|
Name |
Accession |
Description |
Interval |
E-value |
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
1-280 |
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: 602.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19141 31 VAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:cd19141 111 QLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPIVEQAEYHLFQREKVEM 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 240
Cdd:cd19141 191 QLPELFHKIGVGAMTWSPLACGILSGKYDDGVPEYSRASLKGYQWLKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLA 270
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSI 280
Cdd:cd19141 271 IAWCLKNEGVSSVLLGASSTEQLYENLQAIQVLPKLTPNI 310
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-293 |
0e+00 |
|
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos taurus, Rattus norvegicus, Mus musculus, Homo sapiens, and Oryctolagus cuniculus, are founding members of aldo-keto reductase family 6 member A1 (AKR6A1), A2 (AKR6A2), A4 (AKR6A4), A5 (AKR6A5), and A6 (AKR6A6), respectively. KCAB2B, also called Shaker channel b-subunit 2 (Kvb2), or K(+) channel subunit beta-2, or Kv-beta-2, or Kvbeta2, is a cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. It may be involved in the regulation of nerve signaling, and prevents neuronal hyperexcitability.
Pssm-ID: 381384 [Multi-domain] Cd Length: 324 Bit Score: 599.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19158 32 MAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:cd19158 112 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 240
Cdd:cd19158 192 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILGNKPY 293
Cdd:cd19158 272 IAWCLRNEGVSSVLLGASNAEQLMENIGAIQVLPKLSSSIVHEIDSILGNKPY 324
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-292 |
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: 583.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19159 32 VAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:cd19159 112 QLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 240
Cdd:cd19159 192 QLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILGNKP 292
Cdd:cd19159 272 VAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKP 323
|
|
| Kv_beta |
TIGR01293 |
voltage-dependent potassium channel beta subunit, animal; This model describes the conserved ... |
1-288 |
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: 578.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:TIGR01293 30 MAEQLLTLAYENGINLFDTAEVYAAGKAEVVLGNILKKKGWRRSSYVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:TIGR01293 110 QLEYVDIVFANRPDPNTPMEETVRAMTYVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 240
Cdd:TIGR01293 190 QLPELYHKIGVGAMTWSPLACGLVSGKYDSGIPPYSRATLKGYQWLKDKILSEEGRRQQARLKDLQAIAERLGCTLPQLA 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSIL 288
Cdd:TIGR01293 270 IAWCLRNEGVSSVLLGASSAEQLMENLGSLQVLPKLSSSIIHEIDSIL 317
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-292 |
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: 563.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19160 34 TAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLDRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:cd19160 114 QLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVEM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLA 240
Cdd:cd19160 194 QLPELYHKIGVGSVTWSPLACGLITGKYDGRVPDTCRAAVKGYQWLKEKVQSEEGKKQQAKVKELHPIADRLGCTVAQLA 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILGNKP 292
Cdd:cd19160 274 IAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVLSQLTPQTVMEIDALLGNKP 325
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
2-287 |
5.60e-168 |
|
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: 468.61 E-value: 5.60e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAE--TERGLSRKHIIEGLKASLER 79
Cdd:cd19143 33 AKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSDYVVSTKIFWGGGGPppNDRGLSRKHIVEGTKASLKR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVE 159
Cdd:cd19143 113 LQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEWSAQQIEEAHEIADRLGLIPPVMEQPQYNLFHRERVE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 VQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDkILSEEGRRQQAKLKELQAIAERLGCTLPQL 239
Cdd:cd19143 193 VEYAPLYEKYGLGTTTWSPLASGLLTGKYNNGIPEGSRLALPGYEWLKD-RKEELGQEKIEKVRKLKPIAEELGCSLAQL 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 315434251 240 AIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSI 287
Cdd:cd19143 272 AIAWCLKNPNVSTVITGATKVEQLEENLKALEVLPKLTPEVMEKIEAI 319
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
1-280 |
1.04e-151 |
|
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: 426.24 E-value: 1.04e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFWGGKAE-TERGLSRKHIIEGLKASLER 79
Cdd:cd19074 23 DAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALK--GWPRESYVISTKVFWPTGPGpNDRGLSRKHIFESIHASLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVE 159
Cdd:cd19074 101 LQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLARQFGLIPPVVEQPQYNMLWREIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 vQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKgYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQL 239
Cdd:cd19074 181 -EVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRSRAT-DEDNRDKKRRLLTDENLEKVKKLKPIADELGLTLAQL 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 315434251 240 AIAWCLRNEGVSSVLLGASNADQLMENIGAiqVLPKLSSSI 280
Cdd:cd19074 259 ALAWCLRNPAVSSAIIGASRPEQLEENVKA--SGVKLSPEV 297
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
2-292 |
1.00e-149 |
|
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: 422.64 E-value: 1.00e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAEtERGLSRKHIIEGLKASLERLQ 81
Cdd:cd19142 33 AEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSYIVSTKIYWSYGSE-ERGLSRKHIIESVRASLRRLQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQ 161
Cdd:cd19142 112 LDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSPVEIMEAFSIARQFNCPTPICEQSEYHMFCREKMELY 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 162 LPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGY-----QWLKDKIlsEEGRRQQAKLKELQAIAERLGCTL 236
Cdd:cd19142 192 MPELYNKVGVGLITWSPLSLGLDPGISEETRRLVTKLSFKSSkykvgSDGNGIH--EETRRASHKLRELSLIAERLGCDL 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 315434251 237 PQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLSSSIIHEIDSILGNKP 292
Cdd:cd19142 270 TQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLLPKLNSAVMEELERILDNKP 325
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
2-292 |
1.18e-90 |
|
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: 272.05 E-value: 1.18e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKIFW-GGKAETERGLSRKHIIEGLKASLERL 80
Cdd:COG0667 35 AIAILDAALDAGINFFDTADVYGPGRSEELLGEALK--GRPRDDVVIATKVGRrMGPGPNGRGLSREHIRRAVEASLRRL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfNLTPPICEQAEYHMFQREkVEV 160
Cdd:COG0667 113 GTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAEQLRRALAIAE--GLPPIVAVQNEYSLLDRS-AEE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSG--IPPYSRASLKGYQWlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQ 238
Cdd:COG0667 190 ELLPAARELGVGVLAYSPLAGGLLTGKYRRGatFPEGDRAATNFVQG-------YLTERNLALVDALRAIAAEHGVTPAQ 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 315434251 239 LAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSILGNKP 292
Cdd:COG0667 263 LALAWLLAQPGVTSVIPGARSPEQLEENLAAADL--ELSAEDLAALDAALAAVP 314
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
2-287 |
2.10e-79 |
|
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: 243.25 E-value: 2.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFWG-GKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19087 32 SFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAG---RRDDIVLATKVFGPmGDDPNDRGLSRRHIRRAVEASLRRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEV 160
Cdd:cd19087 109 QTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNFAAWQIAKAQGIAARRGLLRFVSEQPMYNLLKRQ-AEL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPP--YSRASLKGYQwlkDKILSEEGRRQqakLKELQAIAERLGCTLPQ 238
Cdd:cd19087 188 EILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPesGRLVERARYQ---ARYGLEEYRDI---AERFEALAAEAGLTPAS 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 239 LAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19087 262 LALAWVLSHPAVTSPIIGPRTLEQLEDSLAALEI--TLTPELLAEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
2-287 |
1.71e-73 |
|
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: 228.27 E-value: 1.71e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19091 41 ADRLVDIALDAGINFFDTADVYSEGESEEILGKALKG---RRDDVLIATKVrGRMGEGPNDVGLSRHHIIRAVEASLKRL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEV 160
Cdd:cd19091 118 GTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNFSAWQIMKALGISERRGLARFVALQAYYSLLGRD-LEH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPYSRASLKGYQWLkdkILSEEgrRQQAKLKELQAIAERLGCTLPQ 238
Cdd:cd19091 197 ELMPLALDQGVGLLVWSPLAGGLLSGKYrrGQPAPEGSRLRRTGFDFP---PVDRE--RGYDVVDALREIAKETGATPAQ 271
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 239 LAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19091 272 VALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGL--SLTPEEIARLDKV 318
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
2-274 |
1.86e-73 |
|
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: 227.91 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVY--AAGKAEVVLGNIIKK-KGWRRSSLVITTKI---FWGGKaeTERGLSRKHIIEGLKA 75
Cdd:cd19089 31 ARELLRTAFDLGITHFDLANNYgpPPGSAEENFGRILKRdLRPYRDELVISTKAgygMWPGP--YGDGGSRKYLLASLDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 76 SLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQR 155
Cdd:cd19089 109 SLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARRAIALLRELG-VPLIIHQPRYSLLDR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 156 eKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRAsLKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCT 235
Cdd:cd19089 188 -WAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRR-AAESKFLTEEALTPE---KLEQLRKLNKIAAKRGQS 262
|
250 260 270
....*....|....*....|....*....|....*....
gi 315434251 236 LPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLP 274
Cdd:cd19089 263 LAQLALSWVLRDPRVTSVLIGASSPSQLEDNVAALKNLD 301
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
9-285 |
1.21e-70 |
|
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: 220.48 E-value: 1.21e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVD 86
Cdd:cd19084 34 AIDLGINFFDTAPVYGFGHSEEILGKALKG---RRDDVVIATKcgLRWDGGKGVTKDLSPESIRKEVEQSLRRLQTDYID 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAysvarqFNLTPPICEQAEYHMFQREKVEVQLPELf 166
Cdd:cd19084 111 LYQIHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEA------RKYGPIVSLQPPYSMLEREIEEELLPYC- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 167 HKIGVGAMTWSPLACGIVSGKYDSG--IPPY-SRASLKGYQwlkdkilSEEGRRQQAKLKELQAIAERLGCTLPQLAIAW 243
Cdd:cd19084 184 RENGIGVLPYGPLAQGLLTGKYKKEptFPPDdRRSRFPFFR-------GENFEKNLEIVDKLKEIAEKYGKSLAQLAIAW 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 315434251 244 CLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19084 257 TLAQPGVTSAIVGAKNPEQLEENAGALDW--ELTEEELKEID 296
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
2-268 |
1.83e-67 |
|
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications. Members have very distinct functions and include the prokaryotic 2,5-diketo-D-gluconic acid reductases and beta-keto ester reductases, the eukaryotic aldose reductases, aldehyde reductases, hydroxysteroid dehydrogenases, steroid 5beta-reductases, potassium channel beta-subunits, and aflatoxin aldehyde reductases, among others.
Pssm-ID: 381296 [Multi-domain] Cd Length: 232 Bit Score: 210.07 E-value: 1.83e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd06660 19 AFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRG-NRDDVVIATKGgHPPGGDPSRSRLSPEHIRRDLEESLRRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEV 160
Cdd:cd06660 98 GTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAKAHGLPGFAAVQPQYSLLDRSPMEE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrqqaklkelqaiaerlgctLPQLA 240
Cdd:cd06660 178 ELLDWAEENGLPLLAYSPLARG-----------------------------------------------------PAQLA 204
|
250 260
....*....|....*....|....*...
