|
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 ... |
76-386 |
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: 660.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIM 235
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 236 EAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLKEK 315
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 316 IVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV-SKSFCHVI 386
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlPKMTSHVV 312
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
78-378 |
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: 641.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVITTK 157
Cdd:cd19141 2 YRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 LYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEA 237
Cdd:cd19141 82 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 238 YSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLKEKIV 317
Cdd:cd19141 162 YSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKIL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 318 SEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19141 242 SEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQV 302
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
74-378 |
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: 615.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 74 TGMAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLV 153
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTKLYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAME 233
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 234 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLK 313
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 314 EKIVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQV 305
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
78-378 |
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: 583.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVITTK 157
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 LYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEA 237
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 238 YSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLKEKIV 317
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 318 SEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQV 301
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
76-386 |
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: 562.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIM 235
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 236 EAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLKEK 315
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 316 IVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV----SKSFCHVI 386
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpklSSSIVHEI 315
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
76-378 |
1.89e-177 |
|
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: 497.12 E-value: 1.89e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWGGKAE--TERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAME 233
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 234 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYQWLK 313
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 314 EkIVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19143 241 D-RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEV 304
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
85-379 |
7.79e-156 |
|
Shaker potassium channel beta subunit family and similar proteins; This family includes voltage-gated potassium channel subunits, beta-1 (KCAB1B), beta-2 (KCAB2B) and beta-3 (KCAB3B). KCAB1B and KCAB2B are cytoplasmic potassium channel subunits that modulate the characteristics of the channel-forming alpha-subunits. KCAB3B is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. The family also includes Drosophila melanogaster Hk protein, a founding member of aldo-keto reductase family 6 member B1 (AKR6B1), as well as voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa, founding members of AKR6C1and AKR6C2, respectively. Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381300 [Multi-domain] Cd Length: 297 Bit Score: 441.65 E-value: 7.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSSLVITTKLYWGGKA 164
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 E-TERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARQ 243
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 244 FNLIPPVCEQAEYHLFQREKVEvQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASmKSYQWLKEKIVSEDGRK 323
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSR-ATDEDNRDKKRRLLTDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 324 QQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVK 292
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
76-378 |
4.37e-152 |
|
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: 433.04 E-value: 4.37e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWGGKAEtERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIM 235
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 236 EAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSY---QWL 312
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSkykVGS 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 313 KEKIVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19142 240 DGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQL 305
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
76-379 |
2.98e-99 |
|
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: 298.25 E-value: 2.98e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWvTFG---GQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSSL 152
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 153 VITTKLYW-GGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTA 231
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAYSVARqfNLIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKYENG--IPDSSRASMKSY 309
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 310 QWlkekivsEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:COG0667 235 QG-------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLE 297
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
76-379 |
5.99e-89 |
|
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: 271.75 E-value: 5.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTwVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVIT 155
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWG-GKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEI 234
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 235 MEAYSVARQFNLIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKYENG--IPDSSRASMKSYQwl 312
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkrPESGRLVERARYQ-- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 313 kEKIVSEDGRKQQAKLKELghiAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19087 234 -ARYGLEEYRDIAERFEAL---AAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEIT 296
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
76-379 |
2.18e-78 |
|
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: 244.83 E-value: 2.18e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTwVTFG---------GQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkg 146
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 147 wRRSSLVITTKL-YWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWG 225
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 226 TSRWTAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKY--ENGIPDSSR 303
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 304 ASMKSYQWLkekIVSEDgrKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLS 306
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
78-377 |
1.56e-77 |
|
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2). It catalyzes the conversion of 3-hydroxybutanal (3-HB) to 1,3-butanediol (1,3-BDO) by using NADPH as a cofactor.
Pssm-ID: 381315 [Multi-domain] Cd Length: 308 Bit Score: 242.55 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVY--AAGKAEVILGNIIKK-KGWRRSSLVI 154
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 155 TTKL-Y--WGGKaeTERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTA 231
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAYSVARQFNlIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRAsMKSYQW 311
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 312 LKEKIVSEDgrkQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALK 298
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
85-375 |
8.47e-75 |
|
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: 235.11 E-value: 8.47e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWV---TFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTK--LY 159
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 WGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAys 239
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 varqFNLIPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIITGKYENGI---PDSSRASMKSYQwlkeki 316
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEPtfpPDDRRSRFPFFR------ 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 317 vSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGA 282
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
81-381 |
1.23e-71 |
|
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: 227.10 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 81 LGKSGLRVSCLGLGTWVtFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAA-------GKAEVILGNIIKKKGwRRSSLV 153
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTKLYWGgKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAME 233
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 234 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGI-PDSSRASMKSYqwl 312
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEAdLPGSTRRGEAA--- 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 313 kEKIVSEDGRKQqakLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19081 236 -KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGLRLT 300
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
89-374 |
1.52e-71 |
|
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: 224.32 E-value: 1.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTWvTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSSLVITTKL-YWGGKAETE 167
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 168 RGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARQFNLI 247
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 248 PPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmksyqwlkekivsedgrkqqak 327
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207134339 328 lkelghiaeklgctLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLG 374
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
78-377 |
8.31e-68 |
|
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is a founding member of aldo-keto reductase family 14 member A2 (AKR14A2).
Pssm-ID: 381377 [Multi-domain] Cd Length: 309 Bit Score: 217.27 E-value: 8.31e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYA--AGKAEVILGNIIKK--KGWRrSSLV 153
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTKL--------Y--WGgkaeterglSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMY 223
Cdd:cd19151 81 ISTKAgytmwpgpYgdWG---------SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 224 WGTSRWTAMEIMEAYSVARQFNlIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSR 303
Cdd:cd19151 152 VGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 304 ASmKSYQWLKEKIVSEDgrkQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19151 230 AA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
78-378 |
9.60e-68 |
|
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: 217.45 E-value: 9.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWvTFGGQ------ISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSS 151
Cdd:cd19079 2 YVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 152 LVITTKLYWG-GKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWT 230
Cdd:cd19079 80 VVIATKVYFPmGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 231 AMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKvEVQLPELYHKIGVGAMTWSPLACGIITGKYEngiPDSSRASMKSYQ 310
Cdd:cd19079 160 AWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWG---DTTERRRSTTDT 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 311 WLKEKIVSEDGRKQqaKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19079 236 AKLKYDYFTEADKE--IVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
88-378 |
4.95e-67 |
|
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the prototype of this family. It is an NADP(H)-dependent aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NADP(H) as a hydride donor.
Pssm-ID: 381320 [Multi-domain] Cd Length: 328 Bit Score: 215.89 E-value: 4.95e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 88 VSCLGLGTwVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYA-------AGKAEVILGNIIKKKGwRRSSLVITTK--- 157
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 --LYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTP------------------MEEIVRAMTYVIN 217
Cdd:cd19094 79 pgEGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 218 QGMSMYWGTSRWTAMEIMEAYSVARQFNLIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENG 297
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 298 IPDSSRASMKSYQWLKEKIVSEdgrKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19094 238 AARPEGGRLNLFPGYMARYRSP---QALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFD 314
|
.
gi 1207134339 378 V 378
Cdd:cd19094 315 V 315
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
78-377 |
8.41e-63 |
|
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: 204.61 E-value: 8.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYA--AGKAEVILGNIIKKK-GWRRSSLVI 154
Cdd:cd19150 2 YRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 155 TTKL---YWGGKAeTERGlSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTA 231
Cdd:cd19150 82 STKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAYSVARQFNlIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMKSYqw 311
Cdd:cd19150 160 ERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS-- 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 312 LKEKIVSEDgrkQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19150 237 LSPKMLTEA---NLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
91-375 |
1.14e-61 |
|
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: 201.00 E-value: 1.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvTFGGQ---ISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVITTKLyWGGKAETE 167
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 168 RGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqfnlI 247
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 248 PPVCEQAEYHLFqREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPdssrasMKSYQWLKEKIVSEDgrKQQAK 327
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPD------KGPGERRRLLKKGTP--LNLEA 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1207134339 328 LKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:pfam00248 226 LEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGA 273
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
76-376 |
2.79e-61 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 201.76 E-value: 2.79e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYA--AGKAEVILGNIIKKK-GWRRSSL 152
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 153 VITTKL---YWGGKAETerGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRW 229
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 230 TAMEIMEAYSVARQFNlIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASM--K 307
Cdd:PRK09912 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegN 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 308 SYQWLKEKIVSEDGRKQqakLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAI 376
Cdd:PRK09912 250 KVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAL 315
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
81-379 |
2.73e-60 |
|
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381306 [Multi-domain] Cd Length: 307 Bit Score: 197.83 E-value: 2.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 81 LGKSGLRVSCLGLGTwVTFGGQ----ISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITT 156
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 157 KLYWG--GKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEI 234
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 235 MEAYSVARQFNLIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGipDSSRASMKSYQWLKE 314
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 315 KIVSEdgrKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19080 236 GKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLT 297
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
88-379 |
5.40e-52 |
|
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: 175.85 E-value: 5.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 88 VSCLGLGTWV----TFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTKLYwggk 163
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 aetERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARq 243
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 244 fnlipPVCEQAEYHLFQREKVEVQLPEL-YHKIGVgaMTWSPLACGIITGKYENGI---PDSSRasmKSYQWLKEKIVSE 319
Cdd:cd19085 150 -----IDSNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFSSAEdfpPGDAR---TRLFRHFEPGAEE 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 320 dgrKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19085 220 ---ETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDLE 276
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
78-379 |
9.14e-49 |
|
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: 168.22 E-value: 9.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWV----TFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLV 153
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTK--LYWGGKAETE----------RGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMS 221
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 222 MYWGTSRWTAMEIMEaYSVARQFNLIppvceQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIITGKYENG---I 298
Cdd:cd19149 158 RAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 299 PDSSRASMKSYQwlKEKIvsedgRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19149 231 AGDARSGIPWFS--PENR-----EKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
.
