|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
89-382 |
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: 623.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWGGKAETERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIM 219
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEglkgslqrlqleyvdvvfanrpdsntpmeEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 220 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 299
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 300 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 379
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 815891055 380 NKP 382
Cdd:cd19159 321 NKP 323
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
90-370 |
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: 582.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 90 PHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITT 169
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 170 KLYWGGKAETERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIME 220
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEglkaslerlqleyvdivfanrpdpntpmeEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERI 300
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 301 VSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHV 370
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
87-382 |
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: 561.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 87 TGMPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLV 166
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKLYWGGKAETERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAME 217
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEglrgsldrlqleyvdivfanrsdpnspmeEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 218 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 297
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 298 ERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 377
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
....*
gi 815891055 378 LRNKP 382
Cdd:cd19160 321 LGNKP 325
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
91-378 |
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: 520.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK 170
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 LYWGGKAETERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 221
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEglkaslerlqleyvdivfanrpdpntpmeETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 222 YSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIV 301
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891055 302 SEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNIL 378
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
89-383 |
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: 515.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWGGKAETERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIM 219
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEglkaslerlqleyvdvvfanrpdpntpmeETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 220 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 299
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 300 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 379
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 815891055 380 NKPY 383
Cdd:cd19158 321 NKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
89-377 |
5.83e-156 |
|
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: 441.65 E-value: 5.83e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWGGKAE--TERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAME 217
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIvegtkaslkrlqldyvdlvfchrpdpatpIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 218 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLK 297
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 298 ERiVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNI 377
Cdd:cd19143 241 DR-KEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
89-382 |
7.11e-142 |
|
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: 406.46 E-value: 7.11e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWGGKAEtERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIM 219
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIEsvraslrrlqldyidiviihkadpmcpmeEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 220 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSR---ASLKCYQWL 296
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKlsfKSSKYKVGS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 297 KERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDN 376
Cdd:cd19142 240 DGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELER 319
|
....*.
gi 815891055 377 ILRNKP 382
Cdd:cd19142 320 ILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
98-360 |
3.13e-130 |
|
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: 375.78 E-value: 3.13e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKLYWGGKA 177
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 178 E-TERGLSRKHIIE-----------------------------EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 227
Cdd:cd19074 79 GpNDRGLSRKHIFEsihaslkrlqldyvdiyychrydpetpleETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 228 FNMIPPVCEQAEYHLFQREKVEvQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKcYQWLKERIVSEEGRK 307
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 815891055 308 QQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 360
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
89-382 |
3.15e-82 |
|
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: 253.95 E-value: 3.15e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWvTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSL 165
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKLYW-GGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSA 215
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIrraveaslrrlgtdyidlyqlhrpdpdtpIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 216 MEIMEAYSVARqfNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG--VPESSRASLkcy 293
Cdd:COG0667 158 EQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAAT--- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 294 qWLKERIVSEEGRKqqnKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNE 373
Cdd:COG0667 232 -NFVQGYLTERNLA---LVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
....*....
gi 815891055 374 IDNILRNKP 382
Cdd:COG0667 306 LDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
89-377 |
1.38e-73 |
|
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: 231.69 E-value: 1.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVIT 168
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWG-GKAETERGLSRKHII-----------------------------EEIVRAMTHVINQGMAMYWGTSRWSAMEI 218
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRraveaslrrlqtdyidlyqmhhfdrdtplEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 219 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNG-VPESSR-ASLKCYQwl 296
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGkRPESGRlVERARYQ-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 297 kERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDN 376
Cdd:cd19087 234 -ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDE 307
|
.
gi 815891055 377 I 377
Cdd:cd19087 308 L 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
89-362 |
9.05e-66 |
|
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: 211.70 E-value: 9.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkg 159
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 160 wRRSSLVITTKL-YWGGKAETERGLSRKHII-----------------------------EEIVRAMTHVINQGMAMYWG 209
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIraveaslkrlgtdyidlyqlhgfdaltplEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 210 TSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR 287
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 288 ASLKCYQWLkerIVSEEgrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 362
Cdd:cd19091 236 LRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL 305
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
98-375 |
2.03e-59 |
|
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: 194.67 E-value: 2.03e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTK--LY 172
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 WGGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAys 223
Cdd:cd19084 78 WDGGKGVTKDLSPESIrkeveqslrrlqtdyidlyqihwpdpntpIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 224 varqFNMIPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VPESSRASLKCYQwlkeri 300
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFPFFR------ 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 301 vSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 375
Cdd:cd19084 225 -GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
91-364 |
2.64e-55 |
|
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: 184.38 E-value: 2.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVY--AAGKAEVILGSIIKK-KGWRRSSLVI 167
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 168 TTKL-Y--WGGKaeTERGLSRKHII-----------------------------EEIVRAMTHVINQGMAMYWGTSRWSA 215
Cdd:cd19089 81 STKAgYgmWPGP--YGDGGSRKYLLasldqslkrmgldyvdifyhhrydpdtplEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 216 MEIMEAYSVARQFNmIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRAsLKCYQW 295
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891055 296 LKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 364
Cdd:cd19089 236 LTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
102-358 |
3.79e-55 |
|
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: 181.56 E-value: 3.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTWvTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL-YWGGKAETE 180
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 181 RGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMI 231
Cdd:cd06660 79 SRLSPEHIrrdleeslrrlgtdyidlyylhrddpstpVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 232 PPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqwlkerivseegrkqqnk 311
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG--------------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 815891055 312 lkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLG 358
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
94-375 |
6.72e-55 |
|
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: 183.18 E-value: 6.72e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 94 LGKSGLRVSCLGLGTWVtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwRRSSLV 166
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKLYWGgKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAME 217
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIrraveaslrrlqtdyidlyqahwddpatpLEETLGALNDLIRQGKVRYIGASNYSAWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 218 IMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKcyqw 295
Cdd:cd19081 159 LQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEA---- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 296 lKERIVSEEGRKQqnkLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 375
Cdd:cd19081 235 -AKRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
93-362 |
1.24e-51 |
|
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: 174.69 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 93 NLGKSGLRVSCLGLGTWvTFGGQ------ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLV 166
Cdd:cd19079 4 RLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKLYW-GGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAM 216
Cdd:cd19079 82 IATKVYFpMGDGPNGRGLSRKHImaevdaslkrlgtdyidlyqihrwdyetpIEETLEALHDVVKSGKVRYIGASSMYAW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 217 EIMEAYSVARQFNMIPPVCEQAEYHLFQREKvEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVP-ESSRASLKCYQW 295
Cdd:cd19079 162 QFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKY 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891055 296 LKErivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 362
Cdd:cd19079 241 DYF---TEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI 301
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
101-377 |
1.81e-49 |
|
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: 169.67 E-value: 1.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 101 VSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK--- 170
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKvag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 --LYWGGKAETERGLSRKHI-----------------------------------------------IEEIVRAMTHVIN 201
Cdd:cd19094 79 pgEGITWPRGGGTRLDRENIreavegslkrlgtdyidlyqlhwpdrytplfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 202 QGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--G 279
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYldG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 280 NGVPESSRASLkcYQWLKERIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19094 238 AARPEGGRLNL--FPGYMARYRSPQALEAVAEYVK---LARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDA 312
|
330
....*....|....*....
