|
Name |
Accession |
Description |
Interval |
E-value |
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
71-395 |
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: 662.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITT 150
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 151 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGMA 230
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME---------------EIVRAFTHVINQGMA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY 310
Cdd:cd19141 146 MYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 311 SRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPK 390
Cdd:cd19141 226 SRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPK 305
|
....*
gi 315434249 391 LSSSI 395
Cdd:cd19141 306 LTPNI 310
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
70-408 |
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: 655.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 149
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGM 229
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPME---------------ETVRAMTHVINQGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 230 AMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 309
Cdd:cd19158 146 AMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 310 YSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLP 389
Cdd:cd19158 226 YSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLP 305
|
330
....*....|....*....
gi 315434249 390 KLSSSIIHEIDSILGNKPY 408
Cdd:cd19158 306 KLSSSIVHEIDSILGNKPY 324
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
70-407 |
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: 644.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 149
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGM 229
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPME---------------EIVRAMTHVINQGM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 230 AMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 309
Cdd:cd19159 146 AMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 310 YSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLP 389
Cdd:cd19159 226 SSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLP 305
|
330
....*....|....*...
gi 315434249 390 KLSSSIIHEIDSILGNKP 407
Cdd:cd19159 306 KMTSHVVNEIDNILRNKP 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
72-403 |
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: 631.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 72 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK 151
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 152 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGMAM 231
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPME---------------ETVRAMTYVINQGMAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 232 YWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYS 311
Cdd:TIGR01293 146 YWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 312 RASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKL 391
Cdd:TIGR01293 226 RATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKL 305
|
330
....*....|..
gi 315434249 392 SSSIIHEIDSIL 403
Cdd:TIGR01293 306 SSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
68-407 |
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: 627.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 68 TGMKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLV 147
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 148 ITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQ 227
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPME---------------EIVRAMTYVINQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI 307
Cdd:cd19160 146 GMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 PPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 387
Cdd:cd19160 226 PDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQV 305
|
330 340
....*....|....*....|
gi 315434249 388 LPKLSSSIIHEIDSILGNKP 407
Cdd:cd19160 306 LSQLTPQTVMEIDALLGNKP 325
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
70-402 |
0e+00 |
|
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) from Arabidopsis thaliana and Egeria densa are founding members of aldo-keto reductase family 6 member C1 (AKR6C1) and C2 (AKR6C2), respectively. KCAB, also called Shaker channel b-subunit, or K(+) channel subunit beta, or potassium voltage beta 1, or KV-beta1, or KAB1, is a probable accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.
Pssm-ID: 381369 [Multi-domain] Cd Length: 319 Bit Score: 515.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 149
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWGGKAE--TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQ 227
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATP---------------IEETVRAMNDLIDQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI 307
Cdd:cd19143 146 GKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 PPYSRASLKGYQWLKDkILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 387
Cdd:cd19143 226 PEGSRLALPGYEWLKD-RKEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEV 304
|
330
....*....|....*
gi 315434249 388 LPKLSSSIIHEIDSI 402
Cdd:cd19143 305 LPKLTPEVMEKIEAI 319
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
70-407 |
3.09e-165 |
|
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding member of aldo-keto reductase family 6 member B1 (AKR6B1). Hk protein, also called hyperkinetic, is a beta subunit of Shaker (Sh) K+ channels and shows high sequence homology to aldoketoreductase.
Pssm-ID: 381368 [Multi-domain] Cd Length: 325 Bit Score: 466.56 E-value: 3.09e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 149
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWGGKAEtERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGM 229
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIESVRASLRRLQLDYIDIVIIHKADPMCPME---------------EVVRAMSYLIDNGL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 230 AMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP 309
Cdd:cd19142 145 IMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLDPGISEETRRL 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 310 YSRASLKGY-----QWLKDKIlsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19142 225 VTKLSFKSSkykvgSDGNGIH--EETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNS 302
|
330 340
....*....|....*....|...
gi 315434249 385 IQVLPKLSSSIIHEIDSILGNKP 407
Cdd:cd19142 303 LQLLPKLNSAVMEELERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
79-395 |
1.30e-162 |
|
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: 458.98 E-value: 1.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFWGGKA 158
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 E-TERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19074 79 GpNDRGLSRKHIFESIHASLKRLQLDYVDIYYCHRYDPETPLE---------------ETVRAMDDLIRQGKILYWGTSE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEvQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKg 317
Cdd:cd19074 144 WSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT- 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 318 YQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAiqVLPKLSSSI 395
Cdd:cd19074 222 DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
70-407 |
6.08e-102 |
|
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440431 [Multi-domain] Cd Length: 316 Bit Score: 305.18 E-value: 6.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWvTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSL 146
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVI 225
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTP---------------IEETLGALDELV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARqfNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS 305
Cdd:COG0667 143 REGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYRR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 306 G--IPPYSRASLKGYQWlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:COG0667 220 GatFPEGDRAATNFVQG-------YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLA 292
|
330 340
....*....|....*....|....
gi 315434249 384 AIQVlpKLSSSIIHEIDSILGNKP 407
Cdd:COG0667 293 AADL--ELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
70-402 |
8.66e-91 |
|
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, Saccharopolyspora erythraea EryBII, and Streptomyces avermitilis aveBVIII are founding members of aldo-keto reductase family 12 member A1 (AKR12A1), B1 (AKR12B1), and C1(AKR12C1), respectively. TylCII acts as a NDP-hexose 2,3-enoyl reductase. EryBII is a mycarose/desosamine reductase involved in L-mycarose and D-desosamine production. aveBVIII functions as a dTDP-4-keto-6-deoxy-L-hexose-2,3-reductase.
Pssm-ID: 381313 [Multi-domain] Cd Length: 310 Bit Score: 276.76 E-value: 8.66e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVIT 149
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWG-GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVINQG 228
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLE---------------ETLRALDDLVRQG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 229 MAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP 308
Cdd:cd19087 142 KIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 309 P--YSRASLKGYQwlkDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 386
Cdd:cd19087 221 PesGRLVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALE 294
|
330
....*....|....*.
gi 315434249 387 VlpKLSSSIIHEIDSI 402
Cdd:cd19087 295 I--TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
70-402 |
1.44e-81 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 253.30 E-value: 1.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTwVTFG---------GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkg 140
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGggggffgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 141 wRRSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVR 219
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTP---------------LEETLR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 220 AMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIV 299
Cdd:cd19091 142 ALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 300 SGKY--DSGIPPYSRASLKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQ 377
Cdd:cd19091 221 SGKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQ 295
|
330 340
....*....|....*....|....*
gi 315434249 378 LMENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:cd19091 296 LEDNLGAAGL--SLTPEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
72-389 |
2.28e-79 |
|
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: 247.17 E-value: 2.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 72 YRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVY--AAGKAEVVLGNIIKK-KGWRRSSLVI 148
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 149 TTKI---FWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHVI 225
Cdd:cd19089 81 STKAgygMWPGP--YGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLE---------------ETMTALADAV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS 305
Cdd:cd19089 144 RSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 306 GIPPYSRAsLKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 385
Cdd:cd19089 222 GIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAAL 297
|
....
gi 315434249 386 QVLP 389
Cdd:cd19089 298 KNLD 301
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
79-400 |
1.22e-75 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 237.42 E-value: 1.22e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWV---TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IF 153
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 154 WGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYW 233
Cdd:cd19084 78 WDGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIHWPDPNTP---------------IEETAEALEKLKKEGKIRYI 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAysvarqFNLTPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDSG--IPPY- 310
Cdd:cd19084 143 GVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLPYC-RENGIGVLPYGPLAQGLLTGKYKKEptFPPDd 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 311 SRASLKGYQwlkdkilSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpK 390
Cdd:cd19084 216 RRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--E 286
|
330
....*....|
gi 315434249 391 LSSSIIHEID 400
Cdd:cd19084 287 LTEEELKEID 296
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
71-386 |
8.15e-72 |
|
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: 228.06 E-value: 8.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKK--KGWRrSSL 146
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTK---IFWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTH 223
Cdd:cd19151 80 IISTKagyTMWPGPY-GDWG-SKKYLIASLDQSLKRMGLDYVDIFYHHRPDPETP---------------LEETMGALDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKY 303
Cdd:cd19151 143 IVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSGIPPYSRASlKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:cd19151 221 LNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVG 296
|
...
gi 315434249 384 AIQ 386
Cdd:cd19151 297 ALD 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
82-402 |
1.81e-71 |
|
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: 227.45 E-value: 1.81e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 82 VSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-- 152
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 ---FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPM--EGDPFSSSKSRTFI-IEETVRAMTHVIN 226
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHWPDRYTPLfgGGYYTEPSEEEDSVsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 227 QGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG 306
Cdd:cd19094 159 AGKIRHIGLSNETPWGVMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 307 --IPPYSRASL-KGYQwlkdkilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLM 379
Cdd:cd19094 238 aaRPEGGRLNLfPGYM----------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLK 307
|
330 340
....*....|....*....|...
gi 315434249 380 ENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:cd19094 308 ENIDAFDV--PLSDELLAEIDAV 328
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
83-383 |
6.52e-71 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 222.78 E-value: 6.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTWvTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI-FWGGKAETE 161
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 162 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSM 241
Cdd:cd06660 79 SRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTP---------------VEETLEALNELVREGKIRYIGVSNWSAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 242 EIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwl 321
Cdd:cd06660 144 RLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARG------------------------ 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 322 kdkilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:cd06660 200 -----------------------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
71-392 |
1.06e-70 |
|
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381305 [Multi-domain] Cd Length: 312 Bit Score: 225.16 E-value: 1.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLGTWvTFGGQ------ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRS 144
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 145 SLVITTKIFW-GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTH 223
Cdd:cd19079 79 EVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKRLGTDYIDLYQIHRWDYETP---------------IEETLEALHD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKvEVQLPELFHKIGVGAMTWSPLACGIVSGKY 303
Cdd:cd19079 144 VVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-EREMIPLCEEEGIGVIPWSPLARGRLARPW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSGIP-PYSRASLKGYQWLKdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENI 382
Cdd:cd19079 223 GDTTErRRSTTDTAKLKYDY---FTEADKEIVDRVEE---VAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAV 296
|
330
....*....|
gi 315434249 383 GAIQVlpKLS 392
Cdd:cd19079 297 AALDI--KLS 304
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
75-400 |
5.53e-70 |
|
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: 223.25 E-value: 5.53e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 75 LGKSGLRVSCLGLGTWVtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSLV 147
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 148 ITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQ 227
Cdd:cd19081 80 IATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATP---------------LEETLGALNDLIRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI 307
Cdd:cd19081 144 GKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 PPySRASLKGYQWlkDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 387
Cdd:cd19081 224 DL-PGSTRRGEAA--KRYLNERGLRI---LDALDEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL 297
|
330
....*....|...
gi 315434249 388 lpKLSSSIIHEID 400
Cdd:cd19081 298 --RLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
85-403 |
2.08e-65 |
|
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: 210.63 E-value: 2.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvTFGGQ---ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETE 161
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 162 RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSM 241
Cdd:pfam00248 79 SGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTP---------------IEETWDALEELKKEGKIRAIGVSNFDAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 242 EIMEAYSVARqfnlTPPICEQAEYHMFqREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqwL 321
Cdd:pfam00248 144 QIEKALTKGK----IPIVAVQVEYNLL-RRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG--------E 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 322 KDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQvlPKLSSSIIHEIDS 401
Cdd:pfam00248 211 RRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDE 288
|
..
gi 315434249 402 IL 403
Cdd:pfam00248 289 LL 290
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
71-388 |
3.87e-64 |
|
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar proteins; Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ), also called GAP reductase, is a founding member of aldo-keto reductase family 14 member A1 (AKR14A1). It catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). It is also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo.
