|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
76-371 |
0e+00 |
|
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo sapiens, Rattus norvegicus, and Mus musculus, are founding members of aldo-keto reductase family 6 member A9 (AKR6A9), A12 (AKR6A12), A14 (AKR6A14), respectively. KCAB3B, also called Shaker channel b-subunit 3 (Kvb3), K(+) channel subunit beta-3, or Kv-beta-3, is an accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. It alters the functional properties of Kv1.5.
Pssm-ID: 381386 [Multi-domain] Cd Length: 325 Bit Score: 640.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 76 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 155
Cdd:cd19160 1 TGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 156 ITTKIFWGGQAETERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAE 206
Cdd:cd19160 81 VTTKIYWGGQAETERGLSRKHIIEglrgsldrlqleyvdivfanrsdpnspmeEIVRAMTYVINQGMAMYWGTSRWSAME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 207 IMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLK 286
Cdd:cd19160 161 IMEAYSVARQFNLIPPVCEQAEYHLFQREKVEMQLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 287 DKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGL 366
Cdd:cd19160 241 EKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDAL 320
|
....*
gi 2462558728 367 LGNKP 371
Cdd:cd19160 321 LGNKP 325
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
79-359 |
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: 561.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITT 158
Cdd:cd19141 1 PYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 159 KIFWGGQAETERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIME 209
Cdd:cd19141 81 KIFWGGKAETERGLSRKHIIEglkaslerlqleyvdivfanrpdpntpmeEIVRAFTHVINQGMAMYWGTSRWSAMEIME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 210 AYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKV 289
Cdd:cd19141 161 AYSVARQFNLIPPIVEQAEYHLFQREKVEMQLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 290 QSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQT 359
Cdd:cd19141 241 LSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
80-367 |
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: 541.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 80 YRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTK 159
Cdd:TIGR01293 1 YRNLGKSGLRVSCLGLGTWVTFGGQISDEMAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 160 IFWGGQAETERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIMEA 210
Cdd:TIGR01293 81 IFWGGKAETERGLSRKHIIEglkaslerlqleyvdivfanrpdpntpmeETVRAMTYVINQGMAMYWGTSRWSSMEIMEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 211 YSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDKVQ 290
Cdd:TIGR01293 161 YSVARQFNLIPPICEQAEYHMFQREKVEVQLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKIL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558728 291 SEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLL 367
Cdd:TIGR01293 241 SEEGRRQQARLKDLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
78-371 |
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: 519.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVIT 157
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWGGQAETERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIM 208
Cdd:cd19159 81 TKLYWGGKAETERGLSRKHIIEglkgslqrlqleyvdvvfanrpdsntpmeEIVRAMTHVINQGMAMYWGTSRWSAMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 209 EAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDK 288
Cdd:cd19159 161 EAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 289 VQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLLG 368
Cdd:cd19159 241 IVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILR 320
|
...
gi 2462558728 369 NKP 371
Cdd:cd19159 321 NKP 323
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
78-372 |
6.48e-165 |
|
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: 464.17 E-value: 6.48e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVIT 157
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWGGQAETERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIM 208
Cdd:cd19158 81 TKIFWGGKAETERGLSRKHIIEglkaslerlqleyvdvvfanrpdpntpmeETVRAMTHVINQGMAMYWGTSRWSSMEIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 209 EAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLKDK 288
Cdd:cd19158 161 EAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 289 VQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDGLLG 368
Cdd:cd19158 241 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILG 320
|
....
gi 2462558728 369 NKPH 372
Cdd:cd19158 321 NKPY 324
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
78-365 |
1.48e-142 |
|
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: 407.37 E-value: 1.48e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVIT 157
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSWVTFGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWGGQAE--TERGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAE 206
Cdd:cd19143 81 TKIFWGGGGPppNDRGLSRKHIvegtkaslkrlqldyvdlvfchrpdpatpIEETVRAMNDLIDQGKAFYWGTSEWSAQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 207 IMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYQWLK 286
Cdd:cd19143 161 IEEAHEIADRLGLIPPVMEQPQYNLFHRERVEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 287 DKVQsEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVMEIDG 365
Cdd:cd19143 241 DRKE-ELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEA 318
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
78-371 |
6.86e-134 |
|
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: 385.66 E-value: 6.86e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVIT 157
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWSTFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWGGQAEtERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIM 208
Cdd:cd19142 81 TKIYWSYGSE-ERGLSRKHIIEsvraslrrlqldyidiviihkadpmcpmeEVVRAMSYLIDNGLIMYWGTSRWSPVEIM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 209 EAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLItskyDGRVPDTCRASIKGYQWLKDK 288
Cdd:cd19142 160 EAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELYNKVGVGLITWSPLSLGLD----PGISEETRRLVTKLSFKSSKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 289 VQSEDGKK-------QQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVM 361
Cdd:cd19142 236 KVGSDGNGiheetrrASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVME 315
|
330
....*....|
gi 2462558728 362 EIDGLLGNKP 371
Cdd:cd19142 316 ELERILDNKP 325
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
87-349 |
4.71e-119 |
|
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: 346.50 E-value: 4.71e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKskGWRRSSYVITTKIFWGGQA 166
Cdd:cd19074 1 GLKVSELSLGTWLTFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 167 E-TERGLSRKHIIE-----------------------------EIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQ 216
Cdd:cd19074 79 GpNDRGLSRKHIFEsihaslkrlqldyvdiyychrydpetpleETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 217 FNLIPPVCEQAEHHLFQREKVEmQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKgYQWLKDKVQSEDGKK 296
Cdd:cd19074 159 FGLIPPVVEQPQYNMLWREIEE-EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDE 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462558728 297 QQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19074 237 NLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
78-372 |
1.71e-76 |
|
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: 238.92 E-value: 1.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWvTFG---SQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKskGWRRSSY 154
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTM-TFGgpwGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 155 VITTKIFW-GGQAETERGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGA 204
Cdd:COG0667 78 VIATKVGRrMGPGPNGRGLSREHIrraveaslrrlgtdyidlyqlhrpdpdtpIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 205 AEIMEAysMARQFNLIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCRASikgy 282
Cdd:COG0667 158 EQLRRA--LAIAEGLPPIVAVQNEYSLLDRS-AEEELLPAARELGVGVLAYSPLAGGLLTGKYrrGATFPEGDRAA---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 283 qwlKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVME 362
Cdd:COG0667 231 ---TNFVQGYLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAA 305
|
330
....*....|
gi 2462558728 363 IDGLLGNKPH 372
Cdd:COG0667 306 LDAALAAVPA 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
78-366 |
2.67e-62 |
|
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: 202.03 E-value: 2.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVIT 157
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGT-MNFGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWG-GQAETERGLSRKHII-----------------------------EEIVRAMTYVINQGLALYWGTSRWGAAEI 207
Cdd:cd19087 77 TKVFGPmGDDPNDRGLSRRHIRraveaslrrlqtdyidlyqmhhfdrdtplEETLRALDDLVRQGKIRYIGVSNFAAWQI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 208 MEAYSMARQFNLIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKYD-GRVPDTCRAsikgyqwlk 286
Cdd:cd19087 157 AKAQGIAARRGLLRFVSEQPMYNLLKRQ-AELEILPAARAYGLGVIPYSPLAGGLLTGKYGkGKRPESGRL--------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 287 dkVQSEDGKKQQA------KVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTV 360
Cdd:cd19087 227 --VERARYQARYGleeyrdIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELL 302
|
....*.