gi 815891055 360 IQV-LPKmtsHVVNEIDNI 377
Cdd:cd19094 313 FDVpLSD---ELLAEIDAV 328
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
91-361 |
1.02e-48 |
|
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: 167.19 E-value: 1.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 91 HRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKK--KGWRrSSLV 166
Cdd:cd19151 2 YNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKL--------Y--WGGK----AETERGLSRKHI----------------IEEIVRAMTHVINQGMAMYWGTSRWSAM 216
Cdd:cd19151 81 ISTKAgytmwpgpYgdWGSKkyliASLDQSLKRMGLdyvdifyhhrpdpetpLEETMGALDQIVRQGKALYVGISNYPPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 217 EIMEAYSVARQFNmIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlKCYQWL 296
Cdd:cd19151 161 EAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 297 KERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 361
Cdd:cd19151 238 KPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
90-363 |
9.84e-48 |
|
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: 164.55 E-value: 9.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 90 PHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSLV 166
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKL--------Y--WGGK----AETERGLSRKHI----------------IEEIVRAMTHVINQGMAMYWGTSRWSAM 216
Cdd:cd19150 81 ISTKAgydmwpgpYgeWGSRkyllASLDQSLKRMGLdyvdifyshrfdpdtpLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 217 EIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASlkcyqwl 296
Cdd:cd19150 161 RTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRAS------- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891055 297 KERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 363
Cdd:cd19150 233 KERSLSPKMLTEANlnSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
104-378 |
2.58e-47 |
|
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: 162.87 E-value: 2.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvTFGGQ---ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETE 180
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 181 RGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmI 231
Cdd:pfam00248 79 SGGSKENIrksleeslkrlgtdyidlyylhwpdpdtpIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 232 PPVCEQAEYHLFqREKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSRASLKCYQWlkerivseegRKQQ 309
Cdd:pfam00248 155 PIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891055 310 NKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQvlPKMTSHVVNEIDNIL 378
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
101-380 |
4.28e-44 |
|
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: 154.67 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 101 VSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYWGG- 175
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVSPDNl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 -----KAETERGLSR---KHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmipPV 234
Cdd:cd19085 78 tpedvRKSCERSLKRlgtDYIdlyqihwpssdvpLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------ID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 235 CEQAEYHLFQREKVEVQLPEL-YHKIGVgaMTWSPLACGIISGKYGNG---VPESSRASLkcyqwlkeRIVSEEG--RKQ 308
Cdd:cd19085 152 SNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFSSAedfPPGDARTRL--------FRHFEPGaeEET 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815891055 309 QNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 380
Cdd:cd19085 222 FEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEISDP 291
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
94-362 |
7.01e-44 |
|
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: 154.30 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 94 LGKSGLRVSCLGLGTwVTFGGQ----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITT 169
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 170 KLYWG--GKAETERGLSRK-----------------------HI------IEEIVRAMTHVINQGMAMYWGTSRWSAMEI 218
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKnlrrsveaslrrlqtdyidllyvHAwdfttpVEEVMRALDDLVRAGKVLYVGISDTPAWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 219 MEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGvpESSRASLKCYQWLKE 298
Cdd:cd19080 159 ARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 815891055 299 RIVSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 362
Cdd:cd19080 236 GKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL 296
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
89-363 |
1.55e-42 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 152.07 E-value: 1.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA--AGKAEVILGSIIKKK-GWRRSSL 165
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKL---YWGGKAETerGLSRKHII-----------------------------EEIVRAMTHVINQGMAMYWGTSRW 213
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLasldqslkrmgleyvdifyshrvdentpmEETASALAHAVQSGKALYVGISSY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 214 SAMEIMEAYSVARQFNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASL--K 291
Cdd:PRK09912 171 SPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHRegN 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 815891055 292 CYQWLKERIVSEegrKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL 363
Cdd:PRK09912 250 KVRGLTPKMLTE---ANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL 318
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
92-362 |
4.32e-37 |
|
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: 136.63 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 92 RNLGKSGLRVSCLGLGTWV----TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVI 167
Cdd:cd19149 2 RKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 168 TTK--LYWGGKA-----------------------ETERGLSR---KHI-------------IEEIVRAMTHVINQGMAM 206
Cdd:cd19149 79 ATKcgLRWDREGgsfffvrdgvtvyknlspesireEVEQSLKRlgtDYIdlyqthwqdvetpIEETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 207 YWGTSRWSAMEIMEaYSVARQFNMIppvceQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNG---VP 283
Cdd:cd19149 159 AIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPDrefDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 284 ESSRASLKCYQwlkerivsEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 362
Cdd:cd19149 232 GDARSGIPWFS--------PENREKVLALLEkWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
92-377 |
1.12e-35 |
|
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: 132.54 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 92 RNLGKSGLRVSCLGLGTwVTFGGQ-----ISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 166
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTK--LYWGG------------KAETERGLSR----------------KHIIEEIVRAMTHVINQGMAMYWGTSRWSAM 216
Cdd:cd19083 79 IATKgaHKFGGdgsvlnnspeflRSAVEKSLKRlntdyidlyyihfpdgETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 217 EIMEAySVARQFNMIppvceQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGVpessraSLKCYQWL 296
Cdd:cd19083 159 QLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 297 KERIVSEEGRKQQN--KLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 374
Cdd:cd19083 226 NDKPLFKGERFSENldKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFI 303
|
...
gi 815891055 375 DNI 377
Cdd:cd19083 304 DAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
100-359 |
1.56e-35 |
|
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: 131.97 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 100 RVSCLGLGTW------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKlYW 173
Cdd:cd19093 1 EVSPLGLGTWqwgdrlWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATK-FA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 174 GG-------------KAETER-GLSRKHI------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQ 227
Cdd:cd19093 79 PLpwrltrrsvvkalKASLERlGLDSIDLyqlhwpgpwysqIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 228 FNmIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIvseegrk 307
Cdd:cd19093 159 RG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKNLEKV------- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 815891055 308 qQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGA 359
Cdd:cd19093 231 -QPLLDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGA 279
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
90-374 |
7.04e-35 |
|
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: 130.41 E-value: 7.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 90 PHRNLGKSGLRVSCLGLG----TWvtFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 165
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKlyWG-------------GKAE-----TERGLSR---KHI-------------IEEIVRAMTHVINQGMAMYWGTS 211
Cdd:cd19076 76 VIATK--FGivrdpgsgfrgvdGRPEyvraaCEASLKRlgtDVIdlyyqhrvdpnvpIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 212 RWSAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLP---ELyhkiGVGAMTWSPLACGIISGKYGNgvPESSRA 288
Cdd:cd19076 154 EASADTIRRAHAVH------PITAVQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS--PEDLPE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 289 SLkcYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMT 367
Cdd:cd19076 222 DD--FRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLT 296
|
....*..
gi 815891055 368 SHVVNEI 374
Cdd:cd19076 297 PEELAEI 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
98-361 |
9.09e-33 |
|
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: 123.49 E-value: 9.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWVTFGGQIS----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVITTKLY- 172
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysdDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVSp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 WGGKAE-----TERGLSR---KHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfnmI 231
Cdd:cd19072 79 DHLKYDdvikaAKESLKRlgtDYIdlylihwpnpsipIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 232 PPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKYGngvpessraslkcyqwlkerivseegrkqqnk 311
Cdd:cd19072 156 PIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKG-------------------------------- 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 815891055 312 LKDLSPIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENLGAIQ 361
Cdd:cd19072 203 SPLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
99-359 |
2.37e-32 |
|
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: 121.82 E-value: 2.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 99 LRVSCLGLGTWV---TFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL--YW 173
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 174 GGKAETERGLSRKHIIE------------------------------EIVRAMTHVINQGMAMYWGTS---RWSAMEIME 220
Cdd:cd19086 78 DGGPERPQDFSPEYIREaveaslkrlgtdyidlyqlhnppdevldndELFEALEKLKQEGKIRAYGVSvgdPEEALAALR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AYSVArqfnmippvCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKygngvpessraslkcyqwlkeri 300
Cdd:cd19086 158 RGGID---------VVQVIYNLLDQRPEEELFPLA-EEHGVGVIARVPLASGLLTGK----------------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 815891055 301 vseegrkqqnklkdlspiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19086 205 -------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
101-378 |
3.66e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 120.47 E-value: 3.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 101 VSCLGLGTWVTFGGQ------ISDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSsLVITTK-- 170
Cdd:cd19102 1 LTTIGLGTWAIGGGGwgggwgPQDD-RDSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 LYWGGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEImea 221
Cdd:cd19102 77 LLWDEEGRIRRSLKPASIraeceaslrrlgvdvidlyqihwpdpdepIEEAWGALAELKEEGKVRAIGVSNFSVDQM--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 222 ysvaRQFNMIPPVCE-QAEYHLFQREKVEVQLPelY---HKIGVgaMTWSPLACGIISGKYGngvPESSrASLKCYQWLK 297
Cdd:cd19102 154 ----KRCQAIHPIASlQPPYSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT---PERV-ASLPADDWRR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 298 -ERIVSEEGRKQQNKLKD-LSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 375
Cdd:cd19102 222 rSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIE 299
|
...
