvarqfnQIPPICEQAEYH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIISG 336
Cdd:cd19112 150 SAGLVRSIGISNY-DIFLTRdclAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 337 KYDSGVPAysraslkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASTTDQLME 415
Cdd:cd19112 219 EWFGSVSP-----------LDDPVLKD--------------LAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKE 270
|
..
gi 1721957790 416 NI 417
Cdd:cd19112 271 NI 272
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
129-395 |
1.56e-11 |
|
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: 64.85 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKkgW------RRSTLVITTKI 202
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 YWGGkaeterglSRKHIIEG-LKASLERLQLEYVDVVFANRP---------------------DPNTPMEETVRAMTHVI 260
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 261 NQGMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIISGKYD 339
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1721957790 340 SGVPAYSRASLkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCL 395
Cdd:cd19155 224 TGSPSGSSPDL-----LQD--------------PVVKAIAERHGKSPAQVLLRWLM 260
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
128-393 |
2.56e-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: 64.33 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQItdetaEQLMTLAYENGINLFDTAEVYAAgkaETVLGNIIKK-----KGWRRSTLVITTKI 202
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVYGN---EQEVGEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 yWGGKAETErglsrkHIIEGLKASLERLQLEYVDV--------------VFANRPDPN-----TPMEETVRAMTHVINQG 263
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDGTirydsTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 264 MAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgiisgkydsGVP 343
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 344 aySRAslkgyqWLK--DKILSEEGRrqqaklkeLQAIAERLGCTLPQLAIAW 393
Cdd:cd19106 210 --DRP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
129-397 |
2.99e-11 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 63.69 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITD-ETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKKGWRRSTLVITTKIyWGGK 207
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArq 287
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSC-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 288 fnQIPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGiisgkydsgvpaysraslkgyqwlkdKILSEEgr 366
Cdd:cd19156 148 --KVAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG--------------------------KLLSNP-- 193
|
250 260 270
....*....|....*....|....*....|.
gi 1721957790 367 rqqaklkELQAIAERLGCTLPQLAIAWCLRN 397
Cdd:cd19156 194 -------VLKAIGKKYGKSAAQVIIRWDIQH 217
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
143-424 |
8.17e-10 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 59.78 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 143 FGGQITDETAEQLMTL-AYENGINLFDTAEVY----AAGKAetvLGNIIKKKGWRRSTLVITTKIyWGGKAETERglsrk 217
Cdd:cd19129 11 FGTLIPDPSATRNAVKaALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 218 hIIEGLKASLERLQLEYVDVV-----FANRP---------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSPME 277
Cdd:cd19129 82 -VKPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 278 IMEAYSVARqfnqIPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIISGKydsgvpaysraslkgyqwLK 357
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LE 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 358 DKILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGvsSVLLGASTTDQLMENIGaIQVLP 424
Cdd:cd19129 216 DPVIT--------------AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLP 265
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
128-417 |
1.60e-09 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 58.66 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVlGNIIKKKGWRRSTLVITTKIyWGgk 207
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 208 aeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNTP---------------------MEETVRAMTHVINQGMAM 266
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 267 YWGTSRWSPMEIMEAysVARQFNQIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgiisgkyDSGVPAYs 346
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------STNAPLL- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1721957790 347 raslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASTTDQLMENI 417
Cdd:cd19117 219 ------------------------KEPVIIKIAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNF 263
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
128-329 |
2.90e-09 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 57.93 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQITDETAEqlmtlAYENGINLFDTAEVYaagKAETVLGNIIKK---KGWRRSTLVITTKIYW 204
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY---QNEDEVGEGIKEaiaGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 GGKAETERGLSRkhiieglkaSLERLQLEYVDV----------------VFANRPD------PNTPMEETVRAMTHVINQ 262
Cdd:cd19121 80 TYHRRVELCLDR---------SLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDgsrdldWDWNHVDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 263 GMAMYWGTSRWS-PM--EIMEAYSVARQFNQIP--PICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPL 329
Cdd:cd19121 151 GKTKAIGVSNYSiPYleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
128-416 |
1.93e-08 |
|
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: 55.49 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQITDETAEqlmtlAYENGINLFDTAEVYaagKAETVLGNIIKK-----KGWRRSTLVITTKI 202
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKI-----ALKAGYRHLDLAKVY---QNQHEVGQALKEllkeePGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 203 yWGGKAETErglsrkHIIEGLKASLERLQLEYVD-------VVFA--NRPDPNTPME---------------ETVRAMTH 258
Cdd:cd19118 75 -WNNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKptGDLNPLTAVPtnggevdldlsvslvDTWKAMVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 259 VINQGMAMYWGTSRWSP---MEIMEAYSVARQFNQIppiceqaEYH--MFQREKVEvqlpelFHK---IGVGAmtWSPLa 330
Cdd:cd19118 148 LKKTGKVKSIGVSNFSIdhlQAIIEETGVVPAVNQI-------EAHplLLQDELVD------YCKsknIHITA--YSPL- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 331 cgiisGKYDSGVPaysraslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASTT 410
Cdd:cd19118 212 -----GNNLAGLP---------------LLVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTP 260
|
....*.
