|
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 ... |
71-393 |
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: 706.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 150
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 230
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 231 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 310
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 311 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 390
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 27436964 391 NKP 393
Cdd:cd19159 321 NKP 323
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
72-381 |
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: 665.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITT 151
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 152 KLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 231
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 AYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERI 311
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 312 VSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 381
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
69-393 |
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: 640.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 69 TGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLV 148
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 149 ITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 228
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 229 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 308
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 309 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 388
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
....*
gi 27436964 389 LRNKP 393
Cdd:cd19160 321 LGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
73-389 |
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: 599.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 73 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 152
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 232
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 233 YSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIV 312
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436964 313 SEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 389
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
71-394 |
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: 592.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 150
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 230
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 231 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 310
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 311 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 390
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 27436964 391 NKPY 394
Cdd:cd19158 321 NKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
71-388 |
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: 519.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 150
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 228
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 229 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 308
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 309 ERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 388
Cdd:cd19143 241 DR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
71-393 |
1.11e-165 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 467.33 E-value: 1.11e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 150
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWGGKAEtERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 230
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 231 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWL 307
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 308 KERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDN 387
Cdd:cd19142 240 DGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELER 319
|
....*.
gi 27436964 388 ILRNKP 393
Cdd:cd19142 320 ILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
80-371 |
4.38e-156 |
|
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: 441.65 E-value: 4.38e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKA 159
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 E-TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 238
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 FNMIPPVCEQAEYHLFQREKVEvQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRK 318
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27436964 319 QQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 371
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
71-393 |
2.33e-103 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 308.26 E-value: 2.33e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWvTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSL 147
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 226
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcy 304
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 305 qWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 384
Cdd:COG0667 232 -NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
....*....
gi 27436964 385 IDNILRNKP 393
Cdd:COG0667 306 LDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
71-388 |
2.78e-93 |
|
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: 282.54 E-value: 2.78e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVIT 150
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 229
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwl 307
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 308 kERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDN 387
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDE 307
|
.
gi 27436964 388 I 388
Cdd:cd19087 308 L 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
71-373 |
4.16e-84 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 259.47 E-value: 4.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkg 141
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 142 wRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWG 220
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 221 TSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR 298
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 299 ASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 373
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
73-375 |
1.48e-78 |
|
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: 244.86 E-value: 1.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 73 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVI 149
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 150 TTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 226
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQW 306
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 307 LKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 375
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
80-386 |
1.51e-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: 1.51e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LY 154
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 155 WGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAys 234
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 varqFNMIPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkeri 311
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 312 vSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 386
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
84-369 |
4.70e-75 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 233.18 E-value: 4.70e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTWvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETE 162
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 163 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMI 242
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 243 PPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnk 322
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27436964 323 lkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLG 369
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
76-386 |
1.05e-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: 232.10 E-value: 1.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 76 LGKSGLRVSCLGLGTWVtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLV 148
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 149 ITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 228
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 229 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqw 306
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 307 lKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 386
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 ... |
72-373 |
5.91e-72 |
|
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: 227.85 E-value: 5.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLGTWvTFGGQ------ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRS 145
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 146 SLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 224
Cdd:cd19079 79 EVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 225 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKC 303
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAK 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 304 YQWLKErivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 373
Cdd:cd19079 238 LKYDYF---TEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
72-372 |
1.08e-68 |
|
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: 219.20 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSL 147
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKL--------Y--WGgkaeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAM 217
Cdd:cd19151 80 IISTKAgytmwpgpYgdWG---------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 218 YWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESS 297
Cdd:cd19151 151 YVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDS 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 298 RASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19151 229 RAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
72-374 |
3.59e-66 |
|
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: 212.70 E-value: 3.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLV 148
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 149 ITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS 225
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 226 AMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyq 305
Cdd:cd19150 159 PERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS----- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436964 306 wlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 374
Cdd:cd19150 233 --KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
83-388 |
3.42e-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: 210.88 E-value: 3.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 83 VSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK--- 152
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 --LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVIN 212
Cdd:cd19094 79 pgEGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 213 QGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--G 290
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 291 NGVPESSRASLkcYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19094 238 AARPEGGRLNL--FPGYMARYRSPQALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDA 312
|
330
....*....|....*....
gi 27436964 371 IQV-LPKmtsHVVNEIDNI 388
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 ... |
86-389 |
1.78e-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: 207.93 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvTFGGQ---ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETE 162
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 163 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmI 242
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 243 PPVCEQAEYHLFqREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQ 320
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 321 NKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 389
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
71-374 |
5.92e-63 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 205.61 E-value: 5.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSL 147
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 224
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 225 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--K 302
Cdd:PRK09912 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegN 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436964 303 CYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 374
Cdd:PRK09912 250 KVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
76-373 |
1.27e-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: 198.60 E-value: 1.27e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 76 LGKSGLRVSCLGLGTwVTFGGQ----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITT 151
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 152 KLYWG--GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 229
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKE 309
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436964 310 RIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 373
Cdd:cd19080 236 GKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
83-391 |
4.36e-56 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 186.25 E-value: 4.36e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 83 VSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggk 158
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 aetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 238
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 fnmipPVCEQAEYHLFQREKVEVQLPEL-YHKIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSE 314
Cdd:cd19085 150 -----IDSNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFE 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 315 EG--RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 391
Cdd:cd19085 215 PGaeEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
73-373 |
4.07e-51 |
|
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381375 [Multi-domain] Cd Length: 315 Bit Score: 174.00 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 73 YRNLGKSGLRVSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLV 148
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 149 ITTK--LYWGGKAETE----------RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMA 216
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 217 MYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---V 293
Cdd:cd19149 158 RAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 294 PESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19149 231 AGDARSGIPWFS--------PENREKVLALLEkWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGD 302
|
.
