|
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 ... |
80-352 |
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: 598.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 159
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 239
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 240 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 319
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270
....*....|....*....|....*....|...
gi 148683597 320 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVG 352
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVA 273
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
81-351 |
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: 591.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITT 160
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 161 KLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 240
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 241 AYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERI 320
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270
....*....|....*....|....*....|.
gi 148683597 321 VSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAI 271
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
78-351 |
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: 554.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 78 TGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLV 157
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 158 ITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 237
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 238 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 317
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270
....*....|....*....|....*....|....
gi 148683597 318 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAI 274
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
82-351 |
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: 525.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 82 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 161
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 241
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 242 YSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIV 321
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270
....*....|....*....|....*....|
gi 148683597 322 SEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAI 270
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
80-352 |
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: 510.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 159
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 239
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 240 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 319
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270
....*....|....*....|....*....|...
gi 148683597 320 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVG 352
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIA 273
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
80-351 |
1.34e-159 |
|
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: 449.74 E-value: 1.34e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 159
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKLYWGGKAE--TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 237
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 238 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 317
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270
....*....|....*....|....*....|....
gi 148683597 318 ERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19143 241 DR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAI 273
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
80-351 |
1.13e-139 |
|
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: 399.53 E-value: 1.13e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 159
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKLYWGGKAEtERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 239
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 240 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWL 316
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGS 239
|
250 260 270
....*....|....*....|....*....|....*
gi 148683597 317 KERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19142 240 DGNGIHEETRRASHKLRELSLIAERLGCDLTQLLI 274
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
89-352 |
1.05e-136 |
|
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: 390.80 E-value: 1.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKA 168
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 169 E-TERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 247
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 248 FNMIPPVCEQAEYHLFQREKVEvQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRK 327
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260
....*....|....*....|....*
gi 148683597 328 QQNKLKDLSPIAERLGCTLPQLAVG 352
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALA 261
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
80-351 |
1.07e-83 |
|
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: 256.64 E-value: 1.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWvTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSL 156
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 157 VITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 236 MEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcy 313
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT--- 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 148683597 314 qWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAV 351
Cdd:COG0667 232 -NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLAL 265
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
80-351 |
1.45e-77 |
|
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: 240.55 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVIT 159
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKLYWG-GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 238
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 239 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwl 316
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ-- 233
|
250 260 270
....*....|....*....|....*....|....*
gi 148683597 317 kERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLAL 264
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
80-350 |
6.87e-69 |
|
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: 218.64 E-value: 6.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkg 150
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 151 wRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWG 229
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 230 TSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR 307
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148683597 308 ASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVA 273
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
93-294 |
1.63e-67 |
|
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: 211.99 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTWvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETE 171
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 172 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMI 251
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148683597 252 PPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGII 294
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGPA 201
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
82-351 |
1.05e-62 |
|
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: 202.49 E-value: 1.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 82 YRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVI 158
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 159 TTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 236 MEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQW 315
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270
....*....|....*....|....*....|....*.
gi 148683597 316 LKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLAL 268
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
89-351 |
4.77e-62 |
|
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: 200.44 E-value: 4.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LY 163
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 164 WGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAys 243
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 244 varqFNMIPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkeri 320
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR------ 224
|
250 260 270
....*....|....*....|....*....|.
gi 148683597 321 vSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAI 254
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
81-350 |
5.36e-61 |
|
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: 198.19 E-value: 5.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLGTWvTFGGQ------ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRS 154
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 155 SLVITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 233
Cdd:cd19079 79 EVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 234 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKC 312
Cdd:cd19079 159 YAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAK 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 148683597 313 YQWLKErivSEEGRKQQNKLKDlspIAERLGCTLPQLA 350
Cdd:cd19079 238 LKYDYF---TEADKEIVDRVEE---VAKERGVSMAQVA 269
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
85-350 |
3.45e-59 |
|
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: 193.20 E-value: 3.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 85 LGKSGLRVSCLGLGTWVtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLV 157
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 158 ITTKLYWGgKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 237
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 238 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqw 315
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA---- 234
|
250 260 270
....*....|....*....|....*....|....*
gi 148683597 316 lKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLA 350
Cdd:cd19081 235 -AKRYLNERGLRI---LDALDEVAAEHGATPAQVA 265
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
81-351 |
1.91e-54 |
|
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: 181.06 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSL 156
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 157 VITTKL--------Y--WGgkaeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAM 226
Cdd:cd19151 80 IISTKAgytmwpgpYgdWG---------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 227 YWGTSRWSAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESS 306
Cdd:cd19151 151 YVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 148683597 307 RASlKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19151 229 RAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMAL 269
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
92-352 |
1.42e-52 |
|
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: 176.60 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 92 VSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK--- 161
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 --LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP------------------MEEIVRAMTHVIN 221
Cdd:cd19094 79 pgEGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 222 QGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--G 299
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148683597 300 NGVPESSRASLkcYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVG 352
Cdd:cd19094 238 AARPEGGRLNL--FPGYMARYRSPQALEAVAEYVK---LARKHGLSPAQLALA 285
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
81-351 |
4.32e-50 |
|
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: 169.94 E-value: 4.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLV 157
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 158 ITTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWS 234
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 235 AMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyq 314
Cdd:cd19150 159 PERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS----- 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 148683597 315 wlKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19150 233 --KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMAL 269
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
95-351 |
4.93e-50 |
|
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: 169.03 E-value: 4.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvTFGGQ---ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETE 171
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 172 RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmI 251
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 252 PPVCEQAEYHLFqREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQ 329
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNL 223
|
250 260
....*....|....*....|..
