|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
31-342 |
0e+00 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 609.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVAT 110
Cdd:PLN02587 2 RELGSTGLKVSSVGFGASPLGSVFGPVSEEDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALGIPREKYVVST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KCGRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLEVYTY 190
Cdd:PLN02587 82 KCGRYGEGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKLKESGKVRFIGITGLPLAIFTY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 191 VLDRVPPGTIDVVLSYCHYCINDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGPPEWHPASPEIKAACKAAADYCKKN 270
Cdd:PLN02587 162 VLDRVPPGTVDVILSYCHYSLNDSSLEDLLPYLKSKGVGVISASPLAMGLLTENGPPEWHPAPPELKSACAAAATHCKEK 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7SMI_A 271 GKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELETAGKDEKTFAEIENILKPIKNQSWPSGIQQ 342
Cdd:PLN02587 242 GKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELETSGIDEELLSEVEAILAPVKNKTWPSGIQE 313
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
28-318 |
0e+00 |
|
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: 505.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKalGASRDEYI 107
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGPVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALK--GIPRDSYY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKCGRY----AEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFG-SLDQIVNETIPALQKIKESGKTRFIGITG 182
Cdd:cd19163 79 LATKVGRYgldpDKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFApSLDQILNETLPALQKLKEEGKVRFIGITG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 183 LPLEVYTYVLDRVPpGTIDVVLSYCHYCINDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGPPEWHPASPEIKAACKA 262
Cdd:cd19163 159 YPLDVLKEVLERSP-VKIDTVLSYCHYTLNDTSLLELLPFFKEKGVGVINASPLSMGLLTERGPPDWHPASPEIKEACAK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 263 AADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELETAGKDE 318
Cdd:cd19163 238 AAAYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAEEPLDAHLLA 293
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
29-317 |
6.08e-136 |
|
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: 388.05 E-value: 6.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 29 ERRELGNTGLNLSCVGFGASPLGNVFGD-VSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYI 107
Cdd:cd19153 1 FGETLEIALGNVSPVGLGTAALGGVYGDgLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALQVPRSSYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKCGRY-AEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLE 186
Cdd:cd19153 81 VATKVGRYrDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTLKDEGVIKRIGIAGYPLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 187 VYTYVLDRVPPGTIDVVLSYCHYCINDSTLEDMLPYFKS-KGVGVINASPLSMGLHTENGPPEWHPASPEIKAACKAAAD 265
Cdd:cd19153 161 TLTRATRRCSPGSLDAVLSYCHLTLQDARLESDAPGLVRgAGPHVINASPLSMGLLTSQGPPPWHPASGELRHYAAAADA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7SMI_A 266 YCKKNGKNISKLALQYSLSNKD-ISTTLVGMNSVKQVEENVGAALELETAGKD 317
Cdd:cd19153 241 VCASVEASLPDLALQYSLAAHAgVGTVLLGPSSLAQLRSMLAAVDAVASLGAA 293
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
43-308 |
1.92e-92 |
|
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: 277.13 E-value: 1.92e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGatLSEKVLGKCLKALGasRDEYIVATKCGRYAEGF-DF 121
Cdd:cd19090 3 LGLGTAGLGGVFGGVDDDEAVATIRAALDLGINYIDTAPAYG--DSEERLGLALAELP--REPLVLSTKVGRLPEDTaDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 122 SAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIV--NETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRvppGT 199
Cdd:cd19090 79 SADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapGGALEALLELKEEGLIKHIGLGGGPPDLLRRAIET---GD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 200 IDVVLSYCHY-CINDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGP----PEWHPASPEIKAACKAAADYCKKNGKNI 274
Cdd:cd19090 156 FDVVLTANRYtLLDQSAADELLPAAARHGVGVINASPLGMGLLAGRPPervrYTYRWLSPELLDRAKRLYELCDEHGVPL 235
|
250 260 270
....*....|....*....|....*....|....
7SMI_A 275 SKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19090 236 PALALRFLLRDPRISTVLVGASSPEELEQNVAAA 269
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
45-318 |
7.45e-87 |
|
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: 263.37 E-value: 7.45e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 45 FGASPLG-NVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALGAS--RDEYIVATKCGRYA-EGFD 120
Cdd:cd19164 18 FGAATFSyQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGP--SEIILGRALKALRDEfpRDTYFIITKVGRYGpDDFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 121 FSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVnETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRV--PPG 198
Cdd:cd19164 96 YSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVL-EALKELFKLKDEGKIRNVGISGYPLPVLLRLAELArtTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 199 -TIDVVLSYCHYCINDSTLEDMLPYFK-SKGVGVI-NASPLSMGLHTENGPPEWHPASPEIKAACKAAADYCKKNGKNIS 275
Cdd:cd19164 175 rPLDAVLSYCHYTLQNTTLLAYIPKFLaAAGVKVVlNASPLSMGLLRSQGPPEWHPASPELRAAAAKAAEYCQAKGTDLA 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....
7SMI_A 276 KLALQYSLSNKD-ISTTLVGMNSVKQVEENVGAALELETAGKDE 318
Cdd:cd19164 255 DVALRYALREWGgEGPTVVGCSNVDELEEAVEAYWSVLAGASEE 298
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
29-333 |
3.35e-74 |
|
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: 231.61 E-value: 3.35e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 29 ERRELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIV 108
Cdd:COG0667 2 EYRRLGRSGLKVSRLGLGTMTFGGPWGGVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGR--PRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCGRY----AEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFgslDQIVNETIPALQKIKESGKTRFIGITGLP 184
Cdd:COG0667 80 ATKVGRRmgpgPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDP---DTPIEETLGALDELVREGKIRYIGVSNYS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 LEVYTYVLdRVPPGTIDVVLSYCHYCI-NDSTLEDMLPYFKSKGVGVINASPLSMGLHT-----ENGPPE-------WHP 251
Cdd:COG0667 157 AEQLRRAL-AIAEGLPPIVAVQNEYSLlDRSAEEELLPAARELGVGVLAYSPLAGGLLTgkyrrGATFPEgdraatnFVQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 252 --ASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIENIL 328
Cdd:COG0667 236 gyLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAAdLEL-----SAEDLAALDAAL 310
|
....*
7SMI_A 329 KPIKN 333
Cdd:COG0667 311 AAVPA 315
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
38-307 |
4.40e-63 |
|
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: 200.40 E-value: 4.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 38 LNLSCVGFGASPLGN-VFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVATKCGRYA 116
Cdd:cd19086 1 LEVSEIGFGTWGLGGdWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLG---KALKGRRDKVVIATKFGNRF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 117 EGF-----DFSAERVTKSIDESLERLQLEYVDILQCH--DIEFGSLDqivnETIPALQKIKESGKTRFIGITGLPLEVYT 189
Cdd:cd19086 78 DGGperpqDFSPEYIREAVEASLKRLGTDYIDLYQLHnpPDEVLDND----ELFEALEKLKQEGKIRAYGVSVGDPEEAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 190 YVLDRVPPGTIDVVLSYchycINDSTLEDMLPYFKSKGVGVINASPLSMGLHTengppewhpaspeikaackaaadyckk 269
Cdd:cd19086 154 AALRRGGIDVVQVIYNL----LDQRPEEELFPLAEEHGVGVIARVPLASGLLT--------------------------- 202
|
250 260 270
....*....|....*....|....*....|....*...
7SMI_A 270 nGKnISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:cd19086 203 -GK-LAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
43-328 |
3.22e-62 |
|
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: 200.23 E-value: 3.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVATKCGRYAEG--FD 120
Cdd:pfam00248 1 IGLGTWQLGGGWGPISKEEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYPVKRDKVVIATKVPDGDGPwpSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 121 FSAERVTKSIDESLERLQLEYVDILQCHDIEFgSLDQIvnETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRvppGTI 200
Cdd:pfam00248 81 GSKENIRKSLEESLKRLGTDYIDLYYLHWPDP-DTPIE--ETWDALEELKKEGKIRAIGVSNFDAEQIEKALTK---GKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 201 DVVLSYCHYCI-NDSTLEDMLPYFKSKGVGVINASPLSMGLHTEN-------GPPEWHPASPEIKA----ACKAAADYCK 268
Cdd:pfam00248 155 PIVAVQVEYNLlRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKytrdpdkGPGERRRLLKKGTPlnleALEALEEIAK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
7SMI_A 269 KNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA-ALELetagkDEKTFAEIENIL 328
Cdd:pfam00248 235 EHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGAlEFPL-----SDEEVARIDELL 290
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
41-307 |
1.98e-60 |
|
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: 194.38 E-value: 1.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 41 SCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALgaSRDEYIVATKCGRYAEG-- 118
Cdd:cd19095 1 SVLGLGTSGIGRVWGVPSEAEAARLLNTALDLGINLIDTAPAYGR--SEERLGRALAGL--RRDDLFIATKVGTHGEGgr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 119 --FDFSAERVTKSIDESLERLQLEYVDILQCHdieFGSLDQIVNETIPALQKIKESGKTRFIGITGlplevYTYVLDR-V 195
Cdd:cd19095 77 drKDFSPAAIRASIERSLRRLGTDYIDLLQLH---GPSDDELTGEVLETLEDLKAAGKVRYIGVSG-----DGEELEAaI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 196 PPGTIDVVLsyCHYCINDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGPPEwhPASPEIKAACKAAADYckkNGKNIS 275
Cdd:cd19095 149 ASGVFDVVQ--LPYNVLDREEEELLPLAAEAGLGVIVNRPLANGRLRRRVRRR--PLYADYARRPEFAAEI---GGATWA 221
|
250 260 270
....*....|....*....|....*....|..
7SMI_A 276 KLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:cd19095 222 QAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
37-325 |
2.11e-59 |
|
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called general stress protein 69 (GSP69), is a founding member of aldo-keto reductase family 11 member B1 (AKR11B1). It acts as an aldo-keto reductase (AKR) that catalyzes the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor. Escherichia coli YdjG is a founding member of aldo-keto reductase family 11 member B2 (AKR11B2). It catalyzes the NADH-dependent reduction of methylglyoxal (2-oxopropanal) in vitro. It may play some role in intestinal colonization.
Pssm-ID: 381310 [Multi-domain] Cd Length: 296 Bit Score: 193.13 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGNVF-GDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVATKCGRY 115
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWwGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILG---KALKGRRDDVVIATKCGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 116 AEGF-----DFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRFIGITGLP 184
Cdd:cd19084 78 WDGGkgvtkDLSPESIRKEVEQSLRRLQTDYIDLYQIHwpdpntPIE---------ETAEALEKLKKEGKIRYIGVSNFS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 LEVYTYVLDRVPpgtIDVVLsyCHY-CINDSTLEDMLPYFKSKGVGVINASPLSMGLHT---ENGP-----------PEW 249
Cdd:cd19084 149 VEQLEEARKYGP---IVSLQ--PPYsMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTgkyKKEPtfppddrrsrfPFF 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7SMI_A 250 H-PASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELEtagkdEKTFAEIE 325
Cdd:cd19084 224 RgENFEKNLEIVDKLKEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALdWELT-----EEELKEID 296
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
30-305 |
9.80e-57 |
|
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: 184.22 E-value: 9.80e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 30 RRELGNTGLNLSCVGFGASPLGNVfgdvSEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGkclKALGASRDEYIVA 109
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRL----SQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIG---KALKGRRDKVFLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKCGryaegfDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGS-LDQIV--NETIPALQKIKESGKTRFIGITGLPLE 186
Cdd:cd19100 72 TKTG------ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEdLDQVFgpGGALEALLEAKEEGKIRFIGISGHSPE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 187 VYTYVLDRvppGTIDVVL---SYCHYCInDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGPPEWhpaspeikaackaa 263
Cdd:cd19100 146 VLLRALET---GEFDVVLfpiNPAGDHI-DSFREELLPLAREKGVGVIAMKVLAGGRLLSGDPLDP-------------- 207
|
250 260 270 280
....*....|....*....|....*....|....*....|..