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIG 268
Cdd:cd06660 205 LAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-271 |
5.22e-67 |
|
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: 211.49 E-value: 5.22e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 4 QLMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKK--KGWRrSSLVITTK---IFWGGKAeTERGlSRKHIIEGLKAS 76
Cdd:cd19151 34 AMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdlKPYR-DELIISTKagyTMWPGPY-GDWG-SKKYLIASLDQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 77 LERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQRE 156
Cdd:cd19151 111 LKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYVGISNYPPEEAREAAAILKDLG-TPCLIHQPKYSMFNRW 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 157 kVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASlKGYQWLKDKILSEEgrrQQAKLKELQAIAERLGCTL 236
Cdd:cd19151 190 -VEEGLLDVLEEEGIGCIAFSPLAQGLLTDRYLNGIPEDSRAA-KGSSFLKPEQITEE---KLAKVRRLNEIAQARGQKL 264
|
250 260 270
....*....|....*....|....*....|....*
gi 315434251 237 PQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 271
Cdd:cd19151 265 AQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
1-277 |
6.42e-66 |
|
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: 208.98 E-value: 6.42e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIFW-GGKAETERGLSRKHIIEGLKASLER 79
Cdd:cd19079 36 ESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFA-PRDEVVIATKVYFpMGDGPNGRGLSRKHIMAEVDASLKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKvE 159
Cdd:cd19079 115 LGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSMYAWQFAKALHLAEKNGWTKFVSMQNHYNLLYREE-E 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 VQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGYQWLKdkiLSEEGRRQQAKLKElqaIAERLGCTLPQ 238
Cdd:cd19079 194 REMIPLCEEEGIGVIPWSPLARGRLARPWGDTTErRRSTTDTAKLKYDY---FTEADKEIVDRVEE---VAKERGVSMAQ 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 315434251 239 LAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLS 277
Cdd:cd19079 268 VALAWLLSKPGVTAPIVGATKLEHLEDAVAALDI--KLS 304
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
11-285 |
1.19e-65 |
|
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: 207.84 E-value: 1.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 11 DNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSLVITTKIFWGgKAETERGLSRKHIIEGLKASLERLQLE 83
Cdd:cd19081 37 DAGGNFIDTADVYSAwvpgnagGESETIIGRWLKSRG-KRDRVVIATKVGFP-MGPNGPGLSRKHIRRAVEASLRRLQTD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 84 YVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLP 163
Cdd:cd19081 115 YIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWRLQEALELSRQHGLPRYVSLQPEYNLVDRESFEGELL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 164 ELFHKIGVGAMTWSPLACGIVSGKYDSGIPPySRASLKGYQWlkDKILSEEGRRqqaKLKELQAIAERLGCTLPQLAIAW 243
Cdd:cd19081 195 PLCREEGIGVIPYSPLAGGFLTGKYRSEADL-PGSTRRGEAA--KRYLNERGLR---ILDALDEVAAEHGATPAQVALAW 268
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 315434251 244 CLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19081 269 LLARPGVTAPIAGARTVEQLEDLLAAAGL--RLTDEEVARLD 308
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
2-288 |
4.06e-64 |
|
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: 203.31 E-value: 4.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGLSRKHIIEGLKASLERLQ 81
Cdd:pfam00248 20 ALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKV-PDGDGPWPSGGSKENIRKSLEESLKRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFqREKVEVQ 161
Cdd:pfam00248 99 TDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALTKGK----IPIVAVQVEYNLL-RRRQEEE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 162 LPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAI 241
Cdd:pfam00248 174 LLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPG--------ERRRLLKKGTPLNLEALEALEEIAKEHGVSPAQVAL 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 315434251 242 AWCLRNEGVSSVLLGASNADQLMENIGAIQvlPKLSSSIIHEIDSIL 288
Cdd:pfam00248 246 RWALSKPGVTIPIPGASNPEQLEDNLGALE--FPLSDEEVARIDELL 290
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
2-287 |
6.31e-61 |
|
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: 196.63 E-value: 6.31e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-----FWGGKAETERGLSRKHI 69
Cdd:cd19094 20 AHEQLDYAFDEGVNFIDTAEMYPvppspetQGRTEEIIGSWLKKKG-NRDKVVLATKVagpgeGITWPRGGGTRLDRENI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 70 IEGLKASLERLQLEYVDVVFANRPDPNTP------------------MEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA 131
Cdd:cd19094 99 REAVEGSLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVKAGKIRHIGLSNETPWGVMKF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 132 YSVARQFNLTPPICEQAEYHMFQReKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSG--IPPYSRASL-KGYQwlkd 208
Cdd:cd19094 179 LELAEQLGLPRIVSIQNPYSLLNR-NFEEGLAEACHRENVGLLAYSPLAGGVLTGKYLDGaaRPEGGRLNLfPGYM---- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 209 kilseeGRRQQAK----LKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEI 284
Cdd:cd19094 254 ------ARYRSPQaleaVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQLKENIDAFDV--PLSDELLAEI 325
|
...
gi 315434251 285 DSI 287
Cdd:cd19094 326 DAV 328
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
9-273 |
4.73e-60 |
|
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: 193.82 E-value: 4.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLVITTKI---FWGGKAeTERGlSRKHIIEGLKASLERLQL 82
Cdd:cd19150 39 AFDLGITHFDLANNYGppPGSAEENFGRILREDfAGYRDELIISTKAgydMWPGPY-GEWG-SRKYLLASLDQSLKRMGL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 83 EYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNlTPPICEQAEYHMFQREKVEVQL 162
Cdd:cd19150 117 DYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILRELG-TPLLIHQPSYNMLNRWVEESGL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 163 PELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYqwLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIA 242
Cdd:cd19150 196 LDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGSRASKERS--LSPKMLTE---ANLNSIRALNEIAQKRGQSLAQMALA 270
|
250 260 270
....*....|....*....|....*....|.
gi 315434251 243 WCLRNEGVSSVLLGASNADQLMENIGAIQVL 273
Cdd:cd19150 271 WVLRDGRVTSALIGASRPEQLEENVGALDNL 301
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
5-285 |
1.17e-53 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 178.26 E-value: 1.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 5 LMTLAYDNGINLFDTAEVYA--AGKAEVVLGNIIKKK-GWRRSSLVITTKI---FWGGKAETerGLSRKHIIEGLKASLE 78
Cdd:PRK09912 48 ILRKAFDLGITHFDLANNYGppPGSAEENFGRLLREDfAAYRDELIISTKAgydMWPGPYGS--GGSRKYLLASLDQSLK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 79 RLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKV 158
Cdd:PRK09912 126 RMGLEYVDIFYSHRVDENTPMEETASALAHAVQSGKALYVGISSYSPERTQKMVELLREWKI-PLLIHQPSYNLLNRWVD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 159 EVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKG--YQWLKDKILSEEGRRQqakLKELQAIAERLGCTL 236
Cdd:PRK09912 205 KSGLLDTLQNNGVGCIAFTPLAQGLLTGKYLNGIPQDSRMHREGnkVRGLTPKMLTEANLNS---LRLLNEMAQQRGQSM 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 237 PQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLpKLSSSIIHEID 285
Cdd:PRK09912 282 AQMALSWLLKDERVTSVLIGASRAEQLEENVQALNNL-TFSTEELAQID 329
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
9-287 |
5.84e-52 |
|
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is a founding member of aldo-keto reductase family 11 member B3(AKR11B3). It is responsible for methylglyoxal detoxification.
Pssm-ID: 381311 [Multi-domain] Cd Length: 292 Bit Score: 172.39 E-value: 5.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFwggkaetERGLSRKHIIEGLKASLERLQLEYVDVV 88
Cdd:cd19085 32 ALDAGINFFDTAEAYGDGHSEEVLGKALKG---RRDDVVIATKVS-------PDNLTPEDVRKSCERSLKRLGTDYIDLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnltpPICEQAEYHMFQREkVEVQLPELFHK 168
Cdd:cd19085 102 QIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGR------IDSNQLPYNLLWRA-IEYEILPFCRE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 169 IGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKgyqwlkdkILSEEGRRQQAK--LKELQAIAERLGCTLPQLAIAW 243
Cdd:cd19085 175 HGIGVLAYSPLAQGLLTGKFSSAEdfpPGDARTRLF--------RHFEPGAEEETFeaLEKLKEIADELGVTMAQLALAW 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 315434251 244 CLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19085 247 VLQQPGVTSVIVGARNPEQLEENAAAVDL--ELSPSVLERLDEI 288
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
10-285 |
8.65e-51 |
|
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: 169.71 E-value: 8.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 10 YDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFWG--GKAETERGLSRKHIIEGLKASLERLQLEYVDV 87
Cdd:cd19080 41 VEAGGNFIDTANNYTNGTSERLLGEFIAG---NRDRIVLATKYTMNrrPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 88 VFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFH 167
Cdd:cd19080 118 LYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDTPAWVVARANTLAELRGWSPFVALQIEYSLLERT-PERELLPMAR 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 168 KIGVGAMTWSPLACGIVSGKYDSGipPYSRASLKGYQWLKDKILSEegrRQQAKLKELQAIAERLGCTLPQLAIAWCLRN 247
Cdd:cd19080 197 ALGLGVTPWSPLGGGLLTGKYQRG--EEGRAGEAKGVTVGFGKLTE---RNWAIVDVVAAVAEELGRSAAQVALAWVRQK 271
|
250 260 270
....*....|....*....|....*....|....*...
gi 315434251 248 EGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19080 272 PGVVIPIIGARTLEQLKDNLGALDL--TLSPEQLARLD 307
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-288 |
1.19e-46 |
|
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: 158.99 E-value: 1.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSsLVITTK--IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVD 86
Cdd:cd19102 35 ALDLGINWIDTAAVYGLGHSEEVVGRALK--GLRDR-PIVATKcgLLWDEEGRIRRSLKPASIRAECEASLRRLGVDVID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPiceqaeYHMFQREKVEVQLPelF 166
Cdd:cd19102 112 LYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAIHPIASLQPP------YSLLRRGIEAEILP--F 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 167 ---HKIGVgaMTWSPLACGIVSGKYDsgipPYSRASLKGYQWLK-DKILSEEGRRQQAKLKE-LQAIAERLGCTLPQLAI 241
Cdd:cd19102 184 caeHGIGV--IVYSPMQSGLLTGKMT----PERVASLPADDWRRrSPFFQEPNLARNLALVDaLRPIAERHGRTVAQLAI 257
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 315434251 242 AWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSIL 288
Cdd:cd19102 258 AWVLRRPEVTSAIVGARRPDQIDETVGAADL--RLTPEELAEIEALL 302
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
5-288 |
7.33e-44 |
|
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: 151.62 E-value: 7.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 5 LMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIFW----GGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19078 30 LIRKAVELGITFFDTAEVYGPYTNEELVGEALKP---FRDQVVIATKFGFkidgGKPGPLGLDSRPEHIRKAVEGSLKRL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVarqfnlTPPICEQAEYHMFQREkVEV 160
Cdd:cd19078 107 QTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAV------CPVTAVQSEYSMMWRE-PEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPELFHKIGVGAMTWSPLACGIVSGKYDSGI---PPYSRASLKGYqwlkdkilSEEGRRQQAKLKEL-QAIAERLGCTL 236
Cdd:cd19078 180 EVLPTLEELGIGFVPFSPLGKGFLTGKIDENTkfdEGDDRASLPRF--------TPEALEANQALVDLlKEFAEEKGATP 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 237 PQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSIL 288
Cdd:cd19078 252 AQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADI--ELTPEELREIEDAL 301
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
8-285 |
1.65e-43 |
|
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: 150.46 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 8 LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIfwggkAETERGLSRKHIIEGLKASLERLQLEYVDV 87
Cdd:cd19093 34 AALEAGVNLFDTAEVYGTGRSERLLGRFLKELG-DRDEVVIATKF-----APLPWRLTRRSVVKALKASLERLGLDSIDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 88 VFANRPDPNTPMEETV-RAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQLPELF 166
Cdd:cd19093 108 YQLHWPGPWYSQIEALmDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKERGV-PLASNQVEYSLLYRDPEQNGLLPAC 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 167 HKIGVGAMTWSPLACGIVSGKY-DSGIPPYSRASLKG-YQWLKDKILseegrrqqakLKELQAIAERLGCTLPQLAIAWC 244
Cdd:cd19093 187 DELGITLIAYSPLAQGLLTGKYsPENPPPGGRRRLFGrKNLEKVQPL----------LDALEEIAEKYGKTPAQVALNWL 256
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 315434251 245 LRNEGVssVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19093 257 IAKGVV--PIPGAKNAEQAEENAGALGW--RLSEEEVAELD 293
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
9-287 |
2.12e-43 |
|
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: 150.65 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTK---IFWGGKaeTERGLSRKHIIEGLKASLERLQLEYV 85
Cdd:cd19083 42 ALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVVIATKgahKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 86 DVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAySVARQFNLTppiceQAEYHMFQREKVEVQLPEL 165
Cdd:cd19083 118 DLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLEQLKEA-NKDGYVDVL-----QGEYNLLQREAEEDILPYC 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 166 fHKIGVGAMTWSPLACGIVSGKYDSGIppysraSLKGYQWLKDKILSEEGRRQQ--AKLKELQAIAERLGCTLPQLAIAW 243
Cdd:cd19083 192 -VENNISFIPYFPLASGLLAGKYTKDT------KFPDNDLRNDKPLFKGERFSEnlDKVDKLKSIADEKGVTVAHLALAW 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 315434251 244 CLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19083 265 YLTRPAIDVVIPGAKRAEQVIDNLKALDV--TLTEEEIAFIDAL 306
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
1-287 |
2.63e-42 |
|
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.
Pssm-ID: 381301 [Multi-domain] Cd Length: 304 Bit Score: 147.70 E-value: 2.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIikkkGWRRSSLVITTKI-FWGGKaeterGLSRKHIIEGLKASLER 79
Cdd:cd19075 21 AAAELLDAFLERGHTEIDTARVYPDGTSEELLGEL----GLGERGFKIDTKAnPGVGG-----GLSPENVRKQLETSLKR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQReKVE 159
Cdd:cd19075 92 LKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEICKENGWVLPTVYQGMYNAITR-QVE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 vqlPELF-----HKIGVGAmtWSPLACGIVSGKYDSG--IPPYSR--ASLKGYQWLKDKILSEEgrrQQAKLKELQAIAE 230
Cdd:cd19075 171 ---TELFpclrkLGIRFYA--YSPLAGGFLTGKYKYSedKAGGGRfdPNNALGKLYRDRYWKPS---YFEALEKVEEAAE 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434251 231 RLGCTLPQLAIAWC-----LRNEGVSSVLLGASNADQLMENIGAIQVLPkLSSSIIHEIDSI 287
Cdd:cd19075 243 KEGISLAEAALRWLyhhsaLDGEKGDGVILGASSLEQLEENLAALEKGP-LPEEVVKAIDEA 303
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-284 |
2.74e-41 |
|
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: 144.67 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKifWG---GKAETERGL--SRKHIIEGLKAS 76
Cdd:cd19076 34 SIATLHRALELGVTFLDTADMYGPGTNEELLGKALKD---RRDEVVIATK--FGivrDPGSGFRGVdgRPEYVRAACEAS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 77 LERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMFQR 155
Cdd:cd19076 109 LKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADTIRRAHAVH-------PITAvQSEYSLWTR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 156 EKVEVQLP---ELfhkiGVGAMTWSPLACGIVSGKYDSgippysraslkgyqwlKDKILSEEGRRQQ-----------AK 221
Cdd:cd19076 182 DIEDEVLPtcrEL----GIGFVAYSPLGRGFLTGAIKS----------------PEDLPEDDFRRNNprfqgenfdknLK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315434251 222 L-KELQAIAERLGCTLPQLAIAWCL-RNEGVSSVlLGASNADQLMENIGAIQVlpKLSSSIIHEI 284
Cdd:cd19076 242 LvEKLEAIAAEKGCTPAQLALAWVLaQGDDIVPI-PGTKRIKYLEENVGALDV--VLTPEELAEI 303
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
9-286 |
4.42e-41 |
|
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: 144.72 E-value: 4.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTK--IFWGGKAETE----------RGLSRKHIIEGLKAS 76
Cdd:cd19149 42 ALDLGINLIDTAPAYGFGHSEEIVGKAIKG---RRDKVVLATKcgLRWDREGGSFffvrdgvtvyKNLSPESIREEVEQS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 77 LERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnlTPPICeQAEYHMFQRE 156
Cdd:cd19149 119 LKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAIGASNVSVEQIKEYVKAG-----QLDII-QEKYSMLDRG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 157 KVEVQLPeLFHKIGVGAMTWSPLACGIVSGKYDSGippysRASLKGYQWLKDKILSEEGRRQ-QAKLKELQAIAERLGCT 235
Cdd:cd19149 193 IEKELLP-YCKKNNIAFQAYSPLEQGLLTGKITPD-----REFDAGDARSGIPWFSPENREKvLALLEKWKPLCEKYGCT 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434251 236 LPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDS 286
Cdd:cd19149 267 LAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDI--RLSAEDIATMRS 315
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
2-269 |
1.02e-38 |
|
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.