gi 148683597 330 NKLKDLSPIAERLGCTLPQLAV 351
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVAL 245
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
80-351 |
2.41e-49 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 169.01 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSL 156
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 157 VITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 233
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 234 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--K 311
Cdd:PRK09912 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegN 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148683597 312 CYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:PRK09912 250 KVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMAL 286
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
85-351 |
2.10e-47 |
|
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: 162.77 E-value: 2.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 85 LGKSGLRVSCLGLGTwVTFGGQ----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITT 160
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 161 KLYWG--GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEI 238
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 239 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKE 318
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270
....*....|....*....|....*....|...
gi 148683597 319 RIVSEEGRKQQNKLKDlspIAERLGCTLPQLAV 351
Cdd:cd19080 236 GKLTERNWAIVDVVAA---VAEELGRSAAQVAL 265
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
81-350 |
1.80e-44 |
|
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: 154.68 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLG----TWvtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 156
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 157 VITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 232 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRA 308
Cdd:cd19076 154 EASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPE 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 148683597 309 SLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19076 222 DD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLA 261
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
82-351 |
5.24e-40 |
|
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: 143.57 E-value: 5.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 82 YRNLGKSGLRVSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLV 157
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 158 ITTK--LYWGGKAETE----------RGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMA 225
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 226 MYWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---V 302
Cdd:cd19149 158 RAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefD 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 148683597 303 PESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAERLGCTLPQLAV 351
Cdd:cd19149 231 AGDARSGIPWFS--------PENREKVLALLEkWKPLCEKYGCTLAQLVI 272
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
91-350 |
9.24e-40 |
|
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: 142.37 E-value: 9.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 91 RVSCLGLGTW------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKLyw 164
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 ggkAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSN-TPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 243
Cdd:cd19093 78 ---APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 244 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG--NGVPESSRASLKCYQWLKERIV 321
Cdd:cd19093 155 ALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSpeNPPPGGRRRLFGRKNLEKVQPL 233
|
250 260
....*....|....*....|....*....
gi 148683597 322 seegrkqqnkLKDLSPIAERLGCTLPQLA 350
Cdd:cd19093 234 ----------LDALEEIAEKYGKTPAQVA 252
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
92-350 |
3.31e-39 |
|
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: 140.80 E-value: 3.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 92 VSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwggk 167
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 aetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 247
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 248 fnmipPVCEQAEYHLFQREKVEVQLPEL-YHKIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSE 323
Cdd:cd19085 150 -----IDSNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFE 214
|
250 260
....*....|....*....|....*....
gi 148683597 324 EG--RKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19085 215 PGaeEETFEALEKLKEIADELGVTMAQLA 243
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
89-350 |
5.93e-39 |
|
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: 140.45 E-value: 5.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTW-VTFG-GQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW- 164
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 ---GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 241
Cdd:cd19078 78 idgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 242 YSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlke 318
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF----- 225
|
250 260 270
....*....|....*....|....*....|...
gi 148683597 319 rivSEEGRKQQNKLKDL-SPIAERLGCTLPQLA 350
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIA 255
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
90-297 |
8.68e-38 |
|
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: 135.30 E-value: 8.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 90 LRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YW 164
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTPMEEIVRAMTHVINQGMAMYWGTS---RWSAMEIME 240
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148683597 241 AYSVArqfnmippvCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGK 297
Cdd:cd19086 158 RGGID---------VVQVIYNLLDQRPEEELFPLA-EEHGVGVIARVPLASGLLTGK 204
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
83-351 |
1.18e-37 |
|
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: 137.17 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 83 RNLGKSGLRVSCLGLGTwVTFGGQ-----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 157
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 158 ITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:cd19083 79 IATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 236 MEIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQW 315
Cdd:cd19083 158 EQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDL 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 148683597 316 LKERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19083 225 RNDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLAL 262
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
89-350 |
1.76e-37 |
|
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: 135.43 E-value: 1.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVTFGGQ---ISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLYw 164
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdYSDDKKAiEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 ggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 244
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 245 ARQfnmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivsee 324
Cdd:cd19072 152 LKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG------------------------- 202
|
250 260
....*....|....*....|....*.