gi 27436964 373 V 373
Cdd:cd19149 303 I 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
74-388 |
5.41e-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: 5.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 74 RNLGKSGLRVSCLGLGTwVTFGGQ-----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 148
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 149 ITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 226
Cdd:cd19083 79 IATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQW 306
Cdd:cd19083 158 EQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 307 LKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 384
Cdd:cd19083 225 RNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAF 302
|
....
gi 27436964 385 IDNI 388
Cdd:cd19083 303 IDAL 306
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
72-385 |
3.97e-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: 168.16 E-value: 3.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLG----TWvtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 147
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 222
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 223 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRA 299
Cdd:cd19076 154 EASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 300 SLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMT 378
Cdd:cd19076 222 DD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLT 296
|
....*..
gi 27436964 379 SHVVNEI 385
Cdd:cd19076 297 PEELAEI 303
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
81-370 |
5.87e-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: 5.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 81 LRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YW 155
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIME 231
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 AYSVArqfnmippvCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkeri 311
Cdd:cd19086 158 RGGID---------VVQVIYNLLDQRPEEELFPLA-EEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 312 vseegrkqqnklkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19086 205 -------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
82-370 |
9.99e-47 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 161.63 E-value: 9.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 82 RVSCLGLGTW------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLyw 155
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 ggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 234
Cdd:cd19093 78 ---APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSRAslkcyqwlkeRIVS 313
Cdd:cd19093 155 ALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPEnPPPGGRR----------RLFG 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 314 EEGRKQ-QNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGA 370
Cdd:cd19093 224 RKNLEKvQPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
80-389 |
4.54e-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: 4.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTW-VTFG-GQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW- 155
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 ---GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 232
Cdd:cd19078 78 idgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 233 YSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlke 309
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 310 rivSEEGRKQQNKLKDL-SPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 388
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDA 300
|
.
gi 27436964 389 L 389
Cdd:cd19078 301 L 301
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
80-372 |
5.60e-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: 153.54 E-value: 5.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVTFGGQIS----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYw 155
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysdDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 ggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 235
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 236 ARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivsee 315
Cdd:cd19072 152 LKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG------------------------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436964 316 grkqqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19072 203 -------SPLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
83-389 |
1.91e-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: 153.21 E-value: 1.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 83 VSCLGLGTWVTFGGQ------ISDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK-- 152
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggwgPQDD-RDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImea 232
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 233 ysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPelY---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK 308
Cdd:cd19102 154 ----KRCQAIHPIASlQPPYSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 309 -ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 386
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIE 299
|
...
gi 27436964 387 NIL 389
Cdd:cd19102 300 ALL 302
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
84-370 |
1.06e-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: 151.17 E-value: 1.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-- 157
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 ---KAETERgLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 234
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 VARQFNMIPPVCEQAEYHLFqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLK 302
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 303 CYQwlkerivSEEGRKQQNKLKDLspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
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 ... |
86-388 |
9.17e-41 |
|
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: 9.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterG 164
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 165 LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPP 244
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 245 VCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEe 315
Cdd:cd19075 156 TVYQGMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 316 grkqqnkLKDLSPIAERLGCTLPQLAVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 388
Cdd:cd19075 234 -------LEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
84-370 |
1.01e-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: 137.85 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK---- 152
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 231
Cdd:cd19752 79 pRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 AYSVARQFNMIPPVCEQAEYHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRAS 300
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 301 LKCYqwlkerivseEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19752 230 PEQY----------DGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
71-371 |
3.15e-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: 381331 [Multi-domain] Cd Length: 250 Bit Score: 135.40 E-value: 3.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTwvTFGGQISDEVAERlmtiAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVIT 150
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG--GGLPRESPELLRR----ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVVF---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 227
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 228 E--IMEA-----YSVArqfnMIPpvceqaeY-HLFQREKVEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessr 298
Cdd:cd19105 148 AevLQAAiesgwFDVI----MVA-------YnFLNQPAELEEALAAAAeKGIGVVAMK--TLAGGY-------------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436964 299 aslkcyqwlkerivSEEGRKQQNKLKDLSpiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 371
Cdd:cd19105 201 --------------LQPALLSVLKAKGFS---------LPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
71-390 |
3.56e-37 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 138.06 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 143
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 144 RSSLVITTKLywGGKAET-------ERGLSRKHIIEGLKGSLQRLQLEYVD---VVFANRP-----------DSNTP--- 199
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 200 MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSP 279
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 280 LACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGS 358
Cdd:PRK10625 236 LAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|..