gi 2462558728 361 MEIDGL 366
Cdd:cd19087 303 AEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
78-364 |
1.32e-60 |
|
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: 197.84 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTwVTFGS---------QISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkg 148
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGT-MTFGGgggffgawgGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 149 wRRSSYVITTKI-FWGGQAETERGLSRKHII-----------------------------EEIVRAMTYVINQGLALYWG 198
Cdd:cd19091 78 -RRDDVLIATKVrGRMGEGPNDVGLSRHHIIraveaslkrlgtdyidlyqlhgfdaltplEETLRALDDLVRQGKVRYIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 199 TSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCR 276
Cdd:cd19091 157 VSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 277 ASIKGYQWLK-DKVQSEDgkkqqakVMD-LLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQ 354
Cdd:cd19091 236 LRRTGFDFPPvDRERGYD-------VVDaLREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--S 306
|
330
....*....|
gi 2462558728 355 LTPQTVMEID 364
Cdd:cd19091 307 LTPEEIARLD 316
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
80-350 |
1.80e-51 |
|
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: 173.98 E-value: 1.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 80 YRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVY--AAGKAERTLGNILKS-KGWRRSSYVI 156
Cdd:cd19089 1 YRRCGRSGLHLPAISLGLWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 157 TTKI---FWGGqaETERGLSRKHII-----------------------------EEIVRAMTYVINQGLALYWGTSRWGA 204
Cdd:cd19089 81 STKAgygMWPG--PYGDGGSRKYLLasldqslkrmgldyvdifyhhrydpdtplEETMTALADAVRSGKALYVGISNYPG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 205 AEIMEAYSMARQFNlIPPVCEQAEHHLFQReKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASiKGYQW 284
Cdd:cd19089 159 AKARRAIALLRELG-VPLIIHQPRYSLLDR-WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRA-AESKF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 285 LKDKVQSEDgKKQQAKVMDLLPVAHQLgcTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19089 236 LTEEALTPE-KLEQLRKLNKIAAKRGQ--SLAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALK 298
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
91-344 |
8.50e-50 |
|
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: 166.93 E-value: 8.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 91 SCLGLGTWvTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRSSYVITTKI-FWGGQAETE 169
Cdd:cd06660 1 SRLGLGTM-TFGGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 170 RGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLI 220
Cdd:cd06660 79 SRLSPEHIrrdleeslrrlgtdyidlyylhrddpstpVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 221 PPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLitskydgrvpdtcrasikgyqwlkdkvqsedgkkqqak 300
Cdd:cd06660 159 GFAAVQPQYSLLDRSPMEEELLDWAEENGLPLLAYSPLARGP-------------------------------------- 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462558728 301 vmdllpvahqlgctvAQLAIAWCLRSEGVSSVLLGVSSAEQLIE 344
Cdd:cd06660 201 ---------------AQLALAWLLSQPFVTVPIVGARSPEQLEE 229
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
87-364 |
2.75e-49 |
|
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: 167.70 E-value: 2.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWV---TFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTK--IF 161
Cdd:cd19084 1 DLKVSRIGLGTWAiggTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 162 WGGQAETERGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAys 212
Cdd:cd19084 78 WDGGKGVTKDLSPESIrkeveqslrrlqtdyidlyqihwpdpntpIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 213 marqFNLIPPVCEQAEHHLFQREKVEMQLPeLYHKIGVGSVTWYPLACGLITSKYDGR---VPDTCRASIKgyqwlkdKV 289
Cdd:cd19084 156 ----RKYGPIVSLQPPYSMLEREIEEELLP-YCRENGIGVLPYGPLAQGLLTGKYKKEptfPPDDRRSRFP-------FF 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558728 290 QSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19084 224 RGENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
93-367 |
6.08e-49 |
|
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: 166.72 E-value: 6.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWvTFGSQ---ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIfWGGQAETE 169
Cdd:pfam00248 1 IGLGTW-QLGGGwgpISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 170 RGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlI 220
Cdd:pfam00248 79 SGGSKENIrksleeslkrlgtdyidlyylhwpdpdtpIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----I 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 221 PPVCEQAEHHLFQREKVEMqLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCRASIKGYQWlkdkvqsedgKKQQ 298
Cdd:pfam00248 155 PIVAVQVEYNLLRRRQEEE-LLEYCKKNGIPLIAYSPLGGGLLTGKYtrDPDKGPGERRRLLKKGT----------PLNL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 299 AKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEIDGLL 367
Cdd:pfam00248 224 EALEALEEIAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEF--PLSDEEVARIDELL 290
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
83-364 |
9.14e-49 |
|
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: 166.62 E-value: 9.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 83 LGKSGLRVSCLGLGTWVtFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAA-------GKAERTLGNILKSKGwRRSSYV 155
Cdd:cd19081 2 LGRTGLSVSPLCLGTMV-FGWTADEETSFALLDAFVDAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 156 ITTKI-FWGGQAEteRGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAA 205
Cdd:cd19081 80 IATKVgFPMGPNG--PGLSRKHIrraveaslrrlqtdyidlyqahwddpatpLEETLGALNDLIRQGKVRYIGASNYSAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 206 EIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCRASIKGYQ 283
Cdd:cd19081 158 RLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELLPLCREEGIGVIPYSPLAGGFLTGKYrsEADLPGSTRRGEAAKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 284 WLKDKvqsedgkkqQAKVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVME 362
Cdd:cd19081 238 YLNER---------GLRILDALdEVAAEHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVAR 306
|
..
gi 2462558728 363 ID 364
Cdd:cd19081 307 LD 308
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
79-360 |
5.35e-48 |
|
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: 165.06 E-value: 5.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLGTWvTFGSQ------ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRS 152
Cdd:cd19079 1 EYVRLGNSGLKVSRLCLGCM-SFGDPkwrpwvLDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 153 SYVITTKIF--WGGQAETeRGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSR 201
Cdd:cd19079 79 EVVIATKVYfpMGDGPNG-RGLSRKHImaevdaslkrlgtdyidlyqihrwdyetpIEETLEALHDVVKSGKVRYIGASS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 202 WGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQRE-KVEMqLPeLYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIK 280
Cdd:cd19079 158 MYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREeEREM-IP-LCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 281 GYqWLKDKVQSEDgkkqqAKVMD-LLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQT 359
Cdd:cd19079 236 AK-LKYDYFTEAD-----KEIVDrVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLSEEE 307
|
.
gi 2462558728 360 V 360
Cdd:cd19079 308 I 308
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
79-350 |
3.93e-43 |
|
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: 152.17 E-value: 3.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYA--AGKAERTLGNILKS--KGWRrSSY 154
Cdd:cd19151 1 KYNRCGRSGLKLPAISLGLWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 155 VITTK---IFWGGQ-----------AETERGLSRKHI----------------IEEIVRAMTYVINQGLALYWGTSRWGA 204
Cdd:cd19151 80 IISTKagyTMWPGPygdwgskkyliASLDQSLKRMGLdyvdifyhhrpdpetpLEETMGALDQIVRQGKALYVGISNYPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 205 AEIMEAYSMARQFNlIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASiKGYQW 284
Cdd:cd19151 160 EEAREAAAILKDLG-TPCLIHQPKYSMFNRW-VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 285 LKDKVQSEDgkkQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19151 237 LKPEQITEE---KLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
90-364 |
8.95e-43 |
|
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: 151.56 E-value: 8.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 90 VSCLGLGTwVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYA-------AGKAERTLGNILKSKGwRRSSYVITTKI-- 160
Cdd:cd19094 1 VSEICLGT-MTWGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 ---FWGGQAETERGLSRKHI-----------------------------------------------IEEIVRAMTYVIN 190
Cdd:cd19094 79 pgeGITWPRGGGTRLDRENIreavegslkrlgtdyidlyqlhwpdrytplfgggyytepseeedsvsFEEQLEALGELVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 191 QGLALYWGTSR---WGaaeIMEAYSMARQFNLIPPVCEQAEHHLFQReKVEMQLPELYHKIGVGSVTWYPLACGLITSKY 267
Cdd:cd19094 159 AGKIRHIGLSNetpWG---VMKFLELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 268 DGRVPDTCRASIKGYQWLKDKVQSEDGKKQQAKvmdLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLG 347
Cdd:cd19094 235 LDGAARPEGGRLNLFPGYMARYRSPQALEAVAE---YVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENID 311
|
330
....*....|....*..