gi 148683597 325 grkqqnkLKDLSPIAERLGCTLPQLA 350
Cdd:cd19072 203 -------SPLLDEIAKKYGKTPAQIA 221
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
93-352 |
9.17e-36 |
|
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: 131.52 E-value: 9.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-- 166
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 ---KAETERgLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 243
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 244 VARQFNMIPPVCEQAEYHLFqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLK 311
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRR 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148683597 312 CYQwlkerivSEEGRKQQNKLKDLspiAERLGCTLPQLAVG 352
Cdd:cd19082 232 VYY-------SEENFERLERAKEL---AEEKGVSPTQIALA 262
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
95-307 |
4.53e-34 |
|
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: 127.29 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKaeterG 173
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 174 LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPP 253
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148683597 254 VCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR 307
Cdd:cd19075 156 TVYQGMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGR 210
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
80-231 |
2.80e-31 |
|
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: 118.46 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTwvTFGGQISDEVAERlmtiAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVIT 159
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG--GGLPRESPELLRR----ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683597 160 TKLYWGGKAETerglsRKHIIEGLKGSLQRLQLEYVDVVF---ANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFS 142
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
89-294 |
8.56e-31 |
|
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: 117.67 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvTFGGQIS-----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLY 163
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 164 wggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 243
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148683597 244 VARQfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGII 294
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE 197
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
92-351 |
5.79e-30 |
|
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: 116.23 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 92 VSCLGLGTWVTFGGQ------ISDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRsSLVITTK-- 161
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggwgPQDD-RDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRAL--KGLRD-RPIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEImea 241
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQM--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 242 ysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPelY---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK 317
Cdd:cd19102 154 ----KRCQAIHPIASlQPPYSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRR 221
|
250 260 270
....*....|....*....|....*....|....*.
gi 148683597 318 -ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLAV 351
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAI 257
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
89-297 |
1.17e-29 |
|
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: 115.48 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVT----FGGqiSDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK- 161
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAmEIME 240
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148683597 241 AY-SVARQFNMIPPvceqaeYHLFQREKVEVQLP-ELYHKIGVgaMTWSPLACGIISGK 297
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPyARKHNIVT--LAYGALCRGLLSGK 206
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
80-296 |
2.45e-29 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 114.48 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 159
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TK---LYWGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 233
Cdd:COG4989 81 TKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683597 234 SAMeimeaysvarQFNMI------PPVCEQAEYHLFQREKVE------VQLpelyHKIGVgaMTWSPLACGIISG 296
Cdd:COG4989 161 TPS----------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLAGGRLFG 219
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
80-351 |
1.75e-28 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 113.41 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 152
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 153 RSSLVITTKLywGGKAET-------ERGLSRKHIIEGLKGSLQRLQLEYVD---VVFANRP-----------DSNTP--- 208
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 209 MEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSP 288
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148683597 289 LACGIISGKYGNGV-PESSRASlkcyqwLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:PRK10625 236 LAFGTLTGKYLNGAkPAGARNT------LFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMAL 293
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
88-290 |
2.30e-28 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 110.92 E-value: 2.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 167
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 247
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148683597 248 fnmIPPVCEQAEYHLFQREkvevqlPEL--YHK-IGVGAMTWSPLA 290
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELlaFCReHGIVVEAYSPLG 180
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
87-351 |
3.51e-28 |
|
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: 111.11 E-value: 3.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 87 KSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LY 163
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 164 WGGKAETERG---LSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMeime 240
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 241 aysvarQFNM------IPPVCEQAEYHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessrasl 310
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGG------------------ 208
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148683597 311 kcyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19092 209 --------RLFGGFDERFQRLRAALEELAEEYGVTIEAIAL 241
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
93-350 |
3.69e-28 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 111.27 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK---- 161
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 -LYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 240
Cdd:cd19752 79 pRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 241 AYSVARQFNMIPPVCEQAEYHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRAS 309
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148683597 310 LKCYqwlkerivseEGRKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19752 230 PEQY----------DGPDSDARLAVLEEVAGELGATPNQVV 260
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
83-350 |
3.79e-26 |
|
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: 105.98 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 83 RNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVIT 159
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 160 TKL---YWGGKAETERGlSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 236
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 237 EIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQWL 316
Cdd:cd19145 160 TIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKSH 229
|
250 260 270
....*....|....*....|....*....|....
gi 148683597 317 KeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19145 230 P-RFQGENLEKNKVLYERVEALAKKKGCTPAQLA 262
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
93-290 |
6.07e-26 |
|
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: 104.24 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTWVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKL--YWGGkA 168
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 169 ETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqF 248
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-F 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148683597 249 NMIppvceQAEYHLFQREKVEVqLPELY-HKIGVGAMtwSPLA 290
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLAAeAGLGVIVN--RPLA 188
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
80-350 |
7.43e-26 |
|
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: 105.60 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSL 156
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 157 VITTKlyWGGKAETERGL-----SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:cd19144 79 FLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 232 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRAS 309
Cdd:cd19144 157 ECSAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148683597 310 LKCYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19144 225 FEEGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQLT 267
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
88-350 |
7.61e-25 |
|
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: 101.56 E-value: 7.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWvTFGGQISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYwgg 166
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEiEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 kaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVAR 246
Cdd:cd19138 80 ----PSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 247 QFNMippVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegr 326
Cdd:cd19138 155 GGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENP-------------------- 207
|
250 260
....*....|....*....|....
