|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
89-411 |
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: 703.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 248
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 249 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 328
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 329 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 408
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 1270111343 409 NKP 411
Cdd:cd19159 321 NKP 323
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
90-399 |
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: 664.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 90 PHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITT 169
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 170 KLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 249
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 AYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERI 329
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 330 VSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 399
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
87-411 |
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: 634.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 87 TGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLV 166
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 246
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 247 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 326
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 327 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 406
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
....*
gi 1270111343 407 LRNKP 411
Cdd:cd19160 321 LGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
91-407 |
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: 593.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 170
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 250
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 251 YSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIV 330
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 331 SEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 407
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
89-412 |
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: 585.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 248
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 249 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 328
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 329 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 408
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 1270111343 409 NKPY 412
Cdd:cd19158 321 NKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
89-406 |
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 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 246
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 247 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 326
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 327 ERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 406
Cdd:cd19143 241 DR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
89-411 |
1.43e-162 |
|
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: 460.01 E-value: 1.43e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWGGKAEtERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 248
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 249 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWL 325
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 326 KERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDN 405
Cdd:cd19142 240 DGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELER 319
|
....*.
gi 1270111343 406 ILRNKP 411
Cdd:cd19142 320 ILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
98-389 |
2.62e-155 |
|
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: 440.49 E-value: 2.62e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKA 177
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 E-TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 256
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 FNMIPPVCEQAEYHLFQREKVEvQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRK 336
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1270111343 337 QQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 389
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
89-411 |
9.20e-102 |
|
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: 305.18 E-value: 9.20e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWvTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSL 165
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 244
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 245 MEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcy 322
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 323 qWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 402
Cdd:COG0667 232 -NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
....*....
gi 1270111343 403 IDNILRNKP 411
Cdd:COG0667 306 LDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
89-406 |
4.09e-91 |
|
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: 277.53 E-value: 4.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVIT 168
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 247
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwl 325
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 326 kERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDN 405
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDE 307
|
.
gi 1270111343 406 I 406
Cdd:cd19087 308 L 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
89-391 |
3.43e-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: 252.53 E-value: 3.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkg 159
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 160 wRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWG 238
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 239 TSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR 316
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 317 ASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
98-404 |
2.60e-77 |
|
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: 241.66 E-value: 2.60e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LY 172
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 173 WGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAys 252
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 varqFNMIPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkeri 329
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 330 vSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 404
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
91-393 |
3.34e-77 |
|
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: 241.78 E-value: 3.34e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVI 167
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 168 TTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 244
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 245 MEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQW 324
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 325 LKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 393
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
102-387 |
1.86e-74 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 232.02 E-value: 1.86e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTWvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETE 180
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 181 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMI 260
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 261 PPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnk 340
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1270111343 341 lkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLG 387
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
94-404 |
7.92e-73 |
|
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: 230.56 E-value: 7.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 94 LGKSGLRVSCLGLGTWVtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLV 166
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 246
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 247 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqw 324
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 325 lKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 404
Cdd:cd19081 235 -AKRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
93-391 |
3.83e-70 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 223.62 E-value: 3.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 93 NLGKSGLRVSCLGLGTWvTFGGQ------ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLV 166
Cdd:cd19079 4 RLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 245
Cdd:cd19079 82 IATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 246 EIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKCYQW 324
Cdd:cd19079 162 QFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 325 LKErivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19079 241 DYF---TEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
91-390 |
9.80e-67 |
|
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: 214.96 E-value: 9.80e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSLV 166
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKL--------Y--WGgkaeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMY 236
Cdd:cd19151 81 ISTKAgytmwpgpYgdWG---------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 237 WGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR 316
Cdd:cd19151 152 VGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111343 317 ASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19151 230 AA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
101-406 |
7.50e-65 |
|
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: 210.50 E-value: 7.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 101 VSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK--- 170
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 --LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVIN 230
Cdd:cd19094 79 pgEGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 231 QGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--G 308
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 309 NGVPESSRASLkcYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19094 238 AARPEGGRLNL--FPGYMARYRSPQALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDA 312
|
330
....*....|....*....
gi 1270111343 389 IQV-LPKmtsHVVNEIDNI 406
Cdd:cd19094 313 FDVpLSD---ELLAEIDAV 328
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
104-407 |
2.20e-64 |
|
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: 208.32 E-value: 2.20e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvTFGGQ---ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETE 180
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 181 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmI 260
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 261 PPVCEQAEYHLFqREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQ 338
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 339 NKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 407
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
90-392 |
2.21e-64 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 208.85 E-value: 2.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 90 PHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLV 166
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS 243
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 244 AMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyq 323
Cdd:cd19150 159 PERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS----- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270111343 324 wlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 392
Cdd:cd19150 233 --KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
89-392 |
2.19e-61 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 202.14 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSL 165
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 242
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 243 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--K 320
Cdd:PRK09912 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegN 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 321 CYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 392
Cdd:PRK09912 250 KVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
94-391 |
7.06e-60 |
|
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: 197.06 E-value: 7.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 94 LGKSGLRVSCLGLGTwVTFGGQ----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITT 169
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 170 KLYWG--GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 247
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKE 327
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111343 328 RIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19080 236 GKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
101-409 |
1.05e-55 |
|
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: 185.87 E-value: 1.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 101 VSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggk 176
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 aetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 256
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 fnmipPVCEQAEYHLFQREKVEVQLPEL-YHKIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSE 332
Cdd:cd19085 150 -----IDSNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 333 EG--RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 409
Cdd:cd19085 215 PGaeEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
92-391 |
4.29e-50 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 171.69 E-value: 4.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 92 RNLGKSGLRVSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVI 167
Cdd:cd19149 2 RKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 168 TTK--LYWGGKAETE----------RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAM 235
Cdd:cd19149 79 ATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 236 YWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VP 312
Cdd:cd19149 159 AIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 313 ESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19149 232 GDARSGIPWFS--------PENREKVLALLEkWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
92-406 |
8.38e-50 |
|
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto reductase IolS, also called vegetative protein 147 (VEG147), is a founding member of aldo-keto reductase family 11 member A1 (AKR11A1). It is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose, and methylglyoxal in the presence of NADPH, albeit with poor efficiency in vitro. Bacillus aryabhattai aldo keto reductase is a founding member of aldo-keto reductase family 11 member D1 (AKR11D1).