Pssm-ID: 381376 [Multi-domain] Cd Length: 309 Bit Score: 208.08 E-value: 3.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLV 147
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 148 ITTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHV 224
Cdd:cd19150 81 ISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLE---------------ETMGALDHA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 225 INQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYD 304
Cdd:cd19150 144 VRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 305 SGIPPYSRASLKGYqwLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19150 223 NGIPEGSRASKERS--LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGA 297
|
....
gi 315434249 385 IQVL 388
Cdd:cd19150 298 LDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
70-400 |
9.29e-60 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 197.90 E-value: 9.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSL 146
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTKI---FWGGKAETerGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTH 223
Cdd:PRK09912 93 IISTKAgydMWPGPYGS--GGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPME---------------ETASALAH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY 303
Cdd:PRK09912 156 AVQSGKALYVGISSYSPERTQKMVELLREWKI-PLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSGIPPYSRASLKG--YQWLKDKILSEEGRRQqakLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMEN 381
Cdd:PRK09912 235 LNGIPQDSRMHREGnkVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEEN 311
|
330
....*....|....*....
gi 315434249 382 IGAIQVLpKLSSSIIHEID 400
Cdd:PRK09912 312 VQALNNL-TFSTEELAQID 329
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
75-400 |
5.29e-55 |
|
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: 184.34 E-value: 5.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 75 LGKSGLRVSCLGLGTwVTFGGQ----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITT 150
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 151 KIFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQG 228
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTP---------------VEEVMRALDDLVRAG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 229 MAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGip 308
Cdd:cd19080 144 KVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 309 PYSRASLKGYQWLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVl 388
Cdd:cd19080 221 EEGRAGEAKGVTVGFGKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL- 296
|
330
....*....|..
gi 315434249 389 pKLSSSIIHEID 400
Cdd:cd19080 297 -TLSPEQLARLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
82-402 |
3.06e-52 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 176.62 E-value: 3.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 82 VSCLGLGTWV----TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFwggk 157
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 aetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19085 74 ---PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVP---------------LEETMEALEKLKEEGKIRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARqfnltpPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRAS 314
Cdd:cd19085 136 FGPAQLEEALDAGR------IDSNQLPYNLLWRA-IEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEdfpPGDARTR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 315 LKgyqwlkdkILSEEGRRQQAK--LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLS 392
Cdd:cd19085 209 LF--------RHFEPGAEEETFeaLEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELS 278
|
330
....*....|
gi 315434249 393 SSIIHEIDSI 402
Cdd:cd19085 279 PSVLERLDEI 288
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
72-401 |
3.72e-48 |
|
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: 166.68 E-value: 3.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 72 YRNLGKSGLRVSCLGLGTWV----TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLV 147
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 148 ITTK--IFWGGKAETE----------RGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIE 215
Cdd:cd19149 78 LATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETP---------------IE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 216 ETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnlTPPICeQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLA 295
Cdd:cd19149 143 ETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAG-----QLDII-QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 296 CGIVSGKYDSGippysRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASN 374
Cdd:cd19149 216 QGLLTGKITPD-----REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARK 290
|
330 340
....*....|....*....|....*..
gi 315434249 375 ADQLMENIGAIQVlpKLSSSIIHEIDS 401
Cdd:cd19149 291 PEQAEENAKAGDI--RLSAEDIATMRS 315
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
71-399 |
1.20e-46 |
|
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC is a founding member of aldo-keto reductase family 13 member A1 (AKR13A1). It catalyzes the reversible reduction of ketones to the respective alcohols using NADP(+) as a hydride donor. Rauvolfia serpentina PR is a founding member of aldo-keto reductase family 13 member D1 (AKR13D1). It catalyzes the NADPH-dependent reduction of the aldehyde perakine to yield the alcohol raucaffrinoline in the biosynthetic pathway of ajmaline in Rauvolfia, a key step in indole alkaloid biosynthesis. This family also includes Arabidopsis thaliana aldo-keto reductases, ALKR1-6.
Pssm-ID: 381302 [Multi-domain] Cd Length: 303 Bit Score: 162.38 E-value: 1.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLG----TWvtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSL 146
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTKifWG---GKAETERGL--SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAM 221
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVP---------------IEETVGAM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 222 THVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMFQREKVEVQLP---ELfhkiGVGAMTWSPLACG 297
Cdd:cd19076 139 AELVEEGKVRYIGLSEASADTIRRAHAVH-------PITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 298 IVSGKYDSgippysraslkgyqwlKDKILSEEGRRQQ-----------AKL-KELQAIAERLGCTLPQLAIAWCL-RNEG 364
Cdd:cd19076 208 FLTGAIKS----------------PEDLPEDDFRRNNprfqgenfdknLKLvEKLEAIAAEKGCTPAQLALAWVLaQGDD 271
|
330 340 350
....*....|....*....|....*....|....*
gi 315434249 365 VSSVlLGASNADQLMENIGAIQVlpKLSSSIIHEI 399
Cdd:cd19076 272 IVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
73-402 |
4.64e-46 |
|
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: 160.66 E-value: 4.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 73 RNLGKSGLRVSCLGLGTwVTFGGQ-----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLV 147
Cdd:cd19083 2 VKLGKSDIDVNPIGLGT-NAVGGHnlypnLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 148 ITTK---IFWGGKaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiieETVRAMTHV 224
Cdd:cd19083 79 IATKgahKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKA---------------EAVGALQEL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 225 INQGMAMYWGTSRWSSMEIMEAySVARQFNLTppiceQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYD 304
Cdd:cd19083 142 KDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 305 SGIppysraSLKGYQWLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENI 382
Cdd:cd19083 215 KDT------KFPDNDLRNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNL 288
|
330 340
....*....|....*....|
gi 315434249 383 GAIQVlpKLSSSIIHEIDSI 402
Cdd:cd19083 289 KALDV--TLTEEEIAFIDAL 306
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
81-400 |
5.68e-46 |
|
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR (EC 1.1.1.65) is the prototype of this family. It catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+), and is involved in the PLP salvage pathway.
Pssm-ID: 381319 [Multi-domain] Cd Length: 293 Bit Score: 160.09 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 81 RVSCLGLGTWvTFGGQI----TDEMAEQLMT---LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIf 153
Cdd:cd19093 1 EVSPLGLGTW-QWGDRLwwgyGEYGDEDLQAafdAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 154 wggkAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMegdpfsssksrtfiIEETVRAMTHVINQGMAMYW 233
Cdd:cd19093 78 ----APLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSQ--------------IEALMDGLADAVEEGLVRAV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY-DSGIPPYSR 312
Cdd:cd19093 140 GVSNYSADQLRRAHKALKERGV-PLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYsPENPPPGGR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 313 ASLKG-YQWLKDKILseegrrqqakLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIQVlpKL 391
Cdd:cd19093 219 RRLFGrKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWLIAKGVV--PIPGAKNAEQAEENAGALGW--RL 284
|
....*....
gi 315434249 392 SSSIIHEID 400
Cdd:cd19093 285 SEEEVAELD 293
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
79-403 |
3.55e-45 |
|
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: 158.17 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTW-VTFG-GQITD--EMAEqLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFW 154
Cdd:cd19078 1 GLEVSAIGLGCMgMSHGyGPPPDkeEMIE-LIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 ----GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMA 230
Cdd:cd19078 77 kidgGKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVP---------------IEEVAGTMKELIKEGKI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWSSMEIMEAYSVarqfnlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGI--- 307
Cdd:cd19078 142 RHWGLSEAGVETIRRAHAV------CPVTAVQSEYSMMWRE-PEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfd 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 PPYSRASLKGYqwlkdkilSEEGRRQQAKLKEL-QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 386
Cdd:cd19078 215 EGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAAD 286
|
330
....*....|....*..
gi 315434249 387 VlpKLSSSIIHEIDSIL 403
Cdd:cd19078 287 I--ELTPEELREIEDAL 301
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
82-403 |
1.66e-44 |
|
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: 156.68 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 82 VSCLGLGTWVTFGGQI---------TDEMAeqLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSsLVITTK- 151
Cdd:cd19102 1 LTTIGLGTWAIGGGGWgggwgpqddRDSIA--AIRAALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKc 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 152 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMA 230
Cdd:cd19102 76 gLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEP---------------IEEAWGALAELKEEGKV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWSSMEIMEAYSVARQFNLTPPiceqaeYHMFQREKVEVQLPelF---HKIGVgaMTWSPLACGIVSGKYDsgi 307
Cdd:cd19102 141 RAIGVSNFSVDQMKRCQAIHPIASLQPP------YSLLRRGIEAEILP--FcaeHGIGV--IVYSPMQSGLLTGKMT--- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 pPYSRASLKGYQWLK-DKILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 385
Cdd:cd19102 208 -PERVASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAA 286
|
330
....*....|....*...
gi 315434249 386 QVlpKLSSSIIHEIDSIL 403
Cdd:cd19102 287 DL--RLTPEELAEIEALL 302
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
80-384 |
7.01e-44 |
|
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: 153.02 E-value: 7.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 80 LRVSCLGLGTWV---TFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI--FW 154
Cdd:cd19086 1 LEVSEIGFGTWGlggDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNtpmegdpfsssksrTFIIEETVRAMTHVINQGMAMYWG 234
Cdd:cd19086 78 DGGPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDE--------------VLDNDELFEALEKLKQEGKIRAYG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 235 TSrwssmeiMEAYSVARQFNLTPPI-CEQAEYHMFQREKVEvqlpELFHKI---GVGAMTWSPLACGIVSGKydsgippy 310
Cdd:cd19086 144 VS-------VGDPEEALAALRRGGIdVVQVIYNLLDQRPEE----ELFPLAeehGVGVIARVPLASGLLTGK-------- 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434249 311 sraslkgyqwlkdkilseegrrqqaklkelqaiaerlgctLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19086 205 ----------------------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
85-402 |
1.05e-42 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 151.94 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIikkkGWRRSSLVITTKI-FWGGKaeterG 163
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKAnPGVGG-----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 164 LSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEI 243
Cdd:cd19075 76 LSPENVRKQLETSLKRLKVDKVDVFYLHAPDRSTP---------------LEETLAAIDELYKEGKFKEFGLSNYSAWEV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 244 MEAYSVARQFNLTPPICEQAEYHMFQReKVEvqlPELF-----HKIGVGAmtWSPLACGIVSGKYDSG--IPPYSR--AS 314
Cdd:cd19075 141 AEIVEICKENGWVLPTVYQGMYNAITR-QVE---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdPN 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 315 LKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTLPQLAIAWC-----LRNEGVSSVLLGASNADQLMENIGAIQVLP 389
Cdd:cd19075 215 NALGKLYRDRYWKPS---YFEALEKVEEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGP 291
|
330
....*....|...