gi 148683597 327 kqqnklkDLSPIAERLGCTLPQLA 350
Cdd:cd19138 208 -------TLKEIAARHGATPAQVA 224
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
88-352 |
3.72e-23 |
|
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: 97.69 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLG----TWVtfGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITT 160
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 161 KlywGGKAET--ERGLSRKHIIEGLKGSLQRL-QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 237
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 238 IMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlk 317
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL---- 225
|
250 260 270
....*....|....*....|....*....|....*
gi 148683597 318 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVG 352
Cdd:cd19077 226 DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALA 260
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
80-199 |
1.56e-22 |
|
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: 95.70 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSL 156
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 148683597 157 VITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVF 199
Cdd:cd19163 78 YLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQ 121
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
80-196 |
2.07e-22 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 96.81 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 80 MKYRNLGKSGLRVSCLGLGTWvtfGGQISD-EVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVI 158
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110
....*....|....*....|....*....|....*...
gi 148683597 159 TTKLYWGGKaeterglSRKHIIEGLKGSLQRLQLEYVD 196
Cdd:COG1453 73 ATKLPPWVR-------DPEDMRKDLEESLKRLQTDYID 103
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
82-199 |
3.23e-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: 93.70 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 82 YRNLGKSGLRVSCLGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTK 161
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 148683597 162 LYWGGKAETERGLSRkhiieglkgSLQRLQLEYVDVVF 199
Cdd:cd19100 74 TGARDYEGAKRDLER---------SLKRLGTDYIDLYQ 102
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
89-351 |
4.31e-22 |
|
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: 95.18 E-value: 4.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGT------WVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL 162
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 ---YWGGKAETER----GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:cd19146 87 ttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 236 MEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKVEVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASLK 311
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148683597 312 CYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQLAV 351
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVAL 270
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
95-292 |
1.36e-21 |
|
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: 91.95 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGkaetergL 174
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 175 SRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 254
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148683597 255 CEQAEYH--LFQREKVEVQLPelyHKIGVGAmtWSPLACG 292
Cdd:cd19073 145 VNQVEFHpfLYQAELLEYCRE---NDIVITA--YSPLARG 179
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
92-350 |
2.57e-21 |
|
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: 91.51 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 92 VSCLGLGTW-----VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW-- 164
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 244
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 245 ARqfnmIppVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivsee 324
Cdd:cd19088 158 VR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG--------GGDLAQPGG----------------- 204
|
250 260
....*....|....*....|....*.
gi 148683597 325 grkqqnklkDLSPIAERLGCTLPQLA 350
Cdd:cd19088 205 ---------LLAEVAARLGATPAQVA 221
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
89-292 |
2.78e-21 |
|
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: 91.55 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWGGka 168
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMYG-NEAQV--GEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 169 etergLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 248
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148683597 249 nmIPPVCEQAEYH--LFQRekvevQLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19140 148 --APLFTNQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLARG 186
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
81-351 |
1.65e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 90.79 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 81 KYRNLGKSGLRVSCLGLGtwvtfGGQI-------SDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrR 153
Cdd:cd19104 1 KYRRFGRTGLKVSELTFG-----GGGIgglmgrtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 154 SSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFA-NRPDSNTP--------------MEEIVRAMTH 218
Cdd:cd19104 73 AGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDkpvggtlsttdvlgLGGVADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 219 VINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL------FQREKVEV-----QLPELYHKIGVGAMTWS 287
Cdd:cd19104 150 LRSEGKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLlnpsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIR 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148683597 288 PLACGIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnklKDLSPIAERLGCTLPQLAV 351
Cdd:cd19104 225 VLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRA----AAFRALAREWGETLAQLAH 275
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
95-299 |
6.49e-19 |
|
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: 84.84 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGgkaeteRGL 174
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 175 SRKHIIEGLKGSLQRLQLEYVDVV-----FANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 248
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEgGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR-- 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683597 249 nmIPPVCEQAEYHLF--QREKVEvqlpelY-HKIGVGAMTWSPLACGI-----------ISGKYG 299
Cdd:cd19071 147 --IKPAVNQIELHPYlqQKELVE------FcKEHGIVVQAYSPLGRGRrpllddpvlkeIAKKYG 203
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
95-350 |
2.86e-18 |
|
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: 83.37 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGT-WVTFG-GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIkkKGWRRSSLVITTKLywGGKAETER 172
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 173 GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEE-----IVRAMTHVINQGMAMYWGTSRWSAmEIMEAYSVARQ 247
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 248 FNMIPPVCeqaEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivseegrk 327
Cdd:cd19090 156 FDVVLTAN---RYTLLDQSAADELLPAAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE-------- 216
|
250 260
....*....|....*....|...
gi 148683597 328 QQNKLKDLSPIAERLGCTLPQLA 350
Cdd:cd19090 217 LLDRAKRLYELCDEHGVPLPALA 239
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
87-289 |
1.74e-17 |
|
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: 81.69 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 87 KSGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITT 160
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 161 KLYWGGkaetergLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVIN 221
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148683597 222 QGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPL 289
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL 210
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
90-235 |
2.99e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 81.21 E-value: 2.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 90 LRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywG 165
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 166 G----------------KAETERGLSRKHIIEG-------------LKGSLQRLQLEYVDVVFANRP----------DSN 206
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFY 157
|
170 180
....*....|....*....|....*....