Pssm-ID: 381309 [Multi-domain] Cd Length: 307 Bit Score: 170.68 E-value: 8.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 92 RNLGKSGLRVSCLGLGTwVTFGGQ-----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 166
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 244
Cdd:cd19083 79 IATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 245 MEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQW 324
Cdd:cd19083 158 EQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 325 LKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 402
Cdd:cd19083 225 RNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAF 302
|
....
gi 1270111343 403 IDNI 406
Cdd:cd19083 303 IDAL 306
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
90-403 |
1.49e-49 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 170.09 E-value: 1.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 90 PHRNLGKSGLRVSCLGLG----TWvtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 165
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 240
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 241 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRA 317
Cdd:cd19076 154 EASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 318 SLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMT 396
Cdd:cd19076 222 DD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLT 296
|
....*..
gi 1270111343 397 SHVVNEI 403
Cdd:cd19076 297 PEELAEI 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
99-388 |
8.90e-47 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 160.72 E-value: 8.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 99 LRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YW 173
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIME 249
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 AYSVArqfnmippvCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkeri 329
Cdd:cd19086 158 RGGID---------VVQVIYNLLDQRPEEELFPLA-EEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 330 vseegrkqqnklkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19086 205 -------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
100-388 |
4.93e-46 |
|
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: 160.47 E-value: 4.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 100 RVSCLGLGTW------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLyw 173
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 ggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 252
Cdd:cd19093 78 ---APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSRAslkcyqwlkeRIVS 331
Cdd:cd19093 155 ALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPEnPPPGGRR----------RLFG 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 332 EEGRKQ-QNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGA 388
Cdd:cd19093 224 RKNLEKvQPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
98-407 |
6.87e-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: 160.09 E-value: 6.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTW-VTFG-GQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW- 173
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 ---GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 250
Cdd:cd19078 78 idgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 251 YSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlke 327
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 328 rivSEEGRKQQNKLKDL-SPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 406
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDA 300
|
.
gi 1270111343 407 L 407
Cdd:cd19078 301 L 301
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
98-390 |
3.79e-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: 154.69 E-value: 3.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVTFGGQ---ISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYw 173
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdYSDDKKAiEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 ggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 253
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 254 ARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivsee 333
Cdd:cd19072 152 LKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG------------------------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 334 grkqqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19072 203 -------SPLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
101-407 |
8.11e-43 |
|
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: 152.06 E-value: 8.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 101 VSCLGLGTWVTFGGQ------ISDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK-- 170
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggwgPQDD-RDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImea 250
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 251 ysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPelY---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK 326
Cdd:cd19102 154 ----KRCQAIHPIASlQPPYSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 327 -ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 404
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIE 299
|
...
gi 1270111343 405 NIL 407
Cdd:cd19102 300 ALL 302
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
102-388 |
2.27e-42 |
|
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: 150.78 E-value: 2.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-- 175
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 ---KAETERgLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 252
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 VARQFNMIPPVCEQAEYHLFqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLK 320
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 321 CYQwlkerivSEEGRKQQNKLKDLspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19082 232 VYY-------SEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
104-406 |
1.34e-40 |
|
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: 146.16 E-value: 1.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterG 182
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 183 LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPP 262
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 263 VCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEe 333
Cdd:cd19075 156 TVYQGMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 334 grkqqnkLKDLSPIAERLGCTLPQLAVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 406
Cdd:cd19075 234 -------LEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
102-388 |
2.55e-37 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 137.08 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK---- 170
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 249
Cdd:cd19752 79 pRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 AYSVARQFNMIPPVCEQAEYHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRAS 318
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 319 LKCYqwlkerivseEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19752 230 PEQY----------DGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
89-389 |
2.23e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 133.48 E-value: 2.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTwvTFGGQISDEVAERlmtiAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVIT 168
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG--GGLPRESPELLRR----ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVVF---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 245
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 246 E--IMEA-----YSVArqfnMIPpvceqaeY-HLFQREKVEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessr 316
Cdd:cd19105 148 AevLQAAiesgwFDVI----MVA-------YnFLNQPAELEEALAAAAeKGIGVVAMK--TLAGGY-------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111343 317 aslkcyqwlkerivSEEGRKQQNKLKDLSpiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 389
Cdd:cd19105 201 --------------LQPALLSVLKAKGFS---------LPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
89-408 |
9.14e-36 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 134.60 E-value: 9.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHrnlgkSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 161
Cdd:PRK10625 6 IPH-----SSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 162 RSSLVITTKLywGGKAET-------ERGLSRKHIIEGLKGSLQRLQLEYVD---VVFANRP-----------DSNTP--- 217
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 218 MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSP 297
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 298 LACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGS 376
Cdd:PRK10625 236 LAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|..