gi 1207134339 379 S 379
Cdd:cd19149 304 R 304
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
87-375 |
1.97e-47 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 163.94 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 87 RVSCLGLGTW------VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSSLVITTKLyw 160
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 ggkAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSN-TPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYS 239
Cdd:cd19093 78 ---APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWySQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 VARQFNlIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKY--ENGIPDSSRASMKSYQWlkekiv 317
Cdd:cd19093 155 ALKERG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYspENPPPGGRRRLFGRKNL------ 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 318 sedgRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVssVLLGTSNAEQLTENLGA 375
Cdd:cd19093 228 ----EKVQPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
78-379 |
4.89e-46 |
|
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: 160.46 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLG----TWvtFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLV 153
Cdd:cd19076 2 TRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTKlyWG---GKAETERGL--SRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSR 228
Cdd:cd19076 77 IATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 229 WTAMEIMEAYSVArqfnliPPVCEQAEYHLFQREKVEVQLP---ELyhkiGVGAMTWSPLACGIITGKY---ENGIPDSS 302
Cdd:cd19076 155 ASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIkspEDLPEDDF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 303 RASMKSYQwlkekivSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCL-RNEGVSSVlLGTSNAEQLTENLGAIQVS 379
Cdd:cd19076 225 RRNNPRFQ-------GENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDVV 294
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
85-377 |
2.54e-45 |
|
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase. Escherichia coli YeaE may act as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381298 [Multi-domain] Cd Length: 263 Bit Score: 157.39 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTFGGQ---ISDDVA--EQLMTiAYESGVNLFDTAEVYAAGKAEVILGNIIkkKGWRRSSLVITTKLY 159
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdYSDDKKaiEALRY-AIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 wggkaetERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYS 239
Cdd:cd19072 78 -------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 VARQfnlIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGKyengipdssrasmksyqwlkekivse 319
Cdd:cd19072 151 YLKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNA-------------------------- 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 320 dgrKQQAKLKElghIAEKLGCTLPQLAVAWCLRNEGVsSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19072 201 ---KGSPLLDE---IAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
79-378 |
2.83e-44 |
|
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: 156.04 E-value: 2.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 79 RNLGKSGLRVSCLGLGTwVTFGGQ-----ISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSSLV 153
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 154 ITTK--LYWGGKaETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTA 231
Cdd:cd19083 79 IATKgaHKFGGD-GSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAySVARQFNLIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIITGKY--ENGIPDSSrasmksy 309
Cdd:cd19083 158 EQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYtkDTKFPDND------- 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 310 qwLKEKIVSEDGRKQQAKLK---ELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19083 224 --LRNDKPLFKGERFSENLDkvdKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
85-379 |
1.29e-43 |
|
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: 153.93 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTW-VTFG-GQISD-DVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTKLYW- 160
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 ---GGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEA 237
Cdd:cd19078 78 idgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 238 YSVArqfnliPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIITGKY-ENGIPDSS--RASMKSYqwlke 314
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIdENTKFDEGddRASLPRF----- 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 315 kivSEDGRKQQAKLKEL-GHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIE 288
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
86-375 |
6.74e-43 |
|
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: 150.32 E-value: 6.74e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 86 LRVSCLGLGTWV---TFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTKL--YW 160
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 GGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFA-NRPDSNTPMEEIVRAMTYVINQGMSMYWGTS---RWTAMEIME 236
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AYSVArqfnlippvCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIITGKyengipdssrasmksyqwlkeki 316
Cdd:cd19086 158 RGGID---------VVQVIYNLLDQRPEEELFPLA-EEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 317 vsedgrkqqaklkelghiaeklgctLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19086 205 -------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
91-377 |
8.35e-42 |
|
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: 149.24 E-value: 8.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIikkkGWRRSSLVITTKLY-WGGKaeterG 169
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 170 LSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARQFNLIPP 249
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 250 VCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIITGKYENGIP-------DSSRASMKSYQ--WLKEKIVsed 320
Cdd:cd19075 156 TVYQGMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYKYSEDkagggrfDPNNALGKLYRdrYWKPSYF--- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 321 grkqqAKLKELGHIAEKLGCTLPQLAVAWC-----LRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19075 232 -----EALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALE 288
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
89-375 |
1.72e-40 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 145.39 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTwVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAA----GKAEVILGNIIKKKGwRRSSLVITTKlywGG-- 162
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 163 ---KAETERgLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYS 239
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 VARQFNLIPPVCEQAEYHLFqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIITGKYENGIPDSSRASMK 307
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRRV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 308 SYqwlkekivSEDGRKQQAKLKELghiAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19082 233 YY--------SEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
88-375 |
1.63e-39 |
|
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: 143.20 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 88 VSCLGLGTWV-----TFGGQISDDVAEQLMTI--AYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSsLVITTK--L 158
Cdd:cd19102 1 LTTIGLGTWAiggggWGGGWGPQDDRDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 YWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAY 238
Cdd:cd19102 78 LWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 239 SVARQFNLIPPvceqaeYHLFQREKVEVQLPelY---HKIGVgaMTWSPLACGIITGKYENGipdsSRASMKSYQWLK-E 314
Cdd:cd19102 158 AIHPIASLQPP------YSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMTPE----RVASLPADDWRRrS 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 315 KIVSEDGRKQQAKLKE-LGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19102 224 PFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGA 285
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
76-376 |
4.86e-38 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 137.72 E-value: 4.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGlgtwvtFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIkkKGWRRSSLVIT 155
Cdd:cd19105 1 MPYRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKLYWGGKAETerglsRKHIIEGLKGSLQRMQMEYVDVVF---ANRPDSNTPMEEIVRAMTYVINQGMSMYWGTS----- 227
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSthdnm 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 228 RWTAME---------IMEAYSVARQFNLIPPVceqaeyhlfqrekvevqLPELY-HKIGVGAMTwsplacgiitgkyeng 297
Cdd:cd19105 148 AEVLQAaiesgwfdvIMVAYNFLNQPAELEEA-----------------LAAAAeKGIGVVAMK---------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 298 ipdsSRASMKSYQWLKEKIVSEDGRKQQAKLKelghiaeklgctlpqlavaWCLRNEGVSSVLLGTSNAEQLTENLGAI 376
Cdd:cd19105 195 ----TLAGGYLQPALLSVLKAKGFSLPQAALK-------------------WVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
76-381 |
4.08e-36 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 135.37 E-value: 4.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTwVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAA-------GKAEVILGNIIKKKGwR 148
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 149 RSSLVITTKLywGGKAET-------ERGLSRKHIIEGLKGSLQRMQMEYVD---VVFANRP-----------DSNTP--- 204
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDlyqVHWPQRPtncfgklgyswTDSAPavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 205 MEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSP 284
Cdd:PRK10625 157 LLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 285 LACGIITGKYENGI-PDSSRASMKSyqwlkeKIVSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGT 363
Cdd:PRK10625 236 LAFGTLTGKYLNGAkPAGARNTLFS------RFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330
....*....|....*...
gi 1207134339 364 SNAEQLTENLGAIQVSKS 381
Cdd:PRK10625 310 TTMEQLKTNIESLHLTLS 327
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
89-375 |
8.80e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 132.84 E-value: 8.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTwVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYA-------AGKAEVILGNIIKKKGwRRSSLVITTK---- 157
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 -LYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIME 236
Cdd:cd19752 79 pRDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AYSVARQFNLIPPVCEQAEYHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLACGIITgkyengipdssRAS 305
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPLLSGAYT-----------RPD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 306 MK-SYQWLkekivSEDGRKQQAKLKElghIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19752 227 RPlPEQYD-----GPDSDARLAVLEE---VAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
76-379 |
6.38e-35 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 130.66 E-value: 6.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TK---LYWGGKAETERG---LSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRW 229
Cdd:COG4989 81 TKcgiRLPSEARDNRVKhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 230 TAMeimeaysvarQFNLI------PPVCEQAEYHLFQREKVE------VQLpelyHKIGVgaMTWSPLACGIITGKYeng 297
Cdd:COG4989 161 TPS----------QFELLqsaldqPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAWSPLAGGRLFGGF--- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 298 ipdssrasmksyqwlkekivSEDGRKQQAKLKElghIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:COG4989 222 --------------------DEQFPRLRAALDE---LAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALD 278
|
..
gi 1207134339 378 VS 379
Cdd:COG4989 279 IE 280
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
83-378 |
1.37e-34 |
|
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.