gi 148683597 207 TPMEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:cd19099 158 DRLEEAFEALEEAVAEGKIRYYGISTWDG 186
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
89-292 |
6.35e-17 |
|
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: 79.16 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGK 167
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-----MEEIVRAmthvinqGMAMYWGTSRWSAMEIMEAY 242
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQPFGDVYgawraMEELYKE-------GKIRAIGVSNFYPDRLVDLI 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148683597 243 SvarqFNMIPPVCEQAEYHLFqREKVEVQlpELYHKIGVGAMTWSPLACG 292
Cdd:cd19133 144 L----HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFAEG 186
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
95-292 |
1.61e-16 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 78.18 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGL 174
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 175 srkhiiEGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVArq 247
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148683597 248 fnmipPVCEQAEYH-LFQREkvevQLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19131 153 -----PVVNQIELHpRFQQR----ELRAFHAKHGIQTESWSPLGQG 189
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
83-295 |
2.32e-16 |
|
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: 78.35 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 83 RNLGKSGLRVSCLGLGTwVTFGGQISDEV----AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVI 158
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 159 TTKLYWGGKAETErgLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWsA 235
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148683597 236 MEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIIS 295
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLT 217
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
93-196 |
7.74e-16 |
|
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: 76.06 E-value: 7.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGgkae 169
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100
....*....|....*....|....*..
gi 148683597 170 teRGLSRKHIIEGLKGSLQRLQLEYVD 196
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID 99
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
95-292 |
1.28e-15 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 75.66 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKLywggkAETERGL 174
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 175 SRKhiIEGLKGSLQRLQLEYVDVVFANRPDSNT-PMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPP 253
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148683597 254 VCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG 190
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
95-231 |
1.44e-15 |
|
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: 75.64 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywg 165
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148683597 166 GKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRP-DSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS 139
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
94-301 |
4.73e-15 |
|
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: 74.48 E-value: 4.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 94 CLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAE 169
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 170 TERglsrkhIIEGLKGSLQRLQLEYVDVVFANRP-------------------DSNTPMEEIVRAMTHVINQGMAMYWGT 230
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683597 231 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNG 301
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG 206
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
82-311 |
5.45e-15 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 74.81 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 82 YRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVI 158
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 159 TTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANR---PDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSa 235
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 236 MEIMEaYSVARqfnmIPP-----VCEQAEYHLFQREKVEVqLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASL 310
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
.
gi 148683597 311 K 311
Cdd:PLN02587 226 E 226
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
88-266 |
5.58e-15 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 74.86 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLG------TWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK 161
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 LYW--------GGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 233
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190
....*....|....*....|....*....|...
gi 148683597 234 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQRE 266
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRD 197
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
88-292 |
5.65e-15 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 73.90 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWvTFGGQISDEVAERLMtiayESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 167
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AETERglsrkhIIEGLKGSLQRLQLEYVDVVFANRPDSNTP-------MEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 240
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148683597 241 aysvARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19135 154 ----LLEDCSVVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLAKG 198
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
96-290 |
7.40e-15 |
|
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: 73.81 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 96 GLGTWV--TFGGQISDEVAErLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGKaeterg 173
Cdd:cd19120 10 GTGTAWykSGDDDIQRDLVD-SVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 174 lsrkHIIEGLKGSLQRLQLEYVDVVFANRP----DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfn 249
Cdd:cd19120 80 ----DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK--- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148683597 250 mIPPVCEQAEYHLFqrekVEVQLPELYH---KIGVGAMTWSPLA 290
Cdd:cd19120 153 -IKPAVNQIEFHPY----LYPQQPALLEycrEHGIVVSAYSPLS 191
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
89-268 |
7.41e-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: 74.07 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVTFGgqisDEVAERLMTiAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITTKL 162
Cdd:cd19111 1 GFPMPVIGLGTYQSPP----EEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 YwggkaetERGLSRKHIIEGLKGSLQRLQLEYVDVVFAN-------------RPDSNTPMEEIVRAMTHVINQGMAMYWG 229
Cdd:cd19111 71 P-------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148683597 230 TSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF--QREKV 268
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELR 180
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
97-351 |
1.77e-14 |
|
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: 73.14 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 97 LGTW----------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGG 166
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 kaeteRGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDsntpmeEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYS 243
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPA------DVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 244 VARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIV 321
Cdd:cd19103 156 ILAKAG-VSLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAE 223
|
250 260 270
....*....|....*....|....*....|....