gi 1270111343 377 STPEQLIENLGAIQVlpKMTSHVVNEIDNILR 408
Cdd:PRK10625 310 TTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
102-388 |
1.40e-35 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 131.59 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTWVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkA 177
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 ETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqF 257
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 258 NMIppvceQAEYHLFQREKVEVqLPELY-HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrk 336
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLAAeAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR-------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 337 qqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19095 209 -------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
97-388 |
2.49e-35 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 130.95 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 176
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 AeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 256
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 fnmIPPVCEQAEYHLFQREkvevqlPEL--YHK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEe 333
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELlaFCReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 334 grkqqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENLGA 388
Cdd:COG0656 193 -------------IAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
98-391 |
6.68e-35 |
|
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: 130.00 E-value: 6.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvTFGGQIS-----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLY 172
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 173 wggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 252
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 VARQfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSE 332
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE---------------------KTNRTLEE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 333 egrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVSSVLLgSSTPEQLIENLGAIQV 391
Cdd:cd19137 206 --------------IAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
97-404 |
3.58e-34 |
|
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: 128.14 E-value: 3.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWvTFGGQISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwgg 175
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEiEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 kaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVAR 255
Cdd:cd19138 80 ----PSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 256 QFNMippVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegr 335
Cdd:cd19138 155 GGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENP-------------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 336 kqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 404
Cdd:cd19138 208 -------TLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
98-382 |
5.86e-34 |
|
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: 128.58 E-value: 5.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVT----FGGqiSDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK- 170
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIME 249
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 AY-SVARQFNMIPPvceqaeYHLFQREKVEVQLP-ELYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKC 321
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPyARKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111343 322 YQwlkerivseEGRKQQ-----NKLKDLSpiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 382
Cdd:cd19148 225 FQ---------EPRFSQylaavEELDKLA--QERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
96-396 |
7.22e-34 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 127.67 E-value: 7.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 96 KSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LY 172
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 173 WGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeime 249
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 aysvarQFNM------IPPVCEQAEYHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessrasl 319
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGG------------------ 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 320 kcyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 396
Cdd:cd19092 209 --------RLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
89-411 |
1.76e-33 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 127.56 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSL 165
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 240
Cdd:cd19144 79 FLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 241 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRAS 318
Cdd:cd19144 157 ECSAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 319 LKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 396
Cdd:cd19144 225 FEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLT 302
|
330
....*....|....*
gi 1270111343 397 SHVVNEIDNILRNKP 411
Cdd:cd19144 303 EEEEKEIREIAEEAE 317
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
89-396 |
1.12e-32 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 124.88 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 242
Cdd:COG4989 81 TKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 243 SAMeimeaysvarQFNMI------PPVCEQAEYHLFQREKVE------VQLpelyHKIGVgaMTWSPLACGIISGKYgng 310
Cdd:COG4989 161 TPS----------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 311 vpessraslkcyqwlkerivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 390
Cdd:COG4989 222 --------------------DEQFPRLRAALDE---LAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALD 278
|
....*.
gi 1270111343 391 VlpKMT 396
Cdd:COG4989 279 I--ELT 282
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
97-404 |
3.94e-32 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 123.50 E-value: 3.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLG----TWVtfGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITT 169
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 170 KlywGGKAET--ERGLSRKHIIEGLKGSLQRL-QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 246
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 247 IMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlk 326
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL---- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 327 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 404
Cdd:cd19077 226 DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
90-403 |
1.15e-31 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 122.16 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 90 PHRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 166
Cdd:cd19145 1 PRVKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 167 ITTKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS 243
Cdd:cd19145 79 LATKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEAS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 244 AMEIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQ 323
Cdd:cd19145 158 ADTIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 324 WLKeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNE 402
Cdd:cd19145 228 SHP-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKE 303
|
.
gi 1270111343 403 I 403
Cdd:cd19145 304 I 304
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
104-390 |
5.65e-30 |
|
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: 116.88 E-value: 5.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGT-WVTFG-GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIkkKGWRRSSLVITTKLywGGKAETER 181
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 182 GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQ 256
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 FNMIPPVCeqaEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrk 336
Cdd:cd19090 156 FDVVLTAN---RYTLLDQSAADELLPAAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE-------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1270111343 337 QQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19090 217 LLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-406 |
1.94e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 113.90 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 91 HRNLGKSGLRVSCLGLGtwvtfGGQI-------SDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRS 163
Cdd:cd19104 2 YRRFGRTGLKVSELTFG-----GGGIgglmgrtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 164 SLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTP--------------MEEIVRAMTHV 228
Cdd:cd19104 74 GPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDkpvggtlsttdvlgLGGVADAFERL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 229 INQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL------FQREKVEV-----QLPELYHKIGVGAMTWSP 297
Cdd:cd19104 151 RSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLlnpsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 298 LACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSS 377
Cdd:cd19104 226 LAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA----AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVK 292
|
330 340
....*....|....*....|....*....
gi 1270111343 378 TPEQLIENLGAIQVLPkMTSHVVNEIDNI 406
Cdd:cd19104 293 NREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
98-407 |
4.51e-27 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 110.21 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGT------WVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL 171
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 ---YWGGKAETER----GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 244
Cdd:cd19146 87 ttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 245 MEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKVEVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLK 320
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 321 CYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVV 400
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEI 308
|
....*..
gi 1270111343 401 NEIDNIL 407
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
101-388 |
6.13e-27 |
|
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde dehydrogenase is a founding member of aldo-keto reductase family 13 member B1 (AKR13B1). phenylacetaldehyde dehydrogenase (EC 1.2.1.39) catalyzes the NAD+-dependent oxidation of phenylactealdehyde to phenylacetic acid.