Pssm-ID: 381312 [Multi-domain] Cd Length: 238 Bit Score: 136.07 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKI--FWGGKAETERGLSRKHIIEGLKASLER 79
Cdd:cd19086 26 AIRALRAALDLGINFFDTADVYGDGHSERLLGKALKG---RRDKVVIATKFgnRFDGGPERPQDFSPEYIREAVEASLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFA-NRPDPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeiMEAYSVARQFNLTPPI-CEQAEYHMFQREK 157
Cdd:cd19086 103 LGTDYIDLYQLhNPPDEVLDNDELFEALEKLKQEGKIRAYGVS-------VGDPEEALAALRRGGIdVVQVIYNLLDQRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 158 VEvqlpELFHKI---GVGAMTWSPLACGIVSGKydsgippysraslkgyqwlkdkilseegrrqqaklkelqaiaerlgc 234
Cdd:cd19086 176 EE----ELFPLAeehGVGVIARVPLASGLLTGK----------------------------------------------- 204
|
250 260 270
....*....|....*....|....*....|....*
gi 315434251 235 tLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19086 205 -LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
9-271 |
1.79e-38 |
|
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: 136.20 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFwggkaetERGLSRKHIIEGLKASLERLQLEYVDVV 88
Cdd:cd19072 35 AIELGINLIDTAEMYGGGHAEELVGKAI--KGFDREDLFITTKVS-------PDHLKYDDVIKAAKESLKRLGTDYIDLY 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQfnlTPPICEQAEYHMFQREkVEVQLPELFHK 168
Cdd:cd19072 106 LIHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYLKK---GPIVANQVEYNLFDRE-EESGLLPYCQK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 169 IGVGAMTWSPLACGIVSGKYDSgippysraslkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNE 248
Cdd:cd19072 182 NGIAIIAYSPLEKGKLSNAKGS--------------------------------PLLDEIAKKYGKTPAQIALNWLISKP 229
|
250 260
....*....|....*....|...
gi 315434251 249 GVsSVLLGASNADQLMENIGAIQ 271
Cdd:cd19072 230 NV-IAIPKASNIEHLEENAGALG 251
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
2-269 |
4.55e-36 |
|
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) and Streptomyces glaucescens aldo-keto reductase (StrT) are founding members of aldo-keto reductase family 10 member A1 (AKR10A1) and A2 (AKR10A2). BlmT is bluensomycin aldo-keto reductase (AKR) and StrT is streptomycin AKR.
Pssm-ID: 381308 [Multi-domain] Cd Length: 291 Bit Score: 130.75 E-value: 4.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAA----GKAEVVLGNIIKKKGwRRSSLVITTKifwGG-----KAETERgLSRKHIIEG 72
Cdd:cd19082 19 AFALLDAFVELGGNFIDTARVYGDwverGASERVIGEWLKSRG-NRDKVVIATK---GGhpdleDMSRSR-LSPEDIRAD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 73 LKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHM 152
Cdd:cd19082 94 LEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNWSTERIAEANAYAKAHGLPGFAASSPQWSL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 153 FqrEKVEVQLP------------ELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRaslkgyqwLKDKILSEEGRRQQA 220
Cdd:cd19082 174 A--RPNEPPWPgptlvamdeemrAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSE--------LRRVYYSEENFERLE 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 221 KLKELqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19082 244 RAKEL---AEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAA 289
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-269 |
7.11e-35 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 127.83 E-value: 7.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYA-------AGKAEVVLGNIIKKKGwRRSSLVITTKI-----FWGGKAETERGLSRKHI 69
Cdd:cd19752 19 SFAILDRYVAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRG-NRDDVVIATKVgagprDPDGGPESPEGLSAETI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 70 IEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAE 149
Cdd:cd19752 98 EQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNFAAWRLERARQIARQQGWAEFSAIQQR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 150 YHMFQR-----EKVEVQL-PELFHKIG----VGAMTWSPLacgiVSGKYDSgippysraslkgyqwlKDKILSEEGRRQ- 218
Cdd:cd19752 178 HSYLRPrpgadFGVQRIVtDELLDYASsrpdLTLLAYSPL----LSGAYTR----------------PDRPLPEQYDGPd 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 219 -QAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19752 238 sDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAA 289
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
8-285 |
2.68e-33 |
|
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this family. It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381364 [Multi-domain] Cd Length: 266 Bit Score: 122.74 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 8 LAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSLVITTKIfWGGKAeterglSRKHIIEGLKASLERLQLEYVDV 87
Cdd:cd19138 37 AGIDLGMTLIDTAEMYGDGGSEELVGEAIRG---RRDKVFLVSKV-LPSNA------SRQGTVRACERSLRRLGTDYLDL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 88 VFANRPDpNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTppiCEQAEYHMFQReKVEVQLPELFH 167
Cdd:cd19138 107 YLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEELWAVPGGGNCA---ANQVLYNLGSR-GIEYDLLPWCR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 168 KIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRN 247
Cdd:cd19138 182 EHGVPVMAYSPLAQG------------------------------GLLRRGLLENPTLKEIAARHGATPAQVALAWVLRD 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 315434251 248 EGVSSVlLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19138 232 GNVIAI-PKSGSPEHARENAAAADL--ELTEEDLAELD 266
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
9-288 |
1.31e-32 |
|
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: 122.03 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTK--IFWGGKAETERGLSRKHIIEGLKASLERLQLEYVD 86
Cdd:cd19148 34 ALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKvgLEWDEGGEVVRNSSPARIRKEVEDSLRRLQTDYID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWsSMEIMEAY-SVARQFNLTPPiceqaeYHMFQREKVEVQLPEL 165
Cdd:cd19148 113 LYQVHWPDPLVPIEETAEALKELLDEGKIRAIGVSNF-SPEQMETFrKVAPLHTVQPP------YNLFEREIEKDVLPYA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 166 fHKIGVGAMTWSPLACGIVSGKY--DSGIPPYS-RASLKGYQwlkdkilseEGRRQQ--AKLKELQAIA-ERLGCTLPQL 239
Cdd:cd19148 186 -RKHNIVTLAYGALCRGLLSGKMtkDTKFEGDDlRRTDPKFQ---------EPRFSQylAAVEELDKLAqERYGKSVIHL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 240 AIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSIL 288
Cdd:cd19148 256 AVRWLLDQPGVSIALWGARKPEQLDAVDEVFGW--SLNDEDMKEIDAIL 302
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
2-271 |
4.24e-32 |
|
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: 119.97 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKkkGWRRSSLVITTKIfwGGKAETERGLSRKHIIEGLKASLERLQ 81
Cdd:cd19090 22 AVATIRAALDLGINYIDTAPAY--GDSEERLGLALA--ELPREPLVLSTKV--GRLPEDTADYSADRVRRSVEESLERLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNTPMEET-----VRAMTHVINQGMAMYWGTSRWSSMEIMEA-----YSVARQFNltppiceqaEYH 151
Cdd:cd19090 96 RDRIDLLMIHDPERVPWVDILapggaLEALLELKEEGLIKHIGLGGGPPDLLRRAietgdFDVVLTAN---------RYT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 152 MFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSGKYDSGIPPysraslkGYQWLKDkilseegrRQQAKLKELQAIAER 231
Cdd:cd19090 167 LLDQSAADELLP-AAARHGVGVINASPLGMGLLAGRPPERVRY-------TYRWLSP--------ELLDRAKRLYELCDE 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 315434251 232 LGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ 271
Cdd:cd19090 231 HGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAAE 270
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
13-272 |
6.00e-31 |
|
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding member of aldo-keto reductase family 3 member F1 (AKR3F1). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381363 [Multi-domain] Cd Length: 260 Bit Score: 116.52 E-value: 6.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 13 GINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFwggkaetERGLSRKHIIEGLKASLERLQLEYVDVVFANR 92
Cdd:cd19137 39 GYTHIDTAEMYGGGHTEELVGKAIKD--FPREDLFIVTKVW-------PTNLRYDDLLRSLQNSLRRLDTDYIDLYLIHW 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 93 PDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKVEVQLPELFHKIGVG 172
Cdd:cd19137 110 PNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQ----TPIVCNQVKYNLEDRDPERDGLLEYCQKNGIT 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 173 AMTWSPLACGIVSGKydsgippysraslkgyqwlkdkilseegrrqqaklKELQAIAERLGCTLPQLAIAWCLRNEGVSS 252
Cdd:cd19137 186 VVAYSPLRRGLEKTN-----------------------------------RTLEEIAKNYGKTIAQIALAWLIQKPNVVA 230
|
250 260
....*....|....*....|
gi 315434251 253 VLLgASNADQLMENIGAIQV 272
Cdd:cd19137 231 IPK-AGRVEHLKENLKATEI 249
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-287 |
6.09e-31 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381330 [Multi-domain] Cd Length: 321 Bit Score: 118.14 E-value: 6.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTL--AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRSSLVITTKIfwgGKAETERGLSRKHIIEGLKASLER 79
Cdd:cd19104 32 EEQIAAVrrALDLGINFFDTAPSYGDGKSEENLGRALKGL---PAGPYITTKV---RLDPDDLGDIGGQIERSVEKSLKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVF------ANRPDPNTPM---------EETVRAMTHVINQGMAMYWGTSRWSSMEIME------AYSVARQF 138
Cdd:cd19104 106 LKRDSVDLLQlhnrigDERDKPVGGTlsttdvlglGGVADAFERLRSEGKIRFIGITGLGNPPAIRelldsgKFDAVQVY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 139 -NL--------TPPICEQAEYHmfqrekvevQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRAslkgyqwlkDK 209
Cdd:cd19104 186 yNLlnpsaaeaRPRGWSAQDYG---------GIIDAAAEHGVGVMGIRVLAAGALTTSLDRGREAPPTS---------DS 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434251 210 ILSEEGRRQQAklkeLQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPkLSSSIIHEIDSI 287
Cdd:cd19104 248 DVAIDFRRAAA----FRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAEAAGP-LPAENLARLEAL 320
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
2-272 |
6.53e-31 |
|
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: 117.27 E-value: 6.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK---IFWGGKAETERG---LSRKHIIEGLKA 75
Cdd:cd19092 26 LLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKcgiRLGDDPRPGRIKhydTSKEHILASVEG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 76 SLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeimeaysvarqfNLTPpiceqAEYHMFQR 155
Cdd:cd19092 106 SLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVS-----------------NFTP-----SQIELLQS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 156 ekvevqlpELFHKIGVGAMTWSPLACGIVsgkyDSGIPPYSRasLKGYQWL------KDKILSEEGRRQQAKLKELQAIA 229
Cdd:cd19092 164 --------YLDQPLVTNQIELSLLHTEAI----DDGTLDYCQ--LLDITPMawsplgGGRLFGGFDERFQRLRAALEELA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 315434251 230 ERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 272
Cdd:cd19092 230 EEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDI 272
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
2-287 |
7.25e-31 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 116.31 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAeterglSRKHIIEGLKASLERLQ 81
Cdd:COG0656 20 AAAAVRTALEAGYRHIDTAAMY---GNEEGVGEAIAASGVPREELFVTTKV-WNDNH------GYDDTLAAFEESLERLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREkvevq 161
Cdd:COG0656 90 LDYLDLYLIHWPGPG-PYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAETG----VKPAVNQVELHPYLQQ----- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 162 lPELF-----HKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTL 236
Cdd:COG0656 160 -RELLafcreHGIVVEA--YSPLGRG--------------------------KLLDDP---------VLAEIAEKHGKTP 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434251 237 PQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:COG0656 202 AQVVLRWHLQR-GV-VVIPKSVTPERIRENLDAFDF--ELSDEDMAAIDAL 248
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
2-287 |
1.47e-30 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 117.65 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAA-------GKAEVVLGNIIKKKGwRRSSLVITTKIfwGGKAET-------ERGLSRK 67
Cdd:PRK10625 32 AHAQLDYAVAQGINLIDVAEMYPVpprpetqGLTETYIGNWLAKRG-SREKLIIASKV--SGPSRNndkgirpNQALDRK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 68 HIIEGLKASLERLQLEYVD---VVFANRPD--------------PNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIME 130
Cdd:PRK10625 109 NIREALHDSLKRLQTDYLDlyqVHWPQRPTncfgklgyswtdsaPAVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 131 AYSVARQFNLTPPICEQAEYHMFQREkVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPY-SRASLKgyqwlkDK 209
Cdd:PRK10625 189 YLHLAEKHDLPRIVTIQNPYSLLNRS-FEVGLAEVSQYEGVELLAYSCLAFGTLTGKYLNGAKPAgARNTLF------SR 261
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434251 210 ILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:PRK10625 262 FTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQLKTNIESLHL--TLSEEVLAEIEAV 337
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
2-269 |
1.13e-29 |
|
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: 113.10 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKkkGWRRSSLVITTKI--FWGGkAETERGLSRKHIIEGLKASLER 79
Cdd:cd19095 22 AARLLNTALDLGINLIDTAPAY--GRSEERLGRALA--GLRRDDLFIATKVgtHGEG-GRDRKDFSPAAIRASIERSLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRwSSMEIMEAYSvarqfnlTPPI-CEQAEYHMFQREKV 158
Cdd:cd19095 97 LGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVSG-DGEELEAAIA-------SGVFdVVQLPYNVLDREEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 159 EVqLPELfHKIGVGAMTWSPLAcgivsgkydSGIPPYSRASLKGYQWLKDKilseegrrqqaklkeLQAIAERLGCTLPQ 238
Cdd:cd19095 169 EL-LPLA-AEAGLGVIVNRPLA---------NGRLRRRVRRRPLYADYARR---------------PEFAAEIGGATWAQ 222
|
250 260 270
....*....|....*....|....*....|.