gi 148683597 322 SEEGRKQQnkLKDLSP----IAERLGCTLPQLAV 351
Cdd:cd19103 224 TYNPLLPQ--LEELTAvmaeIGAKHGASIAQVAI 255
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
95-350 |
1.99e-14 |
|
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: 72.78 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTwVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWG 165
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 166 GKAETER--GLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS--NTPMEEIVRAMTHVINQGM--AMYWGTSRWSAmeim 239
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 240 eAYSVARQFN----MIppvceQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQW 315
Cdd:cd19162 156 -LLRAARRADvdvvMV-----AGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRP 221
|
250 260 270
....*....|....*....|....*....|....*
gi 148683597 316 LKERIVSeegRKQQnklkdLSPIAERLGCTLPQLA 350
Cdd:cd19162 222 ATPEVLA---RARR-----LAAVCRRYGVPLPAAA 248
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
95-289 |
4.99e-14 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 71.54 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfgGQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGGKAEt 170
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLY---GNEAEVGEAIREKiaegVVKREDLFITTKL-WNSYHE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 171 erglsRKHIIEGLKGSLQRLQLEYVDVVFANRP-------DSNTPME---------EIVRAMTHVINQGMAMYWGTSRWS 234
Cdd:cd19116 85 -----REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148683597 235 AMEIMEAYSVARqfnmIPPVCEQAEYHL-FQREKvevqLPELYHKIGVGAMTWSPL 289
Cdd:cd19116 160 SEQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF 207
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
89-299 |
5.02e-14 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 70.93 E-value: 5.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVTfggqISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKA 168
Cdd:cd19126 6 GTRMPWLGLGVFQT----PDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 169 ETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqf 248
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD-- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148683597 249 nmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACGI---------ISGKYG 299
Cdd:cd19126 149 --VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGllsnpvlaaIGEKYG 203
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
87-199 |
2.61e-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: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 87 KSGLRVSCLGLGTwvtFGGQISDEVAE----RLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITT 160
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 148683597 161 KLywGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVF 199
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
87-351 |
2.68e-13 |
|
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: 69.30 E-value: 2.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 87 KSGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLyW 164
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKT-----AIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAETERglsrkhIIEGLKGSLQRLQLEYVDVV-----FANRPDSNTP---------MEEIVRAMTHVINQGMAMYWGT 230
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVRLKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 231 SRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASL 310
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSPGTTWVKK 214
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 148683597 311 KCyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAV 351
Cdd:cd19125 215 NV---LKDPIVTK--------------VAEKLGKTPAQVAL 238
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
95-302 |
4.11e-13 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 68.56 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKaetergl 174
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 175 sRKHIIEGLKGSLQRLQLEYVDVVFANRPDSntPMEEIVRAMTHVIN---QGMAMYWGTSRWSA---MEIMEAYSVArqf 248
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148683597 249 nmipPVCEQAEYH-LFQREkvEVQLPELYHKIGVGAmtWSPLACGiisgkyGNGV 302
Cdd:PRK11565 156 ----PVINQIELHpLMQQR--QLHAWNATHKIQTES--WSPLAQG------GKGV 196
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
89-310 |
1.49e-12 |
|
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381381 [Multi-domain] Cd Length: 307 Bit Score: 67.55 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKL 162
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 YWGGkaeterglSRKHIIEG-LKGSLQRLQLEYVDVVFANRP---------------------DSNTPMEEIVRAMTHVI 220
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 221 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYG 299
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPG 223
|
250
....*....|.
gi 148683597 300 NGVPESSRASL 310
Cdd:cd19155 224 TGSPSGSSPDL 234
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
88-305 |
2.52e-12 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 66.52 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGgqiSDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIK---KKG--WRRSSLVITTKL 162
Cdd:cd19124 1 SGQTMPVIGMGTASDPP---SPEDIKAAVLEAIEVGYRHFDTAAAYGT---EEALGEALAealRLGlvKSRDELFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 yWGGKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP----------------MEEIVRAMTHVINQGMAM 226
Cdd:cd19124 75 -WCSDAH------PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 227 YWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLacGIISGKYG-NGVPE 304
Cdd:cd19124 148 AIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPL--GAPGTKWGsNAVME 217
|
.