Pssm-ID: 381314 [Multi-domain] Cd Length: 256 Bit Score: 108.07 E-value: 6.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 101 VSCLGLGTW-----VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW-- 173
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 253
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 254 ARqfnmIppVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivsee 333
Cdd:cd19088 158 VR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG--------GGDLAQPGG----------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 334 grkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19088 205 ---------LLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
89-386 |
1.31e-25 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 106.83 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTWvtfGGQISD-EVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVI 167
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 168 TTKLYWGGKaeterglSRKHIIEGLKGSLQRLQLEYVDVVFanrpdsntpmeeIvramtHVINQGMAMYWGTSRWSAMEI 247
Cdd:COG1453 73 ATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLYL------------I-----HGLNTEEDLEKVLKPGGALEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAysvARQ----------FNMIPPVCEQA-E-----------YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisg 305
Cdd:COG1453 129 LEK---AKAegkirhigfsTHGSLEVIKEAiDtgdfdfvqlqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 306 kygngvpessraslkcyqwlkerivseegrkqqnKLKDLSPIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQL 382
Cdd:COG1453 202 ----------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQL 247
|
....
gi 1270111343 383 IENL 386
Cdd:COG1453 248 DENL 251
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
89-389 |
1.66e-25 |
|
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: 104.94 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 89 MPHRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSL 165
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV------FAnrPDSNTPMEEIVRAMTHVINQGMAMYW 237
Cdd:cd19163 78 YLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 238 GTSRWSaMEIMeAYSVARQFNMIPPVCEQAEYHLFQREKVEvqLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRA 317
Cdd:cd19163 155 GITGYP-LDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 318 SlkcyQWLKERIvseegrkqqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 389
Cdd:cd19163 228 S----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
104-386 |
7.29e-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: 102.17 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGL 183
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 SRKHIIEGLKGSLQRLQLEYVDVV-----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 257
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 258 nmIPPVCEQAEYHLF--QREKVEvqlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseeg 334
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKELVE------FcKEHGIVVQAYSPLGRG-------------RRPLLDD------------- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 335 rkqqnklKDLSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 386
Cdd:cd19071 193 -------PVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
104-388 |
9.26e-25 |
|
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: 101.96 E-value: 9.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergL 183
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 263
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 264 CEQAEYH--LFQREKVEVQLPelyHKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnkl 341
Cdd:cd19073 145 VNQVEFHpfLYQAELLEYCRE---NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1270111343 342 kdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGA 388
Cdd:cd19073 190 -----IAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
98-386 |
9.46e-25 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 101.95 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGka 177
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 etergLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 257
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 258 nmIPPVCEQAEYH--LFQRekvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegr 335
Cdd:cd19140 148 --APLFTNQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLARG---------------------EVLKDPVLQE--- 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1270111343 336 kqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENL 386
Cdd:cd19140 197 -----------IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
104-394 |
7.26e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 99.91 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywg 174
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 175 GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSv 253
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 254 ARQFNMIppvceQAEYHLF-QREKVEVQLPELyHKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCYQWlkerivse 332
Cdd:cd19097 152 SFKIDII-----QLPFNILdQRFLKSGLLAKL-KKKGIEIHARSVFLQGLL-------LMEPDKLPAKFAPA-------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 333 egrkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK 394
Cdd:cd19097 211 -----KPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
104-388 |
2.81e-23 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 98.97 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTwVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWG 174
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 175 GKAETER--GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeim 248
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 249 eAYSVARQFN----MIPpvceqAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQW 324
Cdd:cd19162 156 -LLRAARRADvdvvMVA-----GRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111343 325 LKERIVSeegRKQQnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19162 222 ATPEVLA---RARR-----LAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-386 |
2.57e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 92.16 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 91 HRNLGKSGLRVSCLGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTK 170
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 LYWGGKAETERGLSRkhiieglkgSLQRLQLEYVDVVF----ANRPDSNTPMEE--IVRAMTHVINQGMAMYWGTS--RW 242
Cdd:cd19100 74 TGARDYEGAKRDLER---------SLKRLGTDYIDLYQlhavDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISghSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 243 SAM-EIMEAYsvarQFNMIPPVCEQAEYHlfQREKVEVQLPELY-HKIGVGAMtwSPLACGiisgkygngvpessraslk 320
Cdd:cd19100 145 EVLlRALETG----EFDVVLFPINPAGDH--IDSFREELLPLAReKGVGVIAM--KVLAGG------------------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111343 321 cyQWLKERIVSeegrkqqnklkdlspiaerlgctlPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 386
Cdd:cd19100 198 --RLLSGDPLD------------------------PEQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
102-388 |
6.00e-21 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 91.47 E-value: 6.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkae 178
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 179 teRGLSRKHIIEGLKGSLQRLQLEYVDvVFA----NRPD------SNTPMEEIVRAMT-----HVinqGMamywgTSRWS 243
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 244 A---MEIMEAYsvarQFNMIppvceQAEYHLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessrasl 319
Cdd:cd19096 144 PellKEILDSY----DFDFV-----QLQYNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA--------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 320 kcyqwlkerivseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19096 200 -------------------NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
90-392 |
3.16e-20 |
|
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: 90.29 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 90 PHRNLGKSGLRVSCLGLGTwVTFGGQISDEV----AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSL 165
Cdd:cd19153 1 FGETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 166 VITTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 242
Cdd:cd19153 80 TVATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 243 sAMEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPE-------- 313
Cdd:cd19153 158 -PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgel 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 314 --SSRASLKcyqWLKERIVSeegrkqqnklkdlspiaerlgctLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19153 232 rhYAAAADA---VCASVEAS-----------------------LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVD 285
|
..