Pssm-ID: 381318 [Multi-domain] Cd Length: 287 Bit Score: 129.60 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 83 KSGLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVITTK---LY 159
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 WGGKAETERG---LSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMeime 236
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 aysvarQFNL------IPPVCEQAEYHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGIITGkyengipdssrasm 306
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGGRLFG-------------- 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 307 ksyqwlkekivsEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19092 213 ------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
85-381 |
2.00e-34 |
|
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: 128.46 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvTFGGQIS-----DDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgWRRSSLVITTKLY 159
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 wggkaetERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYS 239
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 VARQfnliPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKyengipdssrasmksyqwlkekivse 319
Cdd:cd19137 151 KSQT----PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN-------------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 320 dgrkqqaklKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLgTSNAEQLTENLGAIQVSKS 381
Cdd:cd19137 201 ---------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEIKLS 252
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
89-375 |
2.65e-33 |
|
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the prototype of this family. It is a putative aldo-keto reductase that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381321 [Multi-domain] Cd Length: 253 Bit Score: 125.04 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTWVTFG--GQISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIkkKGWRRSSLVITTKL--YWGGkA 164
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRAL--AGLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 ETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAmEIMEAYSVARqF 244
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSGDGE-ELEAAIASGV-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 245 NLIppvceQAEYHLFQREKVEVqLPELY-HKIGVGAMtwSPLAcgiitgkyeNGIPDSSRASMKSYQWLkekivsedgRK 323
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLAAeAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADY---------AR 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 324 QQAKLKELGhiaeklGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19095 208 RPEFAAEIG------GATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
79-378 |
6.52e-32 |
|
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor.
Pssm-ID: 381370 [Multi-domain] Cd Length: 323 Bit Score: 123.32 E-value: 6.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 79 RNLGKSGLRVSCLGLGTW---VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKKGWRRSSLVIT 155
Cdd:cd19144 4 RTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKlyWGGKAETERGL-----SRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWT 230
Cdd:cd19144 82 TK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 231 AMEIMEAYSVArqfnliPPVCEQAEYHLF--QREKVEVQLPELYHKIGVGAMTWSPLACGIITGKY---ENGIPDSSRAS 305
Cdd:cd19144 160 AETLRRAHAVH------PIAAVQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIrspDDFEEGDFRRM 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207134339 306 MKSYQwlkekivSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19144 234 APRFQ-------AENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV 299
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
79-378 |
7.48e-32 |
|
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381371 [Multi-domain] Cd Length: 304 Bit Score: 122.54 E-value: 7.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 79 RNLGKSGLRVSCLGLGTW---VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSSLVIT 155
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 156 TKL---YWGGKAETERGlSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAM 232
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 233 EIMEAYSVArqfnliPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIITGK---YENGIPDSSRASMKSY 309
Cdd:cd19145 160 TIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKaklEELLENSDVRKSHPRF 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 310 QwlkekivSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCL-RNEGVSSVlLGTSNAEQLTENLGAIQV 378
Cdd:cd19145 233 Q-------GENLEKNKVLYERVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV 294
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
84-378 |
1.06e-31 |
|
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: 121.20 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWvtFGGQISDDVAEQLMTI--AYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTKLYwg 161
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 162 gkaetERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPdSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVA 241
Cdd:cd19138 80 -----PSNASRQGTVRACERSLRRLGTDYLDLYLLHWR-GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 242 RQFNLippVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmksyqwlkekivsEDG 321
Cdd:cd19138 154 GGGNC---AANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG------------------------------GLL 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 322 RKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVlLGTSNAEQLTENLGAIQV 378
Cdd:cd19138 200 RRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL 255
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
85-369 |
5.31e-31 |
|
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: 120.10 E-value: 5.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVT----FGGQisdDVAEQLMTI--AYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSSLVITTK- 157
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGGT---DEKEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 -LYWGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAmEIME 236
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AY-SVARQFNLIPPvceqaeYHLFQREKVEVQLPE-LYHKIGVgaMTWSPLACGIITGKYEngiPDSsrasmksyqwlke 314
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPYaRKHNIVT--LAYGALCRGLLSGKMT---KDT------------- 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 315 KIVSEDGRKQQAKLKE------------LGHIA-EKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQL 369
Cdd:cd19148 212 KFEGDDLRRTDPKFQEprfsqylaaveeLDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
78-377 |
8.10e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 120.06 E-value: 8.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLG------TWVTfggqisDDVAEQLMTI--AYESGVNLFDTAEVYAAGKAEVILGNIIKKKgwrR 149
Cdd:cd19104 2 YRRFGRTGLKVSELTFGgggiggLMGR------TTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 150 SSLVITTKlywGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFA-NRPDSNTP--------------MEEIVRAMTY 214
Cdd:cd19104 73 AGPYITTK---VRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDkpvggtlsttdvlgLGGVADAFER 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 215 VINQGMSMYWGTSRW----TAMEIME--AYSVARQF-NLI--------PPVCEQAEYHlfqrekvevQLPELYHKIGVGA 279
Cdd:cd19104 150 LRSEGKIRFIGITGLgnppAIRELLDsgKFDAVQVYyNLLnpsaaearPRGWSAQDYG---------GIIDAAAEHGVGV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 280 MTWSPLACGIITGKYENGIPDSSRAsmksyqwlkEKIVSEDGRkQQAKLKELghiAEKLGCTLPQLAVAWCLRNEGVSSV 359
Cdd:cd19104 221 MGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFR-RAAAFRAL---AREWGETLAQLAHRFALSNPGVSTV 287
|
330
....*....|....*...