gi 27436964 359 STPEQLIENLGAIQVlpKMTSHVVNEIDNILR 390
Cdd:PRK10625 310 TTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
84-370 |
6.46e-36 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 131.97 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTWVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkA 159
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 ETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqF 239
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 240 NMIppvceQAEYHLFQREKVEVqLPELY-HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrk 318
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLAAeAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR-------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27436964 319 qqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19095 209 -------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
79-370 |
1.78e-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: 1.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 158
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 238
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 fnmIPPVCEQAEYHLFQREkvevqlPEL--YHK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEe 315
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELlaFCReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 316 grkqqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENLGA 370
Cdd:COG0656 193 -------------IAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
80-373 |
4.82e-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: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvTFGGQIS-----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLY 154
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 155 wggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 234
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 VARQfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSE 314
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE---------------------KTNRTLEE 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 315 egrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVSSVLLgSSTPEQLIENLGAIQV 373
Cdd:cd19137 206 --------------IAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
79-386 |
1.07e-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: 129.29 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWvTFGGQISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwgg 157
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEiEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 kaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVAR 237
Cdd:cd19138 80 ----PSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 238 QFNMippVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegr 317
Cdd:cd19138 155 GGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENP-------------------- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 318 kqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 386
Cdd:cd19138 208 -------TLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
80-364 |
1.56e-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: 129.73 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVT----FGGqiSDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK- 152
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIME 231
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 AY-SVARQFNMIPPvceqaeYHLFQREKVEVQLPE-LYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKC 303
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPYaRKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436964 304 YQwlkerivseEGRKQQ-----NKLKDLSpiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 364
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 ... |
78-378 |
3.69e-34 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 128.06 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 78 KSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LY 154
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 155 WGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeime 231
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 aysvarQFNM------IPPVCEQAEYHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessrasl 301
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGG------------------ 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436964 302 kcyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 378
Cdd:cd19092 209 --------RLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
71-378 |
2.27e-33 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 126.42 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 150
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 224
Cdd:COG4989 81 TKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 225 SAMeimeaysvarQFNMI------PPVCEQAEYHLFQREKVE------VQLpelyHKIGVgaMTWSPLACGIISGKYgng 292
Cdd:COG4989 161 TPS----------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 293 vpessraslkcyqwlkerivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 372
Cdd:COG4989 222 --------------------DEQFPRLRAALDE---LAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALD 278
|
....*.
gi 27436964 373 VlpKMT 378
Cdd:COG4989 279 I--ELT 282
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
71-393 |
1.75e-32 |
|
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: 124.48 E-value: 1.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSL 147
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 222
Cdd:cd19144 79 FLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 223 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRAS 300
Cdd:cd19144 157 ECSAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 301 LKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 378
Cdd:cd19144 225 FEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLT 302
|
330
....*....|....*
gi 27436964 379 SHVVNEIDNILRNKP 393
Cdd:cd19144 303 EEEEKEIREIAEEAE 317
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
79-386 |
2.90e-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: 2.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLG----TWVtfGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITT 151
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 152 KlywGGKAET--ERGLSRKHIIEGLKGSLQRL-QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 228
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 229 IMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlk 308
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL---- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 309 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 386
Cdd:cd19077 226 DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
74-385 |
3.37e-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: 120.62 E-value: 3.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 74 RNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVIT 150
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 151 TKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 227
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 228 EIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQWL 307
Cdd:cd19145 160 TIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSH 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 308 KeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 385
Cdd:cd19145 230 P-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
86-372 |
4.27e-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: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGT-WVTFG-GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIkkKGWRRSSLVITTKLywGGKAETER 163
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 164 GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQ 238
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 FNMIPPVCeqaEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrk 318
Cdd:cd19090 156 FDVVLTAN---RYTLLDQSAADELLPAAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE-------- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 27436964 319 QQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19090 217 LLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
72-388 |
1.02e-29 |
|
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: 116.98 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 72 KYRNLGKSGLRVSCLGLGtwvtfGGQI-------SDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrR 144
Cdd:cd19104 1 KYRRFGRTGLKVSELTFG-----GGGIgglmgrtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 145 SSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTP--------------MEEIVRAMTH 209
Cdd:cd19104 73 AGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDkpvggtlsttdvlgLGGVADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 210 VINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL------FQREKVEV-----QLPELYHKIGVGAMTWS 278
Cdd:cd19104 150 LRSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLlnpsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 279 PLACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGS 358
Cdd:cd19104 225 VLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA----AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGV 291
|
330 340 350
....*....|....*....|....*....|
gi 27436964 359 STPEQLIENLGAIQVLPkMTSHVVNEIDNI 388
Cdd:cd19104 292 KNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
80-389 |
2.54e-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: 110.59 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGT------WVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL 153
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 ---YWGGKAETER----GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 226
Cdd:cd19146 87 ttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKVEVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLK 302
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 303 CYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVV 382
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEI 308
|
....*..
gi 27436964 383 NEIDNIL 389
Cdd:cd19146 309 QEIEDAY 315
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
71-371 |
3.20e-27 |
|
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: 109.56 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSL 147
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 148 VITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVV------FAnrPDSNTPMEEIVRAMTHVINQGMAMYW 219
Cdd:cd19163 78 YLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 220 GTSRWSaMEIMeAYSVARQFNMIPPVCEQAEYHLFQREKVEvqLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRA 299
Cdd:cd19163 155 GITGYP-LDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436964 300 SlkcyQWLKERIvseegrkqqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 371
Cdd:cd19163 228 S----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
71-368 |
4.38e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.68 E-value: 4.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 71 MKYRNLGKSGLRVSCLGLGTWvtfGGQISD-EVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVI 149
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 150 TTKLYWGGKaeterglSRKHIIEGLKGSLQRLQLEYVDVVFanrpdsntpmeeIvramtHVINQGMAMYWGTSRWSAMEI 229
Cdd:COG1453 73 ATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLYL------------I-----HGLNTEEDLEKVLKPGGALEA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAysvARQ----------FNMIPPVCEQA-E-----------YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisg 287
Cdd:COG1453 129 LEK---AKAegkirhigfsTHGSLEVIKEAiDtgdfdfvqlqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 288 kygngvpessraslkcyqwlkerivseegrkqqnKLKDLSPIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQL 364
Cdd:COG1453 202 ----------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQL 247
|
....