gi 815891055 376 NIL 378
Cdd:cd19102 300 ALL 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
98-378 |
2.49e-30 |
|
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: 118.10 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTW-VTFG-GQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLYW- 173
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 174 ---GGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 221
Cdd:cd19078 78 idgGKPGPLGLDSRPEHIrkavegslkrlqtdyidlyyqhrvdpnvpIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 222 YSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASLKCYqwlke 298
Cdd:cd19078 158 HAVC------PVTAVQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 299 rivSEEGRKQQNKLKDL-SPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNI 377
Cdd:cd19078 226 ---TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDA 300
|
.
gi 815891055 378 L 378
Cdd:cd19078 301 L 301
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
102-359 |
1.99e-27 |
|
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: 109.95 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA----GKAEVILGSIIKKKGwRRSSLVITTKlywGG-- 175
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 ---KAETERgLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYS 223
Cdd:cd19082 76 dleDMSRSR-LSPEDIradleeslerlgtdyidlyflhrddpsvpVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 224 VARQFNMIPPVCEQAEYHLFqrEKVEVQLP------------ELYHKIGVGAMTWSPLACGIISGKYGNGVpESSRASLK 291
Cdd:cd19082 155 YAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGA-EDDSELRR 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815891055 292 CYQwlkerivSEEGRKQQNKLKDLspiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19082 232 VYY-------SEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
97-359 |
1.23e-26 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 106.68 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWG-- 174
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKVWNDnh 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 175 GKAET----ERGLSR---------------KHIIEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVC 235
Cdd:COG0656 73 GYDDTlaafEESLERlgldyldlylihwpgPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 236 EQAEYHLFQREkvevqlPEL--YHK-IGVGAMTWSPLAcgiisgkygngvpessRASLkcyqwLKERIVSEegrkqqnkl 312
Cdd:COG0656 149 NQVELHPYLQQ------RELlaFCReHGIVVEAYSPLG----------------RGKL-----LDDPVLAE--------- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 815891055 313 kdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENLGA 359
Cdd:COG0656 193 -----IAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDA 232
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
97-375 |
2.17e-26 |
|
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: 106.56 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLGTWvTFGGQISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKLY-W- 173
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEiEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVLpSn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 174 ----GGKAETERGLSR---KHI------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMippV 234
Cdd:cd19138 83 asrqGTVRACERSLRRlgtDYLdlyllhwrggvpLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC---A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 235 CEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGiisGKYGNGVPESSraslkcyqwlkerivseegrkqqnklkD 314
Cdd:cd19138 160 ANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG---GLLRRGLLENP---------------------------T 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815891055 315 LSPIAERLGCTLPQLAVAWCLRNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 375
Cdd:cd19138 209 LKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
89-379 |
1.99e-25 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 105.71 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHrnlgkSGLRVSCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAA-------GKAEVILGSIIKKKGwR 161
Cdd:PRK10625 6 IPH-----SSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 162 RSSLVITTKLywGGKAET-------ERGLSRKHIIE-------------------------------------------- 190
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREalhdslkrlqtdyldlyqvhwpqrptncfgklgyswtdsapavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 191 --EIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSP 268
Cdd:PRK10625 157 llETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 269 LACGIISGKYGNGV-PESSRASLKcyqwlkERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGS 347
Cdd:PRK10625 236 LAFGTLTGKYLNGAkPAGARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|..
gi 815891055 348 STPEQLIENLGAIQVlpKMTSHVVNEIDNILR 379
Cdd:PRK10625 310 TTMEQLKTNIESLHL--TLSEEVLAEIEAVHQ 339
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
89-360 |
5.11e-25 |
|
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: 102.28 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTwvTFGGQISDEVAERlmtiAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSLVIT 168
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGG--GGLPRESPELLRR----ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKLYWGGKAETERGLSRK-----------HI----------------IEEIVRAMTHVINQGMAMYWGTSRWSAME--IM 219
Cdd:cd19105 73 TKASPRLDKKDKAELLKSveeslkrlqtdYIdiyqlhgvdtpeerllNEELLEALEKLKKEGKVRFIGFSTHDNMAevLQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 220 EA-----YSVArqfnMIPpvceqaeY-HLFQREKVEVQLPELY-HKIGVGAMTwsPLACGIisgkygngvpessraslkc 292
Cdd:cd19105 153 AAiesgwFDVI----MVA-------YnFLNQPAELEEALAAAAeKGIGVVAMK--TLAGGY------------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 815891055 293 yqwlkerivSEEGRKQQNKLKDLSpiaerlgctLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 360
Cdd:cd19105 201 ---------LQPALLSVLKAKGFS---------LPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
97-375 |
9.63e-25 |
|
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: 102.70 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLG----TWVtfGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEV---ILGSIIKKKGWRRSSLVITT 169
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 170 KLYW--------GGKAETERGL--------SRKHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 220
Cdd:cd19077 79 KGGLdpdtlrpdGSPEAVRKSIenilralgGTKKIdifeparvdpnvpIEETIKALKELVKEGKIRGIGLSEVSAETIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYqwlkERI 300
Cdd:cd19077 159 AHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHL----DRF 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 301 VSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSV-LLGSSTPEQLIENLGAIQVlpKMTSHVVNEID 375
Cdd:cd19077 229 NGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
104-377 |
6.34e-24 |
|
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: 100.32 E-value: 6.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIikkkGWRRSSLVITTKLY-WGGKAETERG 182
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKANpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 183 LsRKHI-------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQ 237
Cdd:cd19075 81 V-RKQLetslkrlkvdkvdvfylhapdrstpLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 238 AEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKY--GNGVPESSR-----ASLKCYQ--WLKERIVSEegrkq 308
Cdd:cd19075 160 GMYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdpnnALGKLYRdrYWKPSYFEA----- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 309 qnkLKDLSPIAERLGCTLPQLAVAWC-----LRNEGVSSVLLGSSTPEQLIENLGAIQV--LPKmtsHVVNEIDNI 377
Cdd:cd19075 234 ---LEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKgpLPE---EVVKAIDEA 303
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
102-359 |
4.50e-23 |
|