gi 315434249 390 kLSSSIIHEIDSI 402
Cdd:cd19075 292 -LPEEVVKAIDEA 303
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
79-386 |
8.28e-42 |
|
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: 148.15 E-value: 8.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVTFGGQ----ITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFw 154
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMskdySDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 ggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWG 234
Cdd:cd19072 78 ------PDHLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNPSIP---------------IEETLRAMEELVEEGKIRYIG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 235 TSRWSSMEIMEAYSVARQfnlTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSgippysras 314
Cdd:cd19072 137 VSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGS--------- 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 315 lkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNADQLMENIGAIQ 386
Cdd:cd19072 204 -----------------------PLLDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
71-402 |
1.14e-40 |
|
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: 147.03 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 71 KYRNLGKSGLRVSCLGLGtwvtfGGQI-----TDEMAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrR 143
Cdd:cd19104 1 KYRRFGRTGLKVSELTFG-----GGGIgglmgRTTREEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 144 SSLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFA-NRPDPNTPMEGDPFSSSKSRTFiIEETVRAMT 222
Cdd:cd19104 73 AGPYITTKV---RLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLhNRIGDERDKPVGGTLSTTDVLG-LGGVADAFE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 223 HVINQGMAMYWGTSRWSSMEIME------AYSVARQF-NL--------TPPICEQAEYHmfqrekvevQLPELFHKIGVG 287
Cdd:cd19104 149 RLRSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVYyNLlnpsaaeaRPRGWSAQDYG---------GIIDAAAEHGVG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 288 AMTWSPLACGIVSGKYDSGIPPYSRAslkgyqwlkDKILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSS 367
Cdd:cd19104 220 VMGIRVLAAGALTTSLDRGREAPPTS---------DSDVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVST 286
|
330 340 350
....*....|....*....|....*....|....*
gi 315434249 368 VLLGASNADQLMENIGAIQVLPkLSSSIIHEIDSI 402
Cdd:cd19104 287 VLVGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
70-402 |
3.48e-39 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 143.46 E-value: 3.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwR 142
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 143 RSSLVITTKIfwGGKAET-------ERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGD---PFSSSKSrTF 212
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREALHDSLKRLQTDYLDLYQVHWPQRPTNCFGKlgySWTDSAP-AV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 213 IIEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWS 292
Cdd:PRK10625 156 SLLETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 293 PLACGIVSGKYDSGIPPY-SRASLKgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLG 371
Cdd:PRK10625 235 CLAFGTLTGKYLNGAKPAgARNTLF------SRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLG 308
|
330 340 350
....*....|....*....|....*....|.
gi 315434249 372 ASNADQLMENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:PRK10625 309 ATTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
70-385 |
4.24e-36 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 132.71 E-value: 4.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGlgtwvtFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVIT 149
Cdd:cd19105 1 MPYRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKIFWGGKAETerglsRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDpfsssksrtfiiEETVRAMTHVINQGM 229
Cdd:cd19105 73 TKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLN------------EELLEALEKLKKEGK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 230 AMYWGTSRWSSME--IMEA-----YSVAR-QFNltppiceqaeyHMFQREKVEVQLPELfHKIGVG--AMtwsplacgiv 299
Cdd:cd19105 136 VRFIGFSTHDNMAevLQAAiesgwFDVIMvAYN-----------FLNQPAELEEALAAA-AEKGIGvvAM---------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 300 sgkydsgippysraslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLM 379
Cdd:cd19105 194 ------------------------KTLA-GGYLQPALLSVLKA----KGFSLPQAALKWVLSNPRVDTVVPGMRNFAELE 244
|
....*.
gi 315434249 380 ENIGAI 385
Cdd:cd19105 245 ENLAAA 250
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
83-384 |
4.55e-36 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 133.83 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAA----GKAEVVLGNIIKKKGwRRSSLVITTKifwGG-- 156
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 157 ---KAETERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYW 233
Cdd:cd19082 76 dleDMSRSR-LSPEDIRADLEESLERLGTDYIDLYFLHRDDPSVP---------------VGEIVDTLNELVRAGKIRAF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFqrEKVEVQLP------------ELFHKIGVGAMTWSPLACGIVSG 301
Cdd:cd19082 140 GASNWSTERIAEANAYAKAHGLPGFAASSPQWSLA--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 302 KYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQAKLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMEN 381
Cdd:cd19082 218 RAAGGAEDDSE--------LRRVYYSEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDS 286
|
...
gi 315434249 382 IGA 384
Cdd:cd19082 287 LAA 289
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
83-384 |
1.32e-35 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 132.46 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTwVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI--- 152
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 --FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMA 230
Cdd:cd19752 79 prDPDGGPESPEGLSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTP---------------LEETLEAFNELVKAGKV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLacgiVS 300
Cdd:cd19752 144 RAIGASNFAAWRLERARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPL----LS 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 301 GKYDSgippysraslkgyqwlKDKILSEEGRRQ--QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQL 378
Cdd:cd19752 220 GAYTR----------------PDRPLPEQYDGPdsDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQL 283
|
....*.
gi 315434249 379 MENIGA 384
Cdd:cd19752 284 EENLAA 289
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
85-386 |
5.89e-34 |
|
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: 127.67 E-value: 5.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGT-WVTFG-GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKIfwGGKAETER 162
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKV--GRLPEDTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 163 GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPntpmegDPFSSSKSRTFIIEE------------------TVRAMTHV 224
Cdd:cd19090 77 DYSADRVRRSVEESLERLGRDRIDLLMIHDPER------VPWVDILAPGGALEAllelkeeglikhiglgggPPDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 225 INQGmamywgtsrwssmeIMEAYSVARQFNLtppICEQAEYHMFqrekvevqlpELFHKIGVGAMTWSPLACGIVSGKYD 304
Cdd:cd19090 151 IETG--------------DFDVVLTANRYTL---LDQSAADELL----------PAAARHGVGVINASPLGMGLLAGRPP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 305 SGIPPysraslkGYQWLKDkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19090 204 ERVRY-------TYRWLSP--------ELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAA 268
|
..
gi 315434249 385 IQ 386
Cdd:cd19090 269 AE 270
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
78-402 |
6.39e-34 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 127.09 E-value: 6.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 157
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 AeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPntpmegDPFsssksrtfiiEETVRAMTHVINQGMAMYWGTSR 237
Cdd:COG0656 72 H------GYDDTLAAFEESLERLGLDYLDLYLIHWPGP------GPY----------VETWRALEELYEEGLIRAIGVSN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREkvevqlPELF-----HKIGVGAmtWSPLACGivsgkydsgippysr 312
Cdd:COG0656 130 FDPEHLEELLAETG----VKPAVNQVELHPYLQQ------RELLafcreHGIVVEA--YSPLGRG--------------- 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 313 aslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLS 392
Cdd:COG0656 183 -----------KLLDDP---------VLAEIAEKHGKTPAQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDF--ELS 238
|
330
....*....|
gi 315434249 393 SSIIHEIDSI 402
Cdd:COG0656 239 DEDMAAIDAL 248
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
78-400 |
1.70e-33 |
|
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: 126.21 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWvtFGGQITDEMAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIfWG 155
Cdd:cd19138 7 DGTKVPALGQGTW--YMGEDPAKRAQEIEALraGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV-LP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 GKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRPdpntpmEGDPFsssksrtfiiEETVRAMTHVINQGMAMYWGT 235
Cdd:cd19138 81 SNA------SRQGTVRACERSLRRLGTDYLDLYLLHWR------GGVPL----------AETVAAMEELKKEGKIRAWGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 236 SRWSSMEIMEAYSVARQFNLTppiCEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysrasl 315
Cdd:cd19138 139 SNFDTDDMEELWAVPGGGNCA---ANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLAQG------------------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 316 kgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVlLGASNADQLMENIGAIQVlpKLSSSI 395
Cdd:cd19138 197 ------------GLLRRGLLENPTLKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEED 261
|
....*
gi 315434249 396 IHEID 400
Cdd:cd19138 262 LAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
79-403 |
2.20e-33 |
|
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: 126.65 E-value: 2.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVT----FGGqiTDEmAEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK- 151
Cdd:cd19148 1 DLPVSRIALGTWAIggwmWGG--TDE-KEAIETIhkALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 152 -IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMA 230
Cdd:cd19148 77 gLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHWPDPLVP---------------IEETAEALKELLDEGKI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWsSMEIMEAY-SVARQFNLTPPiceqaeYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKY--DSGI 307
Cdd:cd19148 142 RAIGVSNF-SPEQMETFrKVAPLHTVQPP------YNLFEREIEKDVLPYA-RKHNIVTLAYGALCRGLLSGKMtkDTKF 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 308 PPYS-RASLKGYQwlkdkilseEGRRQQ--AKLKELQAIA-ERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:cd19148 214 EGDDlRRTDPKFQ---------EPRFSQylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQLDAVDE 284
|
330 340
....*....|....*....|
gi 315434249 384 AIQVlpKLSSSIIHEIDSIL 403
Cdd:cd19148 285 VFGW--SLNDEDMKEIDAIL 302
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
79-387 |
4.64e-33 |
|
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: 124.99 E-value: 4.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvTFGGQIT-----DEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIF 153
Cdd:cd19137 1 GEKIPALGLGTW-GIGGFLTpdysrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 154 wggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMegdpfsssksrtfiiEETVRAMTHVINQGMAMYW 233
Cdd:cd19137 78 -------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPL---------------EETLSAMAEGVRQGLIRYI 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysra 313
Cdd:cd19137 136 GVSNFNRRLLEEAISKSQ----TPIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKTN----------- 200
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434249 314 slkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLgASNADQLMENIGAIQV 387
Cdd:cd19137 201 ------------------------RTLEEIAKNYGKTIAQIALAWLIQKPNVVAIPK-AGRVEHLKENLKATEI 249
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
70-361 |
5.44e-33 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 125.65 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 149
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLGEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TK--IFWGGKAETERG----LSRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEgdpfsssksrtfiIEETVRAMTH 223
Cdd:COG4989 81 TKcgIRLPSEARDNRVkhydTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDP--LMD-------------PEEVAEAFDE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYWGTSRWSSMeimeaysvarQFNL------TPPICEQAEYHMFQREKVE------VQLpelfHKIGVgaMTW 291
Cdd:COG4989 146 LKASGKVRHFGVSNFTPS----------QFELlqsaldQPLVTNQIELSLLHTDAFDdgtldyCQL----NGITP--MAW 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 292 SPLAcgivSGKYDSGippysraslkgyqwlkdkiLSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLR 361
Cdd:COG4989 210 SPLA----GGRLFGG-------------------FDEQFPRLRAALDE---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
77-387 |
8.07e-33 |
|
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: 124.98 E-value: 8.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 77 KSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK---IF 153
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 154 WGGKAETERG---LSRKHIIEGLKASLERLQLEYVDVVFANRPDPntPMEgdpfsssksrtfiIEETVRAMTHVINQGMA 230
Cdd:cd19092 81 GDDPRPGRIKhydTSKEHILASVEGSLKRLGTDYLDLLLLHRPDP--LMD-------------PEEVAEAFDELVKSGKV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTS--RWSSMEIMEAYS----VARQ--FNL--TPPICE-QAEYHMfqrekvevqlpelFHKIGVgaMTWSPLACGIV 299
Cdd:cd19092 146 RYFGVSnfTPSQIELLQSYLdqplVTNQieLSLlhTEAIDDgTLDYCQ-------------LLDITP--MAWSPLGGGRL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 300 SGkydsgippysraslkgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLM 379
Cdd:cd19092 211 FG--------------------------GFDERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIR 264
|
....*...
gi 315434249 380 ENIGAIQV 387
Cdd:cd19092 265 SAVKALDI 272
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
70-385 |
5.84e-31 |
|
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: 119.96 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSL 146
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGgvfGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmegdpFSSSKSRtfIIEETVRAMTHVI 225
Cdd:cd19163 78 YLATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIE---------FAPSLDQ--ILNETLPALQKLK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTS-------RwssmEIMEAYSVARQFNLTppiceQAEYHMFQREKVEvqLPELFHKIGVGAMTWSPLACGI 298
Cdd:cd19163 147 EEGKVRFIGITgypldvlK----EVLERSPVKIDTVLS-----YCHYTLNDTSLLE--LLPFFKEKGVGVINASPLSMGL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 299 VSgkyDSGIPPYSRASlkgyQWLKDKIlseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQL 378
Cdd:cd19163 216 LT---ERGPPDWHPAS----PEIKEAC------------AKAAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENL 276
|
....*..