gi 27436964 365 IENL 368
Cdd:COG1453 248 DENL 251
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
83-370 |
4.80e-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: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 83 VSCLGLGTW-----VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW-- 155
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 235
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 236 ARqfnmIppVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivsee 315
Cdd:cd19088 158 VR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG--------GGDLAQPGG----------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 316 grkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19088 205 ---------LLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
80-368 |
7.53e-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: 7.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGka 159
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 etergLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 239
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 240 nmIPPVCEQAEYH--LFQRekvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegr 317
Cdd:cd19140 148 --APLFTNQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLARG---------------------EVLKDPVLQE--- 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27436964 318 kqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENL 368
Cdd:cd19140 197 -----------IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
86-368 |
9.39e-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: 101.79 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGL 165
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 SRKHIIEGLKGSLQRLQLEYVDVV-----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 239
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 240 nmIPPVCEQAEYHLF--QREKVEvqlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseeg 316
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKELVE------FcKEHGIVVQAYSPLGRG-------------RRPLLDD------------- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 27436964 317 rkqqnklKDLSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 368
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 ... |
86-370 |
1.19e-24 |
|
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: 101.19 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergL 165
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 245
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 246 CEQAEYH--LFQREKVEVQLPelyHKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnkl 323
Cdd:cd19073 145 VNQVEFHpfLYQAELLEYCRE---NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------- 189
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 27436964 324 kdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGA 370
Cdd:cd19073 190 -----IAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
86-376 |
9.79e-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: 99.14 E-value: 9.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywg 156
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 157 GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSv 235
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 236 ARQFNMIppvceQAEYHLF-QREKVEVQLPELyHKIGVGAMTWSPLACGIIsgkygngVPESSRASLKCYQWlkerivse 314
Cdd:cd19097 152 SFKIDII-----QLPFNILdQRFLKSGLLAKL-KKKGIEIHARSVFLQGLL-------LMEPDKLPAKFAPA-------- 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436964 315 egrkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK 376
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, ... |
86-370 |
2.29e-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: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTwVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWG 156
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 157 GKAETER--GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeim 230
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 231 eAYSVARQFN----MIPpvceqAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQW 306
Cdd:cd19162 156 -LLRAARRADvdvvMVA-----GRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRP 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436964 307 LKERIVSeegRKQQnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19162 222 ATPEVLA---RARR-----LAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
73-368 |
4.46e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 94.09 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 73 YRNLGKSGLRVSCLGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTK 152
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 LYWGGKAETERGLSRkhiieglkgSLQRLQLEYVDVVF----ANRPDSNTPMEE--IVRAMTHVINQGMAMYWGTS--RW 224
Cdd:cd19100 74 TGARDYEGAKRDLER---------SLKRLGTDYIDLYQlhavDTEEDLDQVFGPggALEALLEAKEEGKIRFIGISghSP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 225 SAM-EIMEAYsvarQFNMIPPVCEQAEYHlfQREKVEVQLPELY-HKIGVGAMtwSPLACGiisgkygngvpessraslk 302
Cdd:cd19100 145 EVLlRALETG----EFDVVLFPINPAGDH--IDSFREELLPLAReKGVGVIAM--KVLAGG------------------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436964 303 cyQWLKERIVSeegrkqqnklkdlspiaerlgctlPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 368
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 ... |
84-370 |
5.06e-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: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkae 160
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 161 teRGLSRKHIIEGLKGSLQRLQLEYVDvVFA----NRPD------SNTPMEEIVRAMT-----HVinqGMamywgTSRWS 225
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKeglirHI---GF-----SFHDS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 226 A---MEIMEAYsvarQFNMIppvceQAEYHLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessrasl 301
Cdd:cd19096 144 PellKEILDSY----DFDFV-----QLQYNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA--------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 302 kcyqwlkerivseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19096 200 -------------------NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
73-389 |
2.85e-20 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 90.61 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 73 YRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVI 149
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 150 TTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSa 226
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEVqLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASL 301
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 302 KcyqwLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--M 377
Cdd:PLN02587 226 E----LKSacAAAATHCKEK--------------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgI 287
|
330
....*....|..