7SMI_A 264 adyckkngknisKLALQYSLSNKDISTTLVGMNSVKQVEENV 305
Cdd:cd19100 208 ------------EQALRYALSLPPVDVVIVGMDSPEELDENL 237
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
28-308 |
1.58e-55 |
|
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: 181.63 E-value: 1.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASPLGnvfgdvseEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKalGASRDEYI 107
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLP--------RESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALK--GLRRDKVF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKCgrYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVNETIPALQKIKESGKTRFIGIT--GLPL 185
Cdd:cd19105 71 LATKA--SPRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEKLKKEGKVRFIGFSthDNMA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 186 EVYTYVLDrvpPGTIDVVL-SYCHycINDS-TLEDMLPYFKSKGVGVINASPLSMGLhtengppeWHPASPEIKaackaa 263
Cdd:cd19105 149 EVLQAAIE---SGWFDVIMvAYNF--LNQPaELEEALAAAAEKGIGVVAMKTLAGGY--------LQPALLSVL------ 209
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
7SMI_A 264 adycKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19105 210 ----KAKGFSLPQAALKWVLSNPRVDTVVPGMRNFAELEENLAAA 250
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
43-308 |
2.58e-54 |
|
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: 179.86 E-value: 2.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLGNVFgDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIVATKCGRYAEG---- 118
Cdd:cd19162 3 LGLGAASLGNLA-RAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALARH--PRAEYVVSTKVGRLLEPgaag 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 119 --------FDFSAERVTKSIDESLERLQLEYVDILQCHDIEfGSLDQIVNETIPALQKIKESGKTRFIGITGLPLEVYTY 190
Cdd:cd19162 80 rpagadrrFDFSADGIRRSIEASLERLGLDRLDLVFLHDPD-RHLLQALTDAFPALEELRAEGVVGAIGVGVTDWAALLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 191 VLDRvppGTIDVVLSYCHYCI-NDSTLEDMLPYFKSKGVGVINASPLSMGL----HTENGPPEWHPASPEIKAACKAAAD 265
Cdd:cd19162 159 AARR---ADVDVVMVAGRYTLlDRRAATELLPLCAAKGVAVVAAGVFNSGIlatdDPAGDRYDYRPATPEVLARARRLAA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|...
7SMI_A 266 YCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19162 236 VCRRYGVPLPAAALQFPLRHPAVASVVVGAASPAELRDNLALL 278
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
31-308 |
3.85e-54 |
|
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: 180.15 E-value: 3.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVAT 110
Cdd:cd19104 3 RRFGRTGLKVSELTFGGGGIGGLMGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLG---RALKGLPAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KCGRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHD----------IEFGSLDQI--VNETIPALQKIKESGKTRFI 178
Cdd:cd19104 80 KVRLDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNrigderdkpvGGTLSTTDVlgLGGVADAFERLRSEGKIRFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 179 GITGLPLEVYTY-VLDRVPPGTIDVVLSYchycINDSTLEDMLPYF------------KSKGVGVINASPLSMGLHTENG 245
Cdd:cd19104 160 GITGLGNPPAIReLLDSGKFDAVQVYYNL----LNPSAAEARPRGWsaqdyggiidaaAEHGVGVMGIRVLAAGALTTSL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 246 -------PPEWHPASPEIKAAcKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19104 236 drgreapPTSDSDVAIDFRRA-AAFRALAREWGETLAQLAHRFALSNPGVSTVLVGVKNREELEEAVAAE 304
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
29-329 |
1.20e-53 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 180.02 E-value: 1.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 29 ERRELGNTGLNLSCVGFGASPLGNVfgdvSEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALgasRDEYIV 108
Cdd:COG1453 2 QYRRLGKTGLEVSVLGFGGMRLPRK----DEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKGP---RDKVIL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCGRYAEgfdfSAERVTKSIDESLERLQLEYVDILQCHDI-EFGSLDQIV--NETIPALQKIKESGKTRFIGIT--Gl 183
Cdd:COG1453 73 ATKLPPWVR----DPEDMRKDLEESLKRLQTDYIDLYLIHGLnTEEDLEKVLkpGGALEALEKAKAEGKIRHIGFSthG- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 184 PLEVYTYVLDRvppGTIDVVLsyCHYCI---NDSTLEDMLPYFKSKGVGVINASPLSMG-LHTengPPEwhpaspeikaa 259
Cdd:COG1453 148 SLEVIKEAIDT---GDFDFVQ--LQYNYldqDNQAGEEALEAAAEKGIGVIIMKPLKGGrLAN---PPE----------- 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7SMI_A 260 cKAAADYCKKngKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELETAGKDEK-TFAEIENILK 329
Cdd:COG1453 209 -KLVELLCPP--LSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADNLEPLTEEELaILERLAEELG 276
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
43-308 |
5.58e-50 |
|
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: 168.94 E-value: 5.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGasRDEYIVATKCGRY----AEG 118
Cdd:cd19152 3 LGFGTAPLGNLYEAVSDEEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELG--REDYVISTKVGRLlvplQEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 119 -----------------FDFSAERVTKSIDESLERLQLEYVDILQCHDIE--------FGSLDQIVNETIPALQKIKESG 173
Cdd:cd19152 81 eptfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDedlagaesDEHFAQAIKGAFRALEELREEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 174 KTRFIGITGLPLEVYTYVLDRVPPgtiDVVLSYCHYCIND-STLEDMLPYFKSKGVGVINASPLSMGLHTenGPP----- 247
Cdd:cd19152 161 VIKAIGLGVNDWEVILRILEEADL---DWVMLAGRYTLLDhSAARELLPECEKRGVKVVNAGPFNSGFLA--GGDnfdyy 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
7SMI_A 248 EWHPASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19152 236 EYGPAPPELIARRDRIEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
31-314 |
2.63e-47 |
|
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: 162.06 E-value: 2.63e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPLGN--VFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgasRDEYIV 108
Cdd:cd19149 2 RKLGKSGIEASVIGLGTWAIGGgpWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGR---RDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCG----RYAEGFDF-----------SAERVTKSIDESLERLQLEYVDILQCH--DIEFGsldqiVNETIPALQKIKE 171
Cdd:cd19149 79 ATKCGlrwdREGGSFFFvrdgvtvyknlSPESIREEVEQSLKRLGTDYIDLYQTHwqDVETP-----IEETMEALEELKR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 172 SGKTRFIGITGL-PLEVYTYVldRVppGTIDVVLSycHYCINDSTLE-DMLPYFKSKGVGVINASPLSMGLHTENGPPE- 248
Cdd:cd19149 154 QGKIRAIGASNVsVEQIKEYV--KA--GQLDIIQE--KYSMLDRGIEkELLPYCKKNNIAFQAYSPLEQGLLTGKITPDr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 249 ---------WHP-ASPE----IKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELET 313
Cdd:cd19149 228 efdagdarsGIPwFSPEnrekVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGdIRLSA 307
|
.
7SMI_A 314 A 314
Cdd:cd19149 308 E 308
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
40-331 |
3.49e-47 |
|
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: 161.22 E-value: 3.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 40 LSCVGFGASPLG--NVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVATKCGryae 117
Cdd:cd19085 1 VSRLGLGCWQFGggYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLG---KALKGRRDDVVIATKVS---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 118 GFDFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRFIGITGLPLEVYTYV 191
Cdd:cd19085 74 PDNLTPEDVRKSCERSLKRLGTDYIDLYQIHwpssdvPLE---------ETMEALEKLKEEGKIRAIGVSNFGPAQLEEA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 192 LDRvppGTIDVV-LSYchycindSTL-----EDMLPYFKSKGVGVINASPLSMGLHT------ENGPPEWH--------- 250
Cdd:cd19085 145 LDA---GRIDSNqLPY-------NLLwraieYEILPFCREHGIGVLAYSPLAQGLLTgkfssaEDFPPGDArtrlfrhfe 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 251 -PASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIENIL 328
Cdd:cd19085 215 pGAEEETFEALEKLKEIADELGVTMAQLALAWVLQQPGVTSVIVGARNPEQLEENAAAVdLEL-----SPSVLERLDEIS 289
|
...
7SMI_A 329 KPI 331
Cdd:cd19085 290 DPL 292
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
41-306 |
7.12e-44 |
|
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: 150.75 E-value: 7.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 41 SCVGFGASPLGnvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGAsRDEYIVATKCG----RYA 116
Cdd:cd06660 1 SRLGLGTMTFG---GDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKGRGN-RDDVVIATKGGhppgGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 117 EGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFgslDQIVNETIPALQKIKESGKTRFIGITGLPLE------VYTY 190
Cdd:cd06660 77 SRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHRDDP---STPVEETLEALNELVREGKIRYIGVSNWSAErlaealAYAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 191 VLDRVPPGTIDVVLSYCHyciNDSTLEDMLPYFKSKGVGVINASPLSMGLHTengppewhpaspeikaackaaadyckkn 270
Cdd:cd06660 154 AHGLPGFAAVQPQYSLLD---RSPMEEELLDWAEENGLPLLAYSPLARGPAQ---------------------------- 202
|
250 260 270
....*....|....*....|....*....|....*.
7SMI_A 271 gkniskLALQYSLSNKDISTTLVGMNSVKQVEENVG 306
Cdd:cd06660 203 ------LALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
37-308 |
1.54e-43 |
|
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: 151.98 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPlgNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIVATKC---- 112
Cdd:cd19074 1 GLKVSELSLGTWL--TFGGQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGW--PRESYVISTKVfwpt 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 113 --GRYAEGfdFSAERVTKSIDESLERLQLEYVDILQCH--DIefgslDQIVNETIPALQKIKESGKTRFIGITGLPLEVY 188
Cdd:cd19074 77 gpGPNDRG--LSRKHIFESIHASLKRLQLDYVDIYYCHryDP-----ETPLEETVRAMDDLIRQGKILYWGTSEWSAEQI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 189 TYVLD------RVPPGTIDVVLSYchycINDSTLEDMLPYFKSKGVGVINASPLSMGLHT---ENGPPEwhPAS------ 253
Cdd:cd19074 150 AEAHDlarqfgLIPPVVEQPQYNM----LWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTgkyRDGIPP--PSRsratde 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 254 -----------PEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19074 224 dnrdkkrrlltDENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKAS 289
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
41-308 |
1.11e-42 |
|
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: 150.17 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 41 SCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGasRDEYIVATKCGR------ 114
Cdd:cd19161 1 SELGLGTAGLGNLYTAVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKP--RDEFVLSTKVGRllkpar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 ---------------YAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDI---------EFGSLDQIVNETIPALQKIK 170
Cdd:cd19161 79 egsvpdpngfvdplpFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIgvythgdrkERHHFAQLMSGGFKALEELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 171 ESGKTRFIGITGLPLEVYTYVLDRVPpgtIDVVLSYCHYCIND-STLEDMLPYFKSKGVGVINASPLSMGLHTENGPPEW 249
Cdd:cd19161 159 KAGVIKAFGLGVNEVQICLEALDEAD---LDCFLLAGRYSLLDqSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGA 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
7SMI_A 250 H----PASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19161 236 KfnygDAPAEIISRVMEIEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAF 298
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
41-308 |
5.13e-41 |
|
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: 143.86 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 41 SCVGFGAS--PLGNVfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIVATKCgryAEG 118
Cdd:cd19096 1 SVLGFGTMrlPESDD-DSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEG--PREKFYLATKL---PPW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 119 FDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVNE--TIPALQKIKESGKTRFIGITG-LPLEVYTYVLDRv 195
Cdd:cd19096 75 SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNSPEWLEKARKggLLEFLEKAKKEGLIRHIGFSFhDSPELLKEILDS- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 196 ppGTIDVVLsyCHYCINDSTLEDMLP---YFKSKGVGVINASPLSMGLHTENgPPEwhpaspeikaackaAADYCKKNGK 272
Cdd:cd19096 154 --YDFDFVQ--LQYNYLDQENQAGRPgieYAAKKGMGVIIMEPLKGGGLANN-PPE--------------ALAILCGAPL 214
|
250 260 270
....*....|....*....|....*....|....*.
7SMI_A 273 NISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19096 215 SPAEWALRFLLSHPEVTTVLSGMSTPEQLDENIAAA 250
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
31-318 |
1.18e-39 |
|
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: 142.01 E-value: 1.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGaspLGNVFGDVSEEQSIATVIE-AFNQGINFFDTSPYYGAT--LSEKVLGKCLK-ALGASRDEY 106
Cdd:cd19089 2 RRCGRSGLHLPAISLG---LWHNFGDYTSPEEARELLRtAFDLGITHFDLANNYGPPpgSAEENFGRILKrDLRPYRDEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKCGR------YAEGFdfSAERVTKSIDESLERLQLEYVDILQCH--DIefgslDQIVNETIPALQKIKESGKTRFI 178
Cdd:cd19089 79 VISTKAGYgmwpgpYGDGG--SRKYLLASLDQSLKRMGLDYVDIFYHHryDP-----DTPLEETMTALADAVRSGKALYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 179 GITGLPLEVYTYVLD-----RVPpgtidVVLSYCHYCINDSTLEDML-PYFKSKGVGVINASPLSMGLHTE---NGPPEW 249
Cdd:cd19089 152 GISNYPGAKARRAIAllrelGVP-----LIIHQPRYSLLDRWAEDGLlEVLEEAGIGFIAFSPLAQGLLTDkylNGIPPD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 250 HPA------------SPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVgAALELETAGKD 317
Cdd:cd19089 227 SRRaaeskflteealTPEKLEQLRKLNKIAAKRGQSLAQLALSWVLRDPRVTSVLIGASSPSQLEDNV-AALKNLDFSEE 305
|
.