gi 2462558728 348 ALQVlsQLTPQTVMEID 364
Cdd:cd19094 312 AFDV--PLSDELLAEID 326
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
79-352 |
2.97e-41 |
|
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: 147.22 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYA--AGKAERTLGNILKSK-GWRRSSYV 155
Cdd:cd19150 1 QYRRCGKSGLKLPALSLGLWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 156 ITTKI---FWGG----------------QAETERGLSRKHI-----------IEEIVRAMTYVINQGLALYWGTSRWGAA 205
Cdd:cd19150 81 ISTKAgydMWPGpygewgsrkyllasldQSLKRMGLDYVDIfyshrfdpdtpLEETMGALDHAVRSGKALYVGISSYSPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 206 EIMEAYSMARQFNlIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRASIKGYqwL 285
Cdd:cd19150 161 RTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS--L 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558728 286 KDKVQSEDgkkQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVL 352
Cdd:cd19150 238 SPKMLTEA---NLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
83-364 |
3.69e-41 |
|
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: 146.60 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 83 LGKSGLRVSCLGLGTwVTFGSQ----ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITT 158
Cdd:cd19080 3 LGRSGLRVSPLALGT-MTFGTEwgwgADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLAT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 159 KIFWG--GQAETERGLSRK-----------------------HI------IEEIVRAMTYVINQGLALYWGTSR---WGA 204
Cdd:cd19080 79 KYTMNrrPGDPNAGGNHRKnlrrsveaslrrlqtdyidllyvHAwdfttpVEEVMRALDDLVRAGKVLYVGISDtpaWVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 205 AEiMEAYSMARqfNLIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRvpDTCRASIKGYQW 284
Cdd:cd19080 159 AR-ANTLAELR--GWSPFVALQIEYSLLERT-PERELLPMARALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 285 LKDKVQSEDGKKQQAKVMDllpVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19080 233 VGFGKLTERNWAIVDVVAA---VAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
90-364 |
2.03e-36 |
|
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: 133.87 E-value: 2.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 90 VSCLGLGTWV----TFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTKIFWGG- 164
Cdd:cd19085 1 VSRLGLGCWQfgggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVSPDNl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 -----QAETERGLSR---KHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSmarqfnLIPPV 223
Cdd:cd19085 78 tpedvRKSCERSLKRlgtDYIdlyqihwpssdvpLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALD------AGRID 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 224 CEQAEHHLFQREKVEMQLPEL-YHKIGVgsVTWYPLACGLITSKY--DGRVPDT-CRASIKGYQwlkdkvqsEDGKKQQA 299
Cdd:cd19085 152 SNQLPYNLLWRAIEYEILPFCrEHGIGV--LAYSPLAQGLLTGKFssAEDFPPGdARTRLFRHF--------EPGAEEET 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558728 300 -KVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19085 222 fEALEKLkEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLD 286
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
73-364 |
2.49e-36 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 135.12 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 73 GRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYA--AGKAERTLGNILKSK-GW 149
Cdd:PRK09912 8 ERYGQMQYRYCGKSGLRLPALSLGLWHNFGHVNALESQRAILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 150 RRSSYVITTKI---FWGGQAETerGLSRKHII-----------------------------EEIVRAMTYVINQGLALYW 197
Cdd:PRK09912 88 YRDELIISTKAgydMWPGPYGS--GGSRKYLLasldqslkrmgleyvdifyshrvdentpmEETASALAHAVQSGKALYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 198 GTSRWGAAEIMEAYSMARQFNlIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVPDTCRA 277
Cdd:PRK09912 166 GISSYSPERTQKMVELLREWK-IPLLIHQPSYNLLNRWVDKSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 278 SIKG--YQWLKDKVQSEdgkkQQAKVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSq 354
Cdd:PRK09912 245 HREGnkVRGLTPKMLTE----ANLNSLRLLnEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNLT- 319
|
330
....*....|
gi 2462558728 355 LTPQTVMEID 364
Cdd:PRK09912 320 FSTEELAQID 329
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
89-364 |
1.18e-34 |
|
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: 129.27 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 89 RVSCLGLGTWvTFGSQ-------ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRSSYVITTKI- 160
Cdd:cd19093 1 EVSPLGLGTW-QWGDRlwwgygeYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKFa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 --FWGGQAET-----ERGLSRKHI-----------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQ 216
Cdd:cd19093 79 plPWRLTRRSvvkalKASLERLGLdsidlyqlhwpgpwysqIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 217 FNlIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCRASIKGYQWLKDKVqsedg 294
Cdd:cd19093 159 RG-VPLASNQVEYSLLYRDPEQNGLLPACDELGITLIAYSPLAQGLLTGKYspENPPPGGRRRLFGRKNLEKVQP----- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558728 295 kkqqakVMDLL-PVAHQLGCTVAQLAIAWCLrSEGVSsVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19093 233 ------LLDALeEIAEKYGKTPAQVALNWLI-AKGVV-PIPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
81-366 |
1.20e-31 |
|
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: 121.37 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 81 RNLGKSGLRVSCLGLGTWVTFG----SQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKskGWRRSSYVI 156
Cdd:cd19083 2 VKLGKSDIDVNPIGLGTNAVGGhnlyPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 157 TTK---IFWGG-----------QAETERGLSR----------------KHIIEEIVRAMTYVINQGLALYWGTSRWGAAE 206
Cdd:cd19083 80 ATKgahKFGGDgsvlnnspeflRSAVEKSLKRlntdyidlyyihfpdgETPKAEAVGALQELKDEGKIRAIGVSNFSLEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 207 IMEAySMARQFNLIppvceQAEHHLFQREKVEMQLPELyHKIGVGSVTWYPLACGLITSKYDgrvPDTcraSIKGYQWLK 286
Cdd:cd19083 160 LKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC-VENNISFIPYFPLASGLLAGKYT---KDT---KFPDNDLRN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 287 DK--VQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19083 227 DKplFKGERFSENLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFID 304
|
..
gi 2462558728 365 GL 366
Cdd:cd19083 305 AL 306
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
80-364 |
4.66e-30 |
|
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: 117.37 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 80 YRNLGKSGLRVSCLGLGTWV----TFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYV 155
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAigggPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 156 ITTK--IFWGGQA-----------------------ETERGLSR---KHI-------------IEEIVRAMTYVINQGLA 194
Cdd:cd19149 78 LATKcgLRWDREGgsfffvrdgvtvyknlspesireEVEQSLKRlgtDYIdlyqthwqdvetpIEETMEALEELKRQGKI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 195 LYWGTSRWGAAEIMEaYSMARQFNLIppvceQAEHHLFQREKVEMQLPeLYHKIGVGSVTWYPLACGLITSKYD-GR--V 271
Cdd:cd19149 158 RAIGASNVSVEQIKE-YVKAGQLDII-----QEKYSMLDRGIEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITpDRefD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 272 PDTCRASIKGYQwlKDKVqsedgkkqqAKVMDLL----PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLG 347
Cdd:cd19149 231 AGDARSGIPWFS--PENR---------EKVLALLekwkPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAK 299
|
330
....*....|....*..
gi 2462558728 348 ALQVlsQLTPQTVMEID 364
Cdd:cd19149 300 AGDI--RLSAEDIATMR 314
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
87-350 |
6.32e-30 |
|
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: 115.79 E-value: 6.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWVTFGSQIS----DETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVITTKIF- 161
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMSKdysdDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVSp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 162 WGGQAE-----TERGLSR---KHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQfnlI 220
Cdd:cd19072 79 DHLKYDdvikaAKESLKRlgtDYIdlylihwpnpsipIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---G 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 221 PPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVpdtcrasikgyqwlkdkvqsedgkkqqak 300
Cdd:cd19072 156 PIVANQVEYNLFDRE-EESGLLPYCQKNGIAIIAYSPLEKGKLSNAKGSPL----------------------------- 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2462558728 301 vmdLLPVAHQLGCTVAQLAIAWCLRSEGVsSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19072 206 ---LDEIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
79-363 |
3.37e-29 |
|
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: 114.62 E-value: 3.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLG----TWvtFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSY 154
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGcmgmSA--FYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 155 VITTKifWG---GQAETERGL--SRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTS 200
Cdd:cd19076 76 VIATK--FGivrDPGSGFRGVdgRPEYVraaceaslkrlgtdvidlyyqhrvdpnvpIEETVGAMAELVEEGKVRYIGLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 201 RWGAAEIMEAYSmarqfnlIPPVCE-QAEHHLFQREKVEMQLP---ELyhkiGVGSVTWYPLACGLITskydGRVPDTCR 276
Cdd:cd19076 154 EASADTIRRAHA-------VHPITAvQSEYSLWTRDIEDEVLPtcrEL----GIGFVAYSPLGRGFLT----GAIKSPED 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 277 ASIKGYQWLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCL-RSEGVSSVlLGVSSAEQLIEHLGALQVlsQL 355
Cdd:cd19076 219 LPEDDFRRNNPRFQGENFDKNLKLVEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VL 295
|
....*...
gi 2462558728 356 TPQTVMEI 363
Cdd:cd19076 296 TPEELAEI 303
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
87-364 |
3.36e-28 |
|
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: 111.94 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLG----TWvTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTKIFW 162
Cdd:cd19078 1 GLEVSAIGLGcmgmSH-GYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 163 GGQAETERGL----SRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIME 209
Cdd:cd19078 77 KIDGGKPGPLgldsRPEHIrkavegslkrlqtdyidlyyqhrvdpnvpIEEVAGTMKELIKEGKIRHWGLSEAGVETIRR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 210 AYSmarqfnlIPPVCE-QAEHHLFQREKVEMQLPELyHKIGVGSVTWYPLACGLITSKYDGRV---PDTCRASIKGYqwl 285
Cdd:cd19078 157 AHA-------VCPVTAvQSEYSMMWREPEKEVLPTL-EELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 286 kdkvqSEDGKKQQAKVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19078 226 -----TPEALEANQALVDLLkEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIE 298
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
88-348 |
1.72e-26 |
|
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: 105.64 E-value: 1.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 88 LRVSCLGLGTWvTFGSQ----ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTKI--F 161
Cdd:cd19086 1 LEVSEIGFGTW-GLGGDwwgdVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 162 WGGQAETERGLSRKHIIEEI-----------------------VRAMTYVIN-------QGLALYWGTS---RWGAAEIM 208
Cdd:cd19086 77 FDGGPERPQDFSPEYIREAVeaslkrlgtdyidlyqlhnppdeVLDNDELFEaleklkqEGKIRAYGVSvgdPEEALAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 209 EAYSMArqfnlippvCEQAEHHLFQREKVEmQLPELYHKIGVGSVTWYPLACGLITSKydgrvpdtcrasikgyqwlkdk 288
Cdd:cd19086 157 RRGGID---------VVQVIYNLLDQRPEE-ELFPLAEEHGVGVIARVPLASGLLTGK---------------------- 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 289 vqsedgkkqqakvmdllpvahqlgctVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGA 348
Cdd:cd19086 205 --------------------------LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
90-367 |
1.27e-25 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381328 [Multi-domain] Cd Length: 302 Bit Score: 105.06 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 90 VSCLGLGTWV------TFGSQISDETaEDVLTV--AYEHGVNLFDTAEVYAAGKAERTLGNILKskGWRRSSYVITT-KI 160
Cdd:cd19102 1 LTTIGLGTWAiggggwGGGWGPQDDR-DSIAAIraALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDRPIVATKcGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 FWGGQAETERGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEA- 210
Cdd:cd19102 78 LWDEEGRIRRSLKPASIraeceaslrrlgvdvidlyqihwpdpdepIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCq 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 211 -----------YSMARQ--FNLIPPVCEQaehhlfqrekvemqlpelyHKIGVgsVTWYPLACGLITSKYD-GRVpdtcr 276
Cdd:cd19102 158 aihpiaslqppYSLLRRgiEAEILPFCAE-------------------HGIGV--IVYSPMQSGLLTGKMTpERV----- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 277 ASIKGYQWLK-DKVQSEDGKKQQAKVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQ 354
Cdd:cd19102 212 ASLPADDWRRrSPFFQEPNLARNLALVDALrPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADL--R 289
|
330
....*....|...