gi 1207134339 360 LLGTSNAEQLTENLGAIQ 377
Cdd:cd19104 288 LVGVKNREELEEAVAAEA 305
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
91-377 |
1.90e-30 |
|
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH) and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose and, to a much lesser degree, D-arabinose. The family also includes L-galactose dehydrogenase (L-galDH) and D-arabinose 1-dehydrogenase (ARA2). L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381316 [Multi-domain] Cd Length: 278 Bit Score: 118.04 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGT-WVTFG-GQISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIkkKGWRRSSLVITTKLywGGKAETER 168
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 169 GLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEE-----IVRAMTYVINQGMSMYWGTSRWTAmEIMEAYSVARQ 243
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDIlapggALEALLELKEEGLIKHIGLGGGPP-DLLRRAIETGD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 244 FNLIPPVCeqaEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIITGKYENGIPDssrasmkSYQWLkekivsedGRK 323
Cdd:cd19090 156 FDVVLTAN---RYTLLDQSAADELLPAAARH-GVGVINASPLGMGLLAGRPPERVRY-------TYRWL--------SPE 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 324 QQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19090 217 LLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
84-375 |
2.06e-30 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 117.46 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGK 163
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 AeterglSRKHIIEGLKGSLQRMQMEYVDVVFANRPdSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARq 243
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWP-GPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 244 fnlIPPVCEQAEYHLFQREkvevqlPEL--YHK-IGVGAMTWSPLACGIItgkyengipdssrasmksyqwLKEKIVSEd 320
Cdd:COG0656 144 ---VKPAVNQVELHPYLQQ------RELlaFCReHGIVVEAYSPLGRGKL---------------------LDDPVLAE- 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 321 grkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVsSVLLGTSNAEQLTENLGA 375
Cdd:COG0656 193 -------------IAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
84-378 |
1.34e-28 |
|
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: 113.87 E-value: 1.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLG----TWVtfGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEV---ILGNIIKKKGWRRSSLVITT 156
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 157 KlywGGKAET--ERGLSRKHIIEGLKGSLQRMQM-EYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAME 233
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALGGtKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 234 IMEAYSVArqfnliPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKYEN--GIPDS-SRASMKSYQ 310
Cdd:cd19077 156 IRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSlaDIPEGdFRRHLDRFN 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 311 wlkekivSEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSV-LLGTSNAEQLTENLGAIQV 378
Cdd:cd19077 230 -------GENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV 291
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
76-376 |
6.17e-27 |
|
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Pssm-ID: 381389 [Multi-domain] Cd Length: 293 Bit Score: 108.79 E-value: 6.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTwVTFGGQISD-DVAEQLMTI--AYESGVNLFDTAEVYAAGKAEVILGNIIkkKGWRRSSL 152
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGGVFGPvDEEEAIRTVheALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 153 VITTKL--YwGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVV------FAnrPDSNTPMEEIVRAMTYVINQGMSMYW 224
Cdd:cd19163 78 YLATKVgrY-GLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 225 GTSRWtAMEIMeAYSVARQFNLIPPVCEQAEYHLFQREKVEvqLPELYHKIGVGAMTWSPLACGIITgkyENGIPDSSRA 304
Cdd:cd19163 155 GITGY-PLDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERGPPDWHPA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 305 SmksyQWLKEKIvsedgrkqqaklKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAI 376
Cdd:cd19163 228 S----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
91-375 |
4.89e-26 |
|
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: 105.05 E-value: 4.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLYWGGkaetergL 170
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 SRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPV 250
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 251 CEQAEYH--LFQREKVEVQLPelyHKIGVGAmtWSPLAcgiitgkyengipdssrasmksyqwlkekivsedgRKQQAKL 328
Cdd:cd19073 145 VNQVEFHpfLYQAELLEYCRE---NDIVITA--YSPLA-----------------------------------RGEVLRD 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1207134339 329 KELGHIAEKLGCTLPQLAVAWCLRnEGVsSVLLGTSNAEQLTENLGA 375
Cdd:cd19073 185 PVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
88-375 |
2.80e-25 |
|
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: 103.45 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 88 VSCLGLGTW-----VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgwRRSSLVITTKLYW-- 160
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGGLvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 GGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSV 240
Cdd:cd19088 78 TGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 241 ARqfnlIppVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLAcgiitgkyengipdssrasmksyqwlkekivSED 320
Cdd:cd19088 158 VR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG-------------------------------GGD 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 321 GRKQQAKLKELghiAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19088 199 LAQPGGLLAEV---AARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
85-381 |
1.31e-24 |
|
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: 103.27 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGT------WVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSSLVITTKL 158
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 ---YWGGKAETER----GLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTA 231
Cdd:cd19146 87 ttgYRRGGPIKIKsnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAYSVARQFNLIPPVCEQAEYHL----FQREKVEVQLPElyhkiGVGAMTWSPLAcgiiTGKYENGIPDSSRASMK 307
Cdd:cd19146 167 WVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSG 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 308 SYQWLKekivSEDGRKQQAKLKElghIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19146 238 RKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLS 304
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
91-373 |
2.63e-23 |
|
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: 97.94 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGgkaeteRGL 170
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WP------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 SRKHIIEGLKGSLQRMQMEYVDVV-----FANRP-DSNTPMEEIVRAMtyvinqgMSMYW-------GTSRWTAMEIMEA 237
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYlihwpVPGKEgGSKEARLETWRAL-------EELVDeglvrsiGVSNFNVEHLEEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 238 YSVARqfnlIPPVCEQAEYHLF--QREKVEvqlpelY-HKIGVGAMTWSPLACGiitgkyengipdssrasmkSYQWLKE 314
Cdd:cd19071 142 LAAAR----IKPAVNQIELHPYlqQKELVE------FcKEHGIVVQAYSPLGRG-------------------RRPLLDD 192
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 315 KIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVsSVLLGTSNAEQLTENL 373
Cdd:cd19071 193 PVLKE--------------IAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-377 |
4.98e-23 |
|
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: 97.60 E-value: 4.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTwVTFG---------GQISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKKgwrrSSLVITTKLywg 161
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 162 GKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRP-DSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSv 240
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 241 ARQFNLIppvceQAEYHLF-QREKVEVQLPELyHKIGVGAMTWSPLACGIITGKYENgIPDssrasmKSYQWLKekivse 319
Cdd:cd19097 152 SFKIDII-----QLPFNILdQRFLKSGLLAKL-KKKGIEIHARSVFLQGLLLMEPDK-LPA------KFAPAKP------ 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 320 dgrkqqaKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQ 377
Cdd:cd19097 213 -------LLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
76-373 |
7.30e-23 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 98.74 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 76 MAYRNLGKSGLRVSCLGLGTWvtfGGQISD-DVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKkgwRRSSLVI 154
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 155 TTKLYWGGKaeterglSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVR---AMTYV---INQGMSMYWGTS- 227
Cdd:COG1453 73 ATKLPPWVR-------DPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEKVLKpggALEALekaKAEGKIRHIGFSt 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 228 ---RWTAMEIMEAY---SVARQFNLippvceqaeyhLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITgkyengipds 301
Cdd:COG1453 146 hgsLEVIKEAIDTGdfdFVQLQYNY-----------LDQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA---------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 302 srasmksyqwlkekivsedgrkqqAKLKELGHIAEKlGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENL 373
Cdd:COG1453 205 ------------------------NPPEKLVELLCP-PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
85-373 |
4.70e-22 |
|
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: 94.25 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaAGKAEVilGNIIKKKGWRRSSLVITTKLYWGgka 164
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY-GNEAQV--GEAIAASGVPRDELFLTTKVWPD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 eterGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqf 244
Cdd:cd19140 74 ----NYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 245 nlIPPVCEQAEYH--LFQRekvevQLPELYHKIGVGAMTWSPLAcgiitgkyengipdssrasmksyqwlkekivsedgR 322
Cdd:cd19140 148 --APLFTNQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLA-----------------------------------R 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 323 KQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVsSVLLGTSNAEQLTENL 373
Cdd:cd19140 186 GEVLKDPVLQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
78-195 |
1.81e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 92.55 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTWVTfgGQISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKkgwRRSSLVITTK 157
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207134339 158 LYWGGKAETERGLSRkhiieglkgSLQRMQMEYVDVVF 195
Cdd:cd19100 74 TGARDYEGAKRDLER---------SLKRLGTDYIDLYQ 102
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
91-375 |
2.96e-21 |
|
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: 92.81 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTwVTFG--GQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKkkGWRRSSLVITTKL-------YWG 161
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 162 GKAETER--GLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDS--NTPMEEIVRAMTYVINQGM--SMYWGTSRWTAmeim 235
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWAA---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 236 eAYSVARQFNLiPPVCEQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIITGkyengipDSSRASMKSYQWLKEK 315
Cdd:cd19162 156 -LLRAARRADV-DVVMVAGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT-------DDPAGDRYDYRPATPE 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 316 IVsedgrkqqAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19162 226 VL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
79-381 |
1.46e-20 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 91.06 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 79 RNLGKSGLRVSCLGLGTwVTFGGQISD----DVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVI 154
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDgleqDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 155 TTKLYWGGKAETErgLSRKHIIEGLKGSLQRMQMEYVDVVFANR---PDSNTPMEEIVRAMTYVINQGMSMYWGTSRWtA 231
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEaySVARQFNLIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIITgkyENGIPDSSRASmksyq 310
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLT---SQGPPPWHPAS----- 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 311 wlkekivsedGRKQQAKLKELGHIAEKlGCTLPQLAVAWCLRNE-GVSSVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19153 229 ----------GELRHYAAAADAVCASV-EASLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVAS 289
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
78-375 |
1.66e-20 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 91.38 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 78 YRNLGKSGLRVSCLGLGTwVTFG---GQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGWRRSSLVI 154
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 155 TTKLywgGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANR---PDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTa 231
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITGLP- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEaYSVARqfnlIPP-----VCEQAEYHLFQREKVEVqLPELYHKiGVGAMTWSPLACGIITgkyENGIPDSSRASM 306
Cdd:PLN02587 156 LAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPP 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 307 KsyqwLKEKIvsedgRKQQAKLKELGHiaeklgcTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:PLN02587 226 E----LKSAC-----AAAATHCKEKGK-------NISKLALQYSLSNKDISTTLVGMNSVQQVEENVAA 278
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
89-375 |
1.87e-20 |
|
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: 89.93 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTW---VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgWRRSSLVITTKLYWGgkae 165
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 166 teRGLSRKHIIEGLKGSLQRMQMEYVDvVFA----NRPD------SNTPMEEIVRAMT--YVINQGMSmYWGTSRwTAME 233
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKKegLIRHIGFS-FHDSPE-LLKE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 234 IMEAYSVArqFNLIPpvceqaeYHLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIItgkyengipdssrasmksyqwl 312
Cdd:cd19096 150 ILDSYDFD--FVQLQ-------YNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGL---------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207134339 313 kekivsedGRKQQAKLKELghiaEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19096 199 --------ANNPPEALAIL----CGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
86-373 |
9.68e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 89.30 E-value: 9.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 86 LRVSCLGLGTWVtfGGQISDDVAEQLMTIAY--ESGVNLFDTAEVYAAGKAEVILGN----IIKKKGWRRSSLVITTKly 159
Cdd:cd19099 1 LTLSSLGLGTYR--GDSDDETDEEYREALKAalDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 wGG----------------KAETERGLSRKHIIEG-------------LKGSLQRMQMEYVDVVFANRP-------DSNT 203
Cdd:cd19099 77 -AGyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelGEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 204 PMEEIVRAMTYV---INQGMSMYWGTSRWTAmeiMEAYSVARQFNLIPPVCEQAE-----YHLFqreKVeVQLPelYHKI 275
Cdd:cd19099 156 FYDRLEEAFEALeeaVAEGKIRYYGISTWDG---FRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP--LNLL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 276 GVGAMT----WSPLACGIITGKYENGIPDSSRASMKSYQWLKEkivsedgrkqqakLKELGHIAEKLGCTLPQLAVAWCL 351
Cdd:cd19099 227 EPEALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGE-------------LRLADLLALPGGATLAQRALQFAR 293
|
330 340
....*....|....*....|..