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: 96.92 E-value: 4.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTWVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIkkKGWRRSSLVITTKL--YWGGkA 177
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRAL--AGLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 178 ETERGLSRKHII-----------------------------EEIVRAMTHVINQGMAMYWGTSRwSAMEIMEAYSVARqF 228
Cdd:cd19095 76 RDRKDFSPAAIRasierslrrlgtdyidllqlhgpsddeltGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIASGV-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 229 NMIppvceQAEYHLFQREKVEVqLPELY-HKIGVGAMtwSPLAcgiisgkygNGVPESSRASLKCYQWLKERivseegrk 307
Cdd:cd19095 154 DVV-----QLPYNVLDREEEEL-LPLAAeAGLGVIVN--RPLA---------NGRLRRRVRRRPLYADYARR-------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 815891055 308 qqnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19095 209 -------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
96-367 |
3.02e-22 |
|
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: 95.32 E-value: 3.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 96 KSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTK---LY 172
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 WGGKAETERG---LSRKHII-----------------------------EEIVRAMTHVINQGMAMYWGTSRWSAMeime 220
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILasvegslkrlgtdyldllllhrpdplmdpEEVAEAFDELVKSGKVRYFGVSNFTPS---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 aysvarQFNM------IPPVCEQAEYHLFQREKVEV----QLPELYHKIgvgaMTWSPLACGiisgkygngvpessrasl 290
Cdd:cd19092 157 ------QIELlqsyldQPLVTNQIELSLLHTEAIDDgtldYCQLLDITP----MAWSPLGGG------------------ 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 815891055 291 kcyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMT 367
Cdd:cd19092 209 --------RLFGGFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI--ELT 275
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
98-362 |
1.61e-21 |
|
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: 93.02 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvTFGGQIS-----DEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLy 172
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 WGGKAETE----------RGLSRKHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQfn 229
Cdd:cd19137 77 WPTNLRYDdllrslqnslRRLDTDYIdlylihwpnpnipLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 230 miPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIIsgkygngvpessraslkcyqwLKERIVSEegrkqq 309
Cdd:cd19137 155 --PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLE---------------------KTNRTLEE------ 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 815891055 310 nklkdlspIAERLGCTLPQLAVAWCLRNEGVSSVLLgSSTPEQLIENLGAIQV 362
Cdd:cd19137 206 --------IAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
102-359 |
2.36e-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: 381391 [Multi-domain] Cd Length: 291 Bit Score: 93.17 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTwVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYA-------AGKAEVILGSIIKKKGwRRSSLVITTK---- 170
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKvgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 -LYWGGKAETERGLSRK-----------------------HI------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIME 220
Cdd:cd19752 79 pRDPDGGPESPEGLSAEtieqeidkslrrlgtdyidlyyaHVddrdtpLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AYSVARQFNMIPPVCEQAEYHLFQR-----EKVEVQL-PEL-----YHKiGVGAMTWSPLacgiISGKYGNgvpeSSRAS 289
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPL----LSGAYTR----PDRPL 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 290 LKCYqwlkerivseEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19752 230 PEQY----------DGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
89-382 |
4.81e-21 |
|
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: 92.89 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSL 165
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKL----------YWGG------KAETERGLSR---KHI-------------IEEIVRAMTHVINQGMAMYWGTSRW 213
Cdd:cd19144 79 FLATKFgieknvetgeYSVDgspeyvKKACETSLKRlgvDYIdlyyqhrvdgktpIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 214 SAMEIMEAYSVArqfnmiPPVCEQAEYHLF--QREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgngvpeSSRASLK 291
Cdd:cd19144 159 SAETLRRAHAVH------PIAAVQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI------RSPDDFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 292 CYQWLKE--RIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSH 369
Cdd:cd19144 227 EGDFRRMapRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEE 304
|
330
....*....|...
gi 815891055 370 VVNEIDNILRNKP 382
Cdd:cd19144 305 EEKEIREIAEEAE 317
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
98-353 |
5.24e-21 |
|
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: 92.37 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWVT----FGGqiSDEvAERLMTI--AYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK- 170
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 -LYWGGKAETERGLSRKHI-----------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAmEIME 220
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIrkevedslrrlqtdyidlyqvhwpdplvpIEETAEALKELLDEGKIRAIGVSNFSP-EQME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AY-SVARQFNMIPPvceqaeYHLFQREKVEVQLP-ELYHKIGVgaMTWSPLACGIISGKYGngvPESS------RASLKC 292
Cdd:cd19148 156 TFrKVAPLHTVQPP------YNLFEREIEKDVLPyARKHNIVT--LAYGALCRGLLSGKMT---KDTKfegddlRRTDPK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 293 YQwlkerivseEGRKQQ-----NKLKDLSpiAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQL 353
Cdd:cd19148 225 FQ---------EPRFSQylaavEELDKLA--QERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
90-374 |
5.57e-21 |
|
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: 92.11 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 90 PHRNLGKSGLRVSCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLV 166
Cdd:cd19145 1 PRVKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 167 ITTKL---YWGG------------KAETERGLSRKHI----------------IEEIVRAMTHVINQGMAMYWGTSRWSA 215
Cdd:cd19145 79 LATKFgihEIGGsgvevrgdpayvRAACEASLKRLDVdyidlyyqhridttvpIEITMGELKKLVEEGKIKYIGLSEASA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 216 MEIMEAYSVArqfnmiPPVCEQAEYHLFQREkVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASLKCYQW 295
Cdd:cd19145 159 DTIRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGK---AKLEELLENSDVRKS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 296 LKeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVlLGSSTPEQLIENLGAIQVlpKMTSHVVNEI 374
Cdd:cd19145 229 HP-RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-377 |
2.96e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 90.40 E-value: 2.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 91 HRNLGKSGLRVSCLGLGtwvtfGGQI-------SDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRS 163
Cdd:cd19104 2 YRRFGRTGLKVSELTFG-----GGGIgglmgrtTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 164 SLVITTKLYWGG------KAETERGL---------------------------------SRKHII--EEIVRAMTHVINQ 202
Cdd:cd19104 74 GPYITTKVRLDPddlgdiGGQIERSVekslkrlkrdsvdllqlhnrigderdkpvggtlSTTDVLglGGVADAFERLRSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 203 GMAMYWGTSRWSAMEIMEAYSVARQFNMIppvceQAEYHL------FQREKVEV-----QLPELYHKIGVGAMTWSPLAC 271
Cdd:cd19104 154 GKIRFIGITGLGNPPAIRELLDSGKFDAV-----QVYYNLlnpsaaEARPRGWSaqdygGIIDAAAEHGVGVMGIRVLAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 272 GIISGKYGNGVPESSRAslkcyqwlkERIVSEEGRKQqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPE 351
Cdd:cd19104 229 GALTTSLDRGREAPPTS---------DSDVAIDFRRA----AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNRE 295
|
330 340
....*....|....*....|....*.