gi 1270111343 391 VL 392
Cdd:cd19153 286 AV 287
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
99-386 |
7.64e-20 |
|
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: 89.68 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 99 LRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywG 174
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 175 G----------------KAETERGLSRKHIIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSN 215
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 216 TPMEEIVRAMTHVINQGMAMYWGTSRWSAmeiMEAYSVARQFNMIPPVCE---------------QAEYHLFQREKVEVQ 280
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWDG---FRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 281 ---------LPELYHKIGVGAMTWSPLAcgiiSGKYGNGVPESSRAslkcyqwlkerivseegrkqqnklkdlspiAERL 351
Cdd:cd19099 235 ntvkgealsLLEAAKELGLGVIASRPLN----QGQLLGELRLADLL------------------------------ALPG 280
|
330 340 350
....*....|....*....|....*....|....*
gi 1270111343 352 GCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 386
Cdd:cd19099 281 GATLAQRALQFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
96-386 |
9.12e-20 |
|
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: 89.01 E-value: 9.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 96 KSGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITT 169
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 170 KLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVIN 230
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 231 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnG 310
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------G 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 311 VPEssRASLkcyqwlkerIVSEEGRKQQNKLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 386
Cdd:cd19154 212 SPG--RANF---------TKSTGVSPAPNLLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
92-407 |
2.06e-19 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 88.30 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 92 RNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:PLN02587 2 RELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 169 TKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSaM 245
Cdd:PLN02587 81 TKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP-L 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 246 EIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEVqLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASLK 320
Cdd:PLN02587 157 AIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 321 cyqwLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--MT 396
Cdd:PLN02587 227 ----LKSacAAAATHCKEK--------------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgID 288
|
330
....*....|.
gi 1270111343 397 SHVVNEIDNIL 407
Cdd:PLN02587 289 EELLSEVEAIL 299
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
98-386 |
1.31e-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: 84.93 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGK 176
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAY 251
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 252 SvarqFNMIPPVCEQAEYHLFqREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivs 331
Cdd:cd19133 144 L----HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA-------------------------------- 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 332 eEGRKQ--QNKLkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 386
Cdd:cd19133 185 -EGRNNlfENPV--LTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
103-386 |
1.47e-18 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 85.27 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 103 CLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAE 178
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 179 TERglsrkhIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGT 239
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 240 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRAS 318
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTF 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 319 LKCyqwlkerivseegrkqqnklKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 386
Cdd:cd19128 211 LND--------------------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
104-386 |
6.80e-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: 82.81 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGL 183
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 srkhiiEGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArq 256
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 fnmipPVCEQAEYH-LFQREkvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegr 335
Cdd:cd19131 153 -----PVVNQIELHpRFQQR----ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1270111343 336 kqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 386
Cdd:cd19131 200 -----------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
104-391 |
1.09e-17 |
|
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: 83.04 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETE 180
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 181 RGLSRKHIIEGLKG------------------SLQRLQLEYVDVVFANRPDSNTP-----------MEEIVRAMTHVINQ 231
Cdd:cd19152 80 VEPTFEPGFWNPLPfdavfdysydgilrsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 232 GMAMYW--GTSRWS-AMEIME-----AYSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgII 303
Cdd:cd19152 160 GVIKAIglGVNDWEvILRILEeadldWVMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 304 SGKYGNGVpessRASLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLI 383
Cdd:cd19152 218 AGPFNSGF----LAGGDNFDYYEYGPAPPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVE 290
|
....*...
gi 1270111343 384 ENLGAIQV 391
Cdd:cd19152 291 ENVALLAT 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
106-364 |
1.71e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.38 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 106 LGTW----------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGG 175
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 kaeteRGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYS 252
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIV 330
Cdd:cd19103 156 ILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAE 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 1270111343 331 SEEGRKQQnkLKDLSP----IAERLGCTLPQLAVAWCL 364
Cdd:cd19103 224 TYNPLLPQ--LEELTAvmaeIGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
104-412 |
2.14e-17 |
|
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: 82.07 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETEr 181
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 182 glsrkHIIEGLKGSLQRLQLEYVD-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWS 243
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 244 AMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQ 323
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 324 WLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 402
Cdd:cd19123 226 LLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMAT 286
|
330
....*....|
gi 1270111343 403 IDNILRNKPY 412
Cdd:cd19123 287 IAALDRHHRY 296
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
96-386 |
1.28e-16 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 79.70 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 96 KSGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyW 173
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKT-----AIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FANRPDSNTP---------MEEIVRAMTHVINQGMAMYWGT 239
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVRLKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 240 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASL 319
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSPGTTWVKK 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1270111343 320 KCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGvSSVLLGSSTPEQLIENL 386
Cdd:cd19125 215 NV---LKDPIVTK--------------VAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
105-412 |
1.32e-16 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 79.20 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 105 GLGTWV--TFGGQISDEVAErLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterg 182
Cdd:cd19120 10 GTGTAWykSGDDDIQRDLVD-SVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 183 lsrkHIIEGLKGSLQRLQLEYVDVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 258
Cdd:cd19120 80 ----DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 259 mIPPVCEQAEYHLFqrekVEVQLPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRK 336
Cdd:cd19120 153 -IKPAVNQIEFHPY----LYPQQPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGP 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1270111343 337 QQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 412
Cdd:cd19120 201 LDPVLEK---IAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
100-388 |
2.00e-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: 79.18 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 100 RVSCLGLGTWVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYW 173
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETergLSRKHIIEGLKGSLQRLQLEYVDVV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEI 247
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAysvarqfnMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCY 322
Cdd:cd19101 154 LDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKY 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 323 QwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 388
Cdd:cd19101 224 K----LMIDEWGgwDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
104-386 |
3.77e-16 |
|
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: 77.97 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKLywggkAETERGL 183
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 SRKhiIEGLKGSLQRLQLEYVDVVFANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPP 262
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 263 VCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnk 340
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVGRLLDN-----PAVTA------------------------ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1270111343 341 lkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 386
Cdd:cd19134 201 ------IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
88-385 |
7.80e-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: 76.98 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 88 GMPHRNLgKSGLRVSCLGLGTWvTFGGQISDEVAERLMtiayESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVI 167
Cdd:cd19135 1 GTPTVRL-SNGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 168 TTKLyWGGKAETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTS 240
Cdd:cd19135 72 TTKL-WPSDYGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 241 RWSAMEIMEaysvARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslk 320
Cdd:cd19135 145 NFLIEHLEQ----LLEDCSVVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLAKG------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 321 cyQWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIEN 385
Cdd:cd19135 199 --KALEEPTVTE--------------LAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKEN 245
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
98-412 |
1.94e-15 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 76.38 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVTFGgqisDEVAERLMTiAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKL 171
Cdd:cd19111 1 GFPMPVIGLGTYQSPP----EEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 YwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWG 238
Cdd:cd19111 71 P-------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 239 TSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEVQLPelyHKIGVGAmtWSPLacgiisgkygnGVPesSR 316
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPL-----------GSP--GR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 317 ASLkcYQWLKERIVSEEgrkqQNKLKdlspIAERLGCTLPQLAVAWCL-RNEGvssVLLGSSTPEQLIENLGAIQVlpKM 395
Cdd:cd19111 202 ANQ--SLWPDQPDLLED----PTVLA----IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--EL 266
|
330
....*....|....*..