gi 315434251 239 LAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19095 223 AALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
2-246 |
5.41e-29 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 112.17 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTK--IFWGGKAETERG----LSRKHIIEGLKA 75
Cdd:COG4989 33 AAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIELQTKcgIRLPSEARDNRVkhydTSKEHIIASVEG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 76 SLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMeimeaysvarQFNL------TPPICEQAE 149
Cdd:COG4989 113 SLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPS----------QFELlqsaldQPLVTNQIE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 150 YHMFQREKVE------VQLpelfHKIGVgaMTWSPLAcgivSGKYDSGippysraslkgyqwlkdkiLSEEGRRQQAKLK 223
Cdd:COG4989 183 LSLLHTDAFDdgtldyCQL----NGITP--MAWSPLA----GGRLFGG-------------------FDEQFPRLRAALD 233
|
250 260
....*....|....*....|...
gi 315434251 224 ElqaIAERLGCTLPQLAIAWCLR 246
Cdd:COG4989 234 E---LAEKYGVSPEAIALAWLLR 253
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-270 |
9.48e-29 |
|
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: 110.37 E-value: 9.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKIFWGGKAETerglsRKHIIEGLKASLERLQLEYVDVV 88
Cdd:cd19105 34 ALDLGINYFDTAEGYGNGNSEEIIGEAL--KGLRRDKVFLATKASPRLDKKD-----KAELLKSVEESLKRLQTDYIDIY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 F---ANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSME--IMEA-----YSVAR-QFNltppiceqaeyHMFQREK 157
Cdd:cd19105 107 QlhgVDTPEERLLNEELLEALEKLKKEGKVRFIGFSTHDNMAevLQAAiesgwFDVIMvAYN-----------FLNQPAE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 158 VEVQLPELfHKIGVG--AMtwsplacgivsgkydsgippysraslkgyqwlkdKILSeEGRRQQAKLKELQAiaerLGCT 235
Cdd:cd19105 176 LEEALAAA-AEKGIGvvAM----------------------------------KTLA-GGYLQPALLSVLKA----KGFS 215
|
250 260 270
....*....|....*....|....*....|....*
gi 315434251 236 LPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 270
Cdd:cd19105 216 LPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
5-287 |
8.66e-28 |
|
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: 109.45 E-value: 8.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 5 LMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKifWGGKAETERGL-----SRKHIIEGLKASLER 79
Cdd:cd19144 39 VLDAAFELGCTFWDTADIY--GDSEELIGRWFKQNPGKREKIFLATK--FGIEKNVETGEysvdgSPEYVKKACETSLKR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMF--QRE 156
Cdd:cd19144 115 LGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSECSAETLRRAHAVH-------PIAAvQIEYSPFslDIE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 157 KVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDS-----------GIPPYSRASLKGYQWLKDKIlseegrrqqaklkel 225
Cdd:cd19144 188 RPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSpddfeegdfrrMAPRFQAENFPKNLELVDKI--------------- 252
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315434251 226 QAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19144 253 KAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKV--KLTEEEEKEIREI 312
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
4-284 |
1.49e-27 |
|
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: 108.67 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 4 QLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI---FWGGKAETERGlSRKHIIEGLKASLERL 80
Cdd:cd19145 37 ALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQLATKFgihEIGGSGVEVRG-DPAYVRAACEASLKRL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltpPICE-QAEYHMFQREkVE 159
Cdd:cd19145 114 DVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADTIRRAHAVH-------PITAvQLEWSLWTRD-IE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 VQLPELFHKIGVGAMTWSPLACGIVSGK-----------YDSGIPPYSRASLKgyqwlKDKILSEegrrqqaklkELQAI 228
Cdd:cd19145 186 EEIIPTCRELGIGIVPYSPLGRGFFAGKakleellensdVRKSHPRFQGENLE-----KNKVLYE----------RVEAL 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 315434251 229 AERLGCTLPQLAIAWCL-RNEGVSSVlLGASNADQLMENIGAIQVlpKLSSSIIHEI 284
Cdd:cd19145 251 AKKKGCTPAQLALAWVLhQGEDVVPI-PGTTKIKNLNQNIGALSV--KLTKEDLKEI 304
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
4-285 |
4.37e-27 |
|
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: 107.32 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 4 QLMTLAYDNGINLFDTAEVYAAGKAEV---VLGNIIKKKGWRRSSLVITTKifwGGKAET--ERGLSRKHIIEGLKASLE 78
Cdd:cd19077 29 ETMKAALDAGSNLWNGGEFYGPPDPHAnlkLLARFFRKYPEYADKVVLSVK---GGLDPDtlRPDGSPEAVRKSIENILR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 79 RL-QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltPPICEQAEYHMFQREK 157
Cdd:cd19077 106 ALgGTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAETIRRAHAVH------PIAAVEVEYSLFSREI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 158 VEVQLPELFHKIGVGAMTWSPLACGIVSGKY--DSGIPPY-SRASLkgyqwlkDKILSEEGRRQQAKLKELQAIAERLGC 234
Cdd:cd19077 180 EENGVLETCAELGIPIIAYSPLGRGLLTGRIksLADIPEGdFRRHL-------DRFNGENFEKNLKLVDALQELAEKKGC 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 235 TLPQLAIAWCLRNEGVSSV-LLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19077 253 TPAQLALAWILAQSGPKIIpIPGSTTLERVEENLKAANV--ELTDEELKEIN 302
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
9-269 |
7.69e-27 |
|
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: 105.38 E-value: 7.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEvvlgNIIKK--KGWRrSSLVITTKIFW--GGKAETERGLSRKHIIEGLKASLERLQLEY 84
Cdd:cd19088 33 ALELGVNFIDTADSYGPDVNE----RLIAEalHPYP-DDVVIATKGGLvrTGPGWWGPDGSPEYLRQAVEASLRRLGLDR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 85 VDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnltppI-CEQAEYHMFQREKVEVQlp 163
Cdd:cd19088 108 IDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR-------IvSVQNRYNLANRDDEGVL-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 164 ELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseeGRRQQAKLKELQAIAERLGCTLPQLAIAW 243
Cdd:cd19088 179 DYCEAAGIAFIPWFPLG----------------------------------GGDLAQPGGLLAEVAARLGATPAQVALAW 224
|
250 260
....*....|....*....|....*.
gi 315434251 244 CLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19088 225 LLARSPVMLPIPGTSSVEHLEENLAA 250
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
1-269 |
3.41e-25 |
|
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: 100.81 E-value: 3.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergLSRKHIIEGLKASLERL 80
Cdd:cd19073 15 DCANAVKEALELGYRHIDTAEIY---NNEAEVGEAIAESGVPREDLFITTKVWRDH-------LRPEDLKKSVDRSLEKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF--QREKV 158
Cdd:cd19073 85 GTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISP----LPIAVNQVEFHPFlyQAELL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 159 EVQLPelfHKIGVGAmtWSPLAcgivsgkydsgippysraslkgyqwlkdkilseegRRQQAKLKELQAIAERLGCTLPQ 238
Cdd:cd19073 161 EYCRE---NDIVITA--YSPLA-----------------------------------RGEVLRDPVIQEIAEKYDKTPAQ 200
|
250 260 270
....*....|....*....|....*....|.
gi 315434251 239 LAIAWCLRnEGVsSVLLGASNADQLMENIGA 269
Cdd:cd19073 201 VALRWLVQ-KGI-VVIPKASSEDHLKENLAI 229
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
9-269 |
5.14e-24 |
|
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: 98.59 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKkkGWRRSSLVITTKI-------FWGGKAETER--GLSRKHIIEGLKASLER 79
Cdd:cd19162 28 AWDAGIRYFDTAPLYGLGLSERRLGAALA--RHPRAEYVVSTKVgrllepgAAGRPAGADRrfDFSADGIRRSIEASLER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 80 LQLEYVDVVFANRPDP--NTPMEETVRAMTHVINQGM--AMYWGTSRWSsmeimEAYSVARQFNLTPpICEQAEYHMFQR 155
Cdd:cd19162 106 LGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVvgAIGVGVTDWA-----ALLRAARRADVDV-VMVAGRYTLLDR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 156 EKVEVQLPELFHKiGVGAMTWSPLACGIVsgkyDSGIPPYSRASlkgYQWLKDKILseegrrqqAKLKELQAIAERLGCT 235
Cdd:cd19162 180 RAATELLPLCAAK-GVAVVAAGVFNSGIL----ATDDPAGDRYD---YRPATPEVL--------ARARRLAAVCRRYGVP 243
|
250 260 270
....*....|....*....|....*....|....
gi 315434251 236 LPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19162 244 LPAAALQFPLRHPAVASVVVGAASPAELRDNLAL 277
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-275 |
2.40e-22 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 93.75 E-value: 2.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKgwrrSSLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQ 81
Cdd:cd19097 28 AKKILEYALKAGINTLDTAPAY--GDSEKVLGKFLKRL----DKFKIITKL---PPLKEDKKEDEAAIEASVEASLKRLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRP-DPNTPMEETVRAMTHVINQGMAMYWGTSrwssmeimeAYSVarqfnltppicEQAEYhMFQREKVE- 159
Cdd:cd19097 99 VDSLDGLLLHNPdDLLKHGGKLVEALLELKKEGLIRKIGVS---------VYSP-----------EELEK-ALESFKIDi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 160 VQLPelfhkigVGAMTWSPLACGIVSGKYDSGIPPYSRaS--LKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLP 237
Cdd:cd19097 158 IQLP-------FNILDQRFLKSGLLAKLKKKGIEIHAR-SvfLQGLLLMEPDKLPAKFAPAKPLLKKLHELAKKLGLSPL 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 315434251 238 QLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPK 275
Cdd:cd19097 230 ELALGFVLSLPEIDKIVVGVDSLEQLKEIIAAFKKPPL 267
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
17-287 |
5.78e-22 |
|
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin reductase is a founding member of aldo-keto reductase family 3 member F3 (AKR3F3). It is a aldo/keto reductase family oxidoreductase.
Pssm-ID: 381366 [Multi-domain] Cd Length: 253 Bit Score: 92.32 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 17 FDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGkaetergLSRKHIIEGLKASLERLQLEYVDVVFANRPDPN 96
Cdd:cd19140 38 IDTAQMY---GNEAQVGEAIAASGVPRDELFLTTKVWPDN-------YSPDDFLASVEESLRKLRTDYVDLLLLHWPNKD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 97 TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF--QRekvevQLPELFHKIGVGAM 174
Cdd:cd19140 108 VPLAETLGALNEAQEAGLARHIGVSNFTVALLREAVELSE----APLFTNQVEYHPYldQR-----KLLDAAREHGIALT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 175 TWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRNEGVsSVL 254
Cdd:cd19140 179 AYSPLARGEV---------------------LKDPV--------------LQEIGRKHGKTPAQVALRWLLQQEGV-AAI 222
|
250 260 270
....*....|....*....|....*....|...
gi 315434251 255 LGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19140 223 PKATNPERLEENLDIFDF--TLSDEEMARIAAL 253
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
1-288 |
7.67e-22 |
|
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and similar proteins; Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV and Aspergillus flavus norsolorinic acid reductase (NOR), are founding members of aldo-keto reductase family 9 member A1-2 (AKR9A1-2), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis.