gi 315434249 379 MENIGAI 385
Cdd:cd19163 277 RKNLEAA 283
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
83-384 |
2.17e-30 |
|
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: 117.34 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTWVTFG--GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIkkKGWRRSSLVITTKI--FWGGkA 158
Cdd:cd19095 1 SVLGLGTSGIGRvwGVPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRAL--AGLRRDDLFIATKVgtHGEG-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 ETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmegdpfsssksrtfIIEETVRAMTHVINQGMAMYWGTSRw 238
Cdd:cd19095 76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHGPSDDE---------------LTGEVLETLEDLKAAGKVRYIGVSG- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 239 SSMEIMEAYSvarqfnlTPPI-CEQAEYHMFQREKVEVqLPELfHKIGVGAMTWSPLAcgivsgkydSGIPPYSRASLKG 317
Cdd:cd19095 140 DGEELEAAIA-------SGVFdVVQLPYNVLDREEEEL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPL 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315434249 318 YQWLKDKilseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19095 202 YADYARR---------------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
70-402 |
3.24e-30 |
|
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: 118.70 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSL 146
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 147 VITTKifWGGKAETERGL-----SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAM 221
Cdd:cd19144 79 FLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTP---------------IEKTVAAM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 222 THVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMF--QREKVEVQLPELFHKIGVGAMTWSPLACGI 298
Cdd:cd19144 142 AELVQEGKIKHIGLSECSAETLRRAHAVH-------PIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGF 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 299 VSGKYDS-----------GIPPYSRASLKGYQWLKDKIlseegrrqqaklkelQAIAERLGCTLPQLAIAWCLRNEGVSS 367
Cdd:cd19144 215 LTGAIRSpddfeegdfrrMAPRFQAENFPKNLELVDKI---------------KAIAKKKNVTAGQLTLAWLLAQGDDII 279
|
330 340 350
....*....|....*....|....*....|....*
gi 315434249 368 VLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:cd19144 280 PIPGTTKLKRLEENLGALKV--KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
73-399 |
1.75e-29 |
|
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: 116.38 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 73 RNLGKSGLRVSCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVIT 149
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAL--KDGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 150 TKI---FWGGKAETERGlSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVIN 226
Cdd:cd19145 81 TKFgihEIGGSGVEVRG-DPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVP---------------IEITMGELKKLVE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 227 QGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGK--- 302
Cdd:cd19145 145 EGKIKYIGLSEASADTIRRAHAVH-------PITAvQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKakl 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 303 --------YDSGIPPYSRASLKgyqwlKDKILSEegrrqqaklkELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGAS 373
Cdd:cd19145 217 eellensdVRKSHPRFQGENLE-----KNKVLYE----------RVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTT 280
|
330 340
....*....|....*....|....*.
gi 315434249 374 NADQLMENIGAIQVlpKLSSSIIHEI 399
Cdd:cd19145 281 KIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
78-400 |
5.73e-29 |
|
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: 114.64 E-value: 5.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLG----TWVtfGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEV---VLGNIIKKKGWRRSSLVITT 150
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 151 KifwGGKAET--ERGLSRKHIIEGLKASLERL-QLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQ 227
Cdd:cd19077 79 K---GGLDPDtlRPDGSPEAVRKSIENILRALgGTKKIDIFEPARVDPNVP---------------IEETIKALKELVKE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWSSMEIMEAYSVArqfnltPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DS 305
Cdd:cd19077 141 GKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLTGRIksLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 306 GIPPY-SRASLkgyqwlkDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV-LLGASNADQLMENIG 383
Cdd:cd19077 215 DIPEGdFRRHL-------DRFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLK 287
|
330
....*....|....*..
gi 315434249 384 AIQVlpKLSSSIIHEID 400
Cdd:cd19077 288 AANV--ELTDEELKEIN 302
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
70-382 |
7.82e-27 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 110.29 E-value: 7.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 70 MKYRNLGKSGLRVSCLGLGTWvtfGGQITD-EMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVI 148
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 149 TTKIfwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVF---ANRPD--PNTPMEGDPFsssksrtfiieETVRAMth 223
Cdd:COG1453 73 ATKL-------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLihgLNTEEdlEKVLKPGGAL-----------EALEKA-- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 vINQGMAMYWGtsrWSS-------MEIMEAY---SVARQFNLtppiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSP 293
Cdd:COG1453 133 -KAEGKIRHIG---FSThgsleviKEAIDTGdfdFVQLQYNY-----------LDQDNQAGEEALEAAAEKGIGVIIMKP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 294 LACGivsgkydsgippysraslkgyqwlkdkilseegrrqqaKLKELQAIAERLGC---TLPQLAIAWCLRNEGVSSVLL 370
Cdd:COG1453 198 LKGG--------------------------------------RLANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLS 239
|
330
....*....|..
gi 315434249 371 GASNADQLMENI 382
Cdd:COG1453 240 GMSTPEQLDENL 251
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
85-384 |
1.17e-26 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti isatin reductase and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381299 [Multi-domain] Cd Length: 243 Bit Score: 106.97 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergL 164
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19073 69 RPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVP---------------LEETLGALKELKEAGKVKSIGVSNFTIELLE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAYSVARqfnlTPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkydsgippysraslkgyqwlk 322
Cdd:cd19073 134 EALDISP----LPIAVNQVEFHPFlyQAELLEYCRE---NDIVITA--YSPLA--------------------------- 177
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 323 dkilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENIGA 384
Cdd:cd19073 178 --------RGEVLRDPVIQEIAEKYDKTPAQVALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
85-390 |
2.64e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 101.06 E-value: 2.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTwVTFG---------GQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKgwrrSSLVITTKIfwg 155
Cdd:cd19097 3 LALGT-AQFGldygianksGKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 GKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmegDPFSSSKSrtfIIEetvrAMTHVINQGMAMYWGT 235
Cdd:cd19097 73 PPLKEDKKEDEAAIEASVEASLKRLKVDSLDGLLLHNPD-------DLLKHGGK---LVE----ALLELKKEGLIRKIGV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 236 SrwssmeimeAYSVarqfnltppicEQAEYhMFQREKVE-VQLPelfhkigVGAMTWSPLACGIVSGKYDSGIPPYSRaS 314
Cdd:cd19097 139 S---------VYSP-----------EELEK-ALESFKIDiIQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR-S 189
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 315 --LKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPK 390
Cdd:cd19097 190 vfLQGLLLMEPDKLPAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
79-403 |
2.69e-24 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 102.50 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGT------WVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI 152
Cdd:cd19146 8 GVRVSPLCLGAmsfgeaWKSMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 FWGGK-AETER------GLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmegdpFSSSksrtfiIEETVRAMTHVI 225
Cdd:cd19146 87 TTGYRrGGPIKiksnyqGNHAKSLRLSVEASLKKLQTSYIDILYVHWWD---------YTTS------IPELMQSLNHLV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHM----FQREKVEVQLPElfhkiGVGAMTWSPLAcgivSG 301
Cdd:cd19146 152 AAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLG----QG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 302 KYDSGIPPYSRASLKGYQWLKdkilSEEGRRQQAKLKElqaIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMEN 381
Cdd:cd19146 223 QFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGN 295
|
330 340
....*....|....*....|..
gi 315434249 382 IGAIQVlpKLSSSIIHEIDSIL 403
Cdd:cd19146 296 IEALGI--SLSDEEIQEIEDAY 315
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
82-384 |
3.25e-24 |
|
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: 100.37 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 82 VSCLGLGTW-----VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEvvlgNIIKK--KGWRrSSLVITTKIFW 154
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNE----RLIAEalHPYP-DDVVIATKGGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 --GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMY 232
Cdd:cd19088 76 vrTGPGWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVP---------------FEEQLGALAELQDEGLIRH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 233 WGTSRWSSMEIMEAYSVARqfnltppI-CEQAEYHMFQREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippys 311
Cdd:cd19088 141 IGLSNVTVAQIEEARAIVR-------IvSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLG---------------- 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 312 raslkgyqwlkdkilseeGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19088 196 ------------------GGDLAQPGGLLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
85-400 |
3.59e-24 |
|
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: 100.25 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 164
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWP-------TDH 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDpfsssksrtFIIEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19071 69 GYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGGSK---------EARLETWRALEELVDEGLVRSIGVSNFNVEHLE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAYSVARqfnlTPPICEQAEYHMF--QREkvevqLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlk 322
Cdd:cd19071 140 ELLAAAR----IKPAVNQIELHPYlqQKE-----LVEFCKEHGIVVQAYSPLG--------------------------- 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 323 dkilseEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 400
Cdd:cd19071 184 ------RGRRPLLDDPVLKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
79-402 |
4.47e-24 |
|
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: 100.03 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGka 158
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPDN-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 etergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRW 238
Cdd:cd19140 75 -----YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVP---------------LAETLGALNEAQEAGLARHIGVSNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 239 SSMEIMEAYSVArqfnlTPPI-CEQAEYHMF--QRekvevQLPELFHKIGVGAMTWSPLACGIVsgkydsgippysrasl 315
Cdd:cd19140 135 TVALLREAVELS-----EAPLfTNQVEYHPYldQR-----KLLDAAREHGIALTAYSPLARGEV---------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 316 kgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVsSVLLGASNADQLMENIGAIQVlpKLSSSI 395
Cdd:cd19140 189 -----LKDPV--------------LQEIGRKHGKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEE 246
|
....*..
gi 315434249 396 IHEIDSI 402
Cdd:cd19140 247 MARIAAL 253
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
72-189 |
9.14e-24 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 98.71 E-value: 9.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 72 YRNLGKSGLRVSCLGLGTWVTfgGQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTK 151
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPL--GRLSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
90 100 110
....*....|....*....|....*....|....*...
gi 315434249 152 IfwggkaeTERglSRKHIIEGLKASLERLQLEYVDVVF 189
Cdd:cd19100 74 T-------GAR--DYEGAKRDLERSLKRLGTDYIDLYQ 102
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
72-403 |
1.03e-23 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 100.62 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 72 YRNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 148
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGA-SPLGsvfGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 149 TTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmegdpFSSSKSrtfIIEETVRAMTHVINQG 228
Cdd:PLN02587 80 STKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIE---------FGSLDQ---IVNETIPALQKLKESG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 229 MAMYWGTSRwSSMEIMEaYSVARqfnlTPP-----ICEQAEYHMFQREKVEVqLPELFHKiGVGAMTWSPLACGIVSgky 303
Cdd:PLN02587 145 KVRFIGITG-LPLAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL-LPYLKSK-GVGVISASPLAMGLLT--- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSGIPPYSRASLKgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:PLN02587 214 ENGPPEWHPAPPE----LK------SACAAAATHCKEK------GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVA 277
|
330 340
....*....|....*....|..
gi 315434249 384 AIQVLPKLS--SSIIHEIDSIL 403
Cdd:PLN02587 278 AATELETSGidEELLSEVEAIL 299
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
73-395 |
1.26e-22 |
|
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: 96.84 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 73 RNLGKSGLRVSCLGLGTwVTFGGQITDEM----AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVI 148
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLeqdeAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 149 TTKIFWGGKAETErgLSRKHIIEGLKASLERLQLEYVDVVFANrpdpntPME-GDPFSssksrtfIIEETVRAMTHVINQ 227
Cdd:cd19153 82 ATKVGRYRDSEFD--YSAERVRASVATSLERLHTTYLDVVYLH------DIEfVDYDT-------LVDEALPALRTLKDE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWsSMEIMEaySVARQFNLTPPICEQAEYHM-FQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKydsG 306
Cdd:cd19153 147 GVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ---G 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 307 IPPYSRAS--LKGYQWLKDKILSEEGRrqqaklkelqaiaerlgcTLPQLAIAWCLRNE-GVSSVLLGASNADQLMENIG 383
Cdd:cd19153 221 PPPWHPASgeLRHYAAAADAVCASVEA------------------SLPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLA 282
|
330
....*....|..