gi 27436964 378 TSHVVNEIDNIL 389
Cdd:PLN02587 288 DEELLSEVEAIL 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
74-374 |
5.13e-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: 89.52 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 74 RNLGKSGLRVSCLGLGTwVTFGGQISDEV----AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVI 149
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 150 TTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWsA 226
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPE---------- 295
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgelrh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 296 SSRASLKcyqWLKERIVSeegrkqqnklkdlspiaerlgctLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQVL 374
Cdd:cd19153 234 YAAAADA---VCASVEAS-----------------------LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAV 287
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
81-368 |
6.47e-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: 6.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 81 LRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywG 156
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 157 G----------------KAETERGLSRKHIIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSN 197
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 198 TPMEEIVRAMTHVINQGMAMYWGTSRWSAmeiMEAYSVARQFNMIPPVCE---------------QAEYHLFQREKVEVQ 262
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWDG---FRAPPALPGHLSLEKLVAaaeevggdnhhfkviQLPLNLLEPEALTEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 263 ---------LPELYHKIGVGAMTWSPLAcgiiSGKYGNGVPESSRAslkcyqwlkerivseegrkqqnklkdlspiAERL 333
Cdd:cd19099 235 ntvkgealsLLEAAKELGLGVIASRPLN----QGQLLGELRLADLL------------------------------ALPG 280
|
330 340 350
....*....|....*....|....*....|....*
gi 27436964 334 GCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 368
Cdd:cd19099 281 GATLAQRALQFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
78-368 |
8.29e-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: 8.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 78 KSGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITT 151
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 152 KLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVIN 212
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 213 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnG 292
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------G 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 293 VPESSRASLKCYQWlkerivseegrKQQNKLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 368
Cdd:cd19154 212 SPGRANFTKSTGVS-----------PAPNLLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
85-368 |
1.27e-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: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 85 CLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAE 160
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 161 TERglsrkhIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGT 221
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 222 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRAS 300
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTF 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 301 LKCyqwlkerivseegrkqqnklKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 368
Cdd:cd19128 211 LND--------------------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
80-368 |
1.79e-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: 84.16 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGK 158
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAY 233
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 234 SvarqFNMIPPVCEQAEYHLFqREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivs 313
Cdd:cd19133 144 L----HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA-------------------------------- 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 27436964 314 eEGRKQ--QNKLkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 368
Cdd:cd19133 185 -EGRNNlfENPV--LTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
86-368 |
5.73e-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: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGL 165
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 srkhiiEGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArq 238
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 fnmipPVCEQAEYH-LFQREkvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegr 317
Cdd:cd19131 153 -----PVVNQIELHpRFQQR----ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27436964 318 kqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 368
Cdd:cd19131 200 -----------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
86-373 |
9.45e-18 |
|
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: 9.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETE 162
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 163 RGLSRKHIIEGLKG------------------SLQRLQLEYVDVVFANRPDSNTP-----------MEEIVRAMTHVINQ 213
Cdd:cd19152 80 VEPTFEPGFWNPLPfdavfdysydgilrsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 214 GMAMYW--GTSRWS-AMEIME-----AYSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgII 285
Cdd:cd19152 160 GVIKAIglGVNDWEvILRILEeadldWVMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 286 SGKYGNGVpessRASLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLI 365
Cdd:cd19152 218 AGPFNSGF----LAGGDNFDYYEYGPAPPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVE 290
|
....*...
gi 27436964 366 ENLGAIQV 373
Cdd:cd19152 291 ENVALLAT 298
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
88-346 |
9.91e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.77 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 88 LGTW----------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGG 157
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 kaeteRGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYS 234
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIV 312
Cdd:cd19103 156 ILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAE 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 27436964 313 SEEGRKQQnkLKDLSP----IAERLGCTLPQLAVAWCL 346
Cdd:cd19103 224 TYNPLLPQ--LEELTAvmaeIGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
86-394 |
1.87e-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: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETEr 163
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 164 glsrkHIIEGLKGSLQRLQLEYVD-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWS 225
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 226 AMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQ 305
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 306 WLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 384
Cdd:cd19123 226 LLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMAT 286
|
330
....*....|
gi 27436964 385 IDNILRNKPY 394
Cdd:cd19123 287 IAALDRHHRY 296
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
78-368 |
7.70e-17 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 80.08 E-value: 7.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 78 KSGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyW 155
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKT-----AIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FANRPDSNTP---------MEEIVRAMTHVINQGMAMYWGT 221
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVRLKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 222 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASL 301
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSPGTTWVKK 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27436964 302 KCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGvSSVLLGSSTPEQLIENL 368
Cdd:cd19125 215 NV---LKDPIVTK--------------VAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
87-394 |
1.11e-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: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 87 GLGTWV--TFGGQISDEVAErLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterg 164
Cdd:cd19120 10 GTGTAWykSGDDDIQRDLVD-SVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 165 lsrkHIIEGLKGSLQRLQLEYVDVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 240
Cdd:cd19120 80 ----DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 241 mIPPVCEQAEYHLFqrekVEVQLPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRK 318
Cdd:cd19120 153 -IKPAVNQIEFHPY----LYPQQPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGP 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27436964 319 QQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 394
Cdd:cd19120 201 LDPVLEK---IAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
82-370 |
1.55e-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: 79.56 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 82 RVSCLGLGTWVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYW 155
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETergLSRKHIIEGLKGSLQRLQLEYVDVV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEI 229
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAysvarqfnMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCY 304
Cdd:cd19101 154 LDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKY 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 305 QwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 370
Cdd:cd19101 224 K----LMIDEWGgwDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
86-368 |
3.36e-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: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKLywggkAETERGL 165
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 SRKhiIEGLKGSLQRLQLEYVDVVFANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPP 244
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 245 VCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnk 322
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVGRLLDN-----PAVTA------------------------ 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 27436964 323 lkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 368
Cdd:cd19134 201 ------IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
79-367 |
6.78e-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: 6.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWvTFGGQISDEVAERLMtiayESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 158
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 231
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 aysvARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERI 311
Cdd:cd19135 154 ----LLEDCSVVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLAKG---------------------KALEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 27436964 312 VSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIEN 367
Cdd:cd19135 206 VTE--------------LAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKEN 245
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
80-394 |
1.73e-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: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVTFGgqisDEVAERLMTiAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKL 153
Cdd:cd19111 1 GFPMPVIGLGTYQSPP----EEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 YwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWG 220
Cdd:cd19111 71 P-------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 221 TSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKVEVQLPelyHKIGVGAmtWSPLacgiisgkygnGVPesSR 298
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPL-----------GSP--GR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 299 ASLkcYQWLKERIVSEEgrkqQNKLKdlspIAERLGCTLPQLAVAWCL-RNEGvssVLLGSSTPEQLIENLGAIQVlpKM 377
Cdd:cd19111 202 ANQ--SLWPDQPDLLED----PTVLA----IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--EL 266
|
330
....*....|....*..