gi 1207134339 352 RNEGVSSVLLGTSNAEQLTENL 373
Cdd:cd19099 294 STPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
93-351 |
1.70e-19 |
|
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: 88.16 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 93 LGTW----------VTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKkgWRRSSLVITTKLYWGG 162
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 163 kaeteRGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPD---SNTPmEEIVRAMTYVINQgmsmyWGTSRWTAMEIMEAYS 239
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPAdveRWTP-ELIPLLKSGKVKH-----VGVSNHNLAEIKRANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 240 VARQFNL-IPPVceQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIITGKY--ENGIP-DSSRAsmKSYQWLKEK 315
Cdd:cd19103 156 ILAKAGVsLSAV--QNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYdtKHPLPeGSGRA--ETYNPLLPQ 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207134339 316 IvsedgRKQQAKLKELGhiaEKLGCTLPQLAVAWCL 351
Cdd:cd19103 232 L-----EELTAVMAEIG---AKHGASIAQVAIAWAI 259
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
87-375 |
3.01e-19 |
|
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: 87.65 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 87 RVSCLGLGTWVTFGG---QISDDVAEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKKGW---RRSSLVITTKLYW 160
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 GGKAETergLSRKHIIEGLKGSLQRMQMEYVDVV-FANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRW-TAM--EIME 236
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqFHWWDYSDPGYLDAAKHLAELQEEGKIRHLGLTNFdTERlrEILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AysvarqfnLIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIITGKY----ENGIPDSSRASMKSYQWL 312
Cdd:cd19101 156 A--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvpEPTGPALETRSLQKYKLM 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207134339 313 KEKIVSEDGrkQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGA 375
Cdd:cd19101 227 IDEWGGWDL--FQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
83-373 |
1.20e-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: 82.85 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 83 KSGLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKkgW------RRSSLVITT 156
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 157 KLYWGGkaetergLSRKHIIEGLKGSLQRMQMEYVDVVFANRP-------------------DSNTPMEEIVRAMTYVIN 217
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 218 QGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiitGKYENG 297
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------GSPGRA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 298 IPDSSRASMKSYQWLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVsSVLLGTSNAEQLTENL 373
Cdd:cd19154 217 NFTKSTGVSPAPNLLQDPIVKA--------------IAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
91-379 |
3.52e-17 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 81.50 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTwVTFGG---QISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwrRSSLVITTKLYWGGKAETE 167
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 168 RGLSRKHIIEGLKG------------------SLQRMQMEYVDVVFANRPDSNTP-----------MEEIVRAMTYVINQ 218
Cdd:cd19152 80 VEPTFEPGFWNPLPfdavfdysydgilrsiedSLQRLGLSRIDLLSIHDPDEDLAgaesdehfaqaIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 219 GMSMYW--GTSRWT-AMEIME-----AYSVARQFNLIppvcEQAEYHLFqrekvevqLPELyHKIGVGAMTWSPLACGII 290
Cdd:cd19152 160 GVIKAIglGVNDWEvILRILEeadldWVMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKVVNAGPFNSGFL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 291 TGkyengipdSSRASMKSYQwlkekivsEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLT 370
Cdd:cd19152 227 AG--------GDNFDYYEYG--------PAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVE 290
|
....*....
gi 1207134339 371 ENLGAIQVS 379
Cdd:cd19152 291 ENVALLATE 299
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
90-373 |
4.31e-17 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 80.64 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 90 CLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVY----AAGKAeviLGNIIKKKGWRRSSLVITTKLyWGGKAE 165
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 166 TERglsrkhIIEGLKGSLQRMQMEYVDVVFANRP-------------------DSNTPMEEIVRAMTYVINQGMSMYWGT 226
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafdmdtdgdprddnqiqsLSKKPLEDTWRAMEQCVDEKLTKNIGV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 227 SRWTAMEIMEAYSVARqfnlIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLacgiitgkyengipdssras 305
Cdd:cd19128 148 SNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPL-------------------- 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 306 MKSYqwlkekivsEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCL-RNEGVSSVLLGTSNAEQLTENL 373
Cdd:cd19128 200 GGSY---------GDGNLTFLNDSELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
85-373 |
8.71e-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: 79.54 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDD-VAEQLMTIAYESGVNLFDTAEVYAAGKAeviLGNIIKKKGWRRSSLVITTKLyWGGK 163
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDPeECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 AETERglsrkhIIEGLKGSLQRMQMEYVDVvfanrpdsntpmeeivramtYVINQGMSMYWGTsrWTAMEimEAYSVAR- 242
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDL--------------------YLIHQPFGDVYGA--WRAME--ELYKEGKi 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 243 -----------------QFNLIPPVCEQAEYHLFqREKVEVQlpELYHKIGVGAMTWSPLACGiitgkyENGIpdssras 305
Cdd:cd19133 127 raigvsnfypdrlvdliLHNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFAEG------RNNL------- 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 306 mksyqwLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWcLRNEGVsSVLLGTSNAEQLTENL 373
Cdd:cd19133 191 ------FENPVLTE--------------IAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
91-373 |
2.42e-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: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGKAETERGL 170
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 srkhiiEGLKGSLQRMQMEYVDVVFANRPdsnTPME----EIVRAMTYVINQGMSMYWGTSRWTA---MEIMEAYSVArq 243
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 244 fnlipPVCEQAEYH-LFQREkvevQLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmksyQWLKEKIvsedgr 322
Cdd:cd19131 153 -----PVVNQIELHpRFQQR----ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPV------ 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 323 kqqaklkeLGHIAEKLGCTLPQLAVAWCLRNEGVssVLLGTSNAEQLTENL 373
Cdd:cd19131 197 --------IGEIAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
92-375 |
9.40e-16 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 76.89 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 92 GLGTWV--TFGGQISDDVAEQLmTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLYWGGKaeterg 169
Cdd:cd19120 10 GTGTAWykSGDDDIQRDLVDSV-KLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 170 lsrkHIIEGLKGSLQRMQMEYVDVVFANRP----DSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqfn 245
Cdd:cd19120 80 ----DPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 246 lIPPVCEQAEYHLFqrekVEVQLPEL--YHKigvgamtwsplACGIITGKYengipdSSRASmksyqwlkekIVSEDGRK 323
Cdd:cd19120 153 -IKPAVNQIEFHPY----LYPQQPALleYCR-----------EHGIVVSAY------SPLSP----------LTRDAGGP 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 324 QQAKLKElghIAEKLGCTLPQLAVAWCLRNEGVssVLLGTSNAEQLTENLGA 375
Cdd:cd19120 201 LDPVLEK---IAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEA 247
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
91-373 |
2.32e-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: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAagkAEVILGNIIKKKGWRRSSLVITTKLywggkAETERGL 170
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 SRKhiIEGLKGSLQRMQMEYVDVVFANRPDSNT-PMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVArqfnLIPP 249
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 250 VCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmksyqwlkekivsedgrkQQAK 327
Cdd:cd19134 155 AVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG-----------------------------------RLLD 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1207134339 328 LKELGHIAEKLGCTLPQLAVAWCLRNEGVssVLLGTSNAEQLTENL 373
Cdd:cd19134 195 NPAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
91-379 |
2.75e-15 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 75.91 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWVTFGGQISDDVAEqlmtiAYESGVNLFDTAEVYAaGKAEV--ILGNIIKKKGWRRSSLVITTKLyWGGKAETEr 168
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 169 glsrkHIIEGLKGSLQRMQMEYVD-------VVF---ANRPDSNT--------PMEEIVRAMTYVINQGMSMYWGTSRWT 230
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 231 AMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiitgkyenGIPDSSRAsMKSYq 310
Cdd:cd19123 162 VKKLEDLLATAR----IKPAVNQVELHPYLQQP---ELLAFCRDNGIHLTAYSPL-----------GSGDRPAA-MKAE- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 311 wlKEKIVSEDgrkqqaklKELGHIAEKLGCTLPQLAVAWCL-RNegvSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19123 222 --GEPVLLED--------PVINKIAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEVE 278
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
89-379 |
6.73e-15 |
|
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: 75.05 E-value: 6.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 89 SCLGLGTwVTFGG---QISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwrRSSLVITTKLywgGK-- 163
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 --AETERGL-----------------SRKHIIEGLKGSLQRMQMEYVDVVF---------ANRPDSN---TPMEEIVRAM 212
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 213 TYVINQG-MSMY-WGTSRWTAM-EIMEAYSVarQFNLIppvceQAEYHLFQREKVEVQLPELyHKIGVGAmtwsplacgI 289