gi 2462558728 355 LTPQTVMEIDGLL 367
Cdd:cd19102 290 LTPEELAEIEALL 302
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
86-364 |
1.88e-23 |
|
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: 98.09 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 86 SGLRVSCLGLGTWvTFGSQISDETAE-DVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTKIF-W- 162
Cdd:cd19138 7 DGTKVPALGQGTW-YMGEDPAKRAQEiEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKVLpSn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 163 ----GGQAETERGLSR---KHI------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLippV 223
Cdd:cd19138 83 asrqGTVRACERSLRRlgtDYLdlyllhwrggvpLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNC---A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 224 CEQAEHHLFQReKVEMQLPELYHKIGVGSVTWYPLAcglitskydgrvpdtcrasikgyqwlkdkvQSEDGKKQQAKVMD 303
Cdd:cd19138 160 ANQVLYNLGSR-GIEYDLLPWCREHGVPVMAYSPLA------------------------------QGGLLRRGLLENPT 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558728 304 LLPVAHQLGCTVAQLAIAWCLRSEGVSSVlLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19138 209 LKEIAARHGATPAQVALAWVLRDGNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
78-349 |
3.55e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381331 [Multi-domain] Cd Length: 250 Bit Score: 96.88 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGlgtwvtFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVIT 157
Cdd:cd19105 1 MPYRTLGKTGLKVSRLG------FGGGGLPRESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TKIFWGGQAETERGLSRKhiIEEIVRAM--TYV-INQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPV---CEQAEHHL 231
Cdd:cd19105 73 TKASPRLDKKDKAELLKS--VEESLKRLqtDYIdIYQLHGVDTPEERLLNEELLEALEKLKKEGKVRFIgfsTHDNMAEV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 232 FQR------------------EKVEMQ--LPELyHKIGVgsvtwyplacGLITSKydgrvpdTCRAsikgyqwlkdkvqs 291
Cdd:cd19105 151 LQAaiesgwfdvimvaynflnQPAELEeaLAAA-AEKGI----------GVVAMK-------TLAG-------------- 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558728 292 edGKKQQAKVMDLLpvahQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19105 199 --GYLQPALLSVLK----AKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
86-366 |
3.42e-22 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 94.35 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 86 SGLRVSCLGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIfWGGQ 165
Cdd:COG0656 1 NGVEIPALGLGTW-----QLPGEEAAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 166 AE-------TERGLSR---------------KHIIEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPV 223
Cdd:COG0656 72 HGyddtlaaFEESLERlgldyldlylihwpgPGPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 224 CEQAEHHLFQREkvemqlPEL--YHK-IGVGSVTWYPLAcglitskyDGRVpdtcrasikgyqwLKDKVqsedgkkqqak 300
Cdd:COG0656 148 VNQVELHPYLQQ------RELlaFCReHGIVVEAYSPLG--------RGKL-------------LDDPV----------- 189
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 301 vmdLLPVAHQLGCTVAQLAIAWCLRsEGVsSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEIDGL 366
Cdd:COG0656 190 ---LAEIAEKHGKTPAQVVLRWHLQ-RGV-VVIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
78-364 |
9.25e-22 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 95.27 E-value: 9.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTWvtfGSQISD-ETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKskgWRRSSYVI 156
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGM---RLPRKDeEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALK---GPRDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 157 TTKIfwGGQAETERGLsrKHIIEEIVRAM--TYV-------INQGLALYWGTSRWGAAEIMEAysmARQFNLI------- 220
Cdd:COG1453 73 ATKL--PPWVRDPEDM--RKDLEESLKRLqtDYIdlylihgLNTEEDLEKVLKPGGALEALEK---AKAEGKIrhigfst 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 221 ---PPVCEQA-EHHLF-----------QREKVEMQLPELYHKIGVGSVTWYPLACGLITskydgRVPDtcrasikgyqwl 285
Cdd:COG1453 146 hgsLEVIKEAiDTGDFdfvqlqynyldQDNQAGEEALEAAAEKGIGVIIMKPLKGGRLA-----NPPE------------ 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 286 kdkvqsedgkkqqaKVMDLLPVahqlGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHlgaLQVLSQLTPQTVMEID 364
Cdd:COG1453 209 --------------KLVELLCP----PLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDEN---LKTADNLEPLTEEELA 266
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
91-349 |
1.69e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 93.17 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 91 SCLGLGTwVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYA-------AGKAERTLGNILKSKGwRRSSYVITTKI--- 160
Cdd:cd19752 1 SELCLGT-MYFGTRTDEETSFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 --FWGGQAETERGLSRK-----------------------HI------IEEIVRAMTYVINQGLALYWGTSRWGAAEIME 209
Cdd:cd19752 79 prDPDGGPESPEGLSAEtieqeidkslrrlgtdyidlyyaHVddrdtpLEETLEAFNELVKAGKVRAIGASNFAAWRLER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 210 AYSMARQFNLIPPVCEQAEHHLFQR-----EKVEMQL-PEL-----YHKiGVGSVTWYPLACGLITSKyDGRVPDTcras 278
Cdd:cd19752 159 ARQIARQQGWAEFSAIQQRHSYLRPrpgadFGVQRIVtDELldyasSRP-DLTLLAYSPLLSGAYTRP-DRPLPEQ---- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462558728 279 ikgyqwlkdkvqsEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19752 233 -------------YDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
91-350 |
3.77e-20 |
|
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: 89.53 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 91 SCLGLGTwVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAA----GKAERTLGNILKSKGwRRSSYVITTKifwGG-- 164
Cdd:cd19082 1 SRIVLGT-ADFGTRIDEEEAFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 ---------------QAETERGLSR---KHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSM 213
Cdd:cd19082 76 dledmsrsrlspediRADLEESLERlgtDYIdlyflhrddpsvpVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 214 ARQFNLIPPVCEQAEHHLFQREK--------VEMQLPEL--YHKIGVGSVTWYPLACGLITSKYDGRVPDtcrASIKGYQ 283
Cdd:cd19082 156 AKAHGLPGFAASSPQWSLARPNEppwpgptlVAMDEEMRawHEENQLPVFAYSSQARGFFSKRAAGGAED---DSELRRV 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558728 284 WLkdkvqSEDGKKQQAKVMDLlpvAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19082 233 YY-----SEENFERLERAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
93-350 |
4.22e-20 |
|
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: 89.54 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKgwrrSSYVITTKI--FWGGQAETER 170
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGE----RGFKIDTKAnpGVGGGLSPEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 171 ------------GLSRKHI-----------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQA 227
Cdd:cd19075 81 vrkqletslkrlKVDKVDVfylhapdrstpLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 228 EHHLFQReKVEMQLPELYHKIGVGSVTWYPLACGLITSKY--DGRVPDTCR--ASIKGYQWLKDKVqsedGKKQQAKVMD 303
Cdd:cd19075 161 MYNAITR-QVETELFPCLRKLGIRFYAYSPLAGGFLTGKYkySEDKAGGGRfdPNNALGKLYRDRY----WKPSYFEALE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2462558728 304 LL-PVAHQLGCTVAQLAIAWC-----LRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19075 236 KVeEAAEKEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALE 288
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
79-366 |
6.22e-20 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 89.25 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 79 KYRNLGKSGLRVSCLGLG------TWVTfgsqISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKgwrRS 152
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGgggiggLMGR----TTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGL---PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 153 SYVITTKIFWGGQ------AETERGL---------------------------------SRKHII--EEIVRAMTYVINQ 191
Cdd:cd19104 74 GPYITTKVRLDPDdlgdigGQIERSVekslkrlkrdsvdllqlhnrigderdkpvggtlSTTDVLglGGVADAFERLRSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 192 GLALYWGTSRWGAAEIME------AYSMARQF-NLI--PPVCEQAEHHLFQREKvemQLPELYHKIGVGSVTWYPLACGL 262
Cdd:cd19104 154 GKIRFIGITGLGNPPAIRelldsgKFDAVQVYyNLLnpSAAEARPRGWSAQDYG---GIIDAAAEHGVGVMGIRVLAAGA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 263 ITSKYD-GRVPDTCRASIkgyqwlkdkvqSEDGKKQQAKVMDLLPvahQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQ 341
Cdd:cd19104 231 LTTSLDrGREAPPTSDSD-----------VAIDFRRAAAFRALAR---EWGETLAQLAHRFALSNPGVSTVLVGVKNREE 296
|
330 340
....*....|....*....|....*..