gi 315434249 384 AIQVLPKLSSSI 395
Cdd:cd19153 283 AVDAVASLGAAI 294
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
85-384 |
1.02e-21 |
|
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381388 [Multi-domain] Cd Length: 290 Bit Score: 94.35 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTwVTFG--GQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI-------FWG 155
Cdd:cd19162 3 LGLGA-ASLGnlARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 GKAETER--GLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmegdpfsssksrTFIIEETVRAMTHVINQGM--AM 231
Cdd:cd19162 80 RPAGADRrfDFSADGIRRSIEASLERLGLDRLDLVFLHDPDRHL-------------LQALTDAFPALEELRAEGVvgAI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 232 YWGTSRWSsmeimEAYSVARQFNLTpPICEQAEYHMFQREKVEVQLPELFHKiGVGAMTWSPLACGIVsgkyDSGIPPYS 311
Cdd:cd19162 147 GVGVTDWA-----ALLRAARRADVD-VVMVAGRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAGD 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 312 RASlkgYQWLKDKILseegrrqqAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 384
Cdd:cd19162 216 RYD---YRPATPEVL--------ARARRLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
85-387 |
2.14e-21 |
|
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: 93.83 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTwVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIFWGGKAETE 161
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 162 RGLSRKHII--------------EGLKA----SLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRTfiieETVRAMTH 223
Cdd:cd19152 80 VEPTFEPGFwnplpfdavfdysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESDEHFAQAIK----GAFRALEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYW--GTSRWSSME----------IMeaysVARQFNLTppicEQAEYHMFqrekvevqLPELF-HKIGVgamt 290
Cdd:cd19152 156 LREEGVIKAIglGVNDWEVILrileeadldwVM----LAGRYTLL----DHSAAREL--------LPECEkRGVKV---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 291 wsplacgIVSGKYDSGIppysrasLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLL 370
Cdd:cd19152 216 -------VNAGPFNSGF-------LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAP 281
|
330
....*....|....*..
gi 315434249 371 GASNADQLMENIGAIQV 387
Cdd:cd19152 282 GASSPERVEENVALLAT 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
80-382 |
5.45e-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: 381325 [Multi-domain] Cd Length: 316 Bit Score: 92.77 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 80 LRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGN----IIKKKGWRRSSLVITTKifwG 155
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---A 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 G----------------KAETERGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRPdpntPMEgdpFSS 206
Cdd:cd19099 78 GyipgdgdeplrplkylEEKLGRGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNP----EEQ---LLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 207 SKSRTF--IIEETVRAMTHVINQGMAMYWGTSRWSsmeIMEAYSVARQFNLTPPICEQAE-----YHMFqreKVeVQLPe 279
Cdd:cd19099 151 LGEEEFydRLEEAFEALEEAVAEGKIRYYGISTWD---GFRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 280 lFHKIGVGAMT----WSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLA 355
Cdd:cd19099 223 -LNLLEPEALTekntVKGEALSLLEAAKELGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRA 288
|
330 340
....*....|....*....|....*..
gi 315434249 356 IAWCLRNEGVSSVLLGASNADQLMENI 382
Cdd:cd19099 289 LQFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
83-384 |
2.22e-20 |
|
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S oxidoreductase that belongs to aldo-keto reductase (AKR) superfamily. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381322 [Multi-domain] Cd Length: 255 Bit Score: 89.93 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTW---VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGgkae 159
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 160 teRGLSRKHIIEGLKASLERLQLEYVDvVFA----NRPD-PNTPMEGDPFSssksrtFII----EETVRAM---TH---- 223
Cdd:cd19096 75 --SVKSAEDFRRILEESLKRLGVDYID-FYLlhglNSPEwLEKARKGGLLE------FLEkakkEGLIRHIgfsFHdspe 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYwgtsRWSSMEImeaysvarQFNLtppiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgky 303
Cdd:cd19096 146 LLKEILDSY----DFDFVQL--------QYNY-----------LDQENQAGRPGIEYAAKKGMGVIIMEPLKGG------ 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 dsgippysraslkgyqwlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIG 383
Cdd:cd19096 197 ----------------------------GLANNPPEALAILCGAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIA 248
|
.
gi 315434249 384 A 384
Cdd:cd19096 249 A 249
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
77-402 |
5.33e-20 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 89.78 E-value: 5.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 77 KSGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITT 150
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 151 KIFWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRTFII----EETVRAMTHVIN 226
Cdd:cd19154 77 KLWTHE-------HAPEDVEEALRESLKKLQLEYVDLYLIHAPAAFKDDEGESGTMENGMSIHDavdvEDVWRGMEKVYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 227 QGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsGKYDSG 306
Cdd:cd19154 150 EGLTKAIGVSNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------GSPGRA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 307 IPPYSRASLKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQ 386
Cdd:cd19154 217 NFTKSTGVSPAPNLLQDPI--------------VKAIAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENFNIFD 280
|
330
....*....|....*.
gi 315434249 387 VlpKLSSSIIHEIDSI 402
Cdd:cd19154 281 F--SLSEEDMATLEEI 294
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
84-382 |
7.62e-19 |
|
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: 86.04 E-value: 7.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 84 CLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVY----AAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAE 159
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 160 TERglsrkhIIEGLKASLERLQLEYVDVVFANRP---DPNTpmEGDPFSS---SKSRTFIIEETVRAMTHVINQGMAMYW 233
Cdd:cd19128 74 PEN------VKEQLLITLQDLQLEYLDLFLIHWPlafDMDT--DGDPRDDnqiQSLSKKPLEDTWRAMEQCVDEKLTKNI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgivsGKYDSGippysr 312
Cdd:cd19128 146 GVSNYSTKLLTDLLNYCK----IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYGDG------ 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315434249 313 aslkgyqwlKDKILSEegrrqqaklKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASNADQLMENI 382
Cdd:cd19128 207 ---------NLTFLND---------SELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
83-390 |
1.04e-17 |
|
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: 83.14 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 83 SCLGLGTwVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIfwgGK-- 157
Cdd:cd19161 1 SELGLGT-AGLGNlytAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRll 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 --AETERGL-----------------SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTpmEGDPFSSSKSRTFiIEETV 218
Cdd:cd19161 75 kpAREGSVPdpngfvdplpfeivydySYDGIMRSFEDSLQRLGLNRIDILYVHDIGVYT--HGDRKERHHFAQL-MSGGF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 219 RAMTHVINQGM--AMYWGTSRWSSM-EIMeaysvaRQFNLTppiCE--QAEYHMFQREKVEVQLPELfHKIGVGAmtwsp 293
Cdd:cd19161 152 KALEELKKAGVikAFGLGVNEVQIClEAL------DEADLD---CFllAGRYSLLDQSAEEEFLPRC-EQRGTSL----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 294 lacgIVSGKYDSGIPPYSRASLKGYQWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGAS 373
Cdd:cd19161 217 ----VIGGVFNSGILATGTKSGAKFNYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGAR 286
|
330
....*....|....*...
gi 315434249 374 NADQLMENIGAIQ-VLPK 390
Cdd:cd19161 287 NPAQLRQNVEAFQtDIPE 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
87-360 |
2.32e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 82.00 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 87 LGTW----------VTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGG 156
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 157 kaeteRGLSRKHIIEGLKASLERLQLEYVDVVFANRPDP---NTPMEGDPFSSSKSRtfiieetvramtHVinqgmamyw 233
Cdd:cd19103 87 -----AGQSADPVADMLEGSLARLGTDYIDIYWIHNPADverWTPELIPLLKSGKVK------------HV--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 234 GTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSR 312
Cdd:cd19103 141 GVSNHNLAEIKRANEILAKAGV-SLSAVQNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGS 219
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 315434249 313 ASLKGYQWLKDKIlseegRRQQAKLKElqaIAERLGCTLPQLAIAWCL 360
Cdd:cd19103 220 GRAETYNPLLPQL-----EELTAVMAE---IGAKHGASIAQVAIAWAI 259
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
85-382 |
8.19e-16 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 76.64 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 164
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 srkhiiEGLKASLERLQLEYVDVVFANRPdpnTPMEGdpfsssksrTFIieETVRAMTHVINQGMAMYWGTSRWSS---M 241
Cdd:cd19131 84 ------RAFDESLRKLGLDYVDLYLIHWP---VPAQD---------KYV--ETWKALIELKKEGRVKSIGVSNFTIehlQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 242 EIMEAYSVArqfnltpPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyq 319
Cdd:cd19131 144 RLIDETGVV-------PVVNQIELHprFQQRE-----LRAFHAKHGIQTESWSPLGQGGL-------------------- 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 320 wLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 382
Cdd:cd19131 192 -LSDPVIGE--------------IAEKHGKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
78-365 |
8.62e-16 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 76.98 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWvTFGGQITDEMAEQLMtlayDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 157
Cdd:cd19135 9 NGVEMPILGLGTS-HSGGYSHEAVVYALK----ECGYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPDPNtpmegdpfSSSKSRTFIIEETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19135 80 YGYES------TKQAFEASLKRLGVDYLDLYLLHWPDCP--------SSGKNVKETRAETWRALEELYDEGLCRAIGVSN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSS---MEIMEAYSVarqfnltPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysras 314
Cdd:cd19135 146 FLIehlEQLLEDCSV-------VPHVNQVEFHPFQNPV---ELIEYCRDNNIVFEGYCPLA------------------- 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434249 315 lkgyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGV 365
Cdd:cd19135 197 -------KGKALEEP---------TVTELAKKYQKTPAQILIRWSIQNGVV 231
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
86-408 |
9.10e-16 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 76.89 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 86 GLGTWVTFGGQIT-DEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKaetergl 164
Cdd:cd19120 10 GTGTAWYKSGDDDiQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 srkHIIEGLKASLERLQLEYVDVVFANrpdpntpmegDPFsSSKSRTFIIEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19120 80 ---DPREALRKSLAKLGVDYVDLYLIH----------SPF-FAKEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAYSVARqfnlTPPICEQAEYHMFqrekVEVQLPEL--FH-KIGVGAMTWSPLAcgivsgkydsgipPYSRaslkgyqwl 321
Cdd:cd19120 146 ELLDTAK----IKPAVNQIEFHPY----LYPQQPALleYCrEHGIVVSAYSPLS-------------PLTR--------- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 322 kdkilseegRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIqvLPKLSSSIIHEIDS 401
Cdd:cd19120 196 ---------DAGGPLDPVLEKIAEKYGVTPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDK 262
|
....*..