Cdd:cd19161 155 EELKKAGvIKAFgLGVNEVQIClEALDEADL--DCFLL-----AGRYSLLDQSAEEEFLPRC-EQRGTSL---------V 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 290 ITGKYENGIPDSSRASMKSYQWLkekivsEDGRKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQL 369
Cdd:cd19161 218 IGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQL 291
|
330
....*....|
gi 1207134339 370 TENLGAIQVS 379
Cdd:cd19161 292 RQNVEAFQTD 301
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
84-379 |
7.35e-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: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLG------TWVTFGGQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAEVILGNIIKKKGwRRSSLVITTK 157
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 LYW--------GGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMTYVINQGMSMYWGTSRW 229
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 230 TAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLAcgiiTGKYEngipdsSRASMKSY 309
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGKFQ------SKKAVEER 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 310 QWLKEKIVSEDGRKQQAKLKE-----LGHIAEKLGC-TLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19147 234 KKNGEGLRSFVGGTEQTPEEVkiseaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIK 309
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
83-373 |
1.16e-14 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 73.92 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 83 KSGLRVSCLGLGTWVTFGGQISDDVAEqlmtiAYESGVNLFDTAEVYAAGKaEV--ILGNIIKKKGWRRSSLVITTKLyW 160
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKT-----AIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 GGKAETERglsrkhIIEGLKGSLQRMQMEYVDVV-----FANRPDSNTP---------MEEIVRAMTYVINQGMSMYWGT 226
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVRLKKGAHMPepeevlppdIPSTWKAMEKLVDSGKVRAIGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 227 SRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiitgkyengipdSSRASM 306
Cdd:cd19125 153 SNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPLG--------------SPGTTW 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 307 KSYQWLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRnEGvSSVLLGTSNAEQLTENL 373
Cdd:cd19125 212 VKKNVLKDPIVTK--------------VAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
91-373 |
1.79e-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: 73.47 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfgGQISDDVAEQLMTIAYESGVNLFDTAEVY----AAGKAeviLGNIIKKKGWRRSSLVITTKLyWGGKAEt 166
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYgneaEVGEA---IREKIAEGVVKREDLFITTKL-WNSYHE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 167 erglsRKHIIEGLKGSLQRMQMEYVDVVFANRP-------DSNTPME---------EIVRAMTYVINQGMSMYWGTSRWT 230
Cdd:cd19116 85 -----REQVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 231 AMEIMEAYSVARqfnlIPPVCEQAEYHL-FQREKvevqLPELYHKIGVGAMTWSPLacgiitgkyenGIPDSSRasmksy 309
Cdd:cd19116 160 SEQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF-----------GRLVPRG------ 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 310 QWLKEKivsedgRKQQAKLKElghIAEKLGCTLPQLAVAWcLRNEGVsSVLLGTSNAEQLTENL 373
Cdd:cd19116 215 QTNPPP------RLDDPTLVA---IAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
84-372 |
1.82e-14 |
|
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: 72.74 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWvTFGGQISDDVAEQLMtiayESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGK 163
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 AETERglsrkhIIEGLKGSLQRMQMEYVDVVFANRPDSNTP-------MEEIVRAMTYVINQGMSMYWGTSRWTAMEIME 236
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AYSVARqfnlIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmksyQWLKEKI 316
Cdd:cd19135 154 LLEDCS----VVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLAKG---------------------KALEEPT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207134339 317 VSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVSSVLLGTSnAEQLTEN 372
Cdd:cd19135 206 VTE--------------LAKKYQKTPAQILIRWSIQN-GVVTIPKSTK-EERIKEN 245
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
85-385 |
3.20e-14 |
|
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: 72.53 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKkgW------RRSSLVITTKL 158
Cdd:cd19111 1 GFPMPVIGLGTY-----QSPPEEVRAAVDYALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 YwggkaetERGLSRKHIIEGLKGSLQRMQMEYVDVVFAN-------------RPDSNTPMEEIVRAMTYVINQGMSMYWG 225
Cdd:cd19111 71 P-------PVYLEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 226 TSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLF--QREKVEVQLPelyHKIGVGAmtWSPL-ACGIITGKYENGIPDSs 302
Cdd:cd19111 144 LSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPLgSPGRANQSLWPDQPDL- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 303 rasmksyqwLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCL-RNEGvssVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19111 214 ---------LEDPTVLA--------------IAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDFELT 267
|
....
gi 1207134339 382 FCHV 385
Cdd:cd19111 268 EEHF 271
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
91-378 |
4.11e-14 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 71.62 E-value: 4.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLYWggkaeteRGL 170
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 SRKHIIEGLKGSLQRMQMEYVDVVFAN--RPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARQFNLIP 248
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHwpSPNDEVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 249 PVCEQAEYhlFQREKVEVQLpelyhkigvgamtwsplacgiitgkYENGIPdssrasMKSYQWLKEKIVSEDgrkqqakl 328
Cdd:cd19139 149 NQIELSPY--LQNRKLVAHC-------------------------KQHGIH------VTSYMTLAYGKVLDD-------- 187
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1207134339 329 KELGHIAEKLGCTLPQLAVAWCLrNEGVsSVLLGTSNAEQLTENLGAIQV 378
Cdd:cd19139 188 PVLAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL 235
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
85-290 |
2.72e-13 |
|
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: 69.39 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTfggqISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGKA 164
Cdd:cd19126 6 GTRMPWLGLGVFQT----PDGDETERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 ETERGLSrkhiieGLKGSLQRMQMEYVDVVFANRP------DSNTPMEEI-----VRAMtyvinqgmsmywGTSRWTAME 233
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPgkdkfiDTWKALEKLyasgkVKAI------------GVSNFQEHH 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207134339 234 IMEAYSVARqfnlIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACGII 290
Cdd:cd19126 140 LEELLAHAD----VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
83-373 |
5.93e-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: 68.84 E-value: 5.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 83 KSGLRVSCLGLGTwvtFGGQISDDVAE----QLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKK--KGWRRSSLVITT 156
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 157 KLywGGKAETERGLSRKHIIEGLKGSLQRMQMEYVDVV------FANRPDSNTPMEEIV--RAMTYVINQGMSMYwgtsr 228
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVylhdveFVADEEVLEALKELFklKDEGKIRNVGISGY----- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 229 wtAMEIMEAYSVARQFNLIPPVCEQAEY--HLFQREKVEVQLPELYHKIGVGA-MTWSPLACGIITgkyENGIPDSSRAS 305
Cdd:cd19164 158 --PLPVLLRLAELARTTAGRPLDAVLSYchYTLQNTTLLAYIPKFLAAAGVKVvLNASPLSMGLLR---SQGPPEWHPAS 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 306 mksyqwlkekivseDGRKQQAklKELGHIAEKLGCTLPQLAVAWCLR-NEGVSSVLLGTSNAEQLTENL 373
Cdd:cd19164 233 --------------PELRAAA--AKAAEYCQAKGTDLADVALRYALReWGGEGPTVVGCSNVDELEEAV 285
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
91-373 |
6.51e-13 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 68.43 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISD-DVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIK----KKGWRRSSLVITTKL--YWGGK 163
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapKDQGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 AETErglsrkhiiEGLKGSLQRMQMEYVDVVFANRP-----DSNTPMEEIVR-----AMTYVINQGMSMYWGTSRWTA-- 231
Cdd:cd19136 76 EKAR---------AACLGSLERLGTDYLDLYLIHWPgvqglKPSDPRNAELRreswrALEDLYKEGKLRAIGVSNYTVrh 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 MEIMEAYSvarqfnLIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiitgkyengipdssrasmkSY 309
Cdd:cd19136 147 LEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DL 196
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 310 QWLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVsSVLLGTSNAEQLTENL 373
Cdd:cd19136 197 RLLEDPTVLA--------------IAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
85-373 |
1.56e-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: 67.94 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKAeviLGNIIKKkgW------RRSSLVITTKL 158
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 YWGGkaeterglSRKHIIEG-LKGSLQRMQMEYVDVVFANRP---------------------DSNTPMEEIVRAMTYVI 216
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 217 NQGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLACGIITgKYEN 296
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSPGAA-HFSP 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 297 GIPDSSRASMKSYQwlkekivsedgrkqqakLKELGHIAEKLGCTLPQLAVAWCLrNEGVsSVLLGTSNAEQLTENL 373
Cdd:cd19155 223 GTGSPSGSSPDLLQ-----------------DPVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
84-373 |
2.44e-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: 66.91 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTFGGqiSDDVAEQLMTiAYESGVNLFDTAEVY----AAGKA--EVILGNIIKKkgwrRSSLVITTK 157