Pssm-ID: 381372 [Multi-domain] Cd Length: 326 Bit Score: 93.26 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIFWGGK-AETER------GLSRKHIIEGL 73
Cdd:cd19146 36 TAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATKYTTGYRrGGPIKiksnyqGNHAKSLRLSV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 74 KASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHM- 152
Cdd:cd19146 115 EASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPAWVVSKANAYARAHGLTQFVVYQGHWSAa 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 153 ---FQREKVEVQLPElfhkiGVGAMTWSPLAcgivSGKYDSGIPPYSRASLKGYQWLKdkilSEEGRRQQAKLKElqaIA 229
Cdd:cd19146 195 frdFERDILPMCEAE-----GMALAPWGVLG----QGQFRTEEEFKRRGRSGRKGGPQ----TEKERKVSEKLEK---VA 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 315434251 230 ERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSIL 288
Cdd:cd19146 259 EEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGI--SLSDEEIQEIEDAY 315
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
2-285 |
2.01e-21 |
|
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: 90.62 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGLSRKHIIEGLKASLERLQ 81
Cdd:cd19071 16 TAEAVLAALEAGYRHIDTAAAY---GNEAEVGEAIRESGVPREELFITTKLWP-------TDHGYERVREALEESLKDLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVV-----FANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF-- 153
Cdd:cd19071 86 LDYLDLYlihwpVPGKEGGSKeARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAAR----IKPAVNQIELHPYlq 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 154 QREkvevqLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGRRQQAKLKELQAIAERLG 233
Cdd:cd19071 162 QKE-----LVEFCKEHGIVVQAYSPLG---------------------------------RGRRPLLDDPVLKEIAKKYG 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 234 CTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19071 204 KTPAQVLLRWALQR-GV-VVIPKSSNPERIKENLDVFDF--ELSEEDMAAID 251
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
9-270 |
3.86e-21 |
|
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: 90.69 E-value: 3.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIkkKGWRRSSLVITTKI-FWGGKAETERGLSRKHIIEGLKASLERLQLEYVDV 87
Cdd:cd19163 42 ALDSGINYIDTAPWYGQGRSETVLGKAL--KGIPRDSYYLATKVgRYGLDPDKMFDFSAERITKSVEESLKRLGLDYIDI 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 88 V------FAnrPDPNTPMEETVRAMTHVINQGMAMYWGTS-------RwssmEIMEAYSVARQFNLTppiceQAEYHMFQ 154
Cdd:cd19163 120 IqvhdieFA--PSLDQILNETLPALQKLKEEGKVRFIGITgypldvlK----EVLERSPVKIDTVLS-----YCHYTLND 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 155 REKVEvqLPELFHKIGVGAMTWSPLACGIVSgkyDSGIPPYSRASlkgyQWLKDKIlseegrrqqaklKELQAIAERLGC 234
Cdd:cd19163 189 TSLLE--LLPFFKEKGVGVINASPLSMGLLT---ERGPPDWHPAS----PEIKEAC------------AKAAAYCKSRGV 247
|
250 260 270
....*....|....*....|....*....|....*.
gi 315434251 235 TLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAI 270
Cdd:cd19163 248 DISKLALQFALSNPDIATTLVGTASPENLRKNLEAA 283
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
2-280 |
1.90e-19 |
|
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: 86.05 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETErgLSRKHIIEGLKASLERLQ 81
Cdd:cd19153 35 AVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYTVATKVGRYRDSEFD--YSAERVRASVATSLERLH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRWsSMEIMEaySVARQFNLTPPICEQAEYHM-FQREK 157
Cdd:cd19153 113 TTYLDVVYLHDiefVDYDTLVDEALPALRTLKDEGVIKRIGIAGY-PLDTLT--RATRRCSPGSLDAVLSYCHLtLQDAR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 158 VEVQLPELFHKIGVGAMTWSPLACGIVSGKydsGIPPYSRAS--LKGYQWLKDKILSEEGRrqqaklkelqaiaerlgcT 235
Cdd:cd19153 190 LESDAPGLVRGAGPHVINASPLSMGLLTSQ---GPPPWHPASgeLRHYAAAADAVCASVEA------------------S 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 315434251 236 LPQLAIAWCLRNE-GVSSVLLGASNADQLMENIGAIQVLPKLSSSI 280
Cdd:cd19153 249 LPDLALQYSLAAHaGVGTVLLGPSSLAQLRSMLAAVDAVASLGAAI 294
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
2-269 |
3.28e-19 |
|
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: 84.92 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGgkaeteRGLSRKHIIEGLKASLERLQ 81
Cdd:cd19096 23 AIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKE--GPREKFYLATKLPPW------SVKSAEDFRRILEESLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDvVFA----NRPD------PNTPMEETVRAMThvinQGMAMYWGTSRWSSMEIMEAYSVARQFNltppICeQAEYH 151
Cdd:cd19096 95 VDYID-FYLlhglNSPEwlekarKGGLLEFLEKAKK----EGLIRHIGFSFHDSPELLKEILDSYDFD----FV-QLQYN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 152 MFQREKVEVQ-LPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrRQQAKLKELQAIAE 230
Cdd:cd19096 165 YLDQENQAGRpGIEYAAKKGMGVIIMEPLKGG----------------------------------GLANNPPEALAILC 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 315434251 231 RLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGA 269
Cdd:cd19096 211 GAPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAA 249
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
2-272 |
5.75e-19 |
|
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: 84.97 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIFWGGKAETERGLSRKHII----------- 70
Cdd:cd19152 22 AKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLLVPLQEVEPTFEPGFwnplpfdavfd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 71 ---EGLKA----SLERLQLEYVDVVFANRPDPNTPMEET-----------VRAMTHVINQGMAMYW--GTSRWSSME--- 127
Cdd:cd19152 100 ysyDGILRsiedSLQRLGLSRIDLLSIHDPDEDLAGAESdehfaqaikgaFRALEELREEGVIKAIglGVNDWEVILril 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 128 -------IMeaysVARQFNLTppicEQAEYHMFqrekvevqLPELF-HKIGVgamtwsplacgIVSGKYDSGIppysras 199
Cdd:cd19152 180 eeadldwVM----LAGRYTLL----DHSAAREL--------LPECEkRGVKV-----------VNAGPFNSGF------- 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434251 200 LKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 272
Cdd:cd19152 226 LAGGDNFDYYEYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALLAT 298
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
9-288 |
7.53e-18 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 82.13 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVV 88
Cdd:PLN02587 40 AFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVSTKC---GRYGEGFDFSAERVTKSVDESLARLQLDYVDIL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANR---PDPNTPMEETVRAMTHVINQGMAMYWGTSRwSSMEIMEaYSVARqfnlTPP-----ICEQAEYHMFQREKVEV 160
Cdd:PLN02587 117 HCHDiefGSLDQIVNETIPALQKLKESGKVRFIGITG-LPLAIFT-YVLDR----VPPgtvdvILSYCHYSLNDSSLEDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 qLPELFHKiGVGAMTWSPLACGIVSgkyDSGIPPYSRASLKgyqwLKdkilseEGRRQQAKLKELQaiaerlGCTLPQLA 240
Cdd:PLN02587 191 -LPYLKSK-GVGVISASPLAMGLLT---ENGPPEWHPAPPE----LK------SACAAAATHCKEK------GKNISKLA 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 315434251 241 IAWCLRNEGVSSVLLGASNADQLMENIGAIQVLPKLS--SSIIHEIDSIL 288
Cdd:PLN02587 250 LQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGidEELLSEVEAIL 299
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-267 |
2.86e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 80.44 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGN----IIKKKGWRRSSLVITTKifwGG----------------KAETE 61
Cdd:cd19099 23 YREALKAALDSGINVIDTAINYRGGRSERLIGKalreLIEKGGIKRDEVVIVTK---AGyipgdgdeplrplkylEEKLG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 62 RGLSRKHIIEG-------------LKASLERLQLEYVDVVFANRP----------DPNTPMEETVRAMTHVINQGMAMYW 118
Cdd:cd19099 100 RGLIDVADSAGlrhcispayledqIERSLKRLGLDTIDLYLLHNPeeqllelgeeEFYDRLEEAFEALEEAVAEGKIRYY 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 119 GTSRWSsmeIMEAYSVARQFNLTPPICEQAE-----YHMFqreKVeVQLPelFHKIGVGAMT----WSPLACGIVSGKYD 189
Cdd:cd19099 180 GISTWD---GFRAPPALPGHLSLEKLVAAAEevggdNHHF---KV-IQLP--LNLLEPEALTekntVKGEALSLLEAAKE 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315434251 190 SGIPPYSRASLKGYQWLKDKILSEEGrrqqaklkelqaiAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENI 267
Cdd:cd19099 251 LGLGVIASRPLNQGQLLGELRLADLL-------------ALPGGATLAQRALQFARSTPGVDSALVGMRRPEHVDENL 315
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-288 |
5.97e-17 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 79.18 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 10 YDNGINLFDTAEVYaaGKAEVVLGNIIKKKGW---RRSSLVITTKIFWGGKAETergLSRKHIIEGLKASLERLQLEYVD 86
Cdd:cd19101 33 VDAGLTTFDCADIY--GPAEELIGEFRKRLRRerdAADDVQIHTKWVPDPGELT---MTRAYVEAAIDRSLKRLGVDRLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VV---FANRPDPNtpMEETVRAMTHVINQGMAMYWG-----TSRWSsmEIMEAysvarqfnLTPPICEQAEYHMFQReKV 158
Cdd:cd19101 108 LVqfhWWDYSDPG--YLDAAKHLAELQEEGKIRHLGltnfdTERLR--EILDA--------GVPIVSNQVQYSLLDR-RP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 159 EVQLPELFHKIGVGAMTWSPLACGIVSGKY----DSGIPPYSRASLKGYQWLKDKILSEEGrrQQAKLKELQAIAERLGC 234
Cdd:cd19101 175 ENGMAALCEDHGIKLLAYGTLAGGLLSEKYlgvpEPTGPALETRSLQKYKLMIDEWGGWDL--FQELLRTLKAIADKHGV 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 315434251 235 TLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSIL 288
Cdd:cd19101 253 SIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAFSF--RLDDEDRAAIDAVL 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
2-267 |
7.30e-17 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 79.86 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTKIfwggkaeTERGLSRKHIIEGLKASLERLQ 81
Cdd:COG1453 31 AEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKG---PRDKVILATKL-------PPWVRDPEDMRKDLEESLKRLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDV----------VFANRPDPNTPMEETVRAmthvINQGMAMYWGtsrWSS-------MEIMEAY---SVARQFNLt 141
Cdd:COG1453 99 TDYIDLylihglnteeDLEKVLKPGGALEALEKA----KAEGKIRHIG---FSThgsleviKEAIDTGdfdFVQLQYNY- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 142 ppiceqaeyhMFQREKVEVQLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrqqaK 221
Cdd:COG1453 171 ----------LDQDNQAGEEALEAAAEKGIGVIIMKPLKGG--------------------------------------R 202
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 315434251 222 LKELQAIAERLGC---TLPQLAIAWCLRNEGVSSVLLGASNADQLMENI 267
Cdd:COG1453 203 LANPPEKLVELLCpplSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENL 251
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
2-275 |
1.97e-16 |
|
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: 78.14 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwrRSSLVITTKIfwgGK----AETERGL------------- 64
Cdd:cd19161 22 ADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKV---GRllkpAREGSVPdpngfvdplpfei 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 65 ----SRKHIIEGLKASLERLQLEYVDVVF---------ANRPDPN---TPMEETVRAMTHVINQGM--AMYWGTSRWSSM 126
Cdd:cd19161 97 vydySYDGIMRSFEDSLQRLGLNRIDILYvhdigvythGDRKERHhfaQLMSGGFKALEELKKAGVikAFGLGVNEVQIC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 127 -EIMeaysvaRQFNLTppiCE--QAEYHMFQREKVEVQLPELfHKIGVGAmtwsplacgIVSGKYDSGIPPYSRASLKGY 203
Cdd:cd19161 177 lEAL------DEADLD---CFllAGRYSLLDQSAEEEFLPRC-EQRGTSL---------VIGGVFNSGILATGTKSGAKF 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 315434251 204 QWLkdkilsEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQ-VLPK 275
Cdd:cd19161 238 NYG------DAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQtDIPE 304
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
9-245 |
2.09e-15 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381329 [Multi-domain] Cd Length: 299 Bit Score: 75.06 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgWRRSSLVITTKIFWGGkaeteRGLSRKHIIEGLKASLERLQLEYVDVV 88
Cdd:cd19103 41 AMAAGLNLWDTAAVYGMGASEKILGEFLKR--YPREDYIISTKFTPQI-----AGQSADPVADMLEGSLARLGTDYIDIY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDP---NTPmeetvramtHVI---NQGMAMYWGTSRWSSMEIMEAYSVARQFNLtPPICEQAEYHMFQREKVEVQL 162
Cdd:cd19103 114 WIHNPADverWTP---------ELIpllKSGKVKHVGVSNHNLAEIKRANEILAKAGV-SLSAVQNHYSLLYRSSEEAGI 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 163 PELFHKIGVGAMTWSPLACGIVSGKYDSGIP-PYSRASLKGYQWLKDKIlseegRRQQAKLKElqaIAERLGCTLPQLAI 241
Cdd:cd19103 184 LDYCKENGITFFAYMVLEQGALSGKYDTKHPlPEGSGRAETYNPLLPQL-----EELTAVMAE---IGAKHGASIAQVAI 255
|
....
gi 315434251 242 AWCL 245
Cdd:cd19103 256 AWAI 259
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
2-293 |
2.42e-15 |
|
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.