gi 2462558728 342 LIEhlgALQVLSQ--LTPQTVMEIDGL 366
Cdd:cd19104 297 LEE---AVAAEAAgpLPAENLARLEAL 320
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
78-366 |
2.03e-19 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 88.37 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTwVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAA-------GKAERTLGNILKSKGwR 150
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGT-MTFGEQNSEADAHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-S 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 151 RSSYVITTKIfwGGQAET-------ERGLSRKHIIE-------------------------------------------- 179
Cdd:PRK10625 79 REKLIIASKV--SGPSRNndkgirpNQALDRKNIREalhdslkrlqtdyldlyqvhwpqrptncfgklgyswtdsapavs 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 180 --EIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYP 257
Cdd:PRK10625 157 llETLDALAEQQRAGKIRYIGVSNETAFGVMRYLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSC 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 258 LACGLITSKY-DGRVPDTCRASikgyqwLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGV 336
Cdd:PRK10625 236 LAFGTLTGKYlNGAKPAGARNT------LFSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGA 309
|
330 340 350
....*....|....*....|....*....|
gi 2462558728 337 SSAEQLIEHLGALQVlsQLTPQTVMEIDGL 366
Cdd:PRK10625 310 TTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
85-351 |
4.34e-19 |
|
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: 86.46 E-value: 4.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 85 KSGLRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTK--IFW 162
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgIRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 163 GGQAETERG----LSRKHII-----------------------------EEIVRAMTYVINQGLALYWGTSRWGAAEIme 209
Cdd:cd19092 81 GDDPRPGRIkhydTSKEHILasvegslkrlgtdyldllllhrpdplmdpEEVAEAFDELVKSGKVRYFGVSNFTPSQI-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 210 aySMARQFNLIPPVCEQAEhhlfqrekvemqlpelyhkigvgsvtWYPLACGLItskYDGRVpDTCRAsiKGYQWL---- 285
Cdd:cd19092 159 --ELLQSYLDQPLVTNQIE--------------------------LSLLHTEAI---DDGTL-DYCQL--LDITPMawsp 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 286 --KDKVQSEDGKKQQaKVMDLL-PVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQV 351
Cdd:cd19092 205 lgGGRLFGGFDERFQ-RLRAALeELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
93-350 |
7.89e-19 |
|
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: 85.30 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGT-WVTFG-SQISDETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILksKGWRRSSYVITTKIFWGGQAET-- 168
Cdd:cd19090 3 LGLGTaGLGGVfGGVDDDEAVATIRAALDLGINYIDTAPAY--GDSEERLGLAL--AELPREPLVLSTKVGRLPEDTAdy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 169 -------------ERgLSRKHI------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqF 217
Cdd:cd19090 79 sadrvrrsveeslER-LGRDRIdllmihdpervpwvdilaPGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIETGD-F 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 218 NLIPPVCeqaEHHLFQREKVEMQLPELY-HKIGV--GSvtwyPLACGLITSKYDGRVPDTcrasikgYQWLkdkvqsedG 294
Cdd:cd19090 157 DVVLTAN---RYTLLDQSAADELLPAAArHGVGVinAS----PLGMGLLAGRPPERVRYT-------YRWL--------S 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 295 KKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19090 215 PELLDRAKRLYELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
86-364 |
1.07e-18 |
|
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: 85.37 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 86 SGLRVSCLGLG----TWVtfGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTL---GNILKSKGWRRSSYVITT 158
Cdd:cd19077 1 NGKLVGPIGLGlmglTWR--PNPTPDEEAFETMKAALDAGSNLWNGGEFYGPPDPHANLkllARFFRKYPEYADKVVLSV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 159 K---IFWGGQAETERGLSRKHI--------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIME 209
Cdd:cd19077 79 KgglDPDTLRPDGSPEAVRKSIenilralggtkkidifeparvdpnvpIEETIKALKELVKEGKIRGIGLSEVSAETIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 210 AYSMArqfnliPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITskydGRVPDtcRASIKGYQWLK--D 287
Cdd:cd19077 159 AHAVH------PIAAVEVEYSLFSREIEENGVLETCAELGIPIIAYSPLGRGLLT----GRIKS--LADIPEGDFRRhlD 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462558728 288 KVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSV-LLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19077 227 RFNGENFEKNLKLVDALQELAEKKGCTPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
87-364 |
2.25e-18 |
|
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: 83.77 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWVTFGSQI----SDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgWRRSSYVITTKIfW 162
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTpdysRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKV-W 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 163 GGQAETE----------RGLSRKHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARQfnl 219
Cdd:cd19137 78 PTNLRYDdllrslqnslRRLDTDYIdlylihwpnpnipLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 220 iPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSkydgrvpdtcrasikgyqwlKDKVQSedgkkqqa 299
Cdd:cd19137 155 -PIVCNQVKYNLEDRDPERDGLLEYCQKNGITVVAYSPLRRGLEKT--------------------NRTLEE-------- 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558728 300 kvmdllpVAHQLGCTVAQLAIAWCLRSEGVSSVLLGvSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19137 206 -------IAKNYGKTIAQIALAWLIQKPNVVAIPKA-GRVEHLKENLKATEI--KLSEEEMKLLD 260
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
80-160 |
3.44e-18 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381326 [Multi-domain] Cd Length: 238 Bit Score: 82.92 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 80 YRNLGKSGLRVSCLGLGTWVTFGsqISDETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKSkgwRRSSYVITTK 159
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGR--LSQEEAAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATK 73
|
.
gi 2462558728 160 I 160
Cdd:cd19100 74 T 74
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
78-160 |
9.60e-18 |
|
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: 82.60 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTwVTFGS---QISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSY 154
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGA-SPLGGvfgPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSY 77
|
....*.
gi 2462558728 155 VITTKI 160
Cdd:cd19163 78 YLATKV 83
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
91-349 |
1.68e-17 |
|
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: 81.07 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 91 SCLGLGTW---VTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVITTKI------- 160
Cdd:cd19096 1 SVLGFGTMrlpESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEAL--KEGPREKFYLATKLppwsvks 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 ------------------------FWG-GQAETERGLSRKHIIEEIVRAMTyvinQGLALYWGTSRWGAAE----IMEAY 211
Cdd:cd19096 79 aedfrrileeslkrlgvdyidfylLHGlNSPEWLEKARKGGLLEFLEKAKK----EGLIRHIGFSFHDSPEllkeILDSY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 212 SMArqFNLIPpvceqaeHHLFQREKVEMQ-LPELYHKIGVGSVTWYPLACGLItskydGRVPDtcrasikgyqwlkdkvq 290
Cdd:cd19096 155 DFD--FVQLQ-------YNYLDQENQAGRpGIEYAAKKGMGVIIMEPLKGGGL-----ANNPP----------------- 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 291 sedgkkqqaKVMDLLPvahQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19096 204 ---------EALAILC---GAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAA 250
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
78-363 |
1.77e-17 |
|
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: 82.11 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 78 MKYRNLGKSGLRVSCLGLGTW---VTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKSKGWRRSSY 154
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMglsAFYGPPKPDEERFAVLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 155 VITTKIFWGGQAET----------------ERGLSR---KHI-------------IEEIVRAMTYVINQGLALYWGTSRW 202
Cdd:cd19144 79 FLATKFGIEKNVETgeysvdgspeyvkkacETSLKRlgvDYIdlyyqhrvdgktpIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 203 GAAEIMEAYSmarqfnlIPPVCE-QAEHHLF--QREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYdgRVPDTCRAsi 279
Cdd:cd19144 159 SAETLRRAHA-------VHPIAAvQIEYSPFslDIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAI--RSPDDFEE-- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 280 KGYQWLKDKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQT 359
Cdd:cd19144 228 GDFRRMAPRFQAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEE 305
|
....