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS--PEDIKAAVLE-AIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 LyWGGKAEterglsRKHIIEGLKGSLQRMQMEYVDVVFANRPDSNTP----------------MEEIVRAMTYVINQGMS 221
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLYLIHWPVSLKPgkfsfpieeedflpfdIKGVWEAMEECQRLGLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 222 MYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYH-LFQREKvevqLPELYHKIGVGAMTWSPLACGiitgkyenGIPD 300
Cdd:cd19124 147 KAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGAP--------GTKW 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207134339 301 SSRASMKSyqwlkekivsedgrkqqAKLKElghIAEKLGCTLPQLAVAWcLRNEGVsSVLLGTSNAEQLTENL 373
Cdd:cd19124 211 GSNAVMES-----------------DVLKE---IAAAKGKTVAQVSLRW-VYEQGV-SLVVKSFNKERMKQNL 261
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
85-381 |
1.33e-11 |
|
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: 64.21 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAAgkaEVILGNIIKKKGWRRSSLVITTKLywggka 164
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 eteRGlsRKH----IIEGLKGSLQRMQMEYVDVVFANRPD-SNTPMEEIVRAMTYVINQGMSMYWGTSRWTAM---EIME 236
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNpSRDLYVEAWQALIEAREEGLVRSIGVSNFLPEhldRLID 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 237 AYSVArqfnlipPVCEQAEYH-LFQREKVEVqlpelYHK-IGVGAMTWSPLACGiitgkyengipdssrasmksyqwlke 314
Cdd:cd19132 145 ETGVT-------PAVNQIELHpYFPQAEQRA-----YHReHGIVTQSWSPLGRG-------------------------- 186
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 315 kivseDGRKQQAKLKElghIAEKLGCTLPQLAVAWCLRnEGVsSVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19132 187 -----SGLLDEPVIKA---IAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENLAIFDFELS 243
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
91-375 |
1.93e-11 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 63.89 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAaGKAEVilGNIIKKKGWRRSSLVITTKLyWggkaeTERgL 170
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 SRKHIIEGLKGSLQRMQMEYVDVVFAN--RPDSNTPMEEIVRAMTYVINQGMSMYWGTSRWT------AMEIMEAYSVAR 242
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHwpSPNDEVSVEEFMQALLEAKKQGLTREIGISNFTialmkqAIAAVGAENIAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 243 QfnlippvceQAEYH-LFQREKVEVQLPElyHKIGVGA-MTwspLACGiitgkyengipdssrasmksyQWLKEKIvsed 320
Cdd:PRK11172 151 N---------QIELSpYLQNRKVVAFAKE--HGIHVTSyMT---LAYG---------------------KVLKDPV---- 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207134339 321 grkqqaklkeLGHIAEKLGCTLPQLAVAWCLRnEGvSSVLLGTSNAEQLTENLGA 375
Cdd:PRK11172 192 ----------IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
91-288 |
8.53e-11 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 62.01 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGKaetergl 170
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 171 sRKHIIEGLKGSLQRMQMEYVDVVFANRPDSntPMEEIVRAMTYVIN---QGMSMYWGTSRWTA---MEIMEAYSVArqf 244
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT--- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207134339 245 nlipPVCEQAEYH-LFQREkvEVQLPELYHKIGVGAmtWSPLACG 288
Cdd:PRK11565 156 ----PVINQIELHpLMQQR--QLHAWNATHKIQTES--WSPLAQG 192
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
84-349 |
1.18e-10 |
|
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: 62.02 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTFGGQIsddvaEQLMTIAYESGVNLFDTAEVYaAGKAEVilGNIIKK-----KGWRRSSLVITTKL 158
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVY-GNEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 yWGGKAETErglsrkHIIEGLKGSLQRMQMEYVDV--------------VFANRPD-----SNTPMEEIVRAMTYVINQG 219
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLylihwpyafergdnPFPKNPDgtiryDSTHYKETWKAMEKLVDKG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 220 MSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiitgkyenGIP 299
Cdd:cd19106 148 LVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP 209
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207134339 300 DssRAsmksyqWLK--EKIVSEDgrkqqAKLKElghIAEKLGCTLPQLAVAW 349
Cdd:cd19106 210 D--RP------WAKpdEPVLLEE-----PKVKA---LAKKYNKSPAQILLRW 245
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
85-372 |
2.02e-10 |
|
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: 60.99 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISD-DVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGK 163
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 AETERGLSrkhiieGLKGSLQRMQMEYVDVVFANRP------DSNTPMEEI-----VRAMtyvinqgmsmywGTSRWTAM 232
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWPvkgkfkDTWKAFEKLykekkVRAI------------GVSNFHEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 233 EIMEAYSVARqfnlIPPVCEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACGiitgkyengipdssrasmksyqw 311
Cdd:cd19156 139 HLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG----------------------- 187
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 312 lkeKIVSEdgrkqqaklKELGHIAEKLGCTLPQLAVAWCLRNEGVssVLLGTSNAEQLTEN 372
Cdd:cd19156 188 ---KLLSN---------PVLKAIGKKYGKSAAQVIIRWDIQHGII--TIPKSVHEERIQEN 234
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
84-373 |
3.68e-10 |
|
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: 60.58 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTFGGQISDDVAEqlmtiAYESGVNLFDTAEVYaagKAEVILGNIIK---KKGW-RRSSLVITTKLY 159
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKELILN-----AIKIGYRHFDCAADY---KNEKEVGEALAeafKTGLvKREDLFITTKLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 160 wggkaETERGlsrkHIIEGLKGSLQRMQMEYVDVVFANRP-----------------------DSNTPMEEIVRAMTYVI 216
Cdd:cd19112 79 -----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 217 NQGMSMYWGTSRWTA--MEIMEAYSvarqfnLIPPVCEQAEYH-LFQREKVeVQLPeLYHKIGVGAMTwsPLACGiitgk 293
Cdd:cd19112 150 SAGLVRSIGISNYDIflTRDCLAYS------KIKPAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGA----- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 294 yengipdssrasMKSYQWLKEKIVSEDgrkqqAKLKElghIAEKLGCTLPQLAVAWCL-RNegvSSVLLGTSNAEQLTEN 372
Cdd:cd19112 215 ------------AANAEWFGSVSPLDD-----PVLKD---LAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKEN 271
|
.
gi 1207134339 373 L 373
Cdd:cd19112 272 I 272
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
85-373 |
6.10e-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: 59.73 E-value: 6.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTFGGQISDDVAEqlmtiAYESGVNLFDTAEVYAaGKAEVilGNIIKKKGWRRSSLVITTKLYWG--G 162
Cdd:cd19127 6 GVEMPALGLGVFQTPPEETADAVAT-----ALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 163 KAETERGLSRkhiieglkgSLQRMQMEYVDVVFANRPdsnTPME-----EIVRAMTYVINQGMSMYWGTSRWTA---MEI 234
Cdd:cd19127 78 YDKALRGFDA---------SLRRLGLDYVDLYLLHWP---VPNDfdrtiQAYKALEKLLAEGRVRAIGVSNFTPehlERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 235 MEAYSVarqfnlIPPVcEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcGIITgkYENGIPDSSRASMKSYqwlke 314
Cdd:cd19127 146 IDATTV------VPAV-NQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVMR--YGASGPTGPGDVLQDP----- 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207134339 315 kIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRNeGVSSVLLGTsNAEQLTENL 373
Cdd:cd19127 208 -TITG--------------LAEKYGKTPAQIVLRWHLQN-GVSAIPKSV-HPERIAENI 249
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
84-379 |
7.66e-09 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 56.35 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYaAGKAEVilGNIIKKKGWRRSSLVITTKLyWGgk 163
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY-GNEEEV--GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 164 aeTErglsRKHIIEGLKGSLQRMQMEYVDVVFANRP-------DSNTPMEEIVRA--------------MTYVINQGMSM 222
Cdd:cd19117 79 --TW----HRRVEEALDQSLKKLGLDYVDLYLMHWPvpldpdgNDFLFKKDDGTKdhepdwdfiktwelMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 223 YWGTSRWTAMEIMEAysVARQFNLIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcgiitgkyengipdSS 302
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------------ST 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207134339 303 RASMksyqwLKEKIVSEdgrkqqaklkelghIAEKLGCTLPQLAVAWCLRnEGVsSVLLGTSNAEQLTENLGAIQVS 379
Cdd:cd19117 214 NAPL-----LKEPVIIK--------------IAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFTLS 269
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
85-288 |
9.98e-09 |
|
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: 55.86 E-value: 9.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTFGGQISDDVAEQLMTIAYESgvnlFDTAEVYaagKAEVILGNIIKKKGWRRSSLVITTKLyWGGKA 164
Cdd:cd19157 7 GVKMPWLGLGVFKVEEGSEVVNAVKTALKNGYRS----IDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 165 ETERGLsrkhiiEGLKGSLQRMQMEYVDVVFANRPdSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqf 244
Cdd:cd19157 79 GYDSTL------KAFEASLERLGLDYLDLYLIHWP-VKGKYKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE-- 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207134339 245 nlIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACG 288
Cdd:cd19157 150 --IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG 188
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
99-257 |
8.31e-08 |
|
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: 53.23 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 99 FGGQISDDVA-EQLMTIAYESGVNLFDTAEVY----AAGKAeviLGNIIKKKGWRRSSLVITTKLyWGGKAETERglsrk 173
Cdd:cd19129 11 FGTLIPDPSAtRNAVKAALEAGFRHFDCAERYrneaEVGEA---MQEVFKAGKIRREDLFVTTKL-WNTNHRPER----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 174 hIIEGLKGSLQRMQMEYVDVV-----FANRP---------------DSNTPMEEIVRAMTYVINQGMSMYWGTSRWTAME 233
Cdd:cd19129 82 -VKPAFEASLKRLQLDYLDLYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180
....*....|....*....|....