gi 1270111343 396 TSHVVNEIDNILRNKPY 412
Cdd:cd19111 267 TEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
104-409 |
4.14e-15 |
|
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: 75.40 E-value: 4.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEt 179
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 180 erglsRKHIIEGLKGSLQRLQLEYVDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWS 243
Cdd:cd19116 85 -----REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 244 AMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLkcy 322
Cdd:cd19116 160 SEQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRGQTN--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 323 qwlkerivsEEGRKQQNKLKDlspIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVN 401
Cdd:cd19116 218 ---------PPPRLDDPTLVA---IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKEN---IDIFDfQLTPEEVA 280
|
....*...
gi 1270111343 402 EIDNILRN 409
Cdd:cd19116 281 ALNSFNTN 288
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
97-404 |
8.46e-15 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 74.86 E-value: 8.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLG------TWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK 170
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 171 LYW--------GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 242
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 243 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcy 322
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVL---------GGGKFQSKKA----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 323 qwLKERIVSEEGRK------QQNKL-----KDLSPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19147 230 --VEERKKNGEGLRsfvggtEQTPEevkisEALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALS 307
|
330
....*....|....
gi 1270111343 391 VlpKMTSHVVNEID 404
Cdd:cd19147 308 I--KLTPEEIEYLE 319
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
98-386 |
1.20e-14 |
|
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: 74.10 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKL 171
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 YWGGkaeterglSRKHIIEG-LKGSLQRLQLEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVI 229
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 230 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYG 308
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 309 NGVPESSRASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 386
Cdd:cd19155 224 TGSPSGSSPDL-----LQDPVVKA--------------IAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
97-386 |
2.36e-14 |
|
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: 73.07 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGgqiSDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKL 171
Cdd:cd19124 1 SGQTMPVIGMGTASDPP---SPEDIKAAVLEAIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 yWGGKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAM 235
Cdd:cd19124 75 -WCSDAH------PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 236 YWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPE 313
Cdd:cd19124 148 AIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVME 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1270111343 314 SsraslkcyQWLKErivseegrkqqnklkdlspIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 386
Cdd:cd19124 218 S--------DVLKE-------------------IAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
98-308 |
7.12e-14 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 70.93 E-value: 7.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVTfggqISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKA 177
Cdd:cd19126 6 GTRMPWLGLGVFQT----PDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 ETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 257
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1270111343 258 nmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACGI---------ISGKYG 308
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
102-394 |
1.90e-13 |
|
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: 70.43 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 102 SCLGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK-- 176
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 --AETERGL-----------------SRKHIIEGLKGSLQRLQLEYVDVVF---------ANRPDSN---TPMEEIVRAM 225
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 226 THVINQGM--AMYWGTSRWSAM-EIMEAYSVarQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgI 302
Cdd:cd19161 155 EELKKAGVikAFGLGVNEVQIClEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 303 ISGKYGNGVPESSRASLKCYQWlkeRIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 382
Cdd:cd19161 218 IGGVFNSGILATGTKSGAKFNY---GDAPAE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
330
....*....|...
gi 1270111343 383 IENLGAIQ-VLPK 394
Cdd:cd19161 292 RQNVEAFQtDIPE 304
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
104-391 |
2.48e-13 |
|
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: 69.30 E-value: 2.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGL 183
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIP 261
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 262 PVCEQAEYhlFQREKVEVQLPElyHKIGVGAmtWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQQNKL 341
Cdd:cd19139 149 NQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLA---------------------------------YGKVLDDPV 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1270111343 342 kdLSPIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19139 190 --LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
98-386 |
2.54e-13 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 69.61 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggka 177
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 eteRGlsRKH----IIEGLKGSLQRLQLEYVDVVFANRPD-SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM---EIME 249
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 250 AYSVArqfnmipPVCEQAEYH-LFQREKVEVqlpelYHK-IGVGAMTWSPLacgiisGKyGNGVpessraslkcyqwLKE 327
Cdd:cd19132 145 ETGVT-------PAVNQIELHpYFPQAEQRA-----YHReHGIVTQSWSPL------GR-GSGL-------------LDE 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 328 RIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENL 386
Cdd:cd19132 193 PVIKA--------------IAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
96-208 |
3.88e-13 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 69.61 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 96 KSGLRVSCLGLGTwvtFGGQISDEVAE----RLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITT 169
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1270111343 170 KLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVF 208
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
104-311 |
5.97e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.56 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaetergl 183
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 sRKHIIEGLKGSLQRLQLEYVDVVFANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqf 257
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 258 nmipPVCEQAEYH-LFQREkvEVQLPELYHKIGVGAmtWSPLACGiisgkyGNGV 311
Cdd:PRK11565 156 ----PVINQIELHpLMQQR--QLHAWNATHKIQTES--WSPLAQG------GKGV 196
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
97-386 |
6.99e-13 |
|
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: 69.05 E-value: 6.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLY 172
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKELILN-----AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 173 wggkaETERGlsrkHIIEGLKGSLQRLQLEYVDVVFANRP-----------------------DSNTPMEEIVRAMTHVI 229
Cdd:cd19112 79 -----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 230 NQGMAMYWGTSRWSA--MEIMEAYSvarqfnMIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGIISGK 306
Cdd:cd19112 150 SAGLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 307 YGNGVpessraslkcyqwlkerivseegrkqqNKLKD--LSPIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLI 383
Cdd:cd19112 220 WFGSV---------------------------SPLDDpvLKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLK 269
|
...