7SMI_A 318 E 318
Cdd:cd19089 306 E 306
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
30-309 |
1.14e-38 |
|
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: 139.48 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 30 RRELGNTGLNLSCVGFGASPLG--NVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKalGASRDEYI 107
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGghNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLK--EYNRNEVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKCGRY----AEGFDFSAERVTKSIDESLERLQLEYVDILQCHdieFGSLDQIVNETIPALQKIKESGKTRFIGITGL 183
Cdd:cd19083 79 IATKGAHKfggdGSVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIH---FPDGETPKAEAVGALQELKDEGKIRAIGVSNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 184 PLEvytYVLDRVPPGTIDVVLSyCHYCINDSTLEDMLPYFKSKGVGVINASPLSMGL----HTEN---GPPEWHPASPEI 256
Cdd:cd19083 156 SLE---QLKEANKDGYVDVLQG-EYNLLQREAEEDILPYCVENNISFIPYFPLASGLlagkYTKDtkfPDNDLRNDKPLF 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
7SMI_A 257 KAA-----------CKAAADYCkknGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAAL 309
Cdd:cd19083 232 KGErfsenldkvdkLKSIADEK---GVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALD 292
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
33-312 |
5.36e-37 |
|
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: 135.02 E-value: 5.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 33 LGNTGLNLS-----CVGFGASPLGNVFgdVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgASRDEYI 107
Cdd:cd19079 5 LGNSGLKVSrlclgCMSFGDPKWRPWV--LDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEF-APRDEVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKC-GRYAEGFD---FSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRF 177
Cdd:cd19079 82 IATKVyFPMGDGPNgrgLSRKHIMAEVDASLKRLGTDYIDLYQIHrwdyetPIE---------ETLEALHDVVKSGKVRY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 178 IG---ITGLPLEVYTYVLDRvpPGTIDVVLSYCHY-CINDSTLEDMLPYFKSKGVGVINASPLSMGL--HTENGPPEWHP 251
Cdd:cd19079 153 IGassMYAWQFAKALHLAEK--NGWTKFVSMQNHYnLLYREEEREMIPLCEEEGIGVIPWSPLARGRlaRPWGDTTERRR 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 252 ASP---------------EIKAACKAAAdycKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVgAALELE 312
Cdd:cd19079 231 STTdtaklkydyfteadkEIVDRVEEVA---KERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAV-AALDIK 302
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
40-328 |
9.88e-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: 381328 [Multi-domain] Cd Length: 302 Bit Score: 128.94 E-value: 9.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 40 LSCVGFGASPLGN-----VFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgasRDEYIVATKCGR 114
Cdd:cd19102 1 LTTIGLGTWAIGGggwggGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGL---RDRPIVATKCGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YAEG-----FDFSAERVTKSIDESLERLQLEYVDILQCHdieFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLEVYT 189
Cdd:cd19102 78 LWDEegrirRSLKPASIRAECEASLRRLGVDVIDLYQIH---WPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 190 YVLdrvPPGTIDVV---LSYCHYCIndstLEDMLPYFKSKGVGVINASPLSMGLHTENGPPE---------WHPASPEIK 257
Cdd:cd19102 155 RCQ---AIHPIASLqppYSLLRRGI----EAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPErvaslpaddWRRRSPFFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 258 ----AACKAAADYCK----KNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIENIL 328
Cdd:cd19102 228 epnlARNLALVDALRpiaeRHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAAdLRL-----TPEELAEIEALL 302
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
31-327 |
1.06e-33 |
|
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: 126.15 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPLGnvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKalgASRDEYIVAT 110
Cdd:cd19087 4 RTLGRTGLKVSRLCLGTMNFG---GRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIA---GRRDDIVLAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KC-GRYAEGFD---FSAERVTKSIDESLERLQLEYVDILQCHDI-EFGSLDqivnETIPALQKIKESGKTRFIGITGLP- 184
Cdd:cd19087 78 KVfGPMGDDPNdrgLSRRHIRRAVEASLRRLQTDYIDLYQMHHFdRDTPLE----ETLRALDDLVRQGKIRYIGVSNFAa 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 ------LEV-YTYVLDRvppgtidVVLSYCHYCINDSTLE-DMLPYFKSKGVGVINASPLSMGL----HTENGPPEWH-- 250
Cdd:cd19087 154 wqiakaQGIaARRGLLR-------FVSEQPMYNLLKRQAElEILPAARAYGLGVIPYSPLAGGLltgkYGKGKRPESGrl 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 251 ---------PASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVgAALELETagkDEKTF 321
Cdd:cd19087 227 veraryqarYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSHPAVTSPIIGPRTLEQLEDSL-AALEITL---TPELL 302
|
....*.
7SMI_A 322 AEIENI 327
Cdd:cd19087 303 AEIDEL 308
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
28-308 |
2.66e-32 |
|
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: 122.72 E-value: 2.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASPLG--NVF----GDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGA 101
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGggGGFfgawGGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILG---KALKG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 102 SRDEYIVATKC-GRYAEGFD---FSAERVTKSIDESLERLQLEYVDILQCHDieFGSLDQIvNETIPALQKIKESGKTRF 177
Cdd:cd19091 78 RRDDVLIATKVrGRMGEGPNdvgLSRHHIIRAVEASLKRLGTDYIDLYQLHG--FDALTPL-EETLRALDDLVRQGKVRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 178 IGITGLP---LEVYTYVLDRVppGTIDVVLSYCHYCINDSTLE-DMLPYFKSKGVGVINASPLSMGLHT-----ENGPPE 248
Cdd:cd19091 155 IGVSNFSawqIMKALGISERR--GLARFVALQAYYSLLGRDLEhELMPLALDQGVGLLVWSPLAGGLLSgkyrrGQPAPE 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7SMI_A 249 ----------WHPASPE----IKAACKAAAdycKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19091 233 gsrlrrtgfdFPPVDRErgydVVDALREIA---KETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAA 303
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
55-308 |
3.37e-32 |
|
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: 121.09 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 55 GDVSEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALgasrDEYIVATKCGRYAEGFDFSAERVTKSIDESL 134
Cdd:cd19097 21 GKPSEKEAKKILEYALKAGINTLDTAPAYGD--SEKVLGKFLKRL----DKFKIITKLPPLKEDKKEDEAAIEASVEASL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 135 ERLQLEYVDILQCHDIEfgSLDQIVNETIPALQKIKESGKTRFIGITglpleVYT-----YVLDRvppGTIDVV---LSy 206
Cdd:cd19097 95 KRLKVDSLDGLLLHNPD--DLLKHGGKLVEALLELKKEGLIRKIGVS-----VYSpeeleKALES---FKIDIIqlpFN- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 207 chycINDSTL--EDMLPYFKSKGVGVINASPLSMGLHTENgPPEWHPASPEIKAACKAAADYCKKNGKNISKLALQYSLS 284
Cdd:cd19097 164 ----ILDQRFlkSGLLAKLKKKGIEIHARSVFLQGLLLME-PDKLPAKFAPAKPLLKKLHELAKKLGLSPLELALGFVLS 238
|
250 260
....*....|....*....|....
7SMI_A 285 NKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19097 239 LPEIDKIVVGVDSLEQLKEIIAAF 262
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
43-308 |
7.12e-32 |
|
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: 120.80 E-value: 7.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGA----SPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGAsRDEYIVATKcgrYAEG 118
Cdd:cd19093 5 LGLGTwqwgDRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKELGD-RDEVVIATK---FAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 119 F-DFSAERVTKSIDESLERLQLEYVDILQCHdiEFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRVPP 197
Cdd:cd19093 81 PwRLTRRSVVKALKASLERLGLDSIDLYQLH--WPGPWYSQIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAHKALKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 198 GTIDVVLSYCHYCINDSTLE--DMLPYFKSKGVGVINASPLSMGL-----HTENGPPE----------WHPASPEIKAAC 260
Cdd:cd19093 159 RGVPLASNQVEYSLLYRDPEqnGLLPACDELGITLIAYSPLAQGLltgkySPENPPPGgrrrlfgrknLEKVQPLLDALE 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
7SMI_A 261 KAAADYckknGKNISKLALQYSLSNKDISttLVGMNSVKQVEENVGAA 308
Cdd:cd19093 239 EIAEKY----GKTPAQVALNWLIAKGVVP--IPGAKNAEQAEENAGAL 280
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
29-308 |
1.15e-31 |
|
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: 120.78 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 29 ERRELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgasRDEYIV 108
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDR---RDEVVI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCG------RYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIefgslDQIV--NETIPALQKIKESGKTRFIGI 180
Cdd:cd19076 78 ATKFGivrdpgSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRV-----DPNVpiEETVGAMAELVEEGKVRYIGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 181 TglplEVYTYVLDR---VPPgtIDVVLSycHYCINDSTLED-MLPYFKSKGVGVINASPLSMGLHT-----ENGPPE--W 249
Cdd:cd19076 153 S----EASADTIRRahaVHP--ITAVQS--EYSLWTRDIEDeVLPTCRELGIGFVAYSPLGRGFLTgaiksPEDLPEddF 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 250 HPASP-----------EIKAACKAAAdycKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19076 225 RRNNPrfqgenfdknlKLVEKLEAIA---AEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGAL 291
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
32-314 |
1.23e-30 |
|
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: 118.09 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 32 ELGNTGLNLSCVGFGasplGNVFG-DVSEEQSIAtVIEAFNQ-GINFFDTSPYYGAT-------LSEKVLGKCLKALGAs 102
Cdd:cd19081 1 PLGRTGLSVSPLCLG----TMVFGwTADEETSFA-LLDAFVDaGGNFIDTADVYSAWvpgnaggESETIIGRWLKSRGK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 103 RDEYIVATKCGR--YAEGFDFSAERVTKSIDESLERLQLEYVDILQCH-DIEFGSLDqivnETIPALQKIKESGKTRFIG 179
Cdd:cd19081 75 RDRVVIATKVGFpmGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAHwDDPATPLE----ETLGALNDLIRQGKVRYIG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 180 ITGLPLEVYTYVLD-RVPPGTIDVVLSYCHYciN----DSTLEDMLPYFKSKGVGVINASPLSMGL-----HTENGPPEw 249
Cdd:cd19081 151 ASNYSAWRLQEALElSRQHGLPRYVSLQPEY--NlvdrESFEGELLPLCREEGIGVIPYSPLAGGFltgkyRSEADLPG- 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7SMI_A 250 HPASPE------------IKAACKAAADyckKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELETA 314
Cdd:cd19081 228 STRRGEaakrylnerglrILDALDEVAA---EHGATPAQVALAWLLARPGVTAPIAGARTVEQLEDLLAAAgLRLTDE 302
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-305 |
1.53e-30 |
|
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: 117.80 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 38 LNLSCVGFGASPLGNVFGDVseEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKAL----GASRDEYIVATKCG 113
Cdd:cd19099 1 LTLSSLGLGTYRGDSDDETD--EEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekgGIKRDEVVIVTKAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 114 -----------------------------RYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEfGSLDQIVNETIP 164
Cdd:cd19099 79 yipgdgdeplrplkyleeklgrglidvadSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPE-EQLLELGEEEFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 165 --------ALQKIKESGKTRFIGITglplevyTYVLDRVPPGTIDVVLSYCHYCINDSTLED-------MLPY------- 222
Cdd:cd19099 158 drleeafeALEEAVAEGKIRYYGIS-------TWDGFRAPPALPGHLSLEKLVAAAEEVGGDnhhfkviQLPLnllepea 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 223 -----------------FKSKGVGVINASPLSMGLHTENGPPEWHPASPeikaackaaadyckkNGKNISKLALQYSLSN 285
Cdd:cd19099 231 ltekntvkgealslleaAKELGLGVIASRPLNQGQLLGELRLADLLALP---------------GGATLAQRALQFARST 295
|
330 340
....*....|....*....|
7SMI_A 286 KDISTTLVGMNSVKQVEENV 305
Cdd:cd19099 296 PGVDSALVGMRRPEHVDENL 315
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
37-242 |
2.70e-29 |
|
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: 114.33 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGN-VFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGaSRDEYIVATKCG-- 113
Cdd:cd19148 1 DLPVSRIALGTWAIGGwMWGGTDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYG-KRDRVVIATKVGle 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 114 ---RYAEGFDFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRFIGITGL- 183
Cdd:cd19148 80 wdeGGEVVRNSSPARIRKEVEDSLRRLQTDYIDLYQVHwpdplvPIE---------ETAEALKELLDEGKIRAIGVSNFs 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
7SMI_A 184 PLEVYTYvlDRVPPgtidvvLSYCH--YCINDSTLE-DMLPYFKSKGVGVINASPLSMGLHT 242
Cdd:cd19148 151 PEQMETF--RKVAP------LHTVQppYNLFEREIEkDVLPYARKHNIVTLAYGALCRGLLS 204
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
31-312 |
2.13e-28 |
|
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: 112.11 E-value: 2.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGaspLGNVFGDVSE-EQSIATVIEAFNQGINFFDTSPYYG--ATLSEKVLGKCLKA-LGASRDEY 106
Cdd:cd19151 3 NRCGRSGLKLPAISLG---LWHNFGDVDRyENSRAMLRRAFDLGITHFDLANNYGppPGSAEENFGRILKEdLKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKCGRYA-EG--FDF-SAERVTKSIDESLERLQLEYVDILQCHDIEfgsLDQIVNETIPALQKIKESGKTRFIGITG 182
Cdd:cd19151 80 IISTKAGYTMwPGpyGDWgSKKYLIASLDQSLKRMGLDYVDIFYHHRPD---PETPLEETMGALDQIVRQGKALYVGISN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 183 LPLEVYTYVLDRVPPGTIDVVLSYCHYCINDSTLED-MLPYFKSKGVGVINASPLSMGLHTE---NGPPEWHPAS----- 253
Cdd:cd19151 157 YPPEEAREAAAILKDLGTPCLIHQPKYSMFNRWVEEgLLDVLEEEGIGCIAFSPLAQGLLTDrylNGIPEDSRAAkgssf 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 254 -------PEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELE 312
Cdd:cd19151 237 lkpeqitEEKLAKVRRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALDNRE 302
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
28-307 |
1.85e-27 |
|
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: 109.61 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASplgnV-FGD-VSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDE 105
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSW----VtFGNqVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELGWPRSD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 106 YIVATKC-----GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCH--D----IEfgsldqivnETIPALQKIKESGK 174
Cdd:cd19143 77 YVVSTKIfwgggGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHrpDpatpIE---------ETVRAMNDLIDQGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 175 TRFIG--------ITglplEVYTyVLDR---VPPgtidvVLSYCHYCI-NDSTLE-DMLPYFKSKGVGVINASPLSMGLH 241
Cdd:cd19143 148 AFYWGtsewsaqqIE----EAHE-IADRlglIPP-----VMEQPQYNLfHRERVEvEYAPLYEKYGLGTTTWSPLASGLL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 242 T----ENGPP---------EW-----HPASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEE 303
Cdd:cd19143 218 TgkynNGIPEgsrlalpgyEWlkdrkEELGQEKIEKVRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEE 297
|
....