gi 1207134339 234 IMEAYSVARqfnlIPPVCEQAEYH 257
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESH 180
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
148-379 |
2.46e-07 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 51.85 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 148 RRSSLVITTKLyWGGKAETErglsrkHIIEGLKGSLQRMQMEYVDV------VFANRPDSNTPM---------------- 205
Cdd:cd19122 68 KREDLFICTKV-WNHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKlgpdgkyvilkdlten 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 206 -EEIVRAMTYVINQGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSP 284
Cdd:cd19122 141 pEPTWRAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 285 LACgiitgkyENGIPDSSrasmksyqwlkEKiVSEDgrkqqaklKELGHIAEKLGCTLPQLAVAWCLRNEGVssVLLGTS 364
Cdd:cd19122 214 LGS-------QNQVPSTG-----------ER-VSEN--------PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSS 264
|
250
....*....|....*
gi 1207134339 365 NAEQLTENLGAIQVS 379
Cdd:cd19122 265 TPSRIESNFKSIELS 279
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
84-379 |
3.74e-07 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 51.26 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTFGGQISDDVaeqlmTIAYESGVNLFDTAEVYaAGKAEVilGNIIKK-----KGWRRSSLVITTKL 158
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAV-----KIALKAGYRHLDLAKVY-QNQHEV--GQALKEllkeePGVKREDLFITSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 159 yWGGKAETErglsrkHIIEGLKGSLQRMQMEYVD-------VVFANRPDSNTPMEEIVRAMTYVINQGMSMywgTSRWTA 231
Cdd:cd19118 75 -WNNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKPTGDLNPLTAVPTNGGEVDLDLSVSL---VDTWKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 232 M-EIMEA----------YSVARQFNLIP-----PVCEQAEYH--LFQREKVEvqlpelYHK---IGVGAmtWSPLacgii 290
Cdd:cd19118 145 MvELKKTgkvksigvsnFSIDHLQAIIEetgvvPAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 291 tGKYENGIPdssrasmksyqwlkeKIVSEDGRKQqaklkelghIAEKLGCTLPQLAVAWCLRNeGVsSVLLGTSNAEQLT 370
Cdd:cd19118 212 -GNNLAGLP---------------LLVQHPEVKA---------IAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTPSRIR 264
|
....*....
gi 1207134339 371 ENLGAIQVS 379
Cdd:cd19118 265 SNFEQVELS 273
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
84-199 |
1.88e-06 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 49.07 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTFGGQISDDVAEqlmtiAYESGVNLFDTAEVYaAGKAEVILGniIKK---KGWRRSSLVITTKLYW 160
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY-QNEDEVGEG--IKEaiaGGVKREDLFVTTKLWS 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207134339 161 GGKAETERGLSRkhiieglkgSLQRMQMEYVDVVFANRP 199
Cdd:cd19121 80 TYHRRVELCLDR---------SLKSLGLDYVDLYLVHWP 109
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
84-232 |
1.24e-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: 46.72 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWVTfggqiSDDVAEQLMTIAY--ESGVNLFDTAEVYAA----GKAeviLGNIIKKKGWRRSSLVITTK 157
Cdd:cd19119 8 TGASIPALGLGTASP-----HEDRAEVKEAVEAaiKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 158 L---YWggkaeterglsrKHIIEGLKGSLQRMQMEYVDVVFANRP-----DSntpmEEIVRAMTYVINQGMSMYWGTSRW 229
Cdd:cd19119 80 VwptFY------------DEVERSLDESLKALGLDYVDLLLVHWPvcfekDS----DDSGKPFTPVNDDGKTRYAASGDH 143
|
...
gi 1207134339 230 TAM 232
Cdd:cd19119 144 ITT 146
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
85-263 |
4.78e-05 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 44.86 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAAgkaEVILGNIIKK---KGW-RRSSLVITTKLyW 160
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 161 GGKAeterglSRKHIIEGLKGSLQRMQMEYVDVVFANRPDS-------------------------NTPMEEIVRAMTYV 215
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207134339 216 INQGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYHLF-QREK 263
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 ... |
84-265 |
4.86e-05 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 44.74 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 84 SGLRVSCLGLGTWvtfggQISDDVAEQLMTIAYESGVNLFDTAEVYAAGKaEVILG--NIIKKKGWRRSSLVITTKLyWG 161
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 162 GKAEterglsRKHIIEGLKGSLQRMQMEYVDVVFANRPDS-------------------------NTPMEEIVRAMTYVI 216
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAfkfvpieekyppgfycgdgdnfvyeDVPILDTWKALEKLV 153
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170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 217 NQGMSMYWGTSRWTAMEIMEAYSVARqfnlIPPVCEQAEYH--LFQREKVE 265
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHHpyLQQPKLIE 200
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| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
108-381 |
6.33e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 44.64 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 108 AEQLMTIAYESGVNLFDTAEVYaaGKAEVILGNIIKKKGWRRSSLVITTKlyWG------GKAETERGLSRKHIIEGLKG 181
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadWQVDAAVHEVKDHSLARLLK 112
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 182 SLQRMQM---EYVDV-----------VFANrpdsntpmEEIVRAMTYVINQGMSMYWGTSRWT-------AMEImeAYSV 240
Cdd:cd19098 113 QWEETRSllgKHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EIDG 182
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170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 241 ARQFNlippvCEQAEYHLFQREKVEvQLpELYHKIGVGAMTWSPLACGIITGKyeNGIPdssrasmksyqwlkekivsed 320
Cdd:cd19098 183 ARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDR--NPSP--------------------- 232
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250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207134339 321 grKQQAKLKELGHIAEKLGCTLPQLAVAWCLRNEGVSSVLLGTSNAEQLTENLGAIQVSKS 381
Cdd:cd19098 233 --ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLD 291
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| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
91-259 |
5.21e-04 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 41.83 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 91 LGLGTWVTfgGQISDDVAEQLMTIAYESGVNLFDTAEVYaagKAEVILGNIIKKK----GWRRSSLVITTKLyWGGKAET 166
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 167 ErgLSRKhiieGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRamtyVINQGMSMYWGT---SRWTAME------IMEA 237
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVDLYLIHFPVALKPGEELFP----KDENGKLIFDTVdlcATWEAMEkckdagLAKS 157
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170 180 190
....*....|....*....|....*....|....
gi 1207134339 238 YSVA----RQFNLI---P-----PVCEQAEYHLF 259
Cdd:cd19108 158 IGVSnfnrRQLEMIlnkPglkykPVCNQVECHPY 191
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| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
85-233 |
1.92e-03 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 40.09 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207134339 85 GLRVSCLGLGTWVTFGGQISDDVAeqlmtIAYESGVNLFDTAEVYaAGKAEVILG--NIIKKKGWRRSSLVITTKLYwgg 162
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207134339 163 KAETERGLSRkhiiEGLKGSLQRMQMEYVDVVFANRPDSNTPMEEIVRAMtyviNQGMSMYWGTS---RWTAME 233
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPTGFKPGKELFPLD----ESGNVIPSDTTfldTWEAME 137
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