gi 2462558728 360 VMEI 363
Cdd:cd19144 306 EKEI 309
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
87-342 |
4.96e-16 |
|
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: 77.73 E-value: 4.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWVTFGSQ---ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRSSYVITTK--IF 161
Cdd:cd19148 1 DLPVSRIALGTWAIGGWMwggTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 162 WGGQAETERGLSRKHI-----------------------------IEEIVRAMTYVINQGLALYWGTSRWgAAEIMEAYs 212
Cdd:cd19148 80 WDEGGEVVRNSSPARIrkevedslrrlqtdyidlyqvhwpdplvpIEETAEALKELLDEGKIRAIGVSNF-SPEQMETF- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 213 maRQFNLIPPVceQAEHHLFQREKVEMQLPelY-HKIGVGSVTWYPLACGLITSKYDgrvPDTcrasikgyQWLKDKVQS 291
Cdd:cd19148 158 --RKVAPLHTV--QPPYNLFEREIEKDVLP--YaRKHNIVTLAYGALCRGLLSGKMT---KDT--------KFEGDDLRR 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 292 EDGKKQQ-------AKVMDLLPVA-HQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQL 342
Cdd:cd19148 221 TDPKFQEprfsqylAAVEELDKLAqERYGKSVIHLAVRWLLDQPGVSIALWGARKPEQL 279
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
81-355 |
2.18e-15 |
|
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: 75.65 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 81 RNLGKSGLRVSCLGLGTwVTFGSQISDETAEDVL--TV--AYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVI 156
Cdd:cd19153 3 ETLEIALGNVSPVGLGT-AALGGVYGDGLEQDEAvaIVaeAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 157 TTKIFWGGQAETE-----------RGLSRKH-------------------IIEEIVRAMTYVINQGLALYWGTSrwGAAE 206
Cdd:cd19153 82 ATKVGRYRDSEFDysaervrasvaTSLERLHttyldvvylhdiefvdydtLVDEALPALRTLKDEGVIKRIGIA--GYPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 207 IMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKyDGRVPDTCRASIKGYQWLK 286
Cdd:cd19153 160 DTLTRATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRGAGPHVINASPLSMGLLTSQ-GPPPWHPASGELRHYAAAA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 287 DKVQSEDGKKqqakvmdllpvahqlgctVAQLAIAWCLRSE-GVSSVLLGVSSAEQLIEHLGALQVLSQL 355
Cdd:cd19153 239 DAVCASVEAS------------------LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASL 290
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
91-348 |
2.52e-15 |
|
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: 74.96 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 91 SCLGLGTWVTFGSQ--ISDETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILksKGWRRSSYVITTKI--FWGGQa 166
Cdd:cd19095 1 SVLGLGTSGIGRVWgvPSEAEAARLLNTALDLGINLIDTAPAY--GRSEERLGRAL--AGLRRDDLFIATKVgtHGEGG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 167 ETERGLSRKHII-----------------------------EEIVRAMTYVINQGLALYWG-TSRwgAAEIMEAYSMARq 216
Cdd:cd19095 76 RDRKDFSPAAIRasierslrrlgtdyidllqlhgpsddeltGEVLETLEDLKAAGKVRYIGvSGD--GEELEAAIASGV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 217 FNLIppvceQAEHHLFQREkvEMQLPELYHKIGVGSVTWYPLACGLITSKydgrvpdtcRASIKGYQWLKDKvqsedgkk 296
Cdd:cd19095 153 FDVV-----QLPYNVLDRE--EEELLPLAAEAGLGVIVNRPLANGRLRRR---------VRRRPLYADYARR-------- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462558728 297 qqakvmdLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGA 348
Cdd:cd19095 209 -------PEFAAEIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
87-366 |
5.10e-15 |
|
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: 74.22 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIFWGG-- 164
Cdd:cd19140 5 GVRIPALGLGTY-----PLTGEECTRAVEHALELGYRHIDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPDNys 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 ----QAETERGLSR---------------KHI-IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPVC 224
Cdd:cd19140 77 pddfLASVEESLRKlrtdyvdllllhwpnKDVpLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 225 EQAEHH--LFQRekvemQLPELYHKIGVGSVTWYPLAcglitskyDGRVpdtcrasikgyqwLKDKVQSEDGKKqqakvm 302
Cdd:cd19140 153 NQVEYHpyLDQR-----KLLDAAREHGIALTAYSPLA--------RGEV-------------LKDPVLQEIGRK------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558728 303 dllpvaHqlGCTVAQLAIAWCLRSEGVsSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEIDGL 366
Cdd:cd19140 201 ------H--GKTPAQVALRWLLQQEGV-AAIPKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
81-363 |
8.69e-15 |
|
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: 74.01 E-value: 8.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 81 RNLGKSGLRVSCLGLGTW---VTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVIT 157
Cdd:cd19145 3 VKLGSQGLEVSAQGLGCMglsGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKAL--KDGPREKVQLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 158 TK--IFWGGQ-------------AETERGLSRKHI----------------IEEIVRAMTYVINQGLALYWGTSRWGAAE 206
Cdd:cd19145 81 TKfgIHEIGGsgvevrgdpayvrAACEASLKRLDVdyidlyyqhridttvpIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 207 IMEAYSMArqfnliPPVCEQAEHHLFQREkVEMQLPELYHKIGVGSVTWYPLACGLITSK---YDGRVPDTCRASIKgyq 283
Cdd:cd19145 161 IRRAHAVH------PITAVQLEWSLWTRD-IEEEIIPTCRELGIGIVPYSPLGRGFFAGKaklEELLENSDVRKSHP--- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 284 wlkdKVQSEDGKKQQAKVMDLLPVAHQLGCTVAQLAIAWCL-RSEGVSSVlLGVSSAEQLIEHLGALQVlsQLTPQTVME 362
Cdd:cd19145 231 ----RFQGENLEKNKVLYERVEALAKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKE 303
|
.
gi 2462558728 363 I 363
Cdd:cd19145 304 I 304
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
90-349 |
1.01e-14 |
|
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: 73.41 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 90 VSCLGLGTW-----VTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSYVITTKifwGG 164
Cdd:cd19088 1 VSRLGYGAMrltgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHP---YPDDVVIATK---GG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 QAETE---------------------RGLSRKHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEA 210
Cdd:cd19088 75 LVRTGpgwwgpdgspeylrqaveaslRRLGLDRIdlyqlhridpkvpFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 211 YSMARqfnlIppVCEQAEHHLFQREKVEMQlpELYHKIGVGSVTWYPLACGlitskyDGRVPDTcrasikgyqwlkdkvq 290
Cdd:cd19088 155 RAIVR----I--VSVQNRYNLANRDDEGVL--DYCEAAGIAFIPWFPLGGG------DLAQPGG---------------- 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 291 sedgkkqqakvmDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19088 205 ------------LLAEVAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAA 251
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
87-364 |
1.78e-14 |
|
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: 73.61 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTwVTFGSQ-------ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRSSYVITTK 159
Cdd:cd19146 8 GVRVSPLCLGA-MSFGEAwksmmgeCDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 160 I---------------FWGGQAETERgLSRKH----------------------IIEEIVRAMTYVINQGLALYWGTSRW 202
Cdd:cd19146 86 YttgyrrggpikiksnYQGNHAKSLR-LSVEAslkklqtsyidilyvhwwdyttSIPELMQSLNHLVAAGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 203 GAAEIMEAYSMARQFNLIPPVCEQAEHHL----FQREKVEMQLPElyhkiGVGSVTWYPLACGLITSKYDGRVPDTcras 278
Cdd:cd19146 165 PAWVVSKANAYARAHGLTQFVVYQGHWSAafrdFERDILPMCEAE-----GMALAPWGVLGQGQFRTEEEFKRRGR---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 279 ikgyQWLKDKVQSEDGKKQQAKvmdLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVlsQLTPQ 358
Cdd:cd19146 236 ----SGRKGGPQTEKERKVSEK---LEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDE 306
|
....*.