Pssm-ID: 381346 [Multi-domain] Cd Length: 269 Bit Score: 74.19 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKaeterglsrkHIIEGLKASLERLQ 81
Cdd:cd19120 27 LVDSVKLALKAGFRHIDTAEMY---GNEKEVGEALKESGVPREDLFITTKVSPGIK----------DPREALRKSLAKLG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRP----DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFqrek 157
Cdd:cd19120 94 VDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK----IKPAVNQIEFHPY---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 158 VEVQLPEL--FH-KIGVGAMTWSPLAcgivsgkydsgipPYSRaslkgyqwlkdkilseegRRQQAKLKELQAIAERLGC 234
Cdd:cd19120 166 LYPQQPALleYCrEHGIVVSAYSPLS-------------PLTR------------------DAGGPLDPVLEKIAEKYGV 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 315434251 235 TLPQLAIAWCLRNEGVssVLLGASNADQLMENIGAIqvLPKLSSSIIHEIDSILGNKPY 293
Cdd:cd19120 215 TPAQVLLRWALQKGIV--VVTTSSKEERMKEYLEAF--DFELTEEEVEEIDKAGKQKHF 269
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
9-287 |
6.97e-15 |
|
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: 73.60 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKIFWGGkaetergLSRKHIIEGLKASLERLQL 82
Cdd:cd19154 34 ALKAGYRLIDTAFLY---QNEEAIGEALAE--LleegvvKREDLFITTKLWTHE-------HAPEDVEEALRESLKKLQL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 83 EYVDVVFANRP-------DPNTPM------------EETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPP 143
Cdd:cd19154 102 EYVDLYLIHAPaafkddeGESGTMengmsihdavdvEDVWRGMEKVYDEGLTKAIGVSNFNNDQIQRILDNAR----VKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 144 ICEQAEYHMFQREKvevQLPELFHKIGVGAMTWSPLacgivsGKYDSGIPPYSRASLKGYQWLKDKILSEegrrqqaklk 223
Cdd:cd19154 178 HNNQVECHLYFPQK---ELVEFCKKHNISVTSYATL------GSPGRANFTKSTGVSPAPNLLQDPIVKA---------- 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434251 224 elqaIAERLGCTLPQLAIAWCLRNeGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19154 239 ----IAEKHGKTPAQVLLRYLLQR-GI-AVIPKSATPSRIKENFNIFDF--SLSEEDMATLEEI 294
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
9-287 |
3.62e-14 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; Escherichia coli DkgB/YafB (EC 1.1.1.346), also called 2,5-didehydrogluconate reductase (2-dehydro-L-gulonate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, is a founding member of aldo-keto reductase family 3 member F2 (AKR3F2). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381365 [Multi-domain] Cd Length: 248 Bit Score: 70.46 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIFWggkaeteRGLSRKHIIEGLKASLERLQLEYVDVV 88
Cdd:cd19139 23 ALELGYRHIDTAQIY---DNEAAVGQAIAESGVPRDELFITTKIWI-------DNLSKDKLLPSLEESLEKLRTDYVDLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDPN--TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYhmFQREKVEVQLPElf 166
Cdd:cd19139 93 LIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPY--LQNRKLVAHCKQ-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 167 HKIGVGAmtWSPLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLr 246
Cdd:cd19139 169 HGIHVTS--YMTLAYGKV---------------------LDDPV--------------LAAIAERHGATPAQIALAWAM- 210
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 315434251 247 NEGVsSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19139 211 ARGY-AVIPSSTKREHLRSNLLALDL--TLDADDMAAIAAL 248
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-267 |
7.05e-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: 381326 [Multi-domain] Cd Length: 238 Bit Score: 69.43 E-value: 7.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKkgwRRSSLVITTKIfwggkaeTERglSRKHIIEGLKASLERLQ 81
Cdd:cd19100 29 AAAIIRRALDLGINYFDTAPSY--GDSEEKIGKALKG---RRDKVFLATKT-------GAR--DYEGAKRDLERSLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVF----ANRPDPNTPMEE--------------TVRAM---TH---VINQGMAMYWgtsrwssMEIMeaysvarQ 137
Cdd:cd19100 95 TDYIDLYQlhavDTEEDLDQVFGPggalealleakeegKIRFIgisGHspeVLLRALETGE-------FDVV-------L 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 138 FNLTPpiceqAEYHMfqREKVEVQLPEL-FHKIGVGAMtwSPLACGivsgkydsgippysraslkgyQWLKDKILSeegr 216
Cdd:cd19100 161 FPINP-----AGDHI--DSFREELLPLArEKGVGVIAM--KVLAGG---------------------RLLSGDPLD---- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434251 217 rqqaklkelqaiaerlgctlPQLAIAWCLRNEGVSSVLLGASNADQLMENI 267
Cdd:cd19100 207 --------------------PEQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
13-293 |
8.42e-13 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.
Pssm-ID: 381337 [Multi-domain] Cd Length: 286 Bit Score: 67.14 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 13 GINLFDTAEVYaagKAEVVLGNIIKKkgW------RRSSLVITTKIfwggkaeTERGLSRKHIIEGLKASLERLQLEYVD 86
Cdd:cd19111 30 GYRHIDTALSY---QNEKAIGEALKW--WlkngklKREEVFITTKL-------PPVYLEFKDTEKSLEKSLENLKLPYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VVFAN-------------RPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMF 153
Cdd:cd19111 98 LYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKILAYAK----VKPSNLQLECHAY 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 154 --QREKVEVQLPelfHKIGVGAmtWSPLAcgivsgkyDSGIPPYSRASLKgYQWLKD-KILseegrrqqaklkelqAIAE 230
Cdd:cd19111 174 lqQRELRKFCNK---KNIVVTA--YAPLG--------SPGRANQSLWPDQ-PDLLEDpTVL---------------AIAK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 315434251 231 RLGCTLPQLAIAWCL-RNEGvssVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSILGNKPY 293
Cdd:cd19111 225 ELDKTPAQVLLRFVLqRGTG---VLPKSTNKERIEENFEVFDF--ELTEEHFKKLKTLDRNMKY 283
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
13-250 |
1.40e-12 |
|
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.
Pssm-ID: 381361 [Multi-domain] Cd Length: 265 Bit Score: 66.19 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 13 GINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhIIEGLKASLERLQLEYVDVVFANR 92
Cdd:cd19135 39 GYRHIDTAKRY---GCEELLGKAIKESGVPREDLFLTTKL-WPSDYGYES------TKQAFEASLKRLGVDYLDLYLLHW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 93 PDPNTP-------MEETVRAMTHVINQGMAMYWGTSRWSS---MEIMEAYSVarqfnltPPICEQAEYHMFQREKvevQL 162
Cdd:cd19135 109 PDCPSSgknvketRAETWRALEELYDEGLCRAIGVSNFLIehlEQLLEDCSV-------VPHVNQVEFHPFQNPV---EL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 163 PELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAIA 242
Cdd:cd19135 179 IEYCRDNNIVFEGYCPLA--------------------------KGKALEEP---------TVTELAKKYQKTPAQILIR 223
|
....*...
gi 315434251 243 WCLRNEGV 250
Cdd:cd19135 224 WSIQNGVV 231
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
18-267 |
1.69e-12 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 66.22 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 18 DTAEVYAAGKaEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhIIEGLKASLERLQLEYVDVVF------ 89
Cdd:cd19125 42 DCAAIYGNEK-EIgkALKKLFEDGVVKREDLFITSKL-WCTDHAPED------VPPALEKTLKDLQLDYLDLYLihwpvr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 90 ----ANRPDP----NTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYHMFQREKvevQ 161
Cdd:cd19125 114 lkkgAHMPEPeevlPPDIPSTWKAMEKLVDSGKVRAIGVSNFSVKKLEDLLAVAR----VPPAVNQVECHPGWQQD---K 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 162 LPELFHKIGVGAMTWSPLacgivsgkydsGIPpysraslkGYQWLKDKILSEEgrrqqaklkELQAIAERLGCTLPQLAI 241
Cdd:cd19125 187 LHEFCKSKGIHLSAYSPL-----------GSP--------GTTWVKKNVLKDP---------IVTKVAEKLGKTPAQVAL 238
|
250 260
....*....|....*....|....*.
gi 315434251 242 AWCLRnEGvSSVLLGASNADQLMENI 267
Cdd:cd19125 239 RWGLQ-RG-TSVLPKSTNEERIKENI 262
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
2-184 |
1.89e-12 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 65.92 E-value: 1.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGLSrkhiieGLKASLERLQ 81
Cdd:cd19126 25 TERAVQTALENGYRSIDTAAIY---KNEEGVGEAIRESGVPREELFVTTKL-WNDDQRARRTED------AFQESLDRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKVEV 160
Cdd:cd19126 95 LDYVDLYLIHWPGKDK-FIDTWKALEKLYASGKVKAIGVSNFQEHHLEELLAHAD----VVPAVNQVEFHpYLTQKELRG 169
|
170 180
....*....|....*....|....
gi 315434251 161 QLPElfHKIGVGAmtWSPLACGIV 184
Cdd:cd19126 170 YCKS--KGIVVEA--WSPLGQGGL 189
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
2-267 |
2.55e-12 |
|
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid reductase (2,5-DKG reductase) is a founding member of aldo-keto reductase family 5 member F1 (AKR5F1). It catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381359 [Multi-domain] Cd Length: 255 Bit Score: 65.29 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhIIEGLKASLERLQ 81
Cdd:cd19133 25 CERAVLEAIKAGYRLIDTAAAYGNEEA---VGRAIKKSGIPREELFITTKL-WIQDAGYEK------AKKAFERSLKRLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNtpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSvarqFNLTPPICEQAEYHMFQREKVEVq 161
Cdd:cd19133 95 LDYLDLYLIHQPFGD--VYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLIL----HNEVKPAVNQIETHPFNQQIEAV- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 162 lpELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkgyqwlkdkilseEGRRQQAKLKELQAIAERLGCTLPQLAI 241
Cdd:cd19133 168 --EFLKKYGVQIEAWGPFA---------------------------------EGRNNLFENPVLTEIAEKYGKSVAQVIL 212
|
250 260
....*....|....*....|....*.
gi 315434251 242 AWcLRNEGVsSVLLGASNADQLMENI 267
Cdd:cd19133 213 RW-LIQRGI-VVIPKSVRPERIAENF 236
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
2-267 |
3.01e-12 |
|
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: 65.09 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGLsrkhiiEGLKASLERLQ 81
Cdd:cd19131 25 AASAVREALEVGYRSIDTAAIY---GNEEGVGKAIRASGVPREELFITTKL-WNSDQGYDSTL------RAFDESLRKLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPdpnTPME----ETVRAMTHVINQGMAMYWGTSRWSS---MEIMEAYSVArqfnltpPICEQAEYH--M 152
Cdd:cd19131 95 LDYVDLYLIHWP---VPAQdkyvETWKALIELKKEGRVKSIGVSNFTIehlQRLIDETGVV-------PVVNQIELHprF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 153 FQREkvevqLPELFHKIGVGAMTWSPLACGIVsgkydsgippysraslkgyqwLKDKILSEegrrqqaklkelqaIAERL 232
Cdd:cd19131 165 QQRE-----LRAFHAKHGIQTESWSPLGQGGL---------------------LSDPVIGE--------------IAEKH 204
|
250 260 270
....*....|....*....|....*....|....*
gi 315434251 233 GCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 267
Cdd:cd19131 205 GKTPAQVVIRWHLQNGLV--VIPKSVTPSRIAENF 237
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
8-287 |
4.20e-12 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 65.51 E-value: 4.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 8 LAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETErglsrkHIIEGLKASLERLQLEYV 85
Cdd:cd19123 33 QALEAGYRHIDCAAIYG-NEAEIgaALAEVFKEGKVKREDLWITSKL-WNNSHAPE------DVLPALEKTLADLQLDYL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 86 D-------VVF---ANRPDPNT--------PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQ 147
Cdd:cd19123 105 DlylmhwpVALkkgVGFPESGEdllslspiPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLATAR----IKPAVNQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 148 AEYHMFqrekveVQLPELF----HKiGVGAMTWSPLAcgivsgkydSGIPPYSRASLKGYQWLKDKILSEegrrqqaklk 223
Cdd:cd19123 181 VELHPY------LQQPELLafcrDN-GIHLTAYSPLG---------SGDRPAAMKAEGEPVLLEDPVINK---------- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 315434251 224 elqaIAERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:cd19123 235 ----IAEKHGASPAQVLIAWAIqRG---TVVIPKSVNPERIQQNLEAAEV--ELDASDMATIAAL 290
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
2-267 |
6.10e-12 |
|
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: 64.85 E-value: 6.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVY----AAGKAevvLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhIIEGLKASL 77
Cdd:cd19128 16 SKEAVKNAIKAGYRHIDCAYYYgneaFIGIA---FSEIFKDGGVKREDLFITSKL-WPTMHQPEN------VKEQLLITL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 78 ERLQLEYVDVVFANRP---DPNT----------------PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqf 138
Cdd:cd19128 86 QDLQLEYLDLFLIHWPlafDMDTdgdprddnqiqslskkPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDLLNYCK-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 139 nlTPPICEQAEYHM-FQREKVeVQLPeLFHKIGVGAmtWSPLAcgivsGKYDsgippysraslkgyqwlkdkilseEGRR 217
Cdd:cd19128 164 --IKPFMNQIECHPyFQNDKL-IKFC-IENNIHVTA--YRPLG-----GSYG------------------------DGNL 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434251 218 QQAKLKELQAIAERLGCTLPQLAIAWCL-RNEGVSSVLLGASNADQLMENI 267
Cdd:cd19128 209 TFLNDSELKALATKYNTTPPQVIIAWHLqKWPKNYSVIPKSANKSRCQQNF 259
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
2-267 |
9.39e-12 |
|
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: 64.11 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkAETERGLSRKhiIEGLKASLERLQ 81
Cdd:cd19134 26 AERSVSAALEAGYRLIDTAAAYGN---EAAVGRAIAASGIPRGELFVTTKL-----ATPDQGFTAS--QAACRASLERLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNT-PMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAysvarqFNLT--PPICEQAEYH--MFQRE 156
Cdd:cd19134 96 LDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENL------IDLTffTPAVNQIELHplLNQAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 157 kvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdkilseegrrQQAKLKELQAIAERLGCTL 236
Cdd:cd19134 170 -----LRKVNAQHGIVTQAYSPLGVG-----------------------------------RLLDNPAVTAIAAAHGRTP 209
|
250 260 270
....*....|....*....|....*....|.