gi 815891055 352 QLIENLGAIQVLPkMTSHVVNEIDNI 377
Cdd:cd19104 296 ELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
89-357 |
3.50e-20 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 90.65 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTWvtfGGQISD-EVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVI 167
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 168 TTKLY-WGGKAETerglsRKHIIEEIVRAM-T--------HVINQGMAMYWGTSRWSAMEIMEAysvARQ---------- 227
Cdd:COG1453 73 ATKLPpWVRDPED-----MRKDLEESLKRLqTdyidlyliHGLNTEEDLEKVLKPGGALEALEK---AKAegkirhigfs 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 228 FNMIPPVCEQA-E-----------YHLFQREKVEVQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyqw 295
Cdd:COG1453 145 THGSLEVIKEAiDtgdfdfvqlqyNYLDQDNQAGEEALEAAAEKGIGVIIMKPLKGG----------------------- 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 296 lkerivseegrkqqnKLKDLSPIAERLGC---TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENL 357
Cdd:COG1453 202 ---------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
104-361 |
3.99e-20 |
|
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: 89.15 E-value: 3.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGT-WVTFG-GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKkkGWRRSSLVITTKLywGGKAETER 181
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 182 GLSRKHI---IEEIVRA---------MTH---VINQGMAMYWGtsrwSAMEIMEA----------------YSVARQ--- 227
Cdd:cd19090 77 DYSADRVrrsVEESLERlgrdridllMIHdpeRVPWVDILAPG----GALEALLElkeeglikhiglgggpPDLLRRaie 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 228 ---FNMIPPVCEqaeYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGKYgngvPESSRASlkcYQWLKERivsee 304
Cdd:cd19090 153 tgdFDVVLTANR---YTLLDQSAADELLPAAARH-GVGVINASPLGMGLLAGRP----PERVRYT---YRWLSPE----- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 815891055 305 grkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 361
Cdd:cd19090 217 ---LLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
98-378 |
3.92e-17 |
|
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: 81.32 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGT------WVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTKL 171
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 ---------------YWGGKAETERgLSRKH----------------------IIEEIVRAMTHVINQGMAMYWGTSRWS 214
Cdd:cd19146 87 ttgyrrggpikiksnYQGNHAKSLR-LSVEAslkklqtsyidilyvhwwdyttSIPELMQSLNHLVAAGKVLYLGVSDTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 215 AMEIMEAYSVARQFNMIPPVCEQAEYHL----FQREKVEVQLPElyhkiGVGAMTWSPLAcgiiSGKYGNGVPESSRASL 290
Cdd:cd19146 166 AWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 291 KCYQWLKerivSEEGRKQQNKLKDlspIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHV 370
Cdd:cd19146 237 GRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEE 307
|
....*...
gi 815891055 371 VNEIDNIL 378
Cdd:cd19146 308 IQEIEDAY 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
102-359 |
1.38e-16 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 78.76 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTW---VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGG--- 175
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPWSvks 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 KAETERglsrkhIIEEIVRAMT---------HVINQGMaMYWGTSRWSAMEIMEAysvARQ----------FNMIPPVCE 236
Cdd:cd19096 79 AEDFRR------ILEESLKRLGvdyidfyllHGLNSPE-WLEKARKGGLLEFLEK---AKKeglirhigfsFHDSPELLK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 237 QA-----------EYHLFQREKVEVQ-LPELYHKIGVGAMTWSPLACGIISgkygngvpessraslkcyqwlkerivsee 304
Cdd:cd19096 149 EIldsydfdfvqlQYNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGLA----------------------------- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 305 grkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19096 200 -----NNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
98-357 |
3.06e-16 |
|
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: 77.68 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaAGKAEVilGSIIKKKGWRRSSLVITTKLYWGG-- 175
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY-GNEAQV--GEAIAASGVPRDELFLTTKVWPDNys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 ----KAETERGLSR---------------KHI-IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVC 235
Cdd:cd19140 77 pddfLASVEESLRKlrtdyvdllllhwpnKDVpLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 236 EQAEYH--LFQRekvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklk 313
Cdd:cd19140 153 NQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLARG---------------------EVLKDPVLQE---------- 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 815891055 314 dlspIAERLGCTLPQLAVAWCLRNEGVsSVLLGSSTPEQLIENL 357
Cdd:cd19140 197 ----IGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENL 235
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-185 |
3.46e-16 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 77.14 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 91 HRNLGKSGLRVSCLGLGTWVTfgGQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKkgwRRSSLVITTK 170
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90
....*....|....*
gi 815891055 171 LYWGGKAETERGLSR 185
Cdd:cd19100 74 TGARDYEGAKRDLER 88
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
101-359 |
5.43e-16 |
|
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: 76.87 E-value: 5.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 101 VSCLGLGTW-----VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSLVITTKL---- 171
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATKGglvr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 ----YWG--GKAET--------ERGLSRKHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSV 224
Cdd:cd19088 78 tgpgWWGpdGSPEYlrqaveasLRRLGLDRIdlyqlhridpkvpFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 225 ARqfnmIppVCEQAEYHLFQREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkyGNGVPESSRaslkcyqwlkerivsee 304
Cdd:cd19088 158 VR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG--------GGDLAQPGG----------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 305 grkqqnklkDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19088 205 ---------LLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
104-365 |
1.91e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 75.64 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTwVTFG---------GQISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKgwrrSSLVITTKLywg 174
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 175 gKAETERGLSRKHIIEEIVRA-------------MTHviNQGMAMYWGTSRWSAMEIMEA-----------YSVarqfnm 230
Cdd:cd19097 73 -PPLKEDKKEDEAAIEASVEAslkrlkvdsldglLLH--NPDDLLKHGGKLVEALLELKKeglirkigvsvYSP------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 231 ippvcEQAEYhLFQREKVE-VQLPelyhkigVGAMTWSPLACGIISGKYGNGV--------------PESSRASLKCYQW 295
Cdd:cd19097 144 -----EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIeiharsvflqglllMEPDKLPAKFAPA 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 296 lkerivseegrkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK 365
Cdd:cd19097 211 -------------KPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
104-357 |
5.48e-15 |
|
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: 74.06 E-value: 5.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWG---GKAETE 180
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKL-WPtdhGYERVR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 181 RGL--SRKHI------------------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 234
Cdd:cd19071 75 EALeeSLKDLgldyldlylihwpvpgkeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 235 CEQAEYHLF--QREKVEvqlpelY-HKIGVGAMTWSPLACGiisgkygngvpesSRASLKCyqwlkerivseegrkqqnk 311
Cdd:cd19071 151 VNQIELHPYlqQKELVE------FcKEHGIVVQAYSPLGRG-------------RRPLLDD------------------- 192
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 815891055 312 lKDLSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 357
Cdd:cd19071 193 -PVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENL 235
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
89-360 |
1.31e-14 |
|
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: 73.74 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 89 MPHRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIkkKGWRRSSL 165
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKL--YWGGKAET------------ERGLSRKH--------------------IIEEIVRAMTHVINQGMAMYWGTS 211
Cdd:cd19163 78 YLATKVgrYGLDPDKMfdfsaeritksvEESLKRLGldyidiiqvhdiefapsldqILNETLPALQKLKEEGKVRFIGIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 212 RWSaMEIMeAYSVARQFNMIPPVCEQAEYHLFQREKVEvqLPELYHKIGVGAMTWSPLACGIISGKygnGVPESSRASlk 291
Cdd:cd19163 158 GYP-LDVL-KEVLERSPVKIDTVLSYCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGLLTER---GPPDWHPAS-- 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 815891055 292 cyQWLKERIvseegrkqqnklKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAI 360
Cdd:cd19163 229 --PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
98-357 |
1.07e-13 |
|
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: 70.30 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKKGWRRSSLVITTKL----- 171
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKLwiqda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 -YWGGKAETERGLSRKHIieEIVRAMthVINQGMAMYWGTsrWSAMEimEAYSVAR------------------QFNMIP 232
Cdd:cd19133 78 gYEKAKKAFERSLKRLGL--DYLDLY--LIHQPFGDVYGA--WRAME--ELYKEGKiraigvsnfypdrlvdliLHNEVK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 233 PVCEQAEYHLFqREKVEVQlpELYHKIGVGAMTWSPLAcgiisgkygngvpessraslkcyqwlkerivseEGRKQ--QN 310
Cdd:cd19133 150 PAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA---------------------------------EGRNNlfEN 193
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 815891055 311 KLkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENL 357
Cdd:cd19133 194 PV--LTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
104-359 |
2.42e-13 |
|
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: 69.22 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGG------KA 177
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDHlrpedlKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 178 ETERGLSR---KHI-------------IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYH 241
Cdd:cd19073 76 SVDRSLEKlgtDYVdlllihwpnptvpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 242 --LFQREKVEVQLPelyHKIGVGAmtWSPLACGiisgkygnGVPESSRaslkcyqwLKErivseegrkqqnklkdlspIA 319
Cdd:cd19073 152 pfLYQAELLEYCRE---NDIVITA--YSPLARG--------EVLRDPV--------IQE-------------------IA 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 815891055 320 ERLGCTLPQLAVAWCLRnEGVsSVLLGSSTPEQLIENLGA 359
Cdd:cd19073 192 EKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
92-378 |
3.19e-13 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 69.81 E-value: 3.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 92 RNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 168
Cdd:PLN02587 2 RELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 169 TKL--YWGG---KAE-----TERGLSR-------------------KHIIEEIVRAMTHVINQGMAMYWGTSRWSaMEIM 219
Cdd:PLN02587 81 TKCgrYGEGfdfSAErvtksVDESLARlqldyvdilhchdiefgslDQIVNETIPALQKLKESGKVRFIGITGLP-LAIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 220 EaYSVARqfnmIPP-----VCEQAEYHLFQREKVEVqLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRASLKcyq 294
Cdd:PLN02587 160 T-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 295 wLKE--RIVSEEGRKQqnklkdlspiaerlGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPK--MTSHV 370
Cdd:PLN02587 227 -LKSacAAAATHCKEK--------------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETsgIDEEL 291
|
....*...