gi 27436964 378 TSHVVNEIDNILRNKPY 394
Cdd:cd19111 267 TEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
86-391 |
3.71e-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: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEt 161
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 162 erglsRKHIIEGLKGSLQRLQLEYVDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWS 225
Cdd:cd19116 85 -----REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 226 AMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLkcy 304
Cdd:cd19116 160 SEQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRGQTN--- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 305 qwlkerivsEEGRKQQNKLKDlspIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KMTSHVVN 383
Cdd:cd19116 218 ---------PPPRLDDPTLVA---IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKEN---IDIFDfQLTPEEVA 280
|
....*...
gi 27436964 384 EIDNILRN 391
Cdd:cd19116 281 ALNSFNTN 288
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
79-386 |
5.31e-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: 75.25 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLG------TWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK 152
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 LYW--------GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 224
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 225 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcy 304
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVL---------GGGKFQSKKA----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 305 qwLKERIVSEEGRK------QQNKL-----KDLSPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19147 230 --VEERKKNGEGLRsfvggtEQTPEevkisEALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALS 307
|
330
....*....|....
gi 27436964 373 VlpKMTSHVVNEID 386
Cdd:cd19147 308 I--KLTPEEIEYLE 319
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
80-368 |
1.32e-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: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKL 153
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 YWGGkaeterglSRKHIIEG-LKGSLQRLQLEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVI 211
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 212 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYG 290
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 291 NGVPESSRASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 368
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 ... |
79-368 |
1.42e-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: 73.46 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGgqiSDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKL 153
Cdd:cd19124 1 SGQTMPVIGMGTASDPP---SPEDIKAAVLEAIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 yWGGKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAM 217
Cdd:cd19124 75 -WCSDAH------PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 218 YWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPE 295
Cdd:cd19124 148 AIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVME 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27436964 296 SsraslkcyQWLKErivseegrkqqnklkdlspIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 368
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 ... |
80-290 |
5.63e-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: 71.31 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVTfggqISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKA 159
Cdd:cd19126 6 GTRMPWLGLGVFQT----PDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 ETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 239
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27436964 240 nmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACGI---------ISGKYG 290
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
80-368 |
1.34e-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: 69.99 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggka 159
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 eteRGlsRKH----IIEGLKGSLQRLQLEYVDVVFANRPD-SNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM---EIME 231
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 232 AYSVArqfnmipPVCEQAEYH-LFQREKVEVqlpelYHK-IGVGAMTWSPLacgiisGKyGNGVpessraslkcyqwLKE 309
Cdd:cd19132 145 ETGVT-------PAVNQIELHpYFPQAEQRA-----YHReHGIVTQSWSPL------GR-GSGL-------------LDE 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 310 RIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENL 368
Cdd:cd19132 193 PVIKA--------------IAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
84-376 |
1.72e-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: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 84 SCLGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK-- 158
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 --AETERGL-----------------SRKHIIEGLKGSLQRLQLEYVDVVF---------ANRPDSN---TPMEEIVRAM 207
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 208 THVINQGM--AMYWGTSRWSAM-EIMEAYSVarQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgI 284
Cdd:cd19161 155 EELKKAGVikAFGLGVNEVQIClEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 285 ISGKYGNGVPESSRASLKCYQWlkeRIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 364
Cdd:cd19161 218 IGGVFNSGILATGTKSGAKFNY---GDAPAE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
330
....*....|...
gi 27436964 365 IENLGAIQ-VLPK 376
Cdd:cd19161 292 RQNVEAFQtDIPE 304
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
86-373 |
2.28e-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: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGL 165
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIP 243
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 244 PVCEQAEYhlFQREKVEVQLPElyHKIGVGAmtWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQQNKL 323
Cdd:cd19139 149 NQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLA---------------------------------YGKVLDDPV 189
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 27436964 324 kdLSPIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENLGAIQV 373
Cdd:cd19139 190 --LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
78-190 |
3.53e-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: 3.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 78 KSGLRVSCLGLGTwvtFGGQISDEVAE----RLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITT 151
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 27436964 152 KLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVF 190
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
86-293 |
5.45e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.56 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaetergl 165
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 sRKHIIEGLKGSLQRLQLEYVDVVFANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqf 239
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 240 nmipPVCEQAEYH-LFQREkvEVQLPELYHKIGVGAmtWSPLACGiisgkyGNGV 293
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 ... |
79-368 |
5.79e-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: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLY 154
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKELILN-----AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 155 wggkaETERGlsrkHIIEGLKGSLQRLQLEYVDVVFANRP-----------------------DSNTPMEEIVRAMTHVI 211
Cdd:cd19112 79 -----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 212 NQGMAMYWGTSRWSA--MEIMEAYSvarqfnMIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGIISGK 288
Cdd:cd19112 150 SAGLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 289 YGNGVpessraslkcyqwlkerivseegrkqqNKLKD--LSPIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLI 365
Cdd:cd19112 220 WFGSV---------------------------SPLDDpvLKDLAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLK 269
|
...