gi 1270111343 384 ENL 386
Cdd:cd19112 270 ENI 272
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
104-386 |
1.07e-12 |
|
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: 67.66 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGK 176
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 AETErglsrkhiiEGLKGSLQRLQLEYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SA 244
Cdd:cd19136 76 EKAR---------AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 245 MEIMEAYSvarqfnMIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCY 322
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DL 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1270111343 323 QWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 386
Cdd:cd19136 197 RLLEDPTVLA--------------IAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
97-409 |
1.91e-12 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 67.41 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 171
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQVKAAV-----KYALDAGYRHIDCAAVY-GNEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQG 232
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 233 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVP 312
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 313 EssRAslkcyqWLK--ERIVSEEGRkqqnklkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQ 390
Cdd:cd19106 210 D--RP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQ 268
|
330 340
....*....|....*....|
gi 1270111343 391 VLP-KMTSHVVNEIDNILRN 409
Cdd:cd19106 269 VFDfTLSPEEMKQLDALNRN 288
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
104-388 |
7.19e-12 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 65.43 E-value: 7.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgL 183
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 184 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS------AMEIMEAYSVAR 255
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 256 QfnmippvceQAEYH-LFQREKVEVQLPElyHKIGVGA-MTwspLAcgiisgkYGngvpessraslkcyQWLKERIVSEe 333
Cdd:PRK11172 151 N---------QIELSpYLQNRKVVAFAKE--HGIHVTSyMT---LA-------YG--------------KVLKDPVIAR- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1270111343 334 grkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGvSSVLLGSSTPEQLIENLGA 388
Cdd:PRK11172 195 -------------IAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
98-386 |
7.44e-12 |
|
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: 65.51 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--G 175
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 KAETERGLSRkhiieglkgSLQRLQLEYVDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEI 247
Cdd:cd19127 78 YDKALRGFDA---------SLRRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAYSVarqfnmIPPVcEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlke 327
Cdd:cd19127 146 IDATTV------VPAV-NQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 328 rivseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 386
Cdd:cd19127 209 ----------------ITGLAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
98-308 |
1.50e-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: 64.46 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 176
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 AETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 256
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 257 fnmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG---------IISGKYG 308
Cdd:cd19156 149 ---VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
112-403 |
2.94e-11 |
|
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: 64.02 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 112 FGGQISDEVAERLMT-IAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrk 186
Cdd:cd19129 11 FGTLIPDPSATRNAVkAALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 187 hIIEGLKGSLQRLQLEYVDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 246
Cdd:cd19129 82 -VKPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 247 IMEAYSVARqfnmIPPVCEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLACGIisgkygngvpessraslkcyqwlk 326
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGM------------------------ 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 327 erivseegrkQQNKLKD--LSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGaIQVLPKMTSHVVNEI 403
Cdd:cd19129 210 ----------EPKLLEDpvITAIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
97-386 |
2.61e-10 |
|
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: 60.89 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 171
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAV-----KIALKAGYRHLDLAKVY-QNQHEV--GQALKEllkeePGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVD-------VVFANRP-----------------DSNTPMEEIVRAMTH 227
Cdd:cd19118 75 -WNNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKPTGdlnpltavptnggevdlDLSVSLVDTWKAMVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 228 VINQGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH--LFQREKVEvqlpelYHK---IGVGAmtWSPLa 299
Cdd:cd19118 148 LKKTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 300 cgiisgkyGN---GVPessraslkcyqwlkeRIVSEEGRKQqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGS 376
Cdd:cd19118 212 --------GNnlaGLP---------------LLVQHPEVKA---------IAAKLGKTPAQVLIAWGIQR-GH-SVIPKS 257
|
330
....*....|
gi 1270111343 377 STPEQLIENL 386
Cdd:cd19118 258 VTPSRIRSNF 267
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
97-406 |
4.89e-10 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 60.20 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgk 176
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 aeTERglsrKHIIEGLKGSLQRLQLEYVDVVFANRP-------DSNTPMEEIVRA--------------MTHVINQGMAM 235
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 236 YWGTSRWSAMEIMEAysVARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpeSS 315
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------ST 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 316 RASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGAIQvlpkM 395
Cdd:cd19117 214 NAPL-----LKEPVIIK--------------IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 1270111343 396 TSHVVNEIDNI 406
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
98-387 |
5.15e-10 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 59.71 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTW-VTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 176
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 177 AETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 256
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 257 fnmIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEeg 334
Cdd:cd19157 150 ---IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG---------------------QLLDNPVLKE-- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1270111343 335 rkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLG 387
Cdd:cd19157 199 ------------IAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
97-391 |
2.08e-08 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 55.32 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQISDEVAerlMTIAYESGVNLFDTAEVYAaGKAEV---ILGSIIKKKGWRRSSLVITTKLyW 173
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYL-NEDEVgdaVRDFLKENPSVKREDLFICTKV-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETErglsrkHIIEGLKGSLQRLQLEYVDV------VFANRPDSNTPM-----------------EEIVRAMTHVIN 230