gi 815891055 371 VNEIDNIL 378
Cdd:PLN02587 292 LSEVEAIL 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
90-363 |
1.15e-12 |
|
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: 67.95 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 90 PHRNLGKSGLRVSCLGLGTwVTFGGQISDEV----AERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSL 165
Cdd:cd19153 1 FGETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 166 VITTKLYWGGKAETE-----------RGLSRKH-------------------IIEEIVRAMTHVINQGMAMYWGTSRWsA 215
Cdd:cd19153 80 TVATKVGRYRDSEFDysaervrasvaTSLERLHttyldvvylhdiefvdydtLVDEALPALRTLKDEGVIKRIGIAGY-P 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 216 MEIMEaySVARQFNMIPPVCEQAEYHL-FQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKygnGVPE---------- 284
Cdd:cd19153 159 LDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPwhpasgelrh 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 285 SSRASLKcyqWLKERIVSeegrkqqnklkdlspiaerlgctLPQLAVAWCLRNE-GVSSVLLGSSTPEQLIENLGAIQVL 363
Cdd:cd19153 234 YAAAADA---VCASVEAS-----------------------LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAV 287
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
104-359 |
3.32e-12 |
|
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: 66.61 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTwVTFG--GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKkkGWRRSSLVITTKL-------YWG 174
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 175 GKAETER--GLSRKHIIEEIVR------------AMTHVINQGM--AMywgTSRWSAMEIMEAYSVARQFN---MIPPVC 235
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEAslerlgldrldlVFLHDPDRHLlqAL---TDAFPALEELRAEGVVGAIGvgvTDWAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 236 EQA-------------EYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISGkygnGVPESSRASlkcYQWLKERIVS 302
Cdd:cd19162 157 LRAarradvdvvmvagRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGILAT----DDPAGDRYD---YRPATPEVLA 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 815891055 303 eegRKQQnklkdLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19162 229 ---RARR-----LAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
106-335 |
1.36e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 64.66 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 106 LGTW----------VTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgWRRSSLVITTKLYWGG 175
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 KAET--------ERGLSRK----------HIIEEIVRAMTHVI---NQGMAMYWGTSRWSAMEIMEAYSVARQFNmIPPV 234
Cdd:cd19103 87 AGQSadpvadmlEGSLARLgtdyidiywiHNPADVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAG-VSLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 235 CEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYG--NGVPESSraslkcyqwlkERIVSEEGRKQQnkL 312
Cdd:cd19103 166 AVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDtkHPLPEGS-----------GRAETYNPLLPQ--L 232
|
250 260
....*....|....*....|....*..
gi 815891055 313 KDLSP----IAERLGCTLPQLAVAWCL 335
Cdd:cd19103 233 EELTAvmaeIGAKHGASIAQVAIAWAI 259
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
99-201 |
2.62e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 63.88 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 99 LRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILG----SIIKKKGWRRSSLVITTKlywG 174
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGkalrELIEKGGIKRDEVVIVTK---A 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 815891055 175 GK------------AETERGLSRKHIIEEIVRAMTHVIN 201
Cdd:cd19099 78 GYipgdgdeplrplKYLEEKLGRGLIDVADSAGLRHCIS 116
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
104-362 |
8.26e-11 |
|
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: 62.63 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKL--------- 171
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVgrllvplqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 --------YWGG----------KAETER---------GLSRKHI----------------------IEEIVRAMTHVINQ 202
Cdd:cd19152 80 veptfepgFWNPlpfdavfdysYDGILRsiedslqrlGLSRIDLlsihdpdedlagaesdehfaqaIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 203 GMAMYW--GTSRWS-AMEIME-----AYSVARQFNMIppvcEQAEYHLFqrekvevqLPELyHKIGVGAmtwsplacgII 274
Cdd:cd19152 160 GVIKAIglGVNDWEvILRILEeadldWVMLAGRYTLL----DHSAAREL--------LPEC-EKRGVKV---------VN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 275 SGKYGNGVpessRASLKCYQWLKERIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLI 354
Cdd:cd19152 218 AGPFNSGF----LAGGDNFDYYEYGPAPPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVE 290
|
....*...
gi 815891055 355 ENLGAIQV 362
Cdd:cd19152 291 ENVALLAT 298
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
100-359 |
1.13e-10 |
|
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: 61.84 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 100 RVSCLGLGTWVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGW---RRSSLVITTKL-Y 172
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWvP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 WGGKAETERGLSRkHIIE---------------------------EIVRAMTHVINQGMAMYWG-----TSRWSamEIME 220
Cdd:cd19101 79 DPGELTMTRAYVE-AAIDrslkrlgvdrldlvqfhwwdysdpgylDAAKHLAELQEEGKIRHLGltnfdTERLR--EILD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 221 AysvarqfnMIPPVCEQAEYHLFQReKVEVQLPELYHKIGVGAMTWSPLACGIISGKYgNGVPESSR-----ASLKCYQw 295
Cdd:cd19101 156 A--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKY-LGVPEPTGpaletRSLQKYK- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 296 lkeRIVSEEG--RKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGA 359
Cdd:cd19101 225 ---LMIDEWGgwDLFQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRA 287
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
104-357 |
1.46e-10 |
|
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: 61.23 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGKAETERGL 183
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 184 S------RKHIIEEIVRAMTHVINQGMAMYWGTsrWSAMEIMEAYSVAR-----QFNM-----------IPPVCEQAEYH 241
Cdd:cd19131 84 RafdeslRKLGLDYVDLYLIHWPVPAQDKYVET--WKALIELKKEGRVKsigvsNFTIehlqrlidetgVVPVVNQIELH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 242 -LFQREkvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKERIVSEegrkqqnklkdlspIAE 320
Cdd:cd19131 162 pRFQQR----ELRAFHAKHGIQTESWSPLGQG---------------------GLLSDPVIGE--------------IAE 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 815891055 321 RLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 357
Cdd:cd19131 203 KHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
88-356 |
1.64e-10 |
|
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: 61.19 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 88 GMPHRNLgKSGLRVSCLGLGTWvTFGGQISDEVAERLMtiayESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVI 167
Cdd:cd19135 1 GTPTVRL-SNGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 168 TTKLYWG--GKAETER---------------------------GLSRKHIIEEIVRAMTHVINQGMAMYWGTSRWSAMEI 218
Cdd:cd19135 72 TTKLWPSdyGYESTKQafeaslkrlgvdyldlyllhwpdcpssGKNVKETRAETWRALEELYDEGLCRAIGVSNFLIEHL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 219 MEaysvARQFNMIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkcyQWLKE 298
Cdd:cd19135 152 EQ----LLEDCSVVPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLAKG---------------------KALEE 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 815891055 299 RIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIEN 356
Cdd:cd19135 204 PTVTE--------------LAKKYQKTPAQILIRWSIQNGVV--TIPKSTKEERIKEN 245