gi 148683597 305 S 305
Cdd:cd19124 218 S 218
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
88-261 |
7.78e-12 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 65.10 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 162
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQVKAAV-----KYALDAGYRHIDCAAVY-GNEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDV--------------VFANRPD-----SNTPMEEIVRAMTHVINQG 223
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKG 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 148683597 224 MAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH 261
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECH 181
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
89-299 |
1.05e-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: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 167
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AETERGLSrkhiieGLKGSLQRLQLEYVDVVFANRPDSNTpMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 247
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683597 248 fnmIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG---------IISGKYG 299
Cdd:cd19156 149 ---VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
88-292 |
1.63e-11 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 64.43 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIK---KKGW-RRSSLVITTKLY 163
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKELILN-----AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 164 wggkaETERGlsrkHIIEGLKGSLQRLQLEYVDVVFANRP-----------------------DSNTPMEEIVRAMTHVI 220
Cdd:cd19112 79 -----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148683597 221 NQGMAMYWGTSRWSA--MEIMEAYSvarqfnMIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACG 292
Cdd:cd19112 150 SAGLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGA 214
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-351 |
1.69e-11 |
|
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: 64.15 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 91 RVSCLGLGTWVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKLYW 164
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAETergLSRKHIIEGLKGSLQRLQLEYVDVV-FANRPDSNTPMEEIVRAMTHVINQGMAMYWG-----TSRWSamEI 238
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGltnfdTERLR--EI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 239 MEAysvarqfnMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCY 313
Cdd:cd19101 154 LDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKY 223
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148683597 314 QwlkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAV 351
Cdd:cd19101 224 K----LMIDEWGgwDLFQELLRTLKAIADKHGVSIANVAV 259
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
95-269 |
1.13e-10 |
|
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: 61.66 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLyWGGKAETEr 172
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 173 glsrkHIIEGLKGSLQRLQLEYVD-------VVF---ANRPDSNT--------PMEEIVRAMTHVINQGMAMYWGTSRWS 234
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 148683597 235 AMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 269
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHpyLQQPELLA 194
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
95-292 |
1.14e-10 |
|
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: 61.11 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL--YWGGK 167
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AETErglsrkhiiEGLKGSLQRLQLEYVDVVFANRP-----DSNTPMEEIVR-----AMTHVINQGMAMYWGTSRW--SA 235
Cdd:cd19136 76 EKAR---------AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYtvRH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148683597 236 MEIMEAYSvarqfnMIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG 194
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
89-289 |
2.34e-10 |
|
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: 60.50 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--G 166
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 KAETERGLSRkhiieglkgSLQRLQLEYVDVVFANRPdsnTPME-----EIVRAMTHVINQGMAMYWGTSRWSA---MEI 238
Cdd:cd19127 78 YDKALRGFDA---------SLRRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148683597 239 MEAYSVarqfnmIPPVcEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPL 289
Cdd:cd19127 146 IDATTV------VPAV-NQVELHPYFSQK---DLRAFHRRLGIVTQAWSPI 186
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
89-196 |
2.82e-10 |
|
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: 59.98 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKKKGWRRSSLVITTKLywggka 168
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110
....*....|....*....|....*....|..
gi 148683597 169 eteRGlsRKH----IIEGLKGSLQRLQLEYVD 196
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVD 96
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
89-292 |
5.42e-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: 59.33 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTW-VTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 167
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 168 AETERGLsrkhiiEGLKGSLQRLQLEYVDVVFANRPdSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARq 247
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148683597 248 fnmIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACG 292
Cdd:cd19157 150 ---IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG 188
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
95-231 |
1.02e-09 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 58.50 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWggkaeTERgL 174
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148683597 175 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGIS 129
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
95-231 |
2.58e-09 |
|
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: 56.98 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWggkaeteRGL 174
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148683597 175 SRKHIIEGLKGSLQRLQLEYVDVVFAN--RPDSNTPMEEIVRAMTHVINQGMAMYWGTS 231
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVS 127
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
103-261 |
3.15e-09 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 57.47 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 103 FGGQISDEVAERLMT-IAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAETERglsrk 177
Cdd:cd19129 11 FGTLIPDPSATRNAVkAALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 178 hIIEGLKGSLQRLQLEYVDVV-----FANRP---------------DSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAME 237
Cdd:cd19129 82 -VKPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180
....*....|....*....|....
gi 148683597 238 IMEAYSVARqfnmIPPVCEQAEYH 261
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESH 180
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
93-199 |
1.73e-08 |
|
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: 55.02 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 93 SCLGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLywgGK-- 167
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148683597 168 --AETERGL-----------------SRKHIIEGLKGSLQRLQLEYVDVVF 199
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILY 125
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
95-211 |
1.94e-08 |
|
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: 54.92 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKLYWGGKAETE 171
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 148683597 172 RGLSRKHIIEGLKG------------------SLQRLQLEYVDVVFANRPDSNTPMEE 211
Cdd:cd19152 80 VEPTFEPGFWNPLPfdavfdysydgilrsiedSLQRLGLSRIDLLSIHDPDEDLAGAE 137
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