gi 2462558728 359 TVMEID 364
Cdd:cd19146 307 EIQEIE 312
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
93-350 |
3.00e-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: 381323 [Multi-domain] Cd Length: 267 Bit Score: 72.17 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTwVTFGS---------QISDETAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKSKgwrrSSYVITTKI--F 161
Cdd:cd19097 3 LALGT-AQFGLdygianksgKPSEKEAKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKLppL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 162 WGGQAETERG-----------LSRKHI--------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSmARQ 216
Cdd:cd19097 76 KEDKKEDEAAieasveaslkrLKVDSLdglllhnpddllkhGGKLVEALLELKKEGLIRKIGVSVYSPEELEKALE-SFK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 217 FNLIppvceQAEHHLF-QREKVEMQLPELyHKIGVG----SVtwypLACGLITSKYDgRVPDtcrasiKGYQWLKdkvqs 291
Cdd:cd19097 155 IDII-----QLPFNILdQRFLKSGLLAKL-KKKGIEiharSV----FLQGLLLMEPD-KLPA------KFAPAKP----- 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 292 edgkkqqaKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQ 350
Cdd:cd19097 213 --------LLKKLHELAKKLGLSPLELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFK 263
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
80-355 |
2.17e-13 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 70.19 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 80 YRNLGKSGLRVSCLGLGT---WVTFGSqISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVI 156
Cdd:PLN02587 1 LRELGSTGLKVSSVGFGAsplGSVFGP-VSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 157 TTKI--FWGG---QAE-----TERGLSR-------------------KHIIEEIVRAMTYVINQGLALYWGTSrwGAAEI 207
Cdd:PLN02587 80 STKCgrYGEGfdfSAErvtksVDESLARlqldyvdilhchdiefgslDQIVNETIPALQKLKESGKVRFIGIT--GLPLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 208 MEAYSMARqfnlIPP----VCEQAEHHLFQREKVEMQLPELYHKiGVGSVTWYPLACGLITSkydgrvpdtcrasiKGY- 282
Cdd:PLN02587 158 IFTYVLDR----VPPgtvdVILSYCHYSLNDSSLEDLLPYLKSK-GVGVISASPLAMGLLTE--------------NGPp 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558728 283 QWLKDKVQSEDGKKQQAKVMDLlpvahqLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQL 355
Cdd:PLN02587 219 EWHPAPPELKSACAAAATHCKE------KGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETS 285
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
93-364 |
5.12e-12 |
|
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: 64.98 E-value: 5.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIFWGGQ------A 166
Cdd:cd19073 4 LGLGTW-----QLRGDDCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDHLrpedlkK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 167 ETERGLSR---KHI-------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPVCEQAEHH 230
Cdd:cd19073 76 SVDRSLEKlgtDYVdlllihwpnptvpLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFH 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 231 --LFQREkvemqLPELYHKIGVGSVTWYPLACGLItskydgrvpdtcrasikgyqwLKDKVqsedgkkqqakvmdLLPVA 308
Cdd:cd19073 152 pfLYQAE-----LLEYCRENDIVITAYSPLARGEV---------------------LRDPV--------------IQEIA 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 309 HQLGCTVAQLAIAWcLRSEGVsSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19073 192 EKYDKTPAQVALRW-LVQKGI-VVIPKASSEDHLKENLAIFDW--ELTSEDVAKID 243
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
95-341 |
1.30e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 64.66 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 95 LGTW----------VTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgWRRSSYVITTKIFWGG 164
Cdd:cd19103 9 LGTWswgsggaggdQVFGNHLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 QAET--------ERGLSRK----------HIIEEIVRAMTYVI---NQGLALYWGTSRWGAAEIMEAYSMARQFNL-IPP 222
Cdd:cd19103 87 AGQSadpvadmlEGSLARLgtdyidiywiHNPADVERWTPELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAGVsLSA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 223 VceQAEHHLFQREKVEMQLPELYHKIGVGSVTWYPLACGLITSKYDGRVP---DTCRAsiKGYQWLKDKVqsedgkKQQA 299
Cdd:cd19103 167 V--QNHYSLLYRSSEEAGILDYCKENGITFFAYMVLEQGALSGKYDTKHPlpeGSGRA--ETYNPLLPQL------EELT 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2462558728 300 KVMDLLPVAHqlGCTVAQLAIAWClRSEGVSSVlLGVSSAEQ 341
Cdd:cd19103 237 AVMAEIGAKH--GASIAQVAIAWA-IAKGTTPI-IGVTKPHH 274
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
93-364 |
2.52e-11 |
|
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: 63.27 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIFWGGQ--AETER 170
Cdd:cd19071 4 IGLGTY-----KLKPEETAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWPTDHgyERVRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 171 GL--SRKHI------------------------IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPVC 224
Cdd:cd19071 76 ALeeSLKDLgldyldlylihwpvpgkeggskeaRLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 225 EQAEHHLF--QREKVEmqlpelY---HKIGVgsVTWYPLACGlitskydgrvpdtcrasikGYQWLKDKVqsedgkkqqa 299
Cdd:cd19071 152 NQIELHPYlqQKELVE------FckeHGIVV--QAYSPLGRG-------------------RRPLLDDPV---------- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558728 300 kvmdLLPVAHQLGCTVAQLAIAWCLRSeGVsSVLLGVSSAEQLIEHLGALQVlsQLTPQTVMEID 364
Cdd:cd19071 195 ----LKEIAKKYGKTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
93-351 |
4.06e-11 |
|
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.
Pssm-ID: 381378 [Multi-domain] Cd Length: 308 Bit Score: 63.40 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTwVTFGS---QISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwrRSSYVITTKI--------- 160
Cdd:cd19152 3 LGFGT-APLGNlyeAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVgrllvplqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 --------FWGG----------QAETER---------GLSRKHI----------------------IEEIVRAMTYVINQ 191
Cdd:cd19152 80 veptfepgFWNPlpfdavfdysYDGILRsiedslqrlGLSRIDLlsihdpdedlagaesdehfaqaIKGAFRALEELREE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 192 GLALYW--GTSRWGAAE----------IMeaysMARQFNLIppvcEQAEHHLFqrekvemqLPELyHKIGVGSVTWYPLA 259
Cdd:cd19152 160 GVIKAIglGVNDWEVILrileeadldwVM----LAGRYTLL----DHSAAREL--------LPEC-EKRGVKVVNAGPFN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 260 CGLItskydgrvpdtcrASIKGYQWLKDKVQSEDgkkQQAKVMDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSA 339
Cdd:cd19152 223 SGFL-------------AGGDNFDYYEYGPAPPE---LIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSP 286
|
330
....*....|..
gi 2462558728 340 EQLIEHLGALQV 351
Cdd:cd19152 287 ERVEENVALLAT 298
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
88-159 |
6.91e-11 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 62.72 E-value: 6.91e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462558728 88 LRVSCLGLGTWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILK----SKGWRRSSYVITTK 159
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRelieKGGIKRDEVVIVTK 76
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
91-160 |
1.00e-09 |
|
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: 59.26 E-value: 1.00e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558728 91 SCLGLGTwVTFG---SQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwrRSSYVITTKI 160
Cdd:cd19161 1 SELGLGT-AGLGnlyTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV 70
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
94-372 |
1.30e-08 |
|
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: 55.32 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 94 GLGT-WVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIFWGG---QAETE 169
Cdd:cd19120 10 GTGTaWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIkdpREALR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 170 RGLSR--------------------KHIIEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPVCEQAEH 229
Cdd:cd19120 87 KSLAKlgvdyvdlylihspffakegGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 230 HLFqrekVEMQLPEL--YHKigvgsvtwyplACGLITSKYDGRVPdtcrasikgyqwlkdKVQSEDGKKQQAkvmdLLPV 307
Cdd:cd19120 163 HPY----LYPQQPALleYCR-----------EHGIVVSAYSPLSP---------------LTRDAGGPLDPV----LEKI 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558728 308 AHQLGCTVAQLAIAWCLrSEGVsSVLLGVSSAEQLIEHLGALQVLsqLTPQTVMEIDGLLGNKPH 372
Cdd:cd19120 209 AEKYGVTPAQVLLRWAL-QKGI-VVVTTSSKEERMKEYLEAFDFE--LTEEEVEEIDKAGKQKHF 269
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
93-349 |
6.48e-08 |
|
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: 53.52 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTwvtfGSQ-----ISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILksKGWRRSSYVITTKI------- 160
Cdd:cd19162 3 LGLGA----ASLgnlarAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAAL--ARHPRAEYVVSTKVgrllepg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 FWGGQAETER--------------------GLSRKHI-------------IEEIVRAMTYVINQGL--ALYWGTSRWGAA 205
Cdd:cd19162 77 AAGRPAGADRrfdfsadgirrsieaslerlGLDRLDLvflhdpdrhllqaLTDAFPALEELRAEGVvgAIGVGVTDWAAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 206 eiMEAYSMARqFNLIPPVceqAEHHLFQREKVEMQLPELYHKiGVGSVTWYPLACGLItskyDGRVPDTCRAsikgyqwl 285
Cdd:cd19162 157 --LRAARRAD-VDVVMVA---GRYTLLDRRAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAGDRY-------- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462558728 286 kDKVQSEDGKKQQAKvmDLLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGAL 349
Cdd:cd19162 218 -DYRPATPEVLARAR--RLAAVCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
85-256 |
9.48e-08 |
|
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: 53.18 E-value: 9.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 85 KSGLRVSCLGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVY----AAGKAertLGNILKSKGWRRSSYVITTKI 160
Cdd:cd19154 7 SNGVKMPLIGLGTW-----QSKGAEGITAVRTALKAGYRLIDTAFLYqneeAIGEA---LAELLEEGVVKREDLFITTKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 161 FWG--GQAETERGLSRK--------------HI-------------------------IEEIVRAMTYVINQGLALYWGT 199
Cdd:cd19154 79 WTHehAPEDVEEALRESlkklqleyvdlyliHApaafkddegesgtmengmsihdavdVEDVWRGMEKVYDEGLTKAIGV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462558728 200 SRWGAAEIMEAYSMARqfnlIPPVCEQAEHHLFQREKvemQLPELYHKIGVgSVTWY 256
Cdd:cd19154 159 SNFNNDQIQRILDNAR----VKPHNNQVECHLYFPQK---ELVEFCKKHNI-SVTSY 207
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
85-159 |
2.38e-07 |
|
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381390 [Multi-domain] Cd Length: 298 Bit Score: 51.89 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 85 KSGLRVSCLGLGTwvtFGSQISDE----TAEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKS--KGWRRSSYVITT 158
Cdd:cd19164 10 LAGLPPLIFGAAT---FSYQYTTDpesiPPVDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIIT 84
|
.
gi 2462558728 159 K 159
Cdd:cd19164 85 K 85
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
87-372 |
7.93e-06 |
|
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from Leishmania major and Trypanosoma brucei are founding members of aldo-keto reductase family 5 member A1 (AKR5A1) and A2 (AKR5A2), respectively. PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity toward the synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde.