7SMI_A 304 NVGA 307
Cdd:cd19143 298 NLKA 301
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
37-317 |
2.95e-27 |
|
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: 107.70 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGNVF-GDVSEEQSIATVIE-AFNQGINFFDTSPYYGATLSEKVLGKCLKALGasRDEYIVATKcgr 114
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMsKDYSDDKKAIEALRyAIELGINLIDTAEMYGGGHAEELVGKAIKGFD--REDLFITTK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 yAEGFDFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRFIGITGLP---L 185
Cdd:cd19072 76 -VSPDHLKYDDVIKAAKESLKRLGTDYIDLYLIHwpnpsiPIE---------ETLRAMEELVEEGKIRYIGVSNFSleeL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 186 EVYTYVLDRVPPGTIDVvlsycHYCINDSTLE-DMLPYFKSKGVGVINASPLSMGLHTENgppewhPASPEIkaackaaA 264
Cdd:cd19072 146 EEAQSYLKKGPIVANQV-----EYNLFDREEEsGLLPYCQKNGIAIIAYSPLEKGKLSNA------KGSPLL-------D 207
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
7SMI_A 265 DYCKKNGKNISKLALQYSLSNKDIsTTLVGMNSVKQVEENVGaALELETAGKD 317
Cdd:cd19072 208 EIAKKYGKTPAQIALNWLISKPNV-IAIPKASNIEHLEENAG-ALGWELSEED 258
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
31-312 |
6.40e-27 |
|
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: 107.93 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGaspLGNVFGDVSEEQSIATVIE-AFNQGINFFDTSPYYG--ATLSEKVLGKCLKA-LGASRDEY 106
Cdd:cd19150 3 RRCGKSGLKLPALSLG---LWHNFGDDTPLETQRAILRtAFDLGITHFDLANNYGppPGSAEENFGRILREdFAGYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKCGR------YAEGFdfSAERVTKSIDESLERLQLEYVDILQCHDIEfgsLDQIVNETIPALQKIKESGKTRFIGI 180
Cdd:cd19150 80 IISTKAGYdmwpgpYGEWG--SRKYLLASLDQSLKRMGLDYVDIFYSHRFD---PDTPLEETMGALDHAVRSGKALYVGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 181 TGL----PLEVYTYVLDRVPPGTI-DVVLSYCHYCINDSTLEDMLpyfKSKGVGVINASPLSMGLHTE---NGPPEWHPA 252
Cdd:cd19150 155 SSYsperTREAAAILRELGTPLLIhQPSYNMLNRWVEESGLLDTL---QELGVGCIAFTPLAQGLLTDkylNGIPEGSRA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
7SMI_A 253 S-----------PEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELE 312
Cdd:cd19150 232 SkerslspkmltEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALDNLT 302
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
31-307 |
2.33e-26 |
|
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: 106.38 E-value: 2.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGAspLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVAT 110
Cdd:cd19141 3 RNLGKSGLRVSCLGLGT--WVTFGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKGWRRSSYVITT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KC---GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGKTRFIGITGLP--- 184
Cdd:cd19141 81 KIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNT---PMEEIVRAFTHVINQGMAMYWGTSRWSame 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 -LEVYTYV--LDRVPPgtidVVLSYCHYCINDSTLEDMLPYFKSK-GVGVINASPLSMGLHT---ENGPPEWHPAS---- 253
Cdd:cd19141 158 iMEAYSVArqFNLIPP----IVEQAEYHLFQREKVEMQLPELFHKiGVGAMTWSPLACGILSgkyDDGVPEYSRASlkgy 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 254 ------------PEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:cd19141 234 qwlkekilseegRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQA 299
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
35-179 |
5.28e-26 |
|
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: 104.95 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASPLGNVFGDVseEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVATKCG- 113
Cdd:cd19092 1 PEGLEVSRLVLGCMRLADWGESA--EELLSLIEAALELGITTFDHADIYGGGKCEELFGEALALNPGLREKIEIQTKCGi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 114 --------RYAEGFDFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGKTRFIG 179
Cdd:cd19092 79 rlgddprpGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHrpdplmDPE---------EVAEAFDELVKSGKVRYFG 149
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
30-307 |
3.69e-25 |
|
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: 102.90 E-value: 3.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 30 RRELGNTGLNLSCVGFGASPLGNVFGD-VSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKalGASRDEYIV 108
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGDYGApKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALK--DGPREKVQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCG-RYAEG----FDFSAERVTKSIDESLERLQLEYVDILQCHDIefgslDQIV--NETIPALQKIKESGKTRFIGIT 181
Cdd:cd19145 80 ATKFGiHEIGGsgveVRGDPAYVRAACEASLKRLDVDYIDLYYQHRI-----DTTVpiEITMGELKKLVEEGKIKYIGLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 182 glplEVYTYVLDR---VPPGTIdVVLSYCHYCiNDSTlEDMLPYFKSKGVGVINASPLSMGLHTENGPPEWHPASPEI-- 256
Cdd:cd19145 155 ----EASADTIRRahaVHPITA-VQLEWSLWT-RDIE-EEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVrk 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
7SMI_A 257 -------------KAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:cd19145 228 shprfqgenleknKVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGA 291
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
31-330 |
6.01e-25 |
|
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: 102.76 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPlgnVFGD-VSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVA 109
Cdd:cd19160 6 RNLGKSGLRVSCLGLGTWV---TFGSqISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKC---GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGKTRFIGITGLP-- 184
Cdd:cd19160 83 TKIywgGQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVFANRSDPNS---PMEEIVRAMTYVINQGMAMYWGTSRWSam 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 --LEVYTYV--LDRVPPgtidVVLSYCHYCINDSTLEDMLPYFKSK-GVGVINASPLSMGLHT---ENGPPEWHPAS--- 253
Cdd:cd19160 160 eiMEAYSVArqFNLIPP----VCEQAEYHLFQREKVEMQLPELYHKiGVGSVTWSPLACGLITgkyDGRVPDTCRAAvkg 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 254 -------------PEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAaleLETAGK-DEK 319
Cdd:cd19160 236 yqwlkekvqseegKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGS---IQVLSQlTPQ 312
|
330
....*....|...
7SMI_A 320 TFAEIENIL--KP 330
Cdd:cd19160 313 TVMEIDALLgnKP 325
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
29-179 |
7.48e-25 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 102.15 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 29 ERRELGNTGLNLSCVGFGASPLGNvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIV 108
Cdd:COG4989 2 KRIKLGASGLSVSRIVLGCMRLGE--WDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKLSPSLREKIEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCG-RYAEG--------FDFSAERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESG 173
Cdd:COG4989 80 QTKCGiRLPSEardnrvkhYDTSKEHIIASVEGSLRRLGTDYLDLLLLHrpdplmDPE---------EVAEAFDELKASG 150
|
....*.
7SMI_A 174 KTRFIG 179
Cdd:COG4989 151 KVRHFG 156
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
28-300 |
1.04e-24 |
|
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: 102.16 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASPlgnVFG-DVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEY 106
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTWS---TFStAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKGWKRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKC--GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHdiefgSLDQI--VNETIPALQKIKESGKTRFIGITG 182
Cdd:cd19142 78 IVSTKIywSYGSEERGLSRKHIIESVRASLRRLQLDYIDIVIIH-----KADPMcpMEEVVRAMSYLIDNGLIMYWGTSR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 183 L-PLEVY-TYVLDR----VPPgtIDVVLSYCHYCINDSTLEdMLPYFKSKGVGVINASPLSMGL---------------- 240
Cdd:cd19142 153 WsPVEIMeAFSIARqfncPTP--ICEQSEYHMFCREKMELY-MPELYNKVGVGLITWSPLSLGLdpgiseetrrlvtkls 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 241 --HTENGPPEWHPASPE----IKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQ 300
Cdd:cd19142 230 fkSSKYKVGSDGNGIHEetrrASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQ 295
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
25-307 |
2.34e-24 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 101.60 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 25 HQKLERRELGNTGLNLSCVGFGaspLGNVFGDVSEEQSIATVI-EAFNQGINFFDTSPYYG--ATLSEKVLGKCLKA-LG 100
Cdd:PRK09912 10 YGQMQYRYCGKSGLRLPALSLG---LWHNFGHVNALESQRAILrKAFDLGITHFDLANNYGppPGSAEENFGRLLREdFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 101 ASRDEYIVATKCGR------YAEGFdfSAERVTKSIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGK 174
Cdd:PRK09912 87 AYRDELIISTKAGYdmwpgpYGSGG--SRKYLLASLDQSLKRMGLEYVDIFYSHRVDENT---PMEETASALAHAVQSGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 175 TRFIGITGLPLEVYTYVLDRVPPGTIDVVLSYCHYCINDSTLE--DMLPYFKSKGVGVINASPLSMGLHTE---NGPPEW 249
Cdd:PRK09912 162 ALYVGISSYSPERTQKMVELLREWKIPLLIHQPSYNLLNRWVDksGLLDTLQNNGVGCIAFTPLAQGLLTGkylNGIPQD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7SMI_A 250 HPASPEIKAA---------------CKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:PRK09912 242 SRMHREGNKVrgltpkmlteanlnsLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQA 314
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
28-330 |
3.59e-24 |
|
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: 100.89 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGA-SPLGnvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEY 106
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTwVTFG---GQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKC---GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGKTRFIGITGL 183
Cdd:cd19159 78 VITTKLywgGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNT---PMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 184 P----LEVYTYV--LDRVPPgtidVVLSYCHYCINDSTLEDMLPYFKSK-GVGVINASPLSMGLHT---ENGPPEWHPAS 253
Cdd:cd19159 155 SameiMEAYSVArqFNMIPP----VCEQAEYHLFQREKVEVQLPELYHKiGVGAMTWSPLACGIISgkyGNGVPESSRAS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 254 PEI----------------KAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAALELETAgkD 317
Cdd:cd19159 231 LKCyqwlkerivseegrkqQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKM--T 308
|
330
....*....|....*
7SMI_A 318 EKTFAEIENIL--KP 330
Cdd:cd19159 309 SHVVNEIDNILrnKP 323
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
58-327 |
1.12e-23 |
|
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: 99.56 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 58 SEEQSIATVIEAFNQGINFFDTS-----P----YYGATlsEKVLGKCLKALGaSRDEYIVATK-CGRYAEGF-------D 120
Cdd:cd19094 16 TEAEAHEQLDYAFDEGVNFIDTAemypvPpspeTQGRT--EEIIGSWLKKKG-NRDKVVLATKvAGPGEGITwprgggtR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 121 FSAERVTKSIDESLERLQLEYVDILQCHDIE-----FGSLDQIVN----------ETIPALQKIKESGKTRFIGIT---- 181
Cdd:cd19094 93 LDRENIREAVEGSLKRLGTDYIDLYQLHWPDrytplFGGGYYTEPseeedsvsfeEQLEALGELVKAGKIRHIGLSnetp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 182 -------------GLPlevytyvldrvPPGTIDVVLSYchycINDSTLEDM-----------LPYfkskgvgvinaSPLS 237
Cdd:cd19094 173 wgvmkflelaeqlGLP-----------RIVSIQNPYSL----LNRNFEEGLaeachrenvglLAY-----------SPLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 238 MG------LHTENGPPE------WHPA----SPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQV 301
Cdd:cd19094 227 GGvltgkyLDGAARPEGgrlnlfPGYMaryrSPQALEAVAEYVKLARKHGLSPAQLALAWVRSRPFVTSTIIGATTLEQL 306
|
330 340
....*....|....*....|....*..