gi 1721957790 411 DQLMEN 416
Cdd:cd19118 261 SRIRSN 266
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
128-276 |
7.30e-08 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 53.66 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQitdETAEQLMTLAYENGINLFDTAEVYAA----GKAetvLGNIIKKKGWRRSTLVITTKI- 202
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 203 --YWggkaeterglsrKHIIEGLKASLERLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSPM 276
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWPVCfEKDSDDSGKPFTPVNDDGKTRYAASGDHITT 146
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
128-422 |
1.37e-07 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 53.01 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWVTFGGQitDETAEQLMTlAYENGINLFDTAEVYA-AGKAETVLGNIIKKK-GWRRSTLVITTKIyWG 205
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAK--GETYAAVTK-ALDVGYRHLDCAWFYLnEDEVGDAVRDFLKENpSVKREDLFICTKV-WN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 206 GKAETErglsrkHIIEGLKASLERLQLEYVDV------VFANRPDPNTPM-----------------EETVRAMTHVINQ 262
Cdd:cd19122 81 HLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYES 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 263 GMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACgiisgkyDSGV 342
Cdd:cd19122 155 GKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------QNQV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 343 PAysraslkgyqwlkdkilseEGRRQQAKlKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASTTDQLMENIGAIQV 422
Cdd:cd19122 221 PS-------------------TGERVSEN-PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIEL 278
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
129-398 |
2.60e-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: 52.17 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYAAgkaETVLGNIIKK---KGW-RRSTLVITTKIyW 204
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 GGKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRP------DP-------------------NTPMEETVRAMTHV 259
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPipaayvDPaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 260 INQGMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgiisgKY 338
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQ 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1721957790 339 DSGVPAYSRASLKGYQwlkdkILSEEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNE 398
Cdd:cd19114 199 GIQITAYSSFGNAVYT-----KVTKHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRN 255
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
152-422 |
7.98e-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: 50.81 E-value: 7.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 152 AEQLMTLAYENGINLFDTAEVYaaGKAETVLGNIIKKKGWRRSTLVITTKiyWG----------GKAETERGLSRKHIIE 221
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 222 GLKASLERLQlEYVDV-----------VFANrpdpntpmEETVRAMTHVINQGMAMYWGTSRWSPMEIMEA-----YSVA 285
Cdd:cd19098 113 QWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQQAETLRRaleieIDGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 286 RQFNqippiCEQAEYHMFQREKVEvQLpELFHKIGVGAMTWSPLACGIISGKYDSGVPAYSRASLKgyqwlkdkilseeg 365
Cdd:cd19098 184 RLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDRNPSPELAPLMAVLK-------------- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1721957790 366 rrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASTTDQLMENIGAIQV 422
Cdd:cd19098 243 -----------AVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
159-437 |
1.27e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.97 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 159 AYENGINLFDTAEVYAAGkaetVLGNIIkkkgwR------RSTLVITTKIywgGKAETERG-----LSRKHIIEGLKASL 227
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 228 ERLQLEYVDVV------FANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSPMEIMEAYSVArqfnqiPPICEQAEYH 301
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 302 MFQREKvevqlPELFHKIGvgamtwsplACGIisgKYdsgVPAYSrasLKGYQWLKDKILSeegrrqqaklkelqAIAER 381
Cdd:PRK10376 190 LAHRAD-----DALIDALA---------RDGI---AY---VPFFP---LGGFTPLQSSTLS--------------DVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1721957790 382 LGCTLPQLAIAWCLRNEgvSSVLL--GASTTDQLMENIGAIQVlpKLSSSITHEVDSI 437