Cdd:cd19122 80 NHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 231 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiisgkygNG 310
Cdd:cd19122 154 SGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGSQ-------NQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 311 VPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIQ 390
Cdd:cd19122 220 VPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 1270111343 391 V 391
Cdd:cd19122 278 L 278
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
97-298 |
5.41e-08 |
|
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: 53.69 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILGsiIKK---KGWRRSSLVITTKLYW 173
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY-QNEDEVGEG--IKEaiaGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAETERGLSRkhiieglkgSLQRLQLEYVDV----------------VFANRPDSNTPME------EIVRAMTHVINQ 231
Cdd:cd19121 80 TYHRRVELCLDR---------SLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDGSRDLDwdwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 232 GMAMYWGTSRWSAM---EIMEAYSVARQFNMIP--PVCEQAEYHLFQREKvevqlpelyhkiGVGAMTWSPL 298
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
128-406 |
2.22e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.81 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 128 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 196
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 197 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 270
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 271 LFQREkvEVQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwlkerivseegrkqqnklkdLSPIAER 350
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPL---------GGFTPLQSST--------------------------LSDVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 351 LGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 406
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
104-272 |
5.73e-06 |
|
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: 47.61 E-value: 5.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWVtfggqiSDEV----AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGG 175
Cdd:cd19108 14 LGFGTYA------PEEVpkskALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 KAETErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------ 246
Cdd:cd19108 84 FHRPE--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdag 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 1270111343 247 IMEAYSVA----RQFNMI---P-----PVCEQAEYHLF 272
Cdd:cd19108 154 LAKSIGVSnfnrRQLEMIlnkPglkykPVCNQVECHPY 191
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
121-391 |
7.89e-06 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 47.34 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 121 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHIIE 190
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 191 GLKGSLQRLQlEYVDV-----------VFANrpdsntpmEEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYS 252
Cdd:cd19098 113 QWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 253 VARQFNmippvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSE 332
Cdd:cd19098 182 GARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1270111343 333 EGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 391
Cdd:cd19098 233 ELAP---LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
98-276 |
9.74e-06 |
|
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: 47.17 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyW 173
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 174 GGKAeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHV 228
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1270111343 229 INQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF-QREK 276
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKR 190
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
100-409 |
1.12e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 46.88 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 100 RVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYWggka 177
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKLWC---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 178 eterGLSRKHIIE-GLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRamthVINQGMAMYWGTS---RWSAME------I 247
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLP----LDRSGMVIPSDTDfldTWEAMEdlviegL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 248 MEAYSVArQFN-------------MIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisGKYGNGVPes 314
Cdd:cd19110 145 VKNIGVS-NFNheqlerllnkpglRVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL------GGSCEGVD-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 315 sraslkcyqwLKERIVseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENlgaIQVLP- 393
Cdd:cd19110 213 ----------LIDDPV-------------IQRIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKEN---IQVFDf 264
|
330
....*....|....*.
gi 1270111343 394 KMTSHVVNEIDNILRN 409
Cdd:cd19110 265 ELTEHDMDNLLSLDRN 280
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
97-278 |
1.20e-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: 46.67 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKaEVILG--SIIKKKGWRRSSLVITTKLyWG 174
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 175 GKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHVI 229
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAfkfvpieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1270111343 230 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 278
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHpyLQQPKLIE 200
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
97-245 |
2.76e-05 |
|
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: 45.57 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 97 SGLRVSCLGLGTWVTFGGQisdEVAERLMTIAYESGVNLFDTAEVYAA----GKAeviLGSIIKKKGWRRSSLVITTKL- 171
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 172 --YWggkaeterglsrKHIIEGLKGSLQRLQLEYVDVVFANRP-----DSntpmEEIVRAMTHVINQGMAMYWGTSRWSA 244
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWPvcfekDS----DDSGKPFTPVNDDGKTRYAASGDHIT 145
|
.
gi 1270111343 245 M 245
Cdd:cd19119 146 T 146
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
98-298 |
9.86e-05 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 43.95 E-value: 9.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 98 GLRVSCLGLGTWVTFGGQISDEVAerlmtIAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYwgg 175
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 176 KAETERGLSRkhiiEGLKGSLQRLQLEYVDVVFANRPD-------------------SNTPMEEIVRAMTHVINQGMAMY 236
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1270111343 237 WGTSRWSAMEImeaysvARQFNMiP-----PVCEQAEYHLF-QREKvevqLPELYHKIGVGAMTWSPL 298
Cdd:cd19107 148 IGVSNFNHLQI------ERILNK-PglkykPAVNQIECHPYlTQEK----LIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
104-305 |
1.11e-04 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 43.36 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSiikkkGWRRSSLVITTKLyWGGKAETER 181
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIYGneEGVGAAIAAS-----GIPRDELFVTTKL-WNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1270111343 182 GLSrkhiieGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRW--SAMEIMEAYSVar 255
Cdd:cd19130 82 PAA------AFAESLAKLGLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1270111343 256 qfnmIPPVCEQAEYH--LFQREKVEVQlpelyHKIGVGAMTWSPLACGIISG 305
Cdd:cd19130 151 ----VVPAVNQIELHpaYQQRTIRDWA-----QAHDVKIEAWSPLGQGKLLG 193
|
|
| |