gi 315434251 237 PQLAIAWCLRNEGVssVLLGASNADQLMENI 267
Cdd:cd19134 210 AQVLLRWSLQLGNV--VISRSSNPERIASNL 238
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
18-269 |
9.65e-12 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 63.89 E-value: 9.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 18 DTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIfWggkaeTERgLSRKHIIEGLKASLERLQLEYVDVVFANRPDPN- 96
Cdd:PRK11172 34 DTAQIYD-NEAAV--GQAIAESGVPRDELFITTKI-W-----IDN-LAKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 97 -TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTppiCEQAEYHMF-QREKVEVQLPElfHKIGVGA- 173
Cdd:PRK11172 104 eVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENIA---TNQIELSPYlQNRKVVAFAKE--HGIHVTSy 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 174 MTwspLACGIVsgkydsgippysraslkgyqwLKDKIlseegrrqqaklkeLQAIAERLGCTLPQLAIAWCLRnEGvSSV 253
Cdd:PRK11172 179 MT---LAYGKV---------------------LKDPV--------------IARIAAKHNATPAQVILAWAMQ-LG-YSV 218
|
250
....*....|....*.
gi 315434251 254 LLGASNADQLMENIGA 269
Cdd:PRK11172 219 IPSSTKRENLASNLLA 234
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
3-89 |
1.28e-11 |
|
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: 63.84 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 3 EQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKK--KGWRRSSLVITTKIfwGGKAETERGLSRKHIIEGLKASLERL 80
Cdd:cd19164 37 VDIVRRALELGIRAFDTSPYY--GPSEIILGRALKAlrDEFPRDTYFIITKV--GRYGPDDFDYSPEWIRASVERSLRRL 112
|
....*....
gi 315434251 81 QLEYVDVVF 89
Cdd:cd19164 113 HTDYLDLVY 121
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
7-267 |
3.28e-11 |
|
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) is a founding member of the aldo-keto reductase family 5 member B1 (AKR5B1). M6DH (EC 1.1.1.218), also called naloxone reductase, oxidizes the C-6 hydroxy group of morphine and codeine.
Pssm-ID: 381353 [Multi-domain] Cd Length: 268 Bit Score: 62.42 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 7 TLAYDNGINLFDTAEVYAaGKAEVvlGNIIKKKGWRRSSLVITTKIFWG--GKAETERGLsrkhiieglKASLERLQLEY 84
Cdd:cd19127 29 ATALADGYRLIDTAAAYG-NEREV--GEGIRRSGVDRSDIFVTTKLWISdyGYDKALRGF---------DASLRRLGLDY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 85 VDVVFANRPDPNTpMEETV---RAMTHVINQGMAMYWGTSRWSS---MEIMEAYSVArqfnltpPICEQAEYHMFQREKv 158
Cdd:cd19127 97 VDLYLLHWPVPND-FDRTIqayKALEKLLAEGRVRAIGVSNFTPehlERLIDATTVV-------PAVNQVELHPYFSQK- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 159 evQLPELFHKIGVGAMTWSPLAcGIVsgKYDSGIPPySRASLkgyqwLKDKILSEegrrqqaklkelqaIAERLGCTLPQ 238
Cdd:cd19127 168 --DLRAFHRRLGIVTQAWSPIG-GVM--RYGASGPT-GPGDV-----LQDPTITG--------------LAEKYGKTPAQ 222
|
250 260
....*....|....*....|....*....
gi 315434251 239 LAIAWCLRNeGVSSVlLGASNADQLMENI 267
Cdd:cd19127 223 IVLRWHLQN-GVSAI-PKSVHPERIAENI 249
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
13-267 |
4.92e-11 |
|
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like protein is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase similar to Bacillus subtilis glyoxal reductase (YvgN) that reduces glyoxal and methylglyoxal (2-oxopropanal).
Pssm-ID: 381362 [Multi-domain] Cd Length: 262 Bit Score: 61.88 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 13 GINLFDTAEVYaagKAEVVLGNIIK----KKGWRRSSLVITTKIfwgGKAETERGLSRkhiiEGLKASLERLQLEYVDVV 88
Cdd:cd19136 28 GYRLIDTASVY---RNEADIGKALRdllpKYGLSREDIFITSKL---APKDQGYEKAR----AACLGSLERLGTDYLDLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRP-----DPNTPME-----ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEAYSvarqfnLTPPICEQAEYH--MFQ 154
Cdd:cd19136 98 LIHWPgvqglKPSDPRNaelrrESWRALEDLYKEGKLRAIGVSNYtvRHLEELLKYC------EVPPAVNQVEFHphLVQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 155 REkvevqLPELFHKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlKDKILSEEgrrqqaklkELQAIAERLGC 234
Cdd:cd19136 172 KE-----LLKFCKDHGIHLQAYSSLGSG------------------------DLRLLEDP---------TVLAIAKKYGR 213
|
250 260 270
....*....|....*....|....*....|...
gi 315434251 235 TLPQLAIAWCLRNeGVsSVLLGASNADQLMENI 267
Cdd:cd19136 214 TPAQVLLRWALQQ-GI-GVIPKSTNPERIAENI 244
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
1-267 |
9.42e-11 |
|
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).
Pssm-ID: 381358 [Multi-domain] Cd Length: 255 Bit Score: 60.75 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 1 MAEQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKKKGWRRSSLVITTKIfwggkaeteRGlsRKH----IIEGLKAS 76
Cdd:cd19132 21 EGVEAVVAALQAGYRLLDTAFNYEN---EGAVGEAVRRSGVPREELFVTTKL---------PG--RHHgyeeALRTIEES 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 77 LERLQLEYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEA----YSVARQFNLTPPIcEQAE 149
Cdd:cd19132 87 LYRLGLDYVDLYLIHWPNPSRDLYvEAWQALIEAREEGLVRSIGVSNFlpEHLDRLIDetgvTPAVNQIELHPYF-PQAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 150 YHMFQREKvevqlpelfhkiGVGAMTWSPLAcgivsgkydsgippysraslKGYQWLKDKIlseegrrqqaklkeLQAIA 229
Cdd:cd19132 166 QRAYHREH------------GIVTQSWSPLG--------------------RGSGLLDEPV--------------IKAIA 199
|
250 260 270
....*....|....*....|....*....|....*...
gi 315434251 230 ERLGCTLPQLAIAWCLRnEGVsSVLLGASNADQLMENI 267
Cdd:cd19132 200 EKHGKTPAQVVLRWHVQ-LGV-VPIPKSANPERQRENL 235
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
2-285 |
1.21e-10 |
|
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: 61.38 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGwRRSSLVITTKIFW--------GGKAETERGLSRKHIIEGL 73
Cdd:cd19147 36 AFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKFTTdykayevgKGKAVNYCGNHKRSLHVSV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 74 KASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMF 153
Cdd:cd19147 115 RDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDTPAWVVSAANYYATAHGKTPFSVYQGRWNVL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 154 QREKVEVQLPELFHkIGVGAMTWSPLAcgivSGKYDSgiPPYSRASLKGYQWLKDKILSEEGRRQQAKLKE-LQAIAERL 232
Cdd:cd19147 195 NRDFERDIIPMARH-FGMALAPWDVLG----GGKFQS--KKAVEERKKNGEGLRSFVGGTEQTPEEVKISEaLEKVAEEH 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 315434251 233 GC-TLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQVlpKLSSSIIHEID 285
Cdd:cd19147 268 GTeSVTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSI--KLTPEEIEYLE 319
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
17-253 |
1.72e-10 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 60.36 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 17 FDTAEVY----AAGKA--EVVLGNIIKKkgwrRSSLVITTKIfWGGKAEterglsRKHIIEGLKASLERLQLEYVDV--- 87
Cdd:cd19124 37 FDTAAAYgteeALGEAlaEALRLGLVKS----RDELFVTSKL-WCSDAH------PDLVLPALKKSLRNLQLEYVDLyli 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 88 ---------VFANRPDPNTP----MEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH-MF 153
Cdd:cd19124 106 hwpvslkpgKFSFPIEEEDFlpfdIKGVWEAMEECQRLGLTKAIGVSNFSCKKLQELLSFAT----IPPAVNQVEMNpAW 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 154 QREKvevqLPELFHKIGVGAMTWSPLACgivsgkydsgippysraslKGYQWLKDKILSEEgrrqqaklkELQAIAERLG 233
Cdd:cd19124 182 QQKK----LREFCKANGIHVTAYSPLGA-------------------PGTKWGSNAVMESD---------VLKEIAAAKG 229
|
250 260
....*....|....*....|
gi 315434251 234 CTLPQLAIAWcLRNEGVSSV 253
Cdd:cd19124 230 KTVAQVSLRW-VYEQGVSLV 248
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
3-267 |
2.31e-10 |
|
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: 59.99 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 3 EQLMTLAYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAEterglsRKHIIEGLKASLERL 80
Cdd:cd19116 28 RQAVKHAIEAGYRHIDTAYLYG-NEAEVgeAIREKIAEGVVKREDLFITTKL-WNSYHE------REQVEPALRESLKRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 81 QLEYVDVVFANRP-------DPNTPME---------ETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPI 144
Cdd:cd19116 100 GLDYVDLYLIHWPvafkennDSESNGDgslsdidylETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN----IKPA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 145 CEQAEYHM-FQREKvevqLPELFHKIGVGAMTWSPLacGIVSGKYDSGIPPYsraslkgyqwLKDKIlseegrrqqaklk 223
Cdd:cd19116 176 VNQIEVHPtLTQEK----LVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPR----------LDDPT------------- 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 315434251 224 eLQAIAERLGCTLPQLAIAWcLRNEGVsSVLLGASNADQLMENI 267
Cdd:cd19116 227 -LVAIAKKYGKTTAQIVLRY-LIDRGV-VPIPKSSNKKRIKENI 267
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
9-182 |
3.02e-09 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 56.62 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKaeterglsRKHIIEGLKASLERLQLEYVDVV 88
Cdd:PRK11565 37 ALEVGYRSIDTAAIY---KNEEGVGKALKEASVAREELFITTKL-WNDD--------HKRPREALEESLKKLQLDYVDLY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDPntPMEETVRAMTHVIN---QGMAMYWGTSRWSS---MEIMEAYSVArqfnltpPICEQAEYH--MFQRekvEV 160
Cdd:PRK11565 105 LMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVCNFQIhhlQRLIDETGVT-------PVINQIELHplMQQR---QL 172
|
170 180
....*....|....*....|..
gi 315434251 161 QLPELFHKIGVGAmtWSPLACG 182
Cdd:PRK11565 173 HAWNATHKIQTES--WSPLAQG 192
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
9-268 |
1.03e-08 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 55.09 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGLsrkhiiEGLKASLERLQLEYVDVV 88
Cdd:cd19157 33 ALKNGYRSIDTAAIY---GNEEGVGKGIKESGIPREELFITSKV-WNADQGYDSTL------KAFEASLERLGLDYLDLY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 89 FANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH--MFQREkvevqLPELF 166
Cdd:cd19157 103 LIHWPVKGK-YKETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE----IVPMVNQVEFHprLTQKE-----LRDYC 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 167 HKIGVGAMTWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLAIAWCLR 246
Cdd:cd19157 173 KKQGIQLEAWSPLMQG--------------------------QLLDNP---------VLKEIAEKYNKSVAQVILRWDLQ 217
|
250 260
....*....|....*....|..
gi 315434251 247 NEGVssVLLGASNADQLMENIG 268
Cdd:cd19157 218 NGVV--TIPKSIKEHRIIENAD 237
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
9-266 |
2.28e-08 |
|
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: 54.45 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGKAevvLGNIIKKkgW------RRSSLVITTKIFWGGkaeterglSRKHIIEG-LKASLERLQ 81
Cdd:cd19155 34 ALEAGYRHIDTAYVYRNEAA---IGNVLKK--WidsgkvKREELFIVTKLPPGG--------NRREKVEKfLLKSLEKLQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRP---------------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnl 140
Cdd:cd19155 101 LDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARILKNAR---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 141 TPPICEQAEYHMFQREKVEVQLPELfHKIGVGAmtWSPLAC-GIVSGKYDSGIPPYSRASLkgyqwLKDkilseegrrqq 219
Cdd:cd19155 177 IKPANLQVELHVYLQQKDLVDFCST-HSITVTA--YAPLGSpGAAHFSPGTGSPSGSSPDL-----LQD----------- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 315434251 220 aklKELQAIAERLGCTLPQLAIAWCLrNEGVsSVLLGASNADQLMEN 266
Cdd:cd19155 238 ---PVVKAIAERHGKSPAQVLLRWLM-QRGV-VVIPKSTNAARIKEN 279
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
9-284 |
5.17e-08 |
|
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium diazoefficiens DH is the prototype of this family. It belongs to aldo/keto reductase family.