gi 27436964 366 ENL 368
Cdd:cd19112 270 ENI 272
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
86-368 |
7.00e-13 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 68.04 E-value: 7.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGK 158
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AETErglsrkhiiEGLKGSLQRLQLEYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SA 226
Cdd:cd19136 76 EKAR---------AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRH 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 227 MEIMEAYSvarqfnMIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCY 304
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DL 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27436964 305 QWLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 368
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 ... |
79-391 |
1.74e-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: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 153
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQVKAAV-----KYALDAGYRHIDCAAVY-GNEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQG 214
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 215 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVP 294
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 295 EssRAslkcyqWLK--ERIVSEEGRkqqnklkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQ 372
Cdd:cd19106 210 D--RP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQ 268
|
330 340
....*....|....*....|
gi 27436964 373 VLP-KMTSHVVNEIDNILRN 391
Cdd:cd19106 269 VFDfTLSPEEMKQLDALNRN 288
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
86-370 |
6.62e-12 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 65.43 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgL 165
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 166 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS------AMEIMEAYSVAR 237
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 238 QfnmippvceQAEYH-LFQREKVEVQLPElyHKIGVGA-MTwspLAcgiisgkYGngvpessraslkcyQWLKERIVSEe 315
Cdd:PRK11172 151 N---------QIELSpYLQNRKVVAFAKE--HGIHVTSyMT---LA-------YG--------------KVLKDPVIAR- 194
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27436964 316 grkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGvSSVLLGSSTPEQLIENLGA 370
Cdd:PRK11172 195 -------------IAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
80-368 |
6.84e-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: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--G 157
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 KAETERGLSRkhiieglkgSLQRLQLEYVDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEI 229
Cdd:cd19127 78 YDKALRGFDA---------SLRRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAYSVarqfnmIPPVcEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlke 309
Cdd:cd19127 146 IDATTV------VPAV-NQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT---- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 310 rivseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 368
Cdd:cd19127 209 ----------------ITGLAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
80-290 |
1.30e-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: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 158
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 238
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436964 239 fnmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG---------IISGKYG 290
Cdd:cd19156 149 ---VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
94-385 |
2.70e-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: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 94 FGGQISDEVAERLMT-IAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrk 168
Cdd:cd19129 11 FGTLIPDPSATRNAVkAALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 169 hIIEGLKGSLQRLQLEYVDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 228
Cdd:cd19129 82 -VKPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 229 IMEAYSVARqfnmIPPVCEQAEYHLFQRekvEVQLPELYHKIGVGAMTWSPLACGIisgkygngvpessraslkcyqwlk 308
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGM------------------------ 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 309 erivseegrkQQNKLKD--LSPIAERLGCTLPQLAVAWCLRNEGvsSVLLGSSTPEQLIENLGaIQVLPKMTSHVVNEI 385
Cdd:cd19129 210 ----------EPKLLEDpvITAIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
79-368 |
2.41e-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: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 153
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAV-----KIALKAGYRHLDLAKVY-QNQHEV--GQALKEllkeePGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVD-------VVFANRP-----------------DSNTPMEEIVRAMTH 209
Cdd:cd19118 75 -WNNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKPTGdlnpltavptnggevdlDLSVSLVDTWKAMVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 210 VINQGMAMYWGTSRWSA---MEIMEAYSVArqfnmipPVCEQAEYH--LFQREKVEvqlpelYHK---IGVGAmtWSPLa 281
Cdd:cd19118 148 LKKTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 282 cgiisgkyGN---GVPessraslkcyqwlkeRIVSEEGRKQqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGS 358
Cdd:cd19118 212 --------GNnlaGLP---------------LLVQHPEVKA---------IAAKLGKTPAQVLIAWGIQR-GH-SVIPKS 257
|
330
....*....|
gi 27436964 359 STPEQLIENL 368
Cdd:cd19118 258 VTPSRIRSNF 267
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
79-388 |
3.40e-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: 60.59 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgk 158
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 aeTERglsrKHIIEGLKGSLQRLQLEYVDVVFANRP-------DSNTPMEEIVRA--------------MTHVINQGMAM 217
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 218 YWGTSRWSAMEIMEAysVARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiisgkygngvpeSS 297
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------ST 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 298 RASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGAIQvlpkM 377
Cdd:cd19117 214 NAPL-----LKEPVIIK--------------IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 27436964 378 TSHVVNEIDNI 388
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
80-369 |
5.14e-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: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTW-VTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 158
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 159 AETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 238
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 239 fnmIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEeg 316
Cdd:cd19157 150 ---IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG---------------------QLLDNPVLKE-- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27436964 317 rkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLG 369
Cdd:cd19157 199 ------------IAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
79-373 |
1.41e-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: 55.71 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVAerlMTIAYESGVNLFDTAEVYAaGKAEV---ILGSIIKKKGWRRSSLVITTKLyW 155
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYL-NEDEVgdaVRDFLKENPSVKREDLFICTKV-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETErglsrkHIIEGLKGSLQRLQLEYVDV------VFANRPDSNTPM-----------------EEIVRAMTHVIN 212
Cdd:cd19122 80 NHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdltenpEPTWRAMEEIYE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 213 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiisgkygNG 292
Cdd:cd19122 154 SGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGSQ-------NQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 293 VPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIQ 372