7SMI_A 302 EENVGAA-LELetagkDEKTFAEIENI 327
Cdd:cd19094 307 KENIDAFdVPL-----SDELLAEIDAV 328
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
31-307 |
4.47e-23 |
|
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: 97.85 E-value: 4.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGA-SPLGnvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGASRDEYIVA 109
Cdd:cd19158 4 RNLGKSGLRVSCLGLGTwVTFG---GQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVIT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKC---GRYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEfgsLDQIVNETIPALQKIKESGKTRFIGITGLP-- 184
Cdd:cd19158 81 TKIfwgGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPD---PNTPMEETVRAMTHVINQGMAMYWGTSRWSsm 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 185 --LEVYTYV--LDRVPPgtidVVLSYCHYCINDSTLEDMLP-YFKSKGVGVINASPLSMGLHT---ENGPPEWHPASPE- 255
Cdd:cd19158 158 eiMEAYSVArqFNLIPP----ICEQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSgkyDSGIPPYSRASLKg 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
7SMI_A 256 ---------------IKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGA 307
Cdd:cd19158 234 yqwlkdkilseegrrQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGA 300
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
28-324 |
5.66e-23 |
|
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: 97.51 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 28 LERRELGNTGLNLSCVGFGASPLGNVFGDV-SEEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALGASRDEY 106
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYGPPkPDEERFAVLDAAFELGCTFWDTADIYGD--SEELIGRWFKQNPGKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKCGRYAEG------FDFSAERVTKSIDESLERLQLEYVDILQCHDIEfGSLDqiVNETIPALQKIKESGKTRFIGI 180
Cdd:cd19144 79 FLATKFGIEKNVetgeysVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVD-GKTP--IEKTVAAMAELVQEGKIKHIGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 181 TglplEVYTYVLDR---VPPgtIDVV-LSYCHYCIN-DSTLEDMLPYFKSKGVGVINASPLSMGLHT------------- 242
Cdd:cd19144 156 S----ECSAETLRRahaVHP--IAAVqIEYSPFSLDiERPEIGVLDTCRELGVAIVAYSPLGRGFLTgairspddfeegd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 243 --ENGP---PEWHPASPEIKAACKAAADyckKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGaALELETAGKD 317
Cdd:cd19144 230 frRMAPrfqAENFPKNLELVDKIKAIAK---KKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLG-ALKVKLTEEE 305
|
....*..
7SMI_A 318 EKTFAEI 324
Cdd:cd19144 306 EKEIREI 312
|
|
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
37-328 |
5.70e-23 |
|
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: 96.92 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGNVFGDV-SEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVATKCG-- 113
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGPPpDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVG---EALKPFRDQVVIATKFGfk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 114 -----RYAEGFDFSAERVTKSIDESLERLQLEYVDILQCHDIEfgsLDQIVNETIPALQKIKESGKTRFIGITglplEVY 188
Cdd:cd19078 78 idggkPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVD---PNVPIEEVAGTMKELIKEGKIRHWGLS----EAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 189 TYVLDR---VPPgtIDVVLSycHYCINDSTLED-MLPYFKSKGVGVINASPLSMGLHT--------------ENGPPEWh 250
Cdd:cd19078 151 VETIRRahaVCP--VTAVQS--EYSMMWREPEKeVLPTLEELGIGFVPFSPLGKGFLTgkidentkfdegddRASLPRF- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 251 paSPEIKAACKAAADYCKK--NGKNIS--KLALQYSLSNKDISTTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIE 325
Cdd:cd19078 226 --TPEALEANQALVDLLKEfaEEKGATpaQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAAdIEL-----TPEELREIE 298
|
...
7SMI_A 326 NIL 328
Cdd:cd19078 299 DAL 301
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
41-308 |
1.34e-21 |
|
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: 93.00 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 41 SCVGFGASPLGnvfGDVSEEQSIATVIEAFNQGINFFDTSPYYGATL----SEKVLGKCLKALGAsRDEYIVATKCGRYA 116
Cdd:cd19082 1 SRIVLGTADFG---TRIDEEEAFALLDAFVELGGNFIDTARVYGDWVergaSERVIGEWLKSRGN-RDKVVIATKGGHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 117 EGFDF----SAERVTKSIDESLERLQLEYVDILQCH-DiefgSLDQIVNETIPALQKIKESGKTRFIG------------ 179
Cdd:cd19082 77 LEDMSrsrlSPEDIRADLEESLERLGTDYIDLYFLHrD----DPSVPVGEIVDTLNELVRAGKIRAFGasnwsteriaea 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 180 --------ITGL----PLevytYVL-DRVPPGTIDVVLSYCHycindstlEDMLPYFKSKGVGVINASPLSMGLHTENGP 246
Cdd:cd19082 153 nayakahgLPGFaassPQ----WSLaRPNEPPWPGPTLVAMD--------EEMRAWHEENQLPVFAYSSQARGFFSKRAA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 247 PEWHPASPEIKAAC--------KAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19082 221 GGAEDDSELRRVYYseenferlERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAA 290
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
43-312 |
8.16e-21 |
|
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: 89.97 E-value: 8.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPL--GNVFGDVS-EEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGkclKALGASRDEYIVATKCG--RYAE 117
Cdd:cd19088 4 LGYGAMRLtgPGIWGPPAdREEAIAVLRRALELGVNFIDTADSYGPDVNERLIA---EALHPYPDDVVIATKGGlvRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 118 GF---DFSAERVTKSIDESLERLQLEYVDILQCHDIE-FGSLDqivnETIPALQKIKESGKTRFIGITGLPLEVYTYVLD 193
Cdd:cd19088 81 GWwgpDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDpKVPFE----EQLGALAELQDEGLIRHIGLSNVTVAQIEEARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 194 RVPpgtIDVVLSycHYCINDSTLEDMLPYFKSKGVGVINASPLSMGLHTENGPPewhpaspeikaACKAAADYckknGKN 273
Cdd:cd19088 157 IVR---IVSVQN--RYNLANRDDEGVLDYCEAAGIAFIPWFPLGGGDLAQPGGL-----------LAEVAARL----GAT 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
7SMI_A 274 ISKLALQYSLSNKDISTTLVGMNSVKQVEENV-GAALELE 312
Cdd:cd19088 217 PAQVALAWLLARSPVMLPIPGTSSVEHLEENLaAAGLRLS 256
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
38-308 |
6.24e-19 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381391 [Multi-domain] Cd Length: 291 Bit Score: 85.46 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 38 LNLSCVGFGASplgnvfgdVSEEQSIAtVIEAF-NQGINFFDTSPYYG-------ATLSEKVLGKCLKALGAsRDEYIVA 109
Cdd:cd19752 3 LCLGTMYFGTR--------TDEETSFA-ILDRYvAAGGNFLDTANNYAfwteggvGGESERLIGRWLKDRGN-RDDVVIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKCG----------RYAEGFdfSAERVTKSIDESLERLQLEYVDILQCHdIEFGSLDQivNETIPALQKIKESGKTRFIG 179
Cdd:cd19752 73 TKVGagprdpdggpESPEGL--SAETIEQEIDKSLRRLGTDYIDLYYAH-VDDRDTPL--EETLEAFNELVKAGKVRAIG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 180 IT-----------------GLPLEV-----YTYVLDRvpPGTIDVVlsycHYCINDstleDMLPYFKSKG-VGVINASPL 236
Cdd:cd19752 148 ASnfaawrlerarqiarqqGWAEFSaiqqrHSYLRPR--PGADFGV----QRIVTD----ELLDYASSRPdLTLLAYSPL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7SMI_A 237 SMGLHTENGPPE-WHPASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19752 218 LSGAYTRPDRPLpEQYDGPDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
37-186 |
6.98e-19 |
|
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: 84.62 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLgnvfgdvSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRYa 116
Cdd:cd19140 5 GVRIPALGLGTYPL-------TGEECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAASGVPRDELFLTTKVWPD- 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 117 egfDFSAERVTKSIDESLERLQLEYVDILQCHdieFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLE 186
Cdd:cd19140 74 ---NYSPDDFLASVEESLRKLRTDYVDLLLLH---WPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVA 137
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
37-180 |
1.06e-18 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 84.34 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGasplgnVFGdVSEEQSIATVIEAFNQGINFFDTSPYYGAtlsEKVLGKCLKALGASRDEYIVATKcgryA 116
Cdd:COG0656 2 GVEIPALGLG------TWQ-LPGEEAAAAVRTALEAGYRHIDTAAMYGN---EEGVGEAIAASGVPREELFVTTK----V 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
7SMI_A 117 EGFDFSAERVTKSIDESLERLQLEYVDILQCH-----DIEfgsldqivnETIPALQKIKESGKTRFIGI 180
Cdd:COG0656 68 WNDNHGYDDTLAAFEESLERLGLDYLDLYLIHwpgpgPYV---------ETWRALEELYEEGLIRAIGV 127
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
31-312 |
2.47e-18 |
|
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: 84.19 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 31 RELGNTGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAF-NQGINFFDTSPYYGATLSEKVLGKCLKALgasRDEYIVA 109
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEWGWGADREEARAMFDAYvEAGGNFIDTANNYTNGTSERLLGEFIAGN---RDRIVLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKCGRYAEGFDFSA-----ERVTKSIDESLERLQLEYVDILQCHdiefgSLDQI--VNETIPALQKIKESGKTRFIGITG 182
Cdd:cd19080 78 TKYTMNRRPGDPNAggnhrKNLRRSVEASLRRLQTDYIDLLYVH-----AWDFTtpVEEVMRALDDLVRAGKVLYVGISD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 183 LPLEVY----TYVLDRVPPGTIDVVLsycHYCINDSTLE-DMLPYFKSKGVGVINASPLSMGLHT----------ENGPP 247
Cdd:cd19080 153 TPAWVVaranTLAELRGWSPFVALQI---EYSLLERTPErELLPMARALGLGVTPWSPLGGGLLTgkyqrgeegrAGEAK 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7SMI_A 248 EWHPASP-------EIKAACKAAADyckKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGaALELE 312
Cdd:cd19080 230 GVTVGFGklternwAIVDVVAAVAE---ELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLG-ALDLT 297
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
36-325 |
3.16e-18 |
|
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding members of aldo-keto reductase family 8 member A1-2 (AKR8A1-2), respectively. PLR (EC 1.1.1.65), also called PL reductase (PL-red), catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP(+).
Pssm-ID: 381303 [Multi-domain] Cd Length: 302 Bit Score: 83.83 E-value: 3.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 36 TGLNLSCVGFGASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYG---ATLSEKVLGKCLKALGASRDEYIVATKC 112
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNPTPDEEAFETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFRKYPEYADKVVLSVKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 113 GRYAEGF--DFSAERVTKSIDESLERL-QLEYVDILQC------HDIEfgsldqivnETIPALQKIKESGKTRFIGITGL 183
Cdd:cd19077 81 GLDPDTLrpDGSPEAVRKSIENILRALgGTKKIDIFEParvdpnVPIE---------ETIKALKELVKEGKIRGIGLSEV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 184 PLEVYTYVLDRVPPGTIDVVLSYCHYCINDStleDMLPYFKSKGVGVINASPLSMGLHT---------ENGPPEWHPA-- 252
Cdd:cd19077 152 SAETIRRAHAVHPIAAVEVEYSLFSREIEEN---GVLETCAELGIPIIAYSPLGRGLLTgriksladiPEGDFRRHLDrf 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 253 SPEI----KAACKAAADYCKKNGKNISKLALQY--SLSNKDIsTTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIE 325
Cdd:cd19077 229 NGENfeknLKLVDALQELAEKKGCTPAQLALAWilAQSGPKI-IPIPGSTTLERVEENLKAAnVEL-----TDEELKEIN 302
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
43-283 |
1.12e-15 |
|
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.