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
105-383 |
2.12e-10 |
|
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: 60.71 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 105 GLGTWV--TFGGQISDEVAErLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLYWGGK---AET 179
Cdd:cd19120 10 GTGTAWykSGDDDIQRDLVD-SVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIKdprEAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 180 ERGLSR--------------------KHIIEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAE 239
Cdd:cd19120 86 RKSLAKlgvdyvdlylihspffakegGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 240 YHLFqrekVEVQLPEL--YHKigvgamtwsplACGIISGKYGNGVPessraslkcyqwlkerIVSEEGRKQQNKLKDlsp 317
Cdd:cd19120 162 FHPY----LYPQQPALleYCR-----------EHGIVVSAYSPLSP----------------LTRDAGGPLDPVLEK--- 207
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 318 IAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENLGAIqvLPKMTSHVVNEIDNILRNKPY 383
Cdd:cd19120 208 IAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
96-357 |
2.64e-10 |
|
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: 60.89 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 96 KSGLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKkgW------RRSSLVITT 169
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 170 KLYWG--GKAETERGLSRK--------------HI-------------------------IEEIVRAMTHVINQGMAMYW 208
Cdd:cd19154 77 KLWTHehAPEDVEEALRESlkklqleyvdlyliHApaafkddegesgtmengmsihdavdVEDVWRGMEKVYDEGLTKAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 209 GTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPEssRA 288
Cdd:cd19154 157 GVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL-----------GSPG--RA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 815891055 289 SLkcyqwlkerIVSEEGRKQQNKLKD--LSPIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 357
Cdd:cd19154 217 NF---------TKSTGVSPAPNLLQDpiVKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENF 276
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
104-383 |
9.30e-10 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 59.35 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAaGKAEV--ILGSIIKKKGWRRSSLVITTKLY--------- 172
Cdd:cd19123 15 LGLGTWKSKPGEVGQAVKQ-----ALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKLWnnshapedv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 ----------------------W--------GGKAETERGLSRKHI-IEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEA 221
Cdd:cd19123 89 lpalektladlqldyldlylmhWpvalkkgvGFPESGEDLLSLSPIpLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 222 YSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkyGNGVPESSRASLKCYQWLKERIV 301
Cdd:cd19123 169 LATAR----IKPAVNQVELHPYLQQP---ELLAFCRDNGIHLTAYSPL---------GSGDRPAAMKAEGEPVLLEDPVI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 302 SEegrkqqnklkdlspIAERLGCTLPQLAVAWCL-RNegvSSVLLGSSTPEQLIENLGAIQVlpKMTSHVVNEIDNILRN 380
Cdd:cd19123 233 NK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMATIAALDRH 293
|
...
gi 815891055 381 KPY 383
Cdd:cd19123 294 HRY 296
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
103-357 |
5.33e-09 |
|
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: 56.76 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 103 CLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVY----AAGKAeviLGSIIKKKGWRRSSLVITTKLyWGGKAE 178
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 179 TE------------------------------------------RGLSRKHIIEEIVRAMTHVINQGMAMYWGTSRWSAM 216
Cdd:cd19128 74 PEnvkeqllitlqdlqleyldlflihwplafdmdtdgdprddnqIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 217 EIMEAYSVARqfnmIPPVCEQAEYHL-FQREKVeVQLPeLYHKIGVGAmtWSPLAcgiisGKYGNGvpesSRASLKCyqw 295
Cdd:cd19128 154 LLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG----NLTFLND--- 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 815891055 296 lkerivseegrkqqnklKDLSPIAERLGCTLPQLAVAWCL-RNEGVSSVLLGSSTPEQLIENL 357
Cdd:cd19128 214 -----------------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
104-357 |
6.51e-09 |
|
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: 56.40 E-value: 6.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAagkAEVILGSIIKKKGWRRSSLVITTKL------YWGGKA 177
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLatpdqgFTASQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 178 ETERGLSR-------------------KHIieEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVArqfnMIPPVCEQA 238
Cdd:cd19134 86 ACRASLERlgldyvdlylihwpagregKYV--DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTPAVNQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 239 EYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGIISGKygngvPESSRaslkcyqwlkerivseegrkqqnklkdls 316
Cdd:cd19134 160 ELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVGRLLDN-----PAVTA----------------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 815891055 317 pIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQLIENL 357
Cdd:cd19134 201 -IAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
96-357 |
7.51e-09 |
|
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: 56.20 E-value: 7.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 96 KSGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYAAGKaEV--ILGSIIKKKGWRRSSLVITTKLY- 172
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKT-----AIKEGYRHIDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKLWc 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 173 ------------------------------W-----GGKAETERGLSRKHIIEEIVRAMTHVINQGMAMYWGTSRWSAME 217
Cdd:cd19125 80 tdhapedvppalektlkdlqldyldlylihWpvrlkKGAHMPEPEEVLPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 218 IMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLacgiisgkygnGVPESSRASLKCyqwLK 297
Cdd:cd19125 160 LEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSPGTTWVKKNV---LK 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 298 ERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRnEGvSSVLLGSSTPEQLIENL 357
Cdd:cd19125 219 DPIVTK--------------VAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
96-170 |
2.03e-07 |
|
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: 51.89 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 96 KSGLRVSCLGLGTwvtFGGQISDEVAE----RLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKK--KGWRRSSLVITT 169
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
.
gi 815891055 170 K 170
Cdd:cd19164 85 K 85
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
102-365 |
2.12e-07 |
|
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: 51.94 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 102 SCLGLGTwVTFGG---QISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwrRSSLVITTKL------- 171
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVgrllkpa 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 ------------------------YWGGKAETERGLSRK----------HIIEEIVRAMTHVINqgmamYWGTSRWSAME 217
Cdd:cd19161 78 regsvpdpngfvdplpfeivydysYDGIMRSFEDSLQRLglnridilyvHDIGVYTHGDRKERH-----HFAQLMSGGFK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 218 IME---------AYSV-ARQFNMIPPVCEQA---------EYHLFQREKVEVQLPELyHKIGVGAmtwsplacgIISGKY 278
Cdd:cd19161 153 ALEelkkagvikAFGLgVNEVQICLEALDEAdldcfllagRYSLLDQSAEEEFLPRC-EQRGTSL---------VIGGVF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 279 GNGVPESSRASLKCYQWlkeRIVSEEgrkQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLG 358
Cdd:cd19161 223 NSGILATGTKSGAKFNY---GDAPAE---IISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVE 296
|
....*...