Pssm-ID: 381355 [Multi-domain] Cd Length: 295 Bit Score: 53.23 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWGGKAETERglsrkhIIEGLKASLERLQLEYVD 86
Cdd:cd19129 28 ALEAGFRHFDCAERYR-NEAEVgeAMQEVFKAGKIRREDLFVTTKL-WNTNHRPER------VKPAFEASLKRLQLDYLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 87 VV-----FANRP---------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICE 146
Cdd:cd19129 100 LYlihtpFAFQPgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRCKAIGLSDVSLEKLREIFEAAR----IKPAVV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 147 QAEYHMFQRekvEVQLPELFHKIGVGAMTWSPLACGIVSGKydsgippysraslkgyqwLKDKILSeegrrqqaklkelq 226
Cdd:cd19129 176 QVESHPYLP---EWELLDFCKNHGIVLQAFAPLGHGMEPKL------------------LEDPVIT-------------- 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 315434251 227 AIAERLGCTLPQLAIAWCLRNEGvsSVLLGASNADQLMENIGaIQVLPKLSSSIIHEI 284
Cdd:cd19129 221 AIARRVNKTPAQVLLAWAIQRGT--ALLTTSKTPSRIRENFD-ISTLPEDAMREINEG 275
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
17-267 |
1.17e-07 |
|
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 (NADP-dependent D-sorbitol-6-phosphate dehydrogenase or NADP-S6PDH) from Malus domestica, and AKR2A2 (NADPH-dependent mannose-6-phosphate reductase or NADPH-M6PR) from Apium graveolens. NADP-S6PDH (EC 1.1.1.200), also called aldose-6-phosphate reductase [NADPH], synthesizes sorbitol-6-phosphate, a key intermediate in the synthesis of sorbitol which is a major photosynthetic product in many members of the Rosaceae family. NADPH-M6PR (EC 1.1.1.224), also called NADPH-dependent M6P reductase, is a key enzyme involved in mannitol biosynthesis.
Pssm-ID: 381338 [Multi-domain] Cd Length: 308 Bit Score: 52.10 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 17 FDTAEVYAaGKAEV--VLGNIIKKKGWRRSSLVITTKIfWggkaETERGlsrkHIIEGLKASLERLQLEYVDVVFANRP- 93
Cdd:cd19112 41 FDCAADYK-NEKEVgeALAEAFKTGLVKREDLFITTKL-W----NSDHG----HVIEACKDSLKKLQLDYLDLYLVHFPv 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 94 ----------------------DPNTPMEETVRAMTHVINQGMAMYWGTSRWSS--MEIMEAYSVARqfnltpPICEQAE 149
Cdd:cd19112 111 atkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVRSIGISNYDIflTRDCLAYSKIK------PAVNQIE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 150 YH-MFQREKVeVQLPeLFHKIGVGAMTwsPLACGIVSGKYDSGIPPysraslkgyqwLKDKILSEegrrqqaklkelqaI 228
Cdd:cd19112 185 THpYFQRDSL-VKFC-QKHGISVTAHT--PLGGAAANAEWFGSVSP-----------LDDPVLKD--------------L 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 315434251 229 AERLGCTLPQLAIAWCL-RNegvSSVLLGASNADQLMENI 267
Cdd:cd19112 236 AKKYGKSAAQIVLRWGIqRN---TAVIPKSSKPERLKENI 272
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-243 |
4.03e-07 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 50.46 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAaGKAEVvlGNIIKK-----KGWRRSSLVITTKIfWGGKAETErglsrkHIIEGLKASLERLQLE 83
Cdd:cd19106 29 ALDAGYRHIDCAAVYG-NEQEV--GEALKEkvgpgKAVPREDLFVTSKL-WNTKHHPE------DVEPALRKTLKDLQLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 84 YVDV--------------VFANRPDPN-----TPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPI 144
Cdd:cd19106 99 YLDLylihwpyafergdnPFPKNPDGTirydsTHYKETWKAMEKLVDKGLVKAIGLSNFNSRQIDDILSVAR----IKPA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 145 CEQAEYHMFQrekVEVQLPELFHKIGVGAMTWSPLacgivsgkydsGIPpySRAslkgyqWLK--DKILSEEGRrqqakl 222
Cdd:cd19106 175 VLQVECHPYL---AQNELIAHCKARGLVVTAYSPL-----------GSP--DRP------WAKpdEPVLLEEPK------ 226
|
250 260
....*....|....*....|.
gi 315434251 223 keLQAIAERLGCTLPQLAIAW 243
Cdd:cd19106 227 --VKALAKKYNKSPAQILLRW 245
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
2-247 |
4.57e-07 |
|
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: 50.21 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaagKAEVVLGNIIKKKGWRRSSLVITTKIfWGGKAETERGLSrkhiieGLKASLERLQ 81
Cdd:cd19156 25 AENAVKWAIEAGYRHIDTAAIY---KNEEGVGQGIRESGVPREEVFVTTKL-WNSDQGYESTLA------AFEESLEKLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 82 LEYVDVVFANRPDPNTpMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARqfnlTPPICEQAEYH-MFQREKVEV 160
Cdd:cd19156 95 LDYVDLYLIHWPVKGK-FKDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKSCK----VAPMVNQIELHpLLTQEPLRK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 161 QLPElfHKIGVGAmtWSPLACGivsgkydsgippysraslkgyqwlkdKILSEEgrrqqaklkELQAIAERLGCTLPQLA 240
Cdd:cd19156 170 FCKE--KNIAVEA--WSPLGQG--------------------------KLLSNP---------VLKAIGKKYGKSAAQVI 210
|
....*..
gi 315434251 241 IAWCLRN 247
Cdd:cd19156 211 IRWDIQH 217
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-272 |
7.36e-07 |
|
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: 49.65 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 2 AEQLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIKKKGWRRSSLVITTKifWG----------GKAETERGLSRKHIIE 71
Cdd:cd19098 37 THAVLDAAWAAGVRYFDAARSY--GRAEEFLGSWLRSRNIAPDAVFVGSK--WGytytadwqvdAAVHEVKDHSLARLLK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 72 GLKASLERLQlEYVDV-----------VFANrpdpntpmEETVRAMTHVINQGMAMYWGTSRWSSMEIMEA-----YSVA 135
Cdd:cd19098 113 QWEETRSLLG-KHLDLyqihsatlesgVLED--------ADVLAALAELKAEGVKIGLSLSGPQQAETLRRaleieIDGA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 136 RQFNltppiCEQAEYHMFQREKVEvQLpELFHKIGVGAMTWSPLACGIVSGKYDSGippysraslkgyqwlkdkilseeg 215
Cdd:cd19098 184 RLFD-----SVQATWNLLEQSAGE-AL-EEAHEAGMGVIVKEALANGRLTDRNPSP------------------------ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 315434251 216 rRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNADQLMENIGAIQV 272
Cdd:cd19098 233 -ELAPLMAVLKAVADRLGVTPDALALAAVLAQPFVDVVLSGAATPEQLRSNLRALDV 288
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
9-287 |
1.00e-06 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 49.20 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 9 AYDNGINLFDTAEVYAAGkaevVLGNIIkkkgwR------RSSLVITTKIfwgGKAETERG-----LSRKHIIEGLKASL 77
Cdd:PRK10376 49 AVALGVNHIDTSDFYGPH----VTNQLI-----RealhpyPDDLTIVTKV---GARRGEDGswlpaFSPAELRRAVHDNL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 78 ERLQLEYVDVV------FANRPDPNtPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVArqfnltPPICEQAEYH 151
Cdd:PRK10376 117 RNLGLDVLDVVnlrlmgDGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLSNVTPTQVAEARKIA------EIVCVQNHYN 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 152 MFQREkvEVQLPELFHKIGVGAMTWSPLAcgivsgkydsgippysraslkGYQWLKDKILSeegrrqqaklkelqAIAER 231
Cdd:PRK10376 190 LAHRA--DDALIDALARDGIAYVPFFPLG---------------------GFTPLQSSTLS--------------DVAAS 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 315434251 232 LGCTLPQLAIAWCLRNEgvSSVLL--GASNADQLMENIGAIQVlpKLSSSIIHEIDSI 287
Cdd:PRK10376 233 LGATPMQVALAWLLQRS--PNILLipGTSSVAHLRENLAAAEL--VLSEEVLAELDGI 286
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
3-126 |
1.53e-05 |
|
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).
Pssm-ID: 381345 [Multi-domain] Cd Length: 294 Bit Score: 45.57 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 3 EQLMTLAYDNGINLFDTAEVYAA----GKAevvLGNIIKKKGWRRSSLVITTKI---FWggkaeterglsrKHIIEGLKA 75
Cdd:cd19119 30 KEAVEAAIKEGYRHIDTAYAYETedfvGEA---IKRAIDDGSIKREELFITTKVwptFY------------DEVERSLDE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 315434251 76 SLERLQLEYVDVVFANRPDP-NTPMEETVRAMTHVINQGMAMYWGTSRWSSM 126
Cdd:cd19119 95 SLKALGLDYVDLLLVHWPVCfEKDSDDSGKPFTPVNDDGKTRYAASGDHITT 146
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
18-287 |
2.31e-05 |
|
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are founding members of aldo-keto reductase family 3 member A1 (AKR3A1) and A2 (AKR3A2), respectively. Gcy1p, also called galactose-inducible crystallin-like protein 1, is a glycerol dehydrogenase involved in glycerol catabolism under microaerobic conditions. It has mRNA binding activity. Ypr1p acts as a 2-methylbutyraldehyde reductase that displays high specific activity towards 2-methylbutyraldehyde, as well as other aldehydes such as hexanal.
Pssm-ID: 381343 [Multi-domain] Cd Length: 284 Bit Score: 45.18 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 18 DTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGgkaeTERglsrKHIIEGLKASLERLQLEYVDVVFANRPDPNT 97
Cdd:cd19117 45 DTAAIY--GNEEEV-GQGIKDSGVPREEIFITTKL-WC----TWH----RRVEEALDQSLKKLGLDYVDLYLMHWPVPLD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 98 P---------------------MEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAysVARQFNLTPPICEQAEYHMFQRE 156
Cdd:cd19117 113 PdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKL--LASPSAKIVPAVNQIELHPLLPQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 157 KvevQLPELFHKIGVGAMTWSPLAcgivsgkyDSGIPPYsraslkgyqwlkdkilseegrrqqaKLKELQAIAERLGCTL 236
Cdd:cd19117 191 P---KLVDFCKSKGIHATAYSPLG--------STNAPLL-------------------------KEPVIIKIAKKHGKTP 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 315434251 237 PQLAIAWCLRnEGVsSVLLGASNADQLMENIGAIQvlpkLSSSIIHEIDSI 287
Cdd:cd19117 235 AQVIISWGLQ-RGY-SVLPKSVTPSRIESNFKLFT----LSDEEFKEIDEL 279
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
3-267 |
4.63e-04 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 41.00 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 3 EQLMTLAYDNGINLFDTAEVYAAgkaEVVLGNIIKK---KGW-RRSSLVITTKIfWGGKAeterglSRKHIIEGLKASLE 78
Cdd:cd19114 20 EEVIYNAIKVGYRLIDGALLYGN---EAEVGRGIRKaiqEGLvKREDLFIVTKL-WNNFH------GKDHVREAFDRQLK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 79 RLQLEYVDVVFANRPDP-------------------------NTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYS 133
Cdd:cd19114 90 DYGLDYIDLYLIHFPIPaayvdpaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 134 VARqfnlTPPICEQAEYHMF-QREKVevqlpelfhkigvgaMTWSPlacgivsgKYDSGIPPYSRASLKGYQwlkdkILS 212
Cdd:cd19114 170 YAK----IKPAVLQIEHHPYlQQKRL---------------IDWAK--------KQGIQITAYSSFGNAVYT-----KVT 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 315434251 213 EEGRRQQAKLKE--LQAIAERLGCTLPQLAIAWCLRNEGVssVLLGASNADQLMENI 267
Cdd:cd19114 218 KHLKHFTNLLEHpvVKKLADKHKRDTGQVLLRWAVQRNIT--VIPKSVNVERMKTNL 272
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
3-182 |
1.73e-03 |
|
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; Corynebacterium sp. DkgA is a founding member of aldo-keto reductase family 5 member C1 (AKR5C1). DkgA (EC 1.1.1.346), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). 5-keto-D-fructose and dihydroxyacetone can also serve as substrates.
Pssm-ID: 381356 [Multi-domain] Cd Length: 256 Bit Score: 39.12 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 3 EQLMTLAYDNGINLFDTAEVYaaGKAEVVlGNIIKKKGWRRSSLVITTKIfWGGKAETERGLSrkhiieGLKASLERLQL 82
Cdd:cd19130 26 QRAVATALEVGYRHIDTAAIY--GNEEGV-GAAIAASGIPRDELFVTTKL-WNDRHDGDEPAA------AFAESLAKLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315434251 83 EYVDVVFANRPDPNTPME-ETVRAMTHVINQGMAMYWGTSRW--SSMEIMEAYSVarqfnlTPPICEQAEYHMF--QREK 157
Cdd:cd19130 96 DQVDLYLVHWPTPAAGNYvHTWEAMIELRAAGRTRSIGVSNFlpPHLERIVAATG------VVPAVNQIELHPAyqQRTI 169
|
170 180
....*....|....*....|....*
gi 315434251 158 VEVQlpelfHKIGVGAMTWSPLACG 182
Cdd:cd19130 170 RDWA-----QAHDVKIEAWSPLGQG 189
|
|
| |