Pssm-ID: 381297 [Multi-domain] Cd Length: 251 Bit Score: 75.60 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLgnvfgdvSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRYaegfDFS 122
Cdd:cd19071 4 IGLGTYKL-------KPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESGVPREELFITTKLWPT----DHG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 123 AERVTKSIDESLERLQLEYVDILQCH---DIEFGSLDQIVNETIPALQKIKESGKTRFIGITGLPLEVYTYVLD--RVPP 197
Cdd:cd19071 70 YERVREALEESLKDLGLDYLDLYLIHwpvPGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAaaRIKP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 198 gtidVVLSY-CH-YCINDSTLEdmlpYFKSKGVGVINASPLSmglhtenGPPEWHPASPEIKAAckaaadyCKKNGKNIS 275
Cdd:cd19071 150 ----AVNQIeLHpYLQQKELVE----FCKEHGIVVQAYSPLG-------RGRRPLLDDPVLKEI-------AKKYGKTPA 207
|
....*...
7SMI_A 276 KLALQYSL 283
Cdd:cd19071 208 QVLLRWAL 215
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
52-186 |
5.68e-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: 74.29 E-value: 5.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 52 NVFGD-VSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIVATKCGryAEGFDFSAERVTKSI 130
Cdd:cd19103 23 QVFGNhLDEDTLKAVFDKAMAAGLNLWDTAAVYGMGASEKILGEFLKRY--PREDYIISTKFT--PQIAGQSADPVADML 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
7SMI_A 131 DESLERLQLEYVDILQCH---DIEFGSLdqivnETIPALQkikeSGKTRFIGITGLPLE 186
Cdd:cd19103 99 EGSLARLGTDYIDIYWIHnpaDVERWTP-----ELIPLLK----SGKVKHVGVSNHNLA 148
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
43-239 |
6.65e-15 |
|
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: 73.07 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFGASPLgnvfgdvSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRYaegfDFS 122
Cdd:cd19073 4 LGLGTWQL-------RGDDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESGVPREDLFITTKVWRD----HLR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 123 AERVTKSIDESLERLQLEYVDILQCH----DIEfgsldqiVNETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRVPPG 198
Cdd:cd19073 70 PEDLKKSVDRSLEKLGTDYVDLLLIHwpnpTVP-------LEETLGALKELKEAGKVKSIGVSNFTIELLEEALDISPLP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
7SMI_A 199 tIDVVLSYCHYCINDStleDMLPYFKSKGVGVINASPLSMG 239
Cdd:cd19073 143 -IAVNQVEFHPFLYQA---ELLEYCRENDIVITAYSPLARG 179
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
57-180 |
1.62e-14 |
|
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: 72.40 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 57 VSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRYAEGFDfSAERvtkSIDESLER 136
Cdd:cd19131 20 VSNDEAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASGVPREELFITTKLWNSDQGYD-STLR---AFDESLRK 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....
7SMI_A 137 LQLEYVDILQCHdIEFGSLDQIVnETIPALQKIKESGKTRFIGI 180
Cdd:cd19131 93 LGLDYVDLYLIH-WPVPAQDKYV-ETWKALIELKKEGRVKSIGV 134
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
35-327 |
2.69e-14 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 72.96 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASPLGNvfgDVSEEQSIATVIEAFNQGINFFDTSPYYGAT-------LSEKVLGKCLKALGaSRDEYI 107
Cdd:PRK10625 8 HSSLEVSTLGLGTMTFGE---QNSEADAHAQLDYAVAQGINLIDVAEMYPVPprpetqgLTETYIGNWLAKRG-SREKLI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATKCGRYAEGFDFSA--------ERVTKSIDESLERLQLEYVDILQCHDIE-----FGSLDQIVN---------ETIPA 165
Cdd:PRK10625 84 IASKVSGPSRNNDKGIrpnqaldrKNIREALHDSLKRLQTDYLDLYQVHWPQrptncFGKLGYSWTdsapavsllETLDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 166 LQKIKESGKTRFIGITG-LPLEVYTYV-------LDRVppgtidVVLSYCHYCINDSTLEDMLPYFKSKGVGVINASPLS 237
Cdd:PRK10625 164 LAEQQRAGKIRYIGVSNeTAFGVMRYLhlaekhdLPRI------VTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 238 MGLHTE---NGPpewHPA--------------SPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQ 300
Cdd:PRK10625 238 FGTLTGkylNGA---KPAgarntlfsrftrysGEQTQKAVAAYVDIAKRHGLDPAQMALAFVRRQPFVASTLLGATTMEQ 314
|
330 340
....*....|....*....|....*...
7SMI_A 301 VEENVGAA-LELetagkDEKTFAEIENI 327
Cdd:PRK10625 315 LKTNIESLhLTL-----SEEVLAEIEAV 337
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
43-291 |
6.04e-14 |
|
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: 70.72 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 43 VGFG-ASPLGNVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRyaegfdf 121
Cdd:cd19120 7 IAFGtGTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESGVPREDLFITTKVSP------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 122 SAERVTKSIDESLERLQLEYVDILQCHD---IEFGSLDqiVNETIPALQKIKESGKTRFIGITGLPLEVYTYVLD--RVP 196
Cdd:cd19120 77 GIKDPREALRKSLAKLGVDYVDLYLIHSpffAKEGGPT--LAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDtaKIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 197 PgtidVV--LSYCHYCINDStlEDMLPYFKSKGVGVINASPLSmglhtengPPEWHPASPeIKAACKAAAdycKKNGKNI 274
Cdd:cd19120 155 P----AVnqIEFHPYLYPQQ--PALLEYCREHGIVVSAYSPLS--------PLTRDAGGP-LDPVLEKIA---EKYGVTP 216
|
250
....*....|....*..
7SMI_A 275 SKLALQYSLSNKDISTT 291
Cdd:cd19120 217 AQVLLRWALQKGIVVVT 233
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
37-328 |
1.18e-13 |
|
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: 70.92 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGN----VFGDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGaSRDEYIVATKc 112
Cdd:cd19146 8 GVRVSPLCLGAMSFGEawksMMGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASRG-NRDEMVLATK- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 113 grYAEGFDFSAERVTK-------------SIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGKTRFIG 179
Cdd:cd19146 86 --YTTGYRRGGPIKIKsnyqgnhakslrlSVEASLKKLQTSYIDILYVHWWDYTT---SIPELMQSLNHLVAAGKVLYLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 180 ITGLPLEVYTYVLD--RVPPGTIDVVLSYCHYCINDSTLEDMLPYFKSKGVGVINASPLSMG-LHTE--------NGPPE 248
Cdd:cd19146 161 VSDTPAWVVSKANAyaRAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGqFRTEeefkrrgrSGRKG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 249 WhPASPEIKAACKAAADYCKKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVgAALELETAgkdEKTFAEIENIL 328
Cdd:cd19146 241 G-PQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNI-EALGISLS---DEEIQEIEDAY 315
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
58-325 |
1.57e-13 |
|
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: 69.58 E-value: 1.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 58 SEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKclkALGASRDEYIVATKC-GRYAegfdfSAERVTKSIDESLER 136
Cdd:cd19138 27 KRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGE---AIRGRRDKVFLVSKVlPSNA-----SRQGTVRACERSLRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 137 LQLEYVDILQCH---DIEFGsldqivnETIPALQKIKESGKTRFIGITGLPLEVYtYVLDRVPPG---TIDVVLsychYC 210
Cdd:cd19138 99 LGTDYLDLYLLHwrgGVPLA-------ETVAAMEELKKEGKIRAWGVSNFDTDDM-EELWAVPGGgncAANQVL----YN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 211 INDSTLE-DMLPYFKSKGVGVINASPLSMGlhteNGPPEWHPASPEIKaacKAAADYckknGKNISKLALQYSLSNKDIs 289
Cdd:cd19138 167 LGSRGIEyDLLPWCREHGVPVMAYSPLAQG----GLLRRGLLENPTLK---EIAARH----GATPAQVALAWVLRDGNV- 234
|
250 260 270
....*....|....*....|....*....|....*..
7SMI_A 290 TTLVGMNSVKQVEENVGAA-LELetagkDEKTFAEIE 325
Cdd:cd19138 235 IAIPKSGSPEHARENAAAAdLEL-----TEEDLAELD 266
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
45-180 |
4.73e-13 |
|
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: 68.74 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 45 FGASPLGNVFGDVSEEQSiATVIEAFNQ-GINFFDTSPYYGATLSEKVLGkclkALGASRDEYIVATKCgRYAEGFDFSA 123
Cdd:cd19075 5 LGTMTFGSQGRFTTAEAA-AELLDAFLErGHTEIDTARVYPDGTSEELLG----ELGLGERGFKIDTKA-NPGVGGGLSP 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
7SMI_A 124 ERVTKSIDESLERLQLEYVDILQCH------DIEfgsldqivnETIPALQKIKESGK-TRFiGI 180
Cdd:cd19075 79 ENVRKQLETSLKRLKVDKVDVFYLHapdrstPLE---------ETLAAIDELYKEGKfKEF-GL 132
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
35-239 |
7.53e-13 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 67.46 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGasplgnVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGR 114
Cdd:cd19126 4 NNGTRMPWLGLG------VFQTPDGDETERAVQTALENGYRSIDTAAIYK---NEEGVGEAIRESGVPREELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YaegfDFSAERVTKSIDESLERLQLEYVDILQCHdieFGSLDQIVnETIPALQKIKESGKTRFIGITGLP---LEVYTYV 191
Cdd:cd19126 75 D----DQRARRTEDAFQESLDRLGLDYVDLYLIH---WPGKDKFI-DTWKALEKLYASGKVKAIGVSNFQehhLEELLAH 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
7SMI_A 192 LDRVPpgTIDVVlsYCHYCINDstlEDMLPYFKSKGVGVINASPLSMG 239
Cdd:cd19126 147 ADVVP--AVNQV--EFHPYLTQ---KELRGYCKSKGIVVEAWSPLGQG 187
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
37-307 |
1.84e-12 |
|
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: 66.44 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGN-VFGDVS-EEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALgaSRDEYIVATKCGR 114
Cdd:cd19137 1 GEKIPALGLGTWGIGGfLTPDYSrDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDF--PREDLFIVTKVWP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YaegfDFSAERVTKSIDESLERLQLEYVDILQCH----DIEFgsldqivNETIPALQKIKESGKTRFIGITGLPLEVYTY 190
Cdd:cd19137 79 T----NLRYDDLLRSLQNSLRRLDTDYIDLYLIHwpnpNIPL-------EETLSAMAEGVRQGLIRYIGVSNFNRRLLEE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 191 VLDRVppgTIDVVLSYCHYCINDSTLE--DMLPYFKSKGVGVINASPLSMGLHTENgppewhpaspeikaacKAAADYCK 268
Cdd:cd19137 148 AISKS---QTPIVCNQVKYNLEDRDPErdGLLEYCQKNGITVVAYSPLRRGLEKTN----------------RTLEEIAK 208
|
250 260 270
....*....|....*....|....*....|....*....