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
135-336 |
3.51e-06 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 48.37 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYaaGKAETVlGNIIKKKGWRRSTLVITTKIyWGGKAETERGL 214
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 215 SrkhiieGLKASLERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRWSPME---IMEAYSVARQFNQ 290
Cdd:cd19130 84 A------AFAESLAKLGLDQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFLPPHlerIVAATGVVPAVNQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1721957790 291 I---PPICEQAEYHMFQREKVEVQlpelfhkigvgamTWSPLACGIISG 336
Cdd:cd19130 158 IelhPAYQQRTIRDWAQAHDVKIE-------------AWSPLGQGKLLG 193
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
128-301 |
4.50e-05 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 45.13 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYAAgkaETVLGNIIK---KKGW-RRSTLVITTKIy 203
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGN---EKEVGEGVNraiDEGLvKREELFLTSKL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 WGGKAEterglsRKHIIEGLKASLERLQLEYVDVVF-----ANRPDP--------------------NTPMEETVRAMTH 258
Cdd:cd19113 78 WNNFHD------PKNVETALNKTLSDLKLDYVDLFLihfpiAFKFVPieekyppgfycgdgdnfvyeDVPILDTWKALEK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1721957790 259 VINQGMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYH 301
Cdd:cd19113 152 LVDAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHH 190
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
128-301 |
4.98e-05 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 45.10 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 128 SGLRVSCLGLGTWvtfggQITDETAEQLMTLAYENGINLFDTAEVYA----AGKAetvLGNIIKKKGWRRSTLVITTKIy 203
Cdd:cd19115 9 SGYDMPLVGFGLW-----KVNNDTCADQVYNAIKAGYRLFDGACDYGneveAGQG---VARAIKEGIVKREDLFIVSKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 204 WGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP------DP------------------NTPMEETVRAMTHV 259
Cdd:cd19115 80 WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvDPavryppgwfydgkkvefsNAPIQETWTAMEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1721957790 260 INQGMAMYWGTSRWSPMEIMEAYSVARqfnqIPPICEQAEYH 301
Cdd:cd19115 154 VDKGLARSIGVSNFSAQLLMDLLRYAR----IRPATLQIEHH 191
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
131-329 |
2.46e-04 |
|
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: 43.02 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 131 RVSCLGLGTWVTFGGQITDEtaeqlMTLAYENGINLFDTAEVYaAGKAETVLG--NIIKKKGWRRSTLVITTKIYWggka 208
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEA-----VKVAIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKLWC---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 209 eterGLSRKHIIE-GLKASLERLQLEYVDVVFANRP------DPNTPMEE-------------TVRAMTHVINQGMAMYW 268
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRsgmvipsdtdfldTWEAMEDLVIEGLVKNI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1721957790 269 GTSRWSpMEIMEaysvaRQFNQ----IPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 329
Cdd:cd19110 149 GVSNFN-HEQLE-----RLLNKpglrVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
129-329 |
1.05e-03 |
|
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: 40.86 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 129 GLRVSCLGLGTWVTFGGQITDETAeqlmtLAYENGINLFDTAEVYaagKAETVLGNIIKKK----GWRRSTLVITTKIYw 204
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY---QNENEVGEAIQEKikeqVVKREDLFIVSKLW- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 205 ggKAETERGLSRkhiiEGLKASLERLQLEYVDVVFANRPD-------------------PNTPMEETVRAMTHVINQGMA 265
Cdd:cd19107 72 --CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 266 MYWGTSRWSPMEImeaysvARQFNQiP-----PICEQAEYHMF-QREKvevqLPELFHKIGVGAMTWSPL 329
Cdd:cd19107 146 KAIGVSNFNHLQI------ERILNK-PglkykPAVNQIECHPYlTQEK----LIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
135-251 |
6.14e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 38.37 E-value: 6.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1721957790 135 LGLGTWVTfgGQITDETAEQLMTLAYENGINLFDTAEVYaagKAETVLGNIIKKK----GWRRSTLVITTKIyWGGKAET 210
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1721957790 211 ErgLSRKhiieGLKASLERLQLEYVDVVFANRPDPNTPMEE 251
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEE 122
|
|
| |