gi 815891055 359 AIQ-VLPK 365
Cdd:cd19161 297 AFQtDIPE 304
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
104-357 |
3.32e-07 |
|
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: 51.09 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 104 LGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIK----KKGWRRSSLVITTKL------- 171
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKLapkdqgy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 ------------------------YWGGKAETERGlSRKHII--EEIVRAMTHVINQGMAMYWGTSRW--SAMEIMEAYS 223
Cdd:cd19136 76 ekaraaclgslerlgtdyldlyliHWPGVQGLKPS-DPRNAElrRESWRALEDLYKEGKLRAIGVSNYtvRHLEELLKYC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 224 varqfnMIPPVCEQAEYH--LFQREkvevqLPELYHKIGVGAMTWSPLACGiisgkygngvpessraslkCYQWLKERIV 301
Cdd:cd19136 155 ------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG-------------------DLRLLEDPTV 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 302 SEegrkqqnklkdlspIAERLGCTLPQLAVAWCLRNeGVsSVLLGSSTPEQLIENL 357
Cdd:cd19136 205 LA--------------IAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
98-279 |
1.10e-06 |
|
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: 49.44 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvtfggQISD-EVAERLMTIAYESGVNLFDTAEVYaagKAEVILGSIIKKKGWRRSSLVITTKLyWGGK 176
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 177 AETERGL-----SRKHIIEEIV-----------------RAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPV 234
Cdd:cd19156 77 QGYESTLaafeeSLEKLGLDYVdlylihwpvkgkfkdtwKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 815891055 235 CEQAEYH-LFQREKVEVQLPElyHKIGVGAmtWSPLACG---------IISGKYG 279
Cdd:cd19156 153 VNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQGkllsnpvlkAIGKKYG 203
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
97-375 |
2.23e-06 |
|
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: 49.05 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLG------TWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGwRRSSLVITTK 170
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 171 L----------------YWGGKA--------ETERGLSRKHI-------------IEEIVRAMTHVINQGMAMYWGTSRW 213
Cdd:cd19147 85 FttdykayevgkgkavnYCGNHKrslhvsvrDSLRKLQTDWIdilyvhwwdyttsIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 214 SAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHkIGVGAMTWSPLacgiisgkyGNGVPESSRAslkcy 293
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVL---------GGGKFQSKKA----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 294 qwLKERIVSEEGRK------QQNKL-----KDLSPIAERLGC-TLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQ 361
Cdd:cd19147 230 --VEERKKNGEGLRsfvggtEQTPEevkisEALEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALS 307
|
330
....*....|....
gi 815891055 362 VlpKMTSHVVNEID 375
Cdd:cd19147 308 I--KLTPEEIEYLE 319
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
98-357 |
5.99e-06 |
|
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: 47.52 E-value: 5.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAeviLGSIIKKkgW------RRSSLVITTKL 171
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 YWGG-KAETERGLSRK-------------------HIIEE-----------------------IVRAMTHVINQGMAMYW 208
Cdd:cd19155 79 PPGGnRREKVEKFLLKsleklqldyvdlylihfpvGSLSKeddsgkldptgehkqdyttdlldIWKAMEAQVDQGLTRSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 209 GTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKVEVQLPElYHKIGVGAmtWSPLAC-GIISGKYGNGVPESSR 287
Cdd:cd19155 159 GLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCS-THSITVTA--YAPLGSpGAAHFSPGTGSPSGSS 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 288 ASLkcyqwLKERIVSEegrkqqnklkdlspIAERLGCTLPQLAVAWCLrNEGVsSVLLGSSTPEQLIENL 357
Cdd:cd19155 232 PDL-----LQDPVVKA--------------IAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKENF 280
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
98-357 |
6.19e-06 |
|
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: 47.40 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 98 GLRVSCLGLGTWvtfggQISDEVAERLMTIAYESGVNLFDTAEVYAaGKAEVilGSIIKKKGWRRSSLVITTKLYWG--G 175
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 176 KAETERGLSR-------------------KHIIEEIV---RAMTHVINQGMAMYWGTSRWSA---MEIMEAYSVarqfnm 230
Cdd:cd19127 78 YDKALRGFDAslrrlgldyvdlyllhwpvPNDFDRTIqayKALEKLLAEGRVRAIGVSNFTPehlERLIDATTV------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 231 IPPVcEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLAcGIIsgKYGNGVPESSRASLKCYQwlkerivseegrkqqn 310
Cdd:cd19127 152 VPAV-NQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPTGPGDVLQDPT---------------- 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 815891055 311 klkdLSPIAERLGCTLPQLAVAWCLRNeGVSSVlLGSSTPEQLIENL 357
Cdd:cd19127 209 ----ITGLAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
194-362 |
2.55e-05 |
|
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: 45.69 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 194 RAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQREKvevQLPELYHKIGVGAMTWSPLACGi 273
Cdd:cd19122 146 RAMEEIYESGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGSQ- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 274 isgkygNGVPESSraslkcyqwlkERIvseegrkqqNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVssVLLGSSTPEQL 353
Cdd:cd19122 218 ------NQVPSTG-----------ERV---------SENPTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRI 269
|
....*....
gi 815891055 354 IENLGAIQV 362
Cdd:cd19122 270 ESNFKSIEL 278
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
121-362 |
1.61e-04 |
|
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: 43.10 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 121 AERLMTIAYESGVNLFDTAEVYaaGKAEVILGSIIKKKGWRRSSLVITTKlyWG----------GKAETERGLSRKHII- 189
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 190 ------------------------------EEIVRAMTHVINQGMAMYWGTSRWS-------AMEImeAYSVARQFNmip 232
Cdd:cd19098 113 qweetrsllgkhldlyqihsatlesgvledADVLAALAELKAEGVKIGLSLSGPQqaetlrrALEI--EIDGARLFD--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 233 pvCEQAEYHLFQREKVEvQLpELYHKIGVGAmtwsplacgIISGKYGNGvpessRaslkcyqwLKERIVSEEGRKqqnKL 312
Cdd:cd19098 188 --SVQATWNLLEQSAGE-AL-EEAHEAGMGV---------IVKEALANG-----R--------LTDRNPSPELAP---LM 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 815891055 313 KDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQV 362
Cdd:cd19098 239 AVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
97-380 |
5.78e-04 |
|
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: 41.60 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLGTWVTFGGQISDEVaerlmTIAYESGVNLFDTAEVYaAGKAEVilGSIIKK-----KGWRRSSLVITTKL 171
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQVKAAV-----KYALDAGYRHIDCAAVY-GNEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 172 yWGGK--AETERGLSRKHIIE----------------------------------------EIVRAMTHVINQGMAMYWG 209
Cdd:cd19106 75 -WNTKhhPEDVEPALRKTLKDlqldyldlylihwpyafergdnpfpknpdgtirydsthykETWKAMEKLVDKGLVKAIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 210 TSRWSAMEIMEAYSVARqfnmIPPVCEQAEYHLFQrekVEVQLPELYHKIGVGAMTWSPLacgiisgkygnGVPEssRAs 289
Cdd:cd19106 154 LSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSPD--RP- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 290 lkcyqWLK--ERIVSEEGRkqqnklkdLSPIAERLGCTLPQLAVAWcLRNEGVsSVLLGSSTPEQLIENlgaIQVLP-KM 366
Cdd:cd19106 213 -----WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW-QVQRGV-VVIPKSVTPSRIKQN---IQVFDfTL 274
|
330
....*....|....
gi 815891055 367 TSHVVNEIDNILRN 380
Cdd:cd19106 275 SPEEMKQLDALNRN 288
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
97-185 |
1.03e-03 |
|
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: 40.59 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815891055 97 SGLRVSCLGLGTWVTFGGQISDEVAErlmtiAYESGVNLFDTAEVYaAGKAEVILGsiIKK---KGWRRSSLVITTKLYW 173
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCY-QNEDEVGEG--IKEaiaGGVKREDLFVTTKLWS 79
|
90
....*....|..
gi 815891055 174 GGKAETERGLSR 185
Cdd:cd19121 80 TYHRRVELCLDR 91
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
315-377 |
5.02e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 38.41 E-value: 5.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815891055 315 LSPIAERLGCTLPQLAVAWCLRNEgvSSVLL--GSSTPEQLIENLGAIQ-VLPkmtSHVVNEIDNI 377
Cdd:PRK10376 226 LSDVAASLGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAElVLS---EEVLAELDGI 286
|
|
| |