Pssm-ID: 381382 [Multi-domain] Cd Length: 266 Bit Score: 46.74 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWvtfgsQISD-ETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIfWGGQ 165
Cdd:cd19156 6 GVEMPRLGLGVW-----RVQDgAEAENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 166 AETERGL-----SRKHIIEEIV-----------------RAMTYVINQGLALYWGTSRWGAAEIMEAYSMARqfnlIPPV 223
Cdd:cd19156 77 QGYESTLaafeeSLEKLGLDYVdlylihwpvkgkfkdtwKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 224 CEQAE-HHLFQREKVEMQLPElyHKIGVGSvtWYPLACGLItskydgrvpdtcrasikgyqwLKDKVQSEDGKKQqakvm 302
Cdd:cd19156 153 VNQIElHPLLTQEPLRKFCKE--KNIAVEA--WSPLGQGKL---------------------LSNPVLKAIGKKY----- 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 303 dllpvahqlGCTVAQLAIAWCLRSegvSSVLLGVSSAEQLIEHLGALQVLsQLTPQTVMEIDGLlgNKPH 372
Cdd:cd19156 203 ---------GKSAAQVIIRWDIQH---GIITIPKSVHEERIQENFDVFDF-ELTAEEIRQIDGL--NTDH 257
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
93-172 |
1.06e-05 |
|
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: 46.60 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKSKGWRRSSYVITTKIfWGGQAETERGL 172
Cdd:cd19131 13 LGLGVW-----QVSNDEAASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL 83
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
86-364 |
2.44e-05 |
|
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: 45.59 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 86 SGLRVSCLGLG------TWVTFGSQISDETAEDVLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGwRRSSYVITTK 159
Cdd:cd19147 6 AGIRVSPLILGamsigdAWSGFMGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 160 I----------------FWGGQA--------ETERGLSRKHI-------------IEEIVRAMTYVINQGLALYWGTSRW 202
Cdd:cd19147 85 FttdykayevgkgkavnYCGNHKrslhvsvrDSLRKLQTDWIdilyvhwwdyttsIEEVMDSLHILVQQGKVLYLGVSDT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 203 GAAEIMEAYSMARQFNLIPPVCEQAEHHLFQREKVEMQLPELYHkIGVGSVTWYPLACGLITSKydgrvpDTCRASIKGY 282
Cdd:cd19147 165 PAWVVSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARH-FGMALAPWDVLGGGKFQSK------KAVEERKKNG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 283 QWLKDKVQSEDGKKQQAKVMD-LLPVAHQLGC-TVAQLAIAWcLRSEGVSSV-LLGVSSAEQLIEHLGALQVlsQLTPQT 359
Cdd:cd19147 238 EGLRSFVGGTEQTPEEVKISEaLEKVAEEHGTeSVTAIALAY-VRSKAPNVFpLVGGRKIEHLKDNIEALSI--KLTPEE 314
|
....*
gi 2462558728 360 VMEID 364
Cdd:cd19147 315 IEYLE 319
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
93-261 |
5.62e-05 |
|
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: 44.46 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 93 LGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYAagkAERTLGNILKSKGWRRSSYVITTKI------FWGGQA 166
Cdd:cd19134 14 IGLGVG-----ELSDDEAERSVSAALEAGYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLatpdqgFTASQA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 167 ETERGLSR-------------------KHIieEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMArqfnLIPPVCEQA 227
Cdd:cd19134 86 ACRASLERlgldyvdlylihwpagregKYV--DSWGGLMKLREEGLARSIGVSNFTAEHLENLIDLT----FFTPAVNQI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 2462558728 228 EHH--LFQREkvemqLPELYHKIGVGSVTWYPLACG 261
Cdd:cd19134 160 ELHplLNQAE-----LRKVNAQHGIVTQAYSPLGVG 190
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
92-322 |
1.04e-04 |
|
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: 43.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 92 CLGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVY----AAGKAertLGNILKSKGWRRSSYVITTKIfWGGQAE 167
Cdd:cd19128 3 RLGFGTY-----KITESESKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 168 TE------------------------------------------RGLSRKHIIEEIVRAMTYVINQGLALYWGTSRWGAA 205
Cdd:cd19128 74 PEnvkeqllitlqdlqleyldlflihwplafdmdtdgdprddnqIQSLSKKPLEDTWRAMEQCVDEKLTKNIGVSNYSTK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 206 EIMEAYSMARqfnlIPPVCEQAEHHL-FQREKVEMQLPElyHKIGvgsVTWYPLACGliTSKYDGRVPDTCRAsikgyqw 284
Cdd:cd19128 154 LLTDLLNYCK----IKPFMNQIECHPyFQNDKLIKFCIE--NNIH---VTAYRPLGG--SYGDGNLTFLNDSE------- 215
|
250 260 270
....*....|....*....|....*....|....*...
gi 2462558728 285 lkdkvqsedgkkqqakvmdLLPVAHQLGCTVAQLAIAW 322
Cdd:cd19128 216 -------------------LKALATKYNTTPPQVIIAW 234
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
110-362 |
1.86e-04 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 43.10 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 110 AEDVLTVAYEHGVNLFDTAEVYaaGKAERTLGNILKSKGWRRSSYVITTKifWG-------------------------G 164
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdaavhevkdhslarllK 112
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 165 QAETERGLSRKHI----I------------EEIVRAMTYVINQGLALYWGTSRWGAAEIMEA-----YSMARQFNlippv 223
Cdd:cd19098 113 QWEETRSLLGKHLdlyqIhsatlesgvledADVLAALAELKAEGVKIGLSLSGPQQAETLRRaleieIDGARLFD----- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 224 CEQAEHHLFQREKVEmqLPELYHKIGVGSVTWYPLACGLITSkydgRVPDTcrasikgyqwlkdkvqsedgkKQQAKVMD 303
Cdd:cd19098 188 SVQATWNLLEQSAGE--ALEEAHEAGMGVIVKEALANGRLTD----RNPSP---------------------ELAPLMAV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462558728 304 LLPVAHQLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIEHLGALQVLSQLTPQTVME 362
Cdd:cd19098 241 LKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDVSLDLELLAALA 299
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
93-160 |
2.19e-04 |
|
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: 42.62 E-value: 2.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462558728 93 LGLGTWvtfgsQISD-ETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILKS----KGWRRSSYVITTKI 160
Cdd:cd19136 4 LGLGTF-----RLRGeEEVRQAVDAALKAGYRLIDTASVY---RNEADIGKALRDllpkYGLSREDIFITSKL 68
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
178-366 |
9.92e-04 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 40.72 E-value: 9.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 178 IEEIVRAMTYVINQGLALYWGTSRWGAAEIMEAYSMArqfnliPPVCEQAEHHLFQREKVEMqLPELYHKiGVGSVTWYP 257
Cdd:PRK10376 143 IEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYNLAHRADDAL-IDALARD-GIAYVPFFP 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 258 LAcglitskydGRVPdtcrasikgyqwlkdkVQSEDgkkqqakvmdLLPVAHQLGCTVAQLAIAWCL-RSEgvsSVLL-- 334
Cdd:PRK10376 215 LG---------GFTP----------------LQSST----------LSDVAASLGATPMQVALAWLLqRSP---NILLip 256
|
170 180 190
....*....|....*....|....*....|..
gi 2462558728 335 GVSSAEQLIEHLGALQVlsQLTPQTVMEIDGL 366
Cdd:PRK10376 257 GTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
93-163 |
3.86e-03 |
|
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: 38.80 E-value: 3.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462558728 93 LGLGTWvtfgSQISDETAEDVLTVAYEHGVNLFDTAEVY----AAGKAERTLgniLKSKGWRRSSYVITTKIfWG 163
Cdd:cd19116 14 IALGTW----KLKDDEGVRQAVKHAIEAGYRHIDTAYLYgneaEVGEAIREK---IAEGVVKREDLFITTKL-WN 80
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
87-184 |
7.29e-03 |
|
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: 37.89 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462558728 87 GLRVSCLGLGTWvtfgsQISDETAEDVLTVAYEHGVNLFDTAEVYaagKAERTLGNILK----SKGWRRSSYVITTKIFW 162
Cdd:cd19155 9 GEKMPVVGLGTW-----QSSPEEIETAVDTALEAGYRHIDTAYVY---RNEAAIGNVLKkwidSGKVKREELFIVTKLPP 80
|
90 100
....*....|....*....|..
gi 2462558728 163 GGqaeterglSRKHIIEEIVRA 184
Cdd:cd19155 81 GG--------NRREKVEKFLLK 94
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|
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