7SMI_A 269 KNGKNISKLALQYSLSNKDIsTTLVGMNSVKQVEENVGA 307
Cdd:cd19137 209 NYGKTIAQIALAWLIQKPNV-VAIPKAGRVEHLKENLKA 246
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
35-180 |
4.07e-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: 4.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGasplgnVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGR 114
Cdd:cd19133 4 NNGVEMPILGFG------VFQIPDPEECERAVLEAIKAGYRLIDTAAAYG---NEEAVGRAIKKSGIPREELFITTKLWI 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 115 YaegfDFSAERVTKSIDESLERLQLEYVDILQCHDiEFGSldqiVNETIPALQKIKESGKTRFIGI 180
Cdd:cd19133 75 Q----DAGYEKAKKAFERSLKRLGLDYLDLYLIHQ-PFGD----VYGAWRAMEELYKEGKIRAIGV 131
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
36-148 |
6.10e-11 |
|
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes Glycine max NAD(P)H-dependent 6'-deoxychalcone synthase (6DCS, EC 3.1.170), chalcone reductase (CHR, EC 2.3.1.74) from Medicago sativa, Glycyrrhiza echinate, and Glycyrrhiza glabra, which are founding members of aldo-keto reductase family 4 member A1 (AKR4A1), A2 (AKR4A2), A3 (AKR4A3), and A4 (AKR4A4), respectively. NAD(P)H-6DCS co-acts with chalcone synthase in formation of 4,2',4'-trihydroxychalcone, involved in the biosynthesis of glyceollin type phytoalexins. CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. The AKR4B family of AKR includes Sesbania rostrate chalcone reductase (CHR, AKR4B1), Papaver somniferum codeinone reductase (COR, AKR4B2/ AKR4B3), Fragaria x ananassa D-galacturonate reductase (GalUR, AKR4B4), deoxymugineic acid synthase 1 (DMAS1) from Zea mays (AKR4B5), Oryza sativa (AKR4B6), Hordeum vulgare (AKR4B7), Triticum aestivum (AKR4B8), and Erythroxylum coca methylecgonone reductase (MecgoR, AKR4B10). CHR, also called chalcone polyketide reductase, is a key enzyme of the flavonoid/isoflavonoid biosynthesis pathway. NADPH-dependent COR and non-functional NADPH-dependent COR from Papaver somniferum are founding members of aldo-keto reductase family 4 member B2 (AKR4B2) and B3 (AKR4B3), respectively. NADPH-dependent COR (EC 1.1.1.247) reduces codeinone to codeine in the penultimate step in morphine biosynthesis. It can use morphinone, hydrocodone, and hydromorphone as substrates during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrates during oxidative reaction with NADP as cofactor. GalUR (EC 1.1.1.365), also called aldo-keto reductase 2 (AKR2), is involved in ascorbic acid (vitamin C) biosynthesis by catalyzing the conversion from L-galactonate and NADP(+) to D-galacturonate and NADPH. DMAS1 (EC 1.1.1.285) catalyzes the reduction of a 3''-keto intermediate during the biosynthesis of 2'-deoxymugineic acid (DMA) from L-Met. It is involved in the formation of phytosiderophores (MAs) belonging to the mugineic acid family and required to acquire iron. MecgoR catalyzes the stereospecific reduction of methylecgonone to methylecgonine, the penultimate step in cocaine biosynthesis.
Pssm-ID: 381350 [Multi-domain] Cd Length: 281 Bit Score: 62.29 E-value: 6.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 36 TGLNLSCVGFGASPLGnvfgdVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLK---ALG--ASRDEYIVAT 110
Cdd:cd19124 1 SGQTMPVIGMGTASDP-----PSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAealRLGlvKSRDELFVTS 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
7SMI_A 111 K--CGryaegfDFSAERVTKSIDESLERLQLEYVDILQCH 148
Cdd:cd19124 73 KlwCS------DAHPDLVLPALKKSLRNLQLEYVDLYLIH 106
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
35-284 |
6.53e-11 |
|
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: 62.30 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGAsplGNVFGDVSEEQSIATVIEAfnqGINFFDTSPYYGatlSEKVLGKCLKAL----GASRDEYIVAT 110
Cdd:cd19116 6 NDGNEIPAIALGT---WKLKDDEGVRQAVKHAIEA---GYRHIDTAYLYG---NEAEVGEAIREKiaegVVKREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KCGRYAegfdFSAERVTKSIDESLERLQLEYVDILQCH---------DIEFGSLDQIVN----ETIPALQKIKESGKTRF 177
Cdd:cd19116 77 KLWNSY----HEREQVEPALRESLKRLGLDYVDLYLIHwpvafkennDSESNGDGSLSDidylETWRGMEDLVKLGLTRS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 178 IGITGLPLEVYTYVLDR--VPPGTIDVvlsYCHYCINDstlEDMLPYFKSKGVGVINASPLsmGLHTENGPPEWHP--AS 253
Cdd:cd19116 153 IGVSNFNSEQINRLLSNcnIKPAVNQI---EVHPTLTQ---EKLVAYCQSNGIVVMAYSPF--GRLVPRGQTNPPPrlDD 224
|
250 260 270
....*....|....*....|....*....|.
7SMI_A 254 PEIKAackaaadYCKKNGKNISKLALQYSLS 284
Cdd:cd19116 225 PTLVA-------IAKKYGKTTAQIVLRYLID 248
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
35-196 |
7.44e-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: 61.65 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGasplgnVFgDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCgr 114
Cdd:cd19127 4 NNGVEMPALGLG------VF-QTPPEETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSGVDRSDIFVTTKL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YAEgfDFSAERVTKSIDESLERLQLEYVDILQCHDIEFGSLDQIVnETIPALQKIKESGKTRFIGITGLPLEVYTYVLDR 194
Cdd:cd19127 72 WIS--DYGYDKALRGFDASLRRLGLDYVDLYLLHWPVPNDFDRTI-QAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDA 148
|
....*
7SMI_A 195 ---VP 196
Cdd:cd19127 149 ttvVP 153
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
35-236 |
8.89e-11 |
|
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: 61.98 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFG---ASPlgnvfGDVSeeQSIATVIEAfnqGINFFDTSPYYGatlSEKVLGKCLKALGAS----RDEYI 107
Cdd:cd19125 6 NTGAKIPAVGLGtwqADP-----GVVG--NAVKTAIKE---GYRHIDCAAIYG---NEKEIGKALKKLFEDgvvkREDLF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 108 VATK--CGryaegfDFSAERVTKSIDESLERLQLEYVDILQCH--------DIEFGSLDQI---VNETIPALQKIKESGK 174
Cdd:cd19125 73 ITSKlwCT------DHAPEDVPPALEKTLKDLQLDYLDLYLIHwpvrlkkgAHMPEPEEVLppdIPSTWKAMEKLVDSGK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
7SMI_A 175 TRFIGITGLPLEVYTYVLD--RVPPGTIDVvlsYCH-YCINDStledMLPYFKSKGVGVINASPL 236
Cdd:cd19125 147 VRAIGVSNFSVKKLEDLLAvaRVPPAVNQV---ECHpGWQQDK----LHEFCKSKGIHLSAYSPL 204
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
59-180 |
4.11e-10 |
|
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: 59.57 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 59 EEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKAL----GASRDEYIVATKCGRYaegfDFSAERVTKSIDESL 134
Cdd:cd19136 14 EEEVRQAVDAALKAGYRLIDTASVYR---NEADIGKALRDLlpkyGLSREDIFITSKLAPK----DQGYEKARAACLGSL 86
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 135 ERLQLEYVDILQCH----------DIEFGSLDQivnETIPALQKIKESGKTRFIGI 180
Cdd:cd19136 87 ERLGTDYLDLYLIHwpgvqglkpsDPRNAELRR---ESWRALEDLYKEGKLRAIGV 139
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
35-239 |
7.66e-10 |
|
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: 58.77 E-value: 7.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGasplgnVFgDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGR 114
Cdd:cd19130 5 NDGNSIPQLGYG------VF-KVPPADTQRAVATALEVGYRHIDTAAIYG---NEEGVGAAIAASGIPRDELFVTTKLWN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YAEGFDfsaeRVTKSIDESLERLQLEYVDILQCHdIEFGSLDQIVnETIPALQKIKESGKTRFIGITG-LP--LEVYTYV 191
Cdd:cd19130 75 DRHDGD----EPAAAFAESLAKLGLDQVDLYLVH-WPTPAAGNYV-HTWEAMIELRAAGRTRSIGVSNfLPphLERIVAA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
7SMI_A 192 LDRVPP-GTIDVVLSYCHYCINDSTledmlpyfKSKGVGVINASPLSMG 239
Cdd:cd19130 149 TGVVPAvNQIELHPAYQQRTIRDWA--------QAHDVKIEAWSPLGQG 189
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
35-193 |
1.13e-09 |
|
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding member of aldo-keto reductase family 5 member H1 (AKR5H1). It is a NADPH-dependent aldo-keto reductase that reduces methylglyoxal and phenylglyoxal.
Pssm-ID: 381360 [Multi-domain] Cd Length: 263 Bit Score: 58.33 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASPLGnvfgDVSEEQSIATVIEAfnqGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGR 114
Cdd:cd19134 6 NDDNTMPVIGLGVGELS----DDEAERSVSAALEA---GYRLIDTAAAYG---NEAAVGRAIAASGIPRGELFVTTKLAT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7SMI_A 115 YAEGFDFSAErvtkSIDESLERLQLEYVDILQCHdIEFGSLDQIVnETIPALQKIKESGKTRFIGITGLPLEVYTYVLD 193
Cdd:cd19134 76 PDQGFTASQA----ACRASLERLGLDYVDLYLIH-WPAGREGKYV-DSWGGLMKLREEGLARSIGVSNFTAEHLENLID 148
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
35-271 |
1.68e-09 |
|
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase are founding members of aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381383 [Multi-domain] Cd Length: 265 Bit Score: 57.79 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGasplgnVFGDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGR 114
Cdd:cd19157 5 NNGVKMPWLGLG------VFKVEEGSEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESGIPREELFITSKVWN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 115 YAEGFDfsaeRVTKSIDESLERLQLEYVDILQCHDIEFGSLdqivNETIPALQKIKESGKTRFIGITGLPLevytyvldr 194
Cdd:cd19157 76 ADQGYD----STLKAFEASLERLGLDYLDLYLIHWPVKGKY----KETWKALEKLYKDGRVRAIGVSNFQV--------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
7SMI_A 195 vppgtidvvlsycHYcindstLEDMLPYFKSkgVGVINASplsmglhtengppEWHPASPEikaacKAAADYCKKNG 271
Cdd:cd19157 139 -------------HH------LEDLLADAEI--VPMVNQV-------------EFHPRLTQ-----KELRDYCKKQG 176
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
63-239 |
7.70e-09 |
|
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: 55.44 E-value: 7.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 63 IATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCgrYAEgfDFSAERVTKSIDESLERLQLEYV 142
Cdd:cd19139 17 IDSVRTALELGYRHIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKI--WID--NLSKDKLLPSLEESLEKLRTDYV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 143 DILQCHdieFGSLDQIV--NETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRVPPGTIDVVLSYCHYCINDSTLEDML 220
Cdd:cd19139 90 DLTLIH---WPSPNDEVpvEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIAVVGAGAIATNQIELSPYLQNRKLVAHC 166
|
170
....*....|....*....
7SMI_A 221 pyfKSKGVGVINASPLSMG 239
Cdd:cd19139 167 ---KQHGIHVTSYMTLAYG 182
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
35-186 |
2.13e-08 |
|
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: 54.20 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASPLgnvfgdvSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKC-G 113
Cdd:cd19132 2 NDGTQIPAIGFGTYPL-------KGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRRSGVPREELFVTTKLpG 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
7SMI_A 114 RYaEGFdfsaERVTKSIDESLERLQLEYVDILQCHdIEFGSLDQIVnETIPALQKIKESGKTRFIGITGLPLE 186
Cdd:cd19132 72 RH-HGY----EEALRTIEESLYRLGLDYVDLYLIH-WPNPSRDLYV-EAWQALIEAREEGLVRSIGVSNFLPE 137
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
35-329 |
4.46e-08 |
|
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: 53.66 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGA--SPLGNVFgdvseeqsiATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATK- 111
Cdd:cd19117 9 NTGAEIPAVGLGTwqSKPNEVA---------KAVEAALKAGYRHIDTAAIYG---NEEEVGQGIKDSGVPREEIFITTKl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 112 -CGRYaegfdfsaERVTKSIDESLERLQLEYVDILQCH-------------DIEFGSLDQIVNE-----TIPALQKIKES 172
Cdd:cd19117 77 wCTWH--------RRVEEALDQSLKKLGLDYVDLYLMHwpvpldpdgndflFKKDDGTKDHEPDwdfikTWELMQKLPAT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 173 GKTRFIGITGLPLEVYTYVLD----RVPPGTidvvlsychyciNDSTLEDMLP------YFKSKGVGVINASPLSmglhT 242
Cdd:cd19117 149 GKVKAIGVSNFSIKNLEKLLAspsaKIVPAV------------NQIELHPLLPqpklvdFCKSKGIHATAYSPLG----S 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 243 ENGPPEWHPASPEIkaackaaadyCKKNGKNISKLALQYSLsNKDISttlVGMNSVKqvEENVGAALELETAGKDEktFA 322
Cdd:cd19117 213 TNAPLLKEPVIIKI----------AKKHGKTPAQVIISWGL-QRGYS---VLPKSVT--PSRIESNFKLFTLSDEE--FK 274
|
....*..
7SMI_A 323 EIENILK 329
Cdd:cd19117 275 EIDELHK 281
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
57-180 |
4.75e-08 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 53.54 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 57 VSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCgryaegFDFSAERVTKSIDESLER 136
Cdd:PRK11565 25 ASNEEVITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEASVAREELFITTKL------WNDDHKRPREALEESLKK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....
7SMI_A 137 LQLEYVDILQCHdIEFGSLDQIVnETIPALQKIKESGKTRFIGI 180
Cdd:PRK11565 96 LQLDYVDLYLMH-WPVPAIDHYV-EAWKGMIELQKEGLIKSIGV 137
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
35-283 |
6.84e-08 |
|
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding member of aldo-keto reductase family 1 member G1 (AKR1G1). It may catalyze the reversible reduction of ketones to the respective alcohols using NAD(P)H as a hydride donor.