gi 315434249 402 ILGNKPY 408
Cdd:cd19120 263 AGKQKHF 269
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
77-382 |
1.39e-15 |
|
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: 76.62 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 77 KSGLRVSCLGLGTWVTFGGQITDEMAEQLmTLAYDNginlFDTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIfW 154
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPGVVGNAVKTAI-KEGYRH----IDCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAETERglsrkhIIEGLKASLERLQLEYVDVV-----FANRPDPNTPMEGDPFSSSksrtfiIEETVRAMTHVINQGM 229
Cdd:cd19125 79 CTDHAPED------VPPALEKTLKDLQLDYLDLYlihwpVRLKKGAHMPEPEEVLPPD------IPSTWKAMEKLVDSGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 230 AMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsgkydsGIPp 309
Cdd:cd19125 147 VRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---KLHEFCKSKGIHLSAYSPL-----------GSP- 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 310 ysraslkGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNADQLMENI 382
Cdd:cd19125 208 -------GTTWVKKNVLKDP---------IVTKVAEKLGKTPAQVALRWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
79-408 |
6.03e-15 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 74.84 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVTfggqITDEMAEQLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKI 152
Cdd:cd19111 1 GFPMPVIGLGTYQS----PPEEVRAAVDY-ALFVGYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 fwggkaeTERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRTfiIEETVRAMTHVINQGMAMY 232
Cdd:cd19111 71 -------PPVYLEFKDTEKSLEKSLENLKLPYVDLYLIHHPCGFVNKKDKGERELASSD--VTSVWRAMEALVSEGKVKS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 233 WGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF--QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkyDSGIPPY 310
Cdd:cd19111 142 IGLSNFNPRQINKILAYAK----VKPSNLQLECHAYlqQRELRKFCNK---KNIVVTA--YAPLG--------SPGRANQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 311 SRASLKgYQWLKD-KILseegrrqqaklkelqAIAERLGCTLPQLAIAWCL-RNEGvssVLLGASNADQLMENIGAIQVl 388
Cdd:cd19111 205 SLWPDQ-PDLLEDpTVL---------------AIAKELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF- 264
|
330 340
....*....|....*....|
gi 315434249 389 pKLSSSIIHEIDSILGNKPY 408
Cdd:cd19111 265 -ELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
79-382 |
1.29e-14 |
|
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: 73.38 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGK 157
Cdd:cd19133 6 GVEMPILGFGVF-----QIPDpEECERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 AETERglsrkhIIEGLKASLERLQLEYVDVVFANRPdpntpmEGDpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19133 77 AGYEK------AKKAFERSLKRLGLDYLDLYLIHQP------FGD-----------VYGAWRAMEELYKEGKIRAIGVSN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSvarqFNLTPPICEQAEYHMFqREKVEVQlpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkg 317
Cdd:cd19133 134 FYPDRLVDLIL----HNEVKPAVNQIETHPF-NQQIEAV--EFLKKYGVQIEAWGPFA---------------------- 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315434249 318 yqwlkdkilseEGRRQQAKLKELQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNADQLMENI 382
Cdd:cd19133 185 -----------EGRNNLFENPVLTEIAEKYGKSVAQVILRW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
85-402 |
2.24e-14 |
|
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: 73.21 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWVTFGGQitdemAEQLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETEr 162
Cdd:cd19123 15 LGLGTWKSKPGE-----VGQAVKQALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 163 glsrkHIIEGLKASLERLQLEYVDVVF-----ANRPDPNTPMEGDPFSSSKSRTfiIEETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19123 87 -----DVLPALEKTLADLQLDYLDLYLmhwpvALKKGVGFPESGEDLLSLSPIP--LEDTWRAMEELVDKGLCRHIGVSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARqfnlTPPICEQAEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgivsgkydSGIPPYSRA 313
Cdd:cd19123 160 FSVKKLEDLLATAR----IKPAVNQVELHPY------LQQPELLafcrDN-GIHLTAYSPLG---------SGDRPAAMK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 314 SLKGYQWLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENIGAIQVlpKLS 392
Cdd:cd19123 220 AEGEPVLLEDPVINK--------------IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELD 280
|
330
....*....|
gi 315434249 393 SSIIHEIDSI 402
Cdd:cd19123 281 ASDMATIAAL 290
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
81-403 |
2.90e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 73.01 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 81 RVSCLGLGTWVTFGG---QITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGW---RRSSLVITTKIFW 154
Cdd:cd19101 1 TISRVINGMWQLSGGhggIRDEDAAVRAMAAYVDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAETergLSRKHIIEGLKASLERLQLEYVDVV---FANRPDPNtpmegdpfsssksrtFIieETVRAMTHVINQGMAM 231
Cdd:cd19101 79 DPGELT---MTRAYVEAAIDRSLKRLGVDRLDLVqfhWWDYSDPG---------------YL--DAAKHLAELQEEGKIR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 232 YWG-----TSRWSsmEIMEAysvarqfnLTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKY--- 303
Cdd:cd19101 139 HLGltnfdTERLR--EILDA--------GVPIVSNQVQYSLLDR-RPENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgv 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 -DSGIPPYSRASLKGYQWLKDKILSEEGrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENI 382
Cdd:cd19101 208 pEPTGPALETRSLQKYKLMIDEWGGWDL--FQELLRTLKAIADKHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNV 285
|
330 340
....*....|....*....|.
gi 315434249 383 GAIQVlpKLSSSIIHEIDSIL 403
Cdd:cd19101 286 RAFSF--RLDDEDRAAIDAVL 304
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
85-382 |
4.38e-14 |
|
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: 71.81 E-value: 4.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkAETERGL 164
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKhiIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFsssksrtfiieetvRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19134 81 TAS--QAACRASLERLGLDYVDLYLIHWPAGREGKYVDSW--------------GGLMKLREEGLARSIGVSNFTAEHLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAysvarqFNLT--PPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqw 320
Cdd:cd19134 145 NL------IDLTffTPAVNQIELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG----------------------- 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 321 lkdkilseegrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 382
Cdd:cd19134 191 ------------RLLDNPAVTAIAAAHGRTPAQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
79-299 |
7.18e-14 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 70.93 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVTFGGqitDEMAEQLMTlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKA 158
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG---DETERAVQT-ALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 ETERGLSrkhiieGLKASLERLQLEYVDVVFANRPDPNTpmegdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRW 238
Cdd:cd19126 78 RARRTED------AFQESLDRLGLDYVDLYLIHWPGKDK----------------FIDTWKALEKLYASGKVKAIGVSNF 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 239 SSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGIV 299
Cdd:cd19126 136 QEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRGYCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
77-189 |
1.33e-13 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 70.77 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 77 KSGLRVSCLGLGTwvtFGGQITDEMAE----QLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKK--KGWRRSSLVITT 150
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDPESippvDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 315434249 151 KIfwGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVF 189
Cdd:cd19164 85 KV--GRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVY 121
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
79-381 |
1.73e-13 |
|
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: 70.63 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTKI 152
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 FWGGkaeterglSRKHIIEG-LKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRTFIIEETV------RAMTHVI 225
Cdd:cd19155 79 PPGG--------NRREKVEKfLLKSLEKLQLDYVDLYLIHFPVGSLSKEDDSGKLDPTGEHKQDYTTdlldiwKAMEAQV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIVSGKYD 304
Cdd:cd19155 151 DQGLTRSIGLSNFNREQMARILKNAR----IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSPG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315434249 305 SGIPPYSRASLkgyqwLKDkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNADQLMEN 381
Cdd:cd19155 224 TGSPSGSSPDL-----LQD--------------PVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKEN 279
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
85-382 |
3.35e-13 |
|
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a founding member of aldo-keto reductase family 2 member E4 (AKR2E4). It is a NADP-dependent oxidoreductase with high 3-dehydroecdysone reductase activity. It may play a role in the regulation of molting and has lower activity with phenylglyoxal and isatin (in vitro). This family also includes 3-dehydroecdysone 3b-reductase from Spodoptera littoralis and Trichoplusia ni, DL-glyceraldehyde reductase from Drosophila melanogaster, aldo-keto reductase from Bombyx mori, which correspond to aldo-keto reductase family 2 member E1, E2, E3 and E5 (AKR2E1/2/3/5), respectively.
Pssm-ID: 381342 [Multi-domain] Cd Length: 292 Bit Score: 69.62 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfgGQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAEter 162
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYG-NEAEVgeAIREKIAEGVVKREDLFITTKL-WNSYHE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 163 glsRKHIIEGLKASLERLQLEYVDVVFANRPDpNTPMEGDPFSSSKSRTFIIE--ETVRAMTHVINQGMAMYWGTSRWSS 240
Cdd:cd19116 85 ---REQVEPALRESLKRLGLDYVDLYLIHWPV-AFKENNDSESNGDGSLSDIDylETWRGMEDLVKLGLTRSIGVSNFNS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 241 MEIMEAYSVARqfnlTPPICEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacGIVSGKYDSGIPPYsraslkgyq 319
Cdd:cd19116 161 EQINRLLSNCN----IKPAVNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPR--------- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 320 wLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNADQLMENI 382
Cdd:cd19116 222 -LDDPT--------------LVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
85-402 |
3.59e-13 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 68.92 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGL 164
Cdd:cd19139 4 FGLGTF-----RLKDDVVIDSVRTALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19139 69 SKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNDEVP-------------VEEYIGALAEAKEQGLTRHIGVSNFTIALLD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAYSVARQFNLTPPICEQAEYhmFQREKVEVQLPElfHKIGVGAmtWSPLACGIVsgkydsgippysraslkgyqwLKDK 324
Cdd:cd19139 136 EAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ--HGIHVTS--YMTLAYGKV---------------------LDDP 188
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 325 IlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:cd19139 189 V--------------LAAIAERHGATPAQIALAWAM-ARGY-AVIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
85-382 |
4.04e-13 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 68.81 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIK----KKGWRRSSLVITTKIfwgGKAE 159
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKL---APKD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 160 TERGLSRkhiiEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRtfiieETVRAMTHVINQGMAMYWGTSRW- 238
Cdd:cd19136 73 QGYEKAR----AACLGSLERLGTDYLDLYLIHWPGVQGLKPSDPRNAELRR-----ESWRALEDLYKEGKLRAIGVSNYt 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 239 -SSMEIMEAYSvarqfnLTPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysrasl 315
Cdd:cd19136 144 vRHLEELLKYC------EVPPAVNQVEFHphLVQKE-----LLKFCKDHGIHLQAYSSLGSG------------------ 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315434249 316 kgyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENI 382
Cdd:cd19136 195 ------DLRLLEDP---------TVLAIAKKYGRTPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
79-382 |
6.56e-13 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 68.07 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggka 158
Cdd:cd19132 4 GTQIPAIGFGTY-----PLKGDEGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 eteRGlsRKH----IIEGLKASLERLQLEYVDVVFANRPDPntpmegdpfssskSRTFIIeETVRAMTHVINQGMAMYWG 234
Cdd:cd19132 70 ---PG--RHHgyeeALRTIEESLYRLGLDYVDLYLIHWPNP-------------SRDLYV-EAWQALIEAREEGLVRSIG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 235 TSRW--SSMEIMEA----YSVARQFNLTPPIcEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPLAcgivsgkydsgip 308
Cdd:cd19132 131 VSNFlpEHLDRLIDetgvTPAVNQIELHPYF-PQAEQRAYHREH------------GIVTQSWSPLG------------- 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434249 309 pysraslKGYQWLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENI 382
Cdd:cd19132 185 -------RGSGLLDEPV--------------IKAIAEKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
78-400 |
7.29e-13 |
|
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: 69.08 E-value: 7.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLG------TWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK 151
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 152 IFW--------GGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDpntpmegdpFSSSksrtfiIEETVRAMTH 223
Cdd:cd19147 85 FTTdykayevgKGKAVNYCGNHKRSLHVSVRDSLRKLQTDWIDILYVHWWD---------YTTS------IEEVMDSLHI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 224 VINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKY 303
Cdd:cd19147 150 LVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLG----GGKF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSgiPPYSRASLKGYQWLKDKILSEEGRRQQAKLKE-LQAIAERLGC-TLPQLAIAWCLRNEGVSSVLLGASNADQLMEN 381
Cdd:cd19147 225 QS--KKAVEERKKNGEGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDN 302
|
330
....*....|....*....