88-289 |
4.07e-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: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILGsiIKK---KGWRRSSLVITTKLYW 164
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY-QNEDEVGEG--IKEaiaGGVKREDLFVTTKLWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAETERGLSRkhiieglkgSLQRLQLEYVDV----------------VFANRPDSNTPME------EIVRAMTHVINQ 222
Cdd:cd19121 80 TYHRRVELCLDR---------SLKSLGLDYVDLylvhwpvllnpngnhdLFPTLPDGSRDLDwdwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148683597 223 GMAMYWGTSRWSAM---EIMEAYSVARQFNMIP--PVCEQAEYHLFQREKvevqlpelyhkiGVGAMTWSPL 289
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVVPAVNQVEnhPYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
88-208 |
3.03e-07 |
|
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: 51.34 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLyWGgk 167
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIYG-NEEEV--GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 148683597 168 aeTERglsrKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTP 208
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDP 113
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
88-269 |
2.58e-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: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYA----AGK--AEVILGSIIKkkgwrRSSLVITTK 161
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYN-----AIKAGYRLFDGACDYGneveAGQgvARAIKEGIVK-----REDLFIVSK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 162 LyWGGKAETErglsrkHIIEGLKGSLQRLQLEYVDVVFANRP------------------------DSNTPMEEIVRAMT 217
Cdd:cd19115 79 L-WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvdpavryppgwfydgkkveFSNAPIQETWTAME 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148683597 218 HVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 269
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) ... |
95-263 |
4.35e-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: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWVtfggqiSDEV----AERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKK----GWRRSSLVITTKLyWGG 166
Cdd:cd19108 14 LGFGTYA------PEEVpkskALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 KAETErgLSRKhiieGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHvinqGMAMYWGT---SRWSAME------ 237
Cdd:cd19108 84 FHRPE--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEELFPKDEN----GKLIFDTVdlcATWEAMEkckdag 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 148683597 238 IMEAYSVA----RQFNMI---P-----PVCEQAEYHLF 263
Cdd:cd19108 154 LAKSIGVSnfnrRQLEMIlnkPglkykPVCNQVECHPY 191
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
89-267 |
7.37e-06 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 47.17 E-value: 7.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAgkaEVILGSIIKK---KGW-RRSSLVITTKLyW 164
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 165 GGKAeterglSRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHV 219
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148683597 220 INQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLF-QREK 267
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKR 190
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
88-269 |
9.13e-06 |
|
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: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKaEVILG--SIIKKKGWRRSSLVITTKLyWG 165
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 166 GKAEterglsRKHIIEGLKGSLQRLQLEYVDVVFANRPDS-------------------------NTPMEEIVRAMTHVI 220
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAfkfvpieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148683597 221 NQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH--LFQREKVE 269
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHpyLQQPKLIE 200
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
88-236 |
2.12e-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: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQisdEVAERLMTIAYESGVNLFDTAEVYAA----GKAeviLGSIIKKKGWRRSSLVITTKL- 162
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 163 --YWggkaeterglsrKHIIEGLKGSLQRLQLEYVDVVFANRP-----DSntpmEEIVRAMTHVINQGMAMYWGTSRWSA 235
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWPvcfekDS----DDSGKPFTPVNDDGKTRYAASGDHIT 145
|
.
gi 148683597 236 M 236
Cdd:cd19119 146 T 146
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
88-206 |
2.19e-05 |
|
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: 45.48 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 88 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 162
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAV-----KIALKAGYRHLDLAKVY-QNQHEV--GQALKEllkeePGVKREDLFITSKL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 148683597 163 yWGGKAETErglsrkHIIEGLKGSLQRLQLEYVD-------VVFANRPDSN 206
Cdd:cd19118 75 -WNNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKPTGDLN 118
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
91-303 |
3.90e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 44.95 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 91 RVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYWggka 168
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKLWC---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 169 eterGLSRKHIIE-GLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRamthVINQGMAMYWGTS---RWSAME------I 238
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPMGFKPGEPDLP----LDRSGMVIPSDTDfldTWEAMEdlviegL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148683597 239 MEAYSVArQFN-------------MIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisGKYGNGVP 303
Cdd:cd19110 145 VKNIGVS-NFNheqlerllnkpglRVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL------GGSCEGVD 212
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
89-289 |
7.59e-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: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 89 GLRVSCLGLGTWVTFGGQISDEVAerlmtIAYESGVNLFDTAEVYaAGKAEVILG--SIIKKKGWRRSSLVITTKLYwgg 166
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 167 KAETERGLSRkhiiEGLKGSLQRLQLEYVDVVFANRPD-------------------SNTPMEEIVRAMTHVINQGMAMY 227
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTgfkpgkelfpldesgnvipSDTTFLDTWEAMEELVDEGLVKA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148683597 228 WGTSRWSAMEImeaysvARQFNMiP-----PVCEQAEYHLF-QREKvevqLPELYHKIGVGAMTWSPL 289
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; ... |
95-296 |
8.67e-05 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 43.36 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 95 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSiikkkGWRRSSLVITTKLyWGGKAETER 172
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIYGneEGVGAAIAAS-----GIPRDELFVTTKL-WNDRHDGDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 173 GLSrkhiieGLKGSLQRLQLEYVDVVFANRPdsnTPME----EIVRAMTHVINQGMAMYWGTSRW--SAMEIMEAYSVar 246
Cdd:cd19130 82 PAA------AFAESLAKLGLDQVDLYLVHWP---TPAAgnyvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG-- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148683597 247 qfnmIPPVCEQAEYH--LFQREKVEVQlpelyHKIGVGAMTWSPLACGIISG 296
Cdd:cd19130 151 ----VVPAVNQIELHpaYQQRTIRDWA-----QAHDVKIEAWSPLGQGKLLG 193
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
119-266 |
1.34e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 39.95 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 119 AYESGVNLFDTAEVYAAGkaevILGSIIkkkgwR------RSSLVITTKLywgGKAETERG-----LSRKHIIEGLKGSL 187
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148683597 188 QRLQLEYVDVV------FANRPDSNtPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnmiPPVCEQAEYH 261
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
....*
gi 148683597 262 LFQRE 266
Cdd:PRK10376 190 LAHRA 194
|
|
| |