Cdd:cd19122 220 VPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 27436964 373 V 373
Cdd:cd19122 278 L 278
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
79-280 |
5.03e-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: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILGsiIKK---KGWRRSSLVITTKLYW 155
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY-QNEDEVGEG--IKEaiaGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAETERGLSRkhiieglkgSLQRLQLEYVDV----------------VFANRPDSNTPME------EIVRAMTHVINQ 213
Cdd:cd19121 80 TYHRRVELCLDR---------SLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDGSRDLDwdwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27436964 214 GMAMYWGTSRWSAM---EIMEAYSVARQFNMIP--PVCEQAEYHLFQREKvevqlpelyhkiGVGAMTWSPL 280
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
110-388 |
2.07e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 48.81 E-value: 2.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 110 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 178
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 179 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 252
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 253 LFQREkvEVQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcyqwlkerivseegrkqqnklkdLSPIAER 332
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPL---------GGFTPLQSST--------------------------LSDVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 333 LGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 388
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
103-373 |
3.17e-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: 48.49 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 103 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHIIE 172
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 173 GLKGSLQRLQlEYVDV-----------VFANrpdsntpmEEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYS 234
Cdd:cd19098 113 QWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 235 VARQFNmippvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSE 314
Cdd:cd19098 182 GARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 27436964 315 EGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 373
Cdd:cd19098 233 ELAP---LMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
79-260 |
3.17e-06 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 48.57 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYA----AGK--AEVILGSIIKkkgwrRSSLVITTK 152
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYN-----AIKAGYRLFDGACDYGneveAGQgvARAIKEGIVK-----REDLFIVSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 153 LyWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDVVFANRP------------------------DSNTPMEEIVRAMT 208
Cdd:cd19115 79 L-WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfydgkkveFSNAPIQETWTAME 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27436964 209 HVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 260
Cdd:cd19115 152 KLVDKGLARSIGVSNFSAQLLMDLLRYAR----IRPATLQIEHHpyLTQPRLVK 201
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
86-254 |
5.34e-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: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWVtfggqiSDEV----AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGG 157
Cdd:cd19108 14 LGFGTYA------PEEVpkskALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 KAETErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------ 228
Cdd:cd19108 84 FHRPE--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdag 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 27436964 229 IMEAYSVA----RQFNMI---P-----PVCEQAEYHLF 254
Cdd:cd19108 154 LAKSIGVSnfnrRQLEMIlnkPglkykPVCNQVECHPY 191
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
82-391 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 82 RVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYWggka 159
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKLWC---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 160 eterGLSRKHIIE-GLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRamthVINQGMAMYWGTS---RWSAME------I 229
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLP----LDRSGMVIPSDTDfldTWEAMEdlviegL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 230 MEAYSVArQFN-------------MIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisGKYGNGVPes 296
Cdd:cd19110 145 VKNIGVS-NFNheqlerllnkpglRVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL------GGSCEGVD-- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 297 sraslkcyqwLKERIVseegrkqqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENlgaIQVLP- 375
Cdd:cd19110 213 ----------LIDDPV-------------IQRIAKKHGKSPAQILIRFQIQRNVI--VIPKSVTPSRIKEN---IQVFDf 264
|
330
....*....|....*.
gi 27436964 376 KMTSHVVNEIDNILRN 391
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 ... |
79-260 |
1.12e-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: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKaEVILG--SIIKKKGWRRSSLVITTKLyWG 156
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 157 GKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHVI 211
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAfkfvpieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27436964 212 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 260
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHpyLQQPKLIE 200
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
80-258 |
1.24e-05 |
|
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: 46.78 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyW 155
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 156 GGKAeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHV 210
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27436964 211 INQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF-QREK 258
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKR 190
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
79-227 |
2.57e-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: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 79 SGLRVSCLGLGTWVTFGGQisdEVAERLMTIAYESGVNLFDTAEVYAA----GKAeviLGSIIKKKGWRRSSLVITTKL- 153
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 154 --YWggkaeterglsrKHIIEGLKGSLQRLQLEYVDVVFANRP-----DSntpmEEIVRAMTHVINQGMAMYWGTSRWSA 226
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWPvcfekDS----DDSGKPFTPVNDDGKTRYAASGDHIT 145
|
.
gi 27436964 227 M 227
Cdd:cd19119 146 T 146
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
80-280 |
9.21e-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: 9.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 80 GLRVSCLGLGTWVTFGGQISDEVAerlmtIAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYwgg 157
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 158 KAETERGLSRkhiiEGLKGSLQRLQLEYVDVVFANRPD-------------------SNTPMEEIVRAMTHVINQGMAMY 218
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27436964 219 WGTSRWSAMEImeaysvARQFNMiP-----PVCEQAEYHLF-QREKvevqLPELYHKIGVGAMTWSPL 280
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; ... |
86-287 |
1.04e-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: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 86 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSiikkkGWRRSSLVITTKLyWGGKAETER 163
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIYGneEGVGAAIAAS-----GIPRDELFVTTKL-WNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27436964 164 GLSrkhiieGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRW--SAMEIMEAYSVar 237
Cdd:cd19130 82 PAA------AFAESLAKLGLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27436964 238 qfnmIPPVCEQAEYH--LFQREKVEVQlpelyHKIGVGAMTWSPLACGIISG 287
Cdd:cd19130 151 ----VVPAVNQIELHpaYQQRTIRDWA-----QAHDVKIEAWSPLGQGKLLG 193
|
|
| |