gi 315434249 382 IGAIQVlpKLSSSIIHEID 400
Cdd:cd19147 303 IEALSI--KLTPEEIEYLE 319
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
78-368 |
1.97e-11 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 64.21 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGqitDEMAEQLMTLAYDNGINLFDTAEVY----AAGKA--EVVLGNIIKKkgwrRSSLVITTK 151
Cdd:cd19124 1 SGQTMPVIGMGTASDPPS---PEDIKAAVLEAIEVGYRHFDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 152 IfWGGKAEterglsRKHIIEGLKASLERLQLEYVDVV-----FANRPDPNTPmegdPFSSSKSRTFIIEETVRAMTHVIN 226
Cdd:cd19124 74 L-WCSDAH------PDLVLPALKKSLRNLQLEYVDLYlihwpVSLKPGKFSF----PIEEEDFLPFDIKGVWEAMEECQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 227 QGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKvevqLPELFHKIGVGAMTWSPLACgivsgkyds 305
Cdd:cd19124 143 LGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAWQQKK----LREFCKANGIHVTAYSPLGA--------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 306 gippysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWcLRNEGVSSV 368
Cdd:cd19124 206 ----------PGTKWGSNAVMESD---------VLKEIAAAKGKTVAQVSLRW-VYEQGVSLV 248
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
79-382 |
4.12e-11 |
|
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: 63.19 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWG--G 156
Cdd:cd19127 6 GVEMPALGLGVF-----QTPPEETADAVATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 157 KAETERGLsrkhiieglKASLERLQLEYVDVVFANRPdpnTPMEGDpfsssksRTFiieETVRAMTHVINQGMAMYWGTS 236
Cdd:cd19127 78 YDKALRGF---------DASLRRLGLDYVDLYLLHWP---VPNDFD-------RTI---QAYKALEKLLAEGRVRAIGVS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 237 RWSS---MEIMEAYSVArqfnltpPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcGIVsgKYDSGIPPySRA 313
Cdd:cd19127 136 NFTPehlERLIDATTVV-------PAVNQVELHPYFSQK---DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPT-GPG 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315434249 314 SLkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCLRNeGVSSVlLGASNADQLMENI 382
Cdd:cd19127 202 DV-----LQDPTITG--------------LAEKYGKTPAQIVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
85-297 |
5.08e-11 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 62.78 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKaetergl 164
Cdd:PRK11565 18 LGLGVW-----QASNEEVITAIHKALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 sRKHIIEGLKASLERLQLEYVDVVFANRPDPNtpmegdpfsssksrtfiIEETVRAMTHVIN---QGMAMYWGTSRWSS- 240
Cdd:PRK11565 82 -HKRPREALEESLKKLQLDYVDLYLMHWPVPA-----------------IDHYVEAWKGMIElqkEGLIKSIGVCNFQIh 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 315434249 241 --MEIMEAYSVArqfnltpPICEQAEYH--MFQRekvEVQLPELFHKIGVGAmtWSPLACG 297
Cdd:PRK11565 144 hlQRLIDETGVT-------PVINQIELHplMQQR---QLHAWNATHKIQTES--WSPLAQG 192
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
85-384 |
2.74e-10 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 60.42 E-value: 2.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIfWggkaeTERgL 164
Cdd:PRK11172 6 FGLGTF-----RLKDQVVIDSVKTALELGYRAIDTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEgdpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:PRK11172 71 AKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNDEVS-------------VEEFMQALLEAKKQGLTREIGISNFTIALMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EAYSVARQFNLTppiCEQAEYHMF-QREKVEVQLPElfHKIGVGA-MTwspLACGIVsgkydsgippysraslkgyqwLK 322
Cdd:PRK11172 138 QAIAAVGAENIA---TNQIELSPYlQNRKVVAFAKE--HGIHVTSyMT---LAYGKV---------------------LK 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434249 323 DKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGvSSVLLGASNADQLMENIGA 384
Cdd:PRK11172 189 DPV--------------IARIAAKHNATPAQVILAWAMQ-LG-YSVIPSSTKRENLASNLLA 234
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
78-402 |
3.15e-10 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 60.59 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGgk 157
Cdd:cd19117 10 TGAEIPAVGLGTW-----QSKPNEVAKAVEAALKAGYRHIDTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 aeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSKSRTFIIEE------TVRAMTHVINQGMAM 231
Cdd:cd19117 79 --TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLDPDGNDFLFKKDDGTKDHEPdwdfikTWELMQKLPATGKVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 232 YWGTSRWSSMEIMEAysVARQFNLTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYs 311
Cdd:cd19117 153 AIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQP---KLVDFCKSKGIHATAYSPLG--------STNAPLL- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 312 raslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENIGAIQvlpkL 391
Cdd:cd19117 219 ------------------------KEPVIIKIAKKHGKTPAQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----L 268
|
330
....*....|.
gi 315434249 392 SSSIIHEIDSI 402
Cdd:cd19117 269 SDEEFKEIDEL 279
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
78-382 |
3.82e-10 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 60.58 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQITDemaeqLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWg 155
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPGEIKE-----LILNAIKIGYRHFDCAADYK-NEKEVgeALAEAFKTGLVKREDLFITTKL-W- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 gkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP--------DPNTPMEGDPFSSSKSRTFIIEETVRAMTHVINQ 227
Cdd:cd19112 79 ---NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvGTTGSALGEDGVLDIDVTISLETTWHAMEKLVSA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 228 GMAMYWGTSRWSS--MEIMEAYSVARqfnltpPICEQAEYH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIVSGKYD 304
Cdd:cd19112 152 GLVRSIGISNYDIflTRDCLAYSKIK------PAVNQIETHpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315434249 305 SGIPPysraslkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENI 382
Cdd:cd19112 222 GSVSP-----------LDDPVLKD--------------LAKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
78-358 |
5.99e-10 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 60.09 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQItdemaEQLMTLAYDNGINLFDTAEVYAaGKAEVvlGNIIKK-----KGWRRSSLVITTKI 152
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPGQV-----KAAVKYALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 fWGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRPdpnTPME--GDPFSSSKSRTFIIE-----ETVRAMTHVI 225
Cdd:cd19106 75 -WNTKHHPE------DVEPALRKTLKDLQLDYLDLYLIHWP---YAFErgDNPFPKNPDGTIRYDsthykETWKAMEKLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgivsgkyds 305
Cdd:cd19106 145 DKGLVKAIGLSNFNSRQIDDILSVAR----IKPAVLQVECHPYL---AQNELIAHCKARGLVVTAYSPL----------- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 315434249 306 GIPpySRAslkgyqWLK--DKILSEEGRrqqaklkeLQAIAERLGCTLPQLAIAW 358
Cdd:cd19106 207 GSP--DRP------WAKpdEPVLLEEPK--------VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
78-381 |
9.91e-10 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 58.96 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaAGKAEV--VLGNIIKKK-GWRRSSLVITTKIfW 154
Cdd:cd19118 3 TGNKIPAIGLGTWQAEPGEVGAAVKI-----ALKAGYRHLDLAKVY-QNQHEVgqALKELLKEEpGVKREDLFITSKL-W 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAETErglsrkHIIEGLKASLERLQLEYVD-------VVFA--NRPDPNTPMEGDPFSSSKSRTFIIEETVRAMTHVI 225
Cdd:cd19118 76 NNSHRPE------YVEPALDDTLKELGLDYLDlylihwpVAFKptGDLNPLTAVPTNGGEVDLDLSVSLVDTWKAMVELK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 226 NQGMAMYWGTSRWSS---MEIMEAYSVArqfnltpPICEQAEYH--MFQREKVEvqlpelFHK---IGVGAmtWSPLacg 297
Cdd:cd19118 150 KTGKVKSIGVSNFSIdhlQAIIEETGVV-------PAVNQIEAHplLLQDELVD------YCKsknIHITA--YSPL--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 298 ivsGKYDSGIPPysraslkgyqwlkdkILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQ 377
Cdd:cd19118 212 ---GNNLAGLPL---------------LVQHP---------EVKAIAAKLGKTPAQVLIAWGIQR-GH-SVIPKSVTPSR 262
|
....
gi 315434249 378 LMEN 381
Cdd:cd19118 263 IRSN 266
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
93-399 |
2.85e-09 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 57.85 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 93 FGGQITDEMAEQLMTL-AYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhI 169
Cdd:cd19129 11 FGTLIPDPSATRNAVKaALEAGFRHFDCAERYR-NEAEVgeAMQEVFKAGKIRREDLFVTTKL-WNTNHRPER------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 170 IEGLKASLERLQLEYVDVVFANRPDPNTPM-EGDPFSSS------KSRTFIieETVRAMTHVINQGMAMYWGTSRWSSME 242
Cdd:cd19129 83 KPAFEASLKRLQLDYLDLYLIHTPFAFQPGdEQDPRDANgnviydDGVTLL--DTWRAMERLVDEGRCKAIGLSDVSLEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 243 IMEAYSVARqfnlTPPICEQAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwLK 322
Cdd:cd19129 161 LREIFEAAR----IKPAVVQVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315434249 323 DKILSeegrrqqaklkelqAIAERLGCTLPQLAIAWCLRNEGvsSVLLGASNADQLMENIGaIQVLPKLSSSIIHEI 399
Cdd:cd19129 216 DPVIT--------------AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
79-383 |
5.13e-09 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 56.63 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTW-VTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 157
Cdd:cd19157 7 GVKMPWLGLGVFkVEEGSEVVNAVKT-----ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 AETERGLsrkhiiEGLKASLERLQLEYVDVVFANRPDPNtpmegdpfsSSKsrtfiieETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19157 78 QGYDSTL------KAFEASLERLGLDYLDLYLIHWPVKG---------KYK-------ETWKALEKLYKDGRVRAIGVSN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARqfnlTPPICEQAEYH--MFQREkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysrasl 315
Cdd:cd19157 136 FQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYCKKQGIQLEAWSPLMQG------------------ 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 316 kgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIG 383
Cdd:cd19157 189 --------QLLDNP---------VLKEIAEKYNKSVAQVILRWDLQNGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
78-294 |
5.63e-09 |
|
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: 56.77 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYAaGKAEVVLGniIKK---KGWRRSSLVITTKIfW 154
Cdd:cd19121 8 TGASIPAVGLGTWQAKAGEVKAAVAH-----ALKIGYRHIDGALCYQ-NEDEVGEG--IKEaiaGGVKREDLFVTTKL-W 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GgkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEGDPFSSSK---SRTFIIE----ETVRAMTHVINQ 227
Cdd:cd19121 79 S--------TYHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNPNGNHDLFPTLpdgSRDLDWDwnhvDTWKQMEKVLKT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434249 228 GMAMYWGTSRWSSM---EIMEAYSV---ARQFNLTpPICEQAEYHMFQREKvevqlpelfhkiGVGAMTWSPL 294
Cdd:cd19121 151 GKTKAIGVSNYSIPyleELLKHATVvpaVNQVENH-PYLPQQELVDFCKEK------------GILIEAYSPL 210
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
79-362 |
3.35e-08 |
|
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: 54.45 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITD-EMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGK 157
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 158 AETERGLSrkhiieGLKASLERLQLEYVDVVFANRPdpntpmEGDPFsssksrtfiiEETVRAMTHVINQGMAMYWGTSR 237
Cdd:cd19156 77 QGYESTLA------AFEESLEKLGLDYVDLYLIHWP------VKGKF----------KDTWKAFEKLYKEKKVRAIGVSN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 238 WSSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKVEVQLPElfHKIGVGAmtWSPLACGivsgkydsgippysraslk 316
Cdd:cd19156 135 FHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRKFCKE--KNIAVEA--WSPLGQG------------------- 187
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 315434249 317 gyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLRN 362
Cdd:cd19156 188 -------KLLSNP---------VLKAIGKKYGKSAAQVIIRWDIQH 217
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
78-241 |
9.03e-08 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 53.27 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQitdEMAEQLMTLAYDNGINLFDTAEVYAA----GKAevvLGNIIKKKGWRRSSLVITTKI- 152
Cdd:cd19119 8 TGASIPALGLGTASPHEDR---AEVKEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 153 --FWggkaeterglsrKHIIEGLKASLERLQLEYVDVVFANRPdpnTPMEGDPfsssksrtfiiEETVRAMTHVINQGMA 230
Cdd:cd19119 82 ptFY------------DEVERSLDESLKALGLDYVDLLLVHWP---VCFEKDS-----------DDSGKPFTPVNDDGKT 135
|
170
....*....|.
gi 315434249 231 MYWGTSRWSSM 241
Cdd:cd19119 136 RYAASGDHITT 146
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
78-387 |
1.47e-07 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 52.62 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQITDEMAeqlMTLAYDNGINLFDTAEVYAaGKAEV---VLGNIIKKKGWRRSSLVITTKIfW 154
Cdd:cd19122 5 NGVKIPAVGFGTFANEGAKGETYAA---VTKALDVGYRHLDCAWFYL-NEDEVgdaVRDFLKENPSVKREDLFICTKV-W 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAETErglsrkHIIEGLKASLERLQLEYVDV------VFANRPDPNTPMEGD--PFSSSKSRTFIIEETVRAMTHVIN 226
Cdd:cd19122 80 NHLHEPE------DVKWSIDNSLKNLKLDYIDLflvhwpIAAEKNDQRSPKLGPdgKYVILKDLTENPEPTWRAMEEIYE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 227 QGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLACgivsgkyDSG 306
Cdd:cd19122 154 SGKAKAIGVSNWTIPGLKKLLSFAK----VKPHVNQIEIHPFLPNE---ELVDYCFSNDILPEAYSPLGS-------QNQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 307 IPpysraslkgyqwlkdkilsEEGRRQQAKlKELQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIQ 386
Cdd:cd19122 220 VP-------------------STGERVSEN-PTLNEVAEKGGYSLAQVLIAWGLRRGYV--VLPKSSTPSRIESNFKSIE 277
|
.
gi 315434249 387 V 387
Cdd:cd19122 278 L 278
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
109-402 |
1.51e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.58 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 109 AYDNGINLFDTAEVYAAGkaevVLGNIIkkkgwR------RSSLVITTKIfwgGKAETERG-----LSRKHIIEGLKASL 177
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 178 ERLQLEYVDVV-FANRPDPNTPMEGDpfsssksrtfiIEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnlt 256
Cdd:PRK10376 117 RNLGLDVLDVVnLRLMGDGHGPAEGS-----------IEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 257 PPICEQAEYHMFQREkvEVQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkGYQWLKDKILSeegrrqqak 336
Cdd:PRK10376 180 EIVCVQNHYNLAHRA--DDALIDALARDGIAYVPFFPLG---------------------GFTPLQSSTLS--------- 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 337 lkelqAIAERLGCTLPQLAIAWCLRNEgvSSVLL--GASNADQLMENIGAIQVlpKLSSSIIHEIDSI 402
Cdd:PRK10376 228 -----DVAASLGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
79-382 |
2.71e-06 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 48.71 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK---KGW-RRSSLVITTKIfW 154
Cdd:cd19114 1 GDKMPLVGFGTA-----KIKANETEEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-W 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 155 GGKAeterglSRKHIIEGLKASLERLQLEYVDVVFANRPDPNT---PMEGDPFS----SSKSRTF---IIEETVRAMTHV 224
Cdd:cd19114 72 NNFH------GKDHVREAFDRQLKDYGLDYIDLYLIHFPIPAAyvdPAENYPFLwkdkELKKFPLeqsPMQECWREMEKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 225 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgivsgKY 303
Cdd:cd19114 146 VDAGLVRNIGIANFNVQLILDLLTYAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 304 DSGIPPYSRASLKGYQwlkdkILSEEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMEN 381
Cdd:cd19114 199 GIQITAYSSFGNAVYT-----KVTKHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTN 271
|
.
gi 315434249 382 I 382
Cdd:cd19114 272 L 272
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
98-387 |
1.32e-05 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 46.57 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 98 TDEMAEQ---LMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKifWG----------GKAETERGL 164
Cdd:cd19098 30 VEAMRAHthaVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SRKHIIEGLKASLERLQlEYVDVVFANRPDPNTPMEGDpfsssksrtfiiEETVRAMTHVINQGMAMYWGTSRWSSMEIM 244
Cdd:cd19098 106 SLARLLKQWEETRSLLG-KHLDLYQIHSATLESGVLED------------ADVLAALAELKAEGVKIGLSLSGPQQAETL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 245 EA-----YSVARQFNltppiCEQAEYHMFQREKVEvQLpELFHKIGVGAMTWSPLACGIVSGKYDSGippysraslkgyq 319
Cdd:cd19098 173 RRaleieIDGARLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDRNPSP------------- 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434249 320 wlkdkilseegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 387
Cdd:cd19098 233 ------------ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| AKR_AKR1E1-2 |
cd19110 |
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1, ... |
81-294 |
1.79e-05 |
|
AKR1E family of aldo-keto reductase (AKR); The AKR1E family of AKR includes 1,5-anhydro-D-fructose reductase (EC 1.1.1.263) from Mus musculus (liver, AKR1E1) and Homo sapiens (AKR1E2). 1,5-anhydro-D-fructose reductase), also called AF reductase, or aldo-keto reductase family 1 member C-like protein 2 (AKR1CL2), catalyzes the NADPH-dependent reduction of 1,5-anhydro-D-fructose (AF) to 1,5-anhydro-D-glucitol. AKR1E2 is a testis aldo-keto reductase (tAKR), which is also known as testis-specific protein (TSP), or LoopADR.
Pssm-ID: 381336 [Multi-domain] Cd Length: 301 Bit Score: 46.11 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 81 RVSCLGLGTWVTFGGQITDEMAEqlmtlAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIfWGgka 158
Cdd:cd19110 3 DIPAVGLGTWKASPGEVTEAVKV-----AIDAGYRHFDCAYLY-HNESEVGAGirEKIKEGVVRREDLFIVSKL-WC--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 159 eterGLSRKHIIE-GLKASLERLQLEYVDVVFANRP------DPNTPMEGDPFSSSKSRTFIieETVRAMTHVINQGMAM 231
Cdd:cd19110 73 ----TCHKKSLVKtACTRSLKALKLNYLDLYLIHWPmgfkpgEPDLPLDRSGMVIPSDTDFL--DTWEAMEDLVIEGLVK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434249 232 YWGTSRWSSmEIMEaySVARQFNL-TPPICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPL 294
Cdd:cd19110 147 NIGVSNFNH-EQLE--RLLNKPGLrVKPVTNQIECHPYLTQK---KLISFCQSRNVSVTAYRPL 204
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
79-294 |
7.70e-05 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 44.33 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 79 GLRVSCLGLGTWVTFGGQITDEMAeqlmtLAYDNGINLFDTAEVYaAGKAEVVLG--NIIKKKGWRRSSLVITTKIFwgg 156
Cdd:cd19107 1 GAKMPILGLGTWKSPPGQVTEAVK-----VAIDAGYRHIDCAYVY-QNENEVGEAiqEKIKEQVVKREDLFIVSKLW--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 157 KAETERGLSRkhiiEGLKASLERLQLEYVDVVFANRP------DPNTPMEGDPFSSSKSRTFIieETVRAMTHVINQGMA 230
Cdd:cd19107 72 CTFHEKGLVK----GACQKTLSDLKLDYLDLYLIHWPtgfkpgKELFPLDESGNVIPSDTTFL--DTWEAMEELVDEGLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 231 MYWGTSRWSSMEImeaysvARQFNlTP-----PICEQAEYHMF-QREKvevqLPELFHKIGVGAMTWSPL 294
Cdd:cd19107 146 KAIGVSNFNHLQI------ERILN-KPglkykPAVNQIECHPYlTQEK----LIQYCQSKGIVVTAYSPL 204
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
78-266 |
1.20e-04 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 43.59 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKaEVVLG--NIIKKKGWRRSSLVITTKIfWG 155
Cdd:cd19113 7 SGYKMPSVGFGCW-----KLDNATAADQIYQAIKAGYRLFDGAEDYGNEK-EVGEGvnRAIDEGLVKREELFLTSKL-WN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 156 GKAEterglsRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPM---EGDP--FSSSKSRTFIIE-----ETVRAMTHVI 225
Cdd:cd19113 80 NFHD------PKNVETALNKTLSDLKLDYVDLFLIHFPIAFKFVpieEKYPpgFYCGDGDNFVYEdvpilDTWKALEKLV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 315434249 226 NQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH 266
Cdd:cd19113 154 DAGKIKSIGVSNFPGALILDLLRGAT----IKPAVLQIEHH 190
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| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
85-297 |
6.55e-04 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 41.05 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWvtfggQITDEMAEQLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGGKAETERGL 164
Cdd:cd19130 13 LGYGVF-----KVPPADTQRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 165 SrkhiieGLKASLERLQLEYVDVVFANRPdpnTPMEGDpfsssksrtFIieETVRAMTHVINQGMAMYWGTSRW--SSME 242
Cdd:cd19130 84 A------AFAESLAKLGLDQVDLYLVHWP---TPAAGN---------YV--HTWEAMIELRAAGRTRSIGVSNFlpPHLE 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 315434249 243 IMEAYSVarqfnlTPPICEQAEYHMF--QREKVEVQlpelfHKIGVGAMTWSPLACG 297
Cdd:cd19130 144 RIVAATG------VVPAVNQIELHPAyqQRTIRDWA-----QAHDVKIEAWSPLGQG 189
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| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
85-186 |
1.35e-03 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 40.29 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 85 LGLGTWVTfgGQITDEMAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKK----GWRRSSLVITTKIfWGGKAET 160
Cdd:cd19108 14 LGFGTYAP--EEVPKSKALEATKLAIDAGFRHIDSAYLY---QNEEEVGQAIRSKiadgTVKREDIFYTSKL-WCTFHRP 87
|
90 100
....*....|....*....|....*.
gi 315434249 161 ErgLSRKhiieGLKASLERLQLEYVD 186
Cdd:cd19108 88 E--LVRP----ALEKSLKKLQLDYVD 107
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|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
78-266 |
1.91e-03 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 40.10 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 78 SGLRVSCLGLGTWVTFGGQITDEMAEQLMTlaydnGINLFDTAEVYA----AGKAevvLGNIIKKKGWRRSSLVITTKIf 153
Cdd:cd19115 9 SGYDMPLVGFGLWKVNNDTCADQVYNAIKA-----GYRLFDGACDYGneveAGQG---VARAIKEGIVKREDLFIVSKL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434249 154 WGGKAETErglsrkHIIEGLKASLERLQLEYVDVVFANRP------DPNTPMEGDPFSSSKSRTF---IIEETVRAMTHV 224
Cdd:cd19115 80 WNTFHDGE------RVEPICRKQLADWGIDYFDLFLIHFPialkyvDPAVRYPPGWFYDGKKVEFsnaPIQETWTAMEKL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 315434249 225 INQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH 266
Cdd:cd19115 154 VDKGLARSIGVSNFSAQLLMDLLRYAR----IRPATLQIEHH 191
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