Pssm-ID: 381380 [Multi-domain] Cd Length: 303 Bit Score: 53.18 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASplgnvfgDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGAS----RDEYIVAT 110
Cdd:cd19154 7 SNGVKMPLIGLGTW-------QSKGAEGITAVRTALKAGYRLIDTAFLYQ---NEEAIGEALAELLEEgvvkREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 K--CGRYAEgfdfsaERVTKSIDESLERLQLEYVDILQCH--------DIEFGSLDQIVNETIP--------ALQKIKES 172
Cdd:cd19154 77 KlwTHEHAP------EDVEEALRESLKKLQLEYVDLYLIHapaafkddEGESGTMENGMSIHDAvdvedvwrGMEKVYDE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 173 GKTRFIGITGLPLEVYTYVLD--RVPPGTIDVvlsYCHYCINDSTLEDMLpyfKSKGVGVINASPL-SMGLHTENGPPEW 249
Cdd:cd19154 151 GLTKAIGVSNFNNDQIQRILDnaRVKPHNNQV---ECHLYFPQKELVEFC---KKHNISVTSYATLgSPGRANFTKSTGV 224
|
250 260 270
....*....|....*....|....*....|....*
7SMI_A 250 HPA-SPEIKAACKAAAdycKKNGKNISKLALQYSL 283
Cdd:cd19154 225 SPApNLLQDPIVKAIA---EKHGKTPAQVLLRYLL 256
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
35-245 |
1.35e-07 |
|
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, EC 1.1.1.365), also called D-galacturonic acid reductase, or GalUR, is a founding member of aldo-keto reductase family 3 member D1 (AKR3D1). It mediates the reduction of D-galacturonate to L-galactonate, the first step in D-galacturonate catabolic process. It also has activity with D-glucuronate and DL-glyceraldehyde. Its activity is seen only with NADPH and not with NADH.
Pssm-ID: 381347 [Multi-domain] Cd Length: 279 Bit Score: 52.15 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFG---ASPlgnvfGDVSeeqsiATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLK---ALGASRDEYIV 108
Cdd:cd19121 7 NTGASIPAVGLGtwqAKA-----GEVK-----AAVAHALKIGYRHIDGALCYQ---NEDEVGEGIKeaiAGGVKREDLFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 109 ATKCgryaegFDFSAERVTKSIDESLERLQLEYVDILQCH----------DIEF-----GSLDQIVN----ETIPALQKI 169
Cdd:cd19121 74 TTKL------WSTYHRRVELCLDRSLKSLGLDYVDLYLVHwpvllnpngnHDLFptlpdGSRDLDWDwnhvDTWKQMEKV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 170 KESGKTRFIGIT--GLPlevytYVLDRVPPGTidVVLSychycINDSTLEDMLP------YFKSKGVGVINASPL-SMG- 239
Cdd:cd19121 148 LKTGKTKAIGVSnySIP-----YLEELLKHAT--VVPA-----VNQVENHPYLPqqelvdFCKEKGILIEAYSPLgSTGs 215
|
....*..
7SMI_A 240 -LHTENG 245
Cdd:cd19121 216 pLISDEP 222
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
58-280 |
1.57e-07 |
|
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: 52.14 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 58 SEEQSIATVIE-AFNQGINFFDTSPYYGatlSEKVLGKCLKALGAS----RDEYIVATKCGRYAEgfdfSAERVTKSIDE 132
Cdd:cd19155 22 SSPEEIETAVDtALEAGYRHIDTAYVYR---NEAAIGNVLKKWIDSgkvkREELFIVTKLPPGGN----RREKVEKFLLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 133 SLERLQLEYVDILQCH---------DIEF-----GSLDQIVNETIPALQKIKE----SGKTRFIGITGLPLEVYTYVLD- 193
Cdd:cd19155 95 SLEKLQLDYVDLYLIHfpvgslskeDDSGkldptGEHKQDYTTDLLDIWKAMEaqvdQGLTRSIGLSNFNREQMARILKn 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 194 -RVPPGTIDVvlsYCHYCINDSTLEDmlpYFKSKGVGVINASPL-SMGLH----TENGPPEWHPASPEIKAACKAAADYC 267
Cdd:cd19155 175 aRIKPANLQV---ELHVYLQQKDLVD---FCSTHSITVTAYAPLgSPGAAhfspGTGSPSGSSPDLLQDPVVKAIAERHG 248
|
250
....*....|...
7SMI_A 268 KKNGKNISKLALQ 280
Cdd:cd19155 249 KSPAQVLLRWLMQ 261
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
63-200 |
1.99e-07 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 51.56 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 63 IATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCgrYAEgfDFSAERVTKSIDESLERLQLEYV 142
Cdd:PRK11172 19 IDSVKTALELGYRAIDTAQIYD---NEAAVGQAIAESGVPRDELFITTKI--WID--NLAKDKLIPSLKESLQKLRTDYV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
7SMI_A 143 DILQCHDIEFGslDQI-VNETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRVPPGTI 200
Cdd:PRK11172 92 DLTLIHWPSPN--DEVsVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIAAVGAENI 148
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
55-308 |
2.11e-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: 381327 [Multi-domain] Cd Length: 304 Bit Score: 51.83 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 55 GDVSEEQSIATVIEAF-NQGINFFDTSPYYGAtlSEKVLGKCLKAL---GASRDEYIVATK--CGRYAEGFDFSAerVTK 128
Cdd:cd19101 17 GGIRDEDAAVRAMAAYvDAGLTTFDCADIYGP--AEELIGEFRKRLrreRDAADDVQIHTKwvPDPGELTMTRAY--VEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 129 SIDESLERLQLEYVDILQCHDIEFGSLDQIvnETIPALQKIKESGKTRFIGITGLPLEVYTYVLDRVPPgtidVVLSYCH 208
Cdd:cd19101 93 AIDRSLKRLGVDRLDLVQFHWWDYSDPGYL--DAAKHLAELQEEGKIRHLGLTNFDTERLREILDAGVP----IVSNQVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 209 YCINDSTLED-MLPYFKSKGVGVINASPLSMGLHTEN--GPPEWHPASPE----------IKA------------ACKAA 263
Cdd:cd19101 167 YSLLDRRPENgMAALCEDHGIKLLAYGTLAGGLLSEKylGVPEPTGPALEtrslqkyklmIDEwggwdlfqellrTLKAI 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
7SMI_A 264 ADyckKNGKNISKLALQYSLSNKDISTTLVGMNSVKQVEENVGAA 308
Cdd:cd19101 247 AD---KHGVSIANVAVRWVLDQPGVAGVIVGARNSEHIDDNVRAF 288
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
35-241 |
3.00e-07 |
|
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: 51.34 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFG-ASPlgnvfgDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGAS----RDEYIVA 109
Cdd:cd19119 7 NTGASIPALGLGtASP------HEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAIDDgsikREELFIT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKCgryaegFDFSAERVTKSIDESLERLQLEYVDILQCH--------DIEFGSLDQIVN--------------ETIPALQ 167
Cdd:cd19119 78 TKV------WPTFYDEVERSLDESLKALGLDYVDLLLVHwpvcfekdSDDSGKPFTPVNddgktryaasgdhiTTYKQLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 168 KIKESGKTRFIGITGLPlEVYtyvldrvppgtIDVVLSYCHY--CINDSTLEDMLP------YFKSKGVGVINASPLSMG 239
Cdd:cd19119 152 KIYLDGRAKAIGVSNYS-IVY-----------LERLIKECKVvpAVNQVELHPHLPqmdlrdFCFKHGILVTAYSPLGSH 219
|
..
7SMI_A 240 LH 241
Cdd:cd19119 220 GA 221
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
60-289 |
3.09e-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: 50.98 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 60 EQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVATKCGRYAEGFdfsaERVTKSIDESLERLQL 139
Cdd:cd19156 23 AEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESGVPREEVFVTTKLWNSDQGY----ESTLAAFEESLEKLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 140 EYVDILQCHDIEFGSLdqivNETIPALQKIKESGKTRFIGITGLPLEVYTYVLD--RVPPGTIDVVLsycHYCINDSTLE 217
Cdd:cd19156 96 DYVDLYLIHWPVKGKF----KDTWKAFEKLYKEKKVRAIGVSNFHEHHLEELLKscKVAPMVNQIEL---HPLLTQEPLR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
7SMI_A 218 DmlpYFKSKGVGVINASPLSMGLHTENgppewhpasPEIKAackaaadYCKKNGKNISKLALQYSLSNKDIS 289
Cdd:cd19156 169 K---FCKEKNIAVEAWSPLGQGKLLSN---------PVLKA-------IGKKYGKSAAQVIIRWDIQHGIIT 221
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
37-184 |
1.24e-06 |
|
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.
Pssm-ID: 381373 [Multi-domain] Cd Length: 319 Bit Score: 49.44 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLGNVF----GDVSEEQSIATVIEAFNQGINFFDTSPYYGATLSEKVLGKCLKALGaSRDEYIVATKC 112
Cdd:cd19147 7 GIRVSPLILGAMSIGDAWsgfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEWMKSRK-NRDQIVIATKF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 113 G----RYAEGFDFSA------ERVTK-SIDESLERLQLEYVDILQCHDIEFGSldqIVNETIPALQKIKESGKTRFIGIT 181
Cdd:cd19147 86 TtdykAYEVGKGKAVnycgnhKRSLHvSVRDSLRKLQTDWIDILYVHWWDYTT---SIEEVMDSLHILVQQGKVLYLGVS 162
|
...
7SMI_A 182 GLP 184
Cdd:cd19147 163 DTP 165
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
32-285 |
1.98e-06 |
|
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: 48.47 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 32 ELGNtGLNLSCVGFGASPLGNvfgdvseeQSIATVIEAF-NQGINFFDTSPYYGatlSEKVLGKCLKALGASRDEYIVAT 110
Cdd:cd19135 6 RLSN-GVEMPILGLGTSHSGG--------YSHEAVVYALkECGYRHIDTAKRYG---CEELLGKAIKESGVPREDLFLTT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 K--CGryaegfDFSAERVTKSIDESLERLQLEYVDIL-----QCHDIEfGSLDQIVNETIPALQKIKESGKTRFIGITGL 183
Cdd:cd19135 74 KlwPS------DYGYESTKQAFEASLKRLGVDYLDLYllhwpDCPSSG-KNVKETRAETWRALEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 184 PLEVYTYVLD--RVPPgtiDVVLSYCHYCINDSTLEDmlpYFKSKGVGVINASPLSmglhteNGPPEWHPASPEIkaack 261
Cdd:cd19135 147 LIEHLEQLLEdcSVVP---HVNQVEFHPFQNPVELIE---YCRDNNIVFEGYCPLA------KGKALEEPTVTEL----- 209
|
250 260
....*....|....*....|....
7SMI_A 262 aaadyCKKNGKNISKLALQYSLSN 285
Cdd:cd19135 210 -----AKKYQKTPAQILIRWSIQN 228
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
35-184 |
2.33e-06 |
|
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent D-xylose reductase (XR) from Pichia stipites, Kluyveromyces lactis, Pachysolen tannophilus, Candida tropicalis, and Candida tenuis, Gre3p from Saccharomyces cerevisiae, XR from Candida tropicalis, Pichia guilliermondii, Debaryomyces hansenli, and Debaryomyces nepalensis, which correspond to aldo-keto reductase family 2 member B1-B10 (AKR2B1-10), respectively. XR (EC1.1.1.307) catalyzes the NAD(P)H dependent reduction of xylose to xylitol.
Pssm-ID: 381339 [Multi-domain] Cd Length: 310 Bit Score: 48.60 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASPLGNvfgDVSEEQsiatVIEAFNQGINFFDTSPYYGatlSEKVLG----KCLKALGASRDEYIVAT 110
Cdd:cd19113 6 NSGYKMPSVGFGCWKLDN---ATAADQ----IYQAIKAGYRLFDGAEDYG---NEKEVGegvnRAIDEGLVKREELFLTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KCGRyaegfDFSA-ERVTKSIDESLERLQLEYVDILQCH-DIEF---------------GSLDQIVNETIP------ALQ 167
Cdd:cd19113 76 KLWN-----NFHDpKNVETALNKTLSDLKLDYVDLFLIHfPIAFkfvpieekyppgfycGDGDNFVYEDVPildtwkALE 150
|
170
....*....|....*..
7SMI_A 168 KIKESGKTRFIGITGLP 184
Cdd:cd19113 151 KLVDAGKIKSIGVSNFP 167
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
59-181 |
6.93e-06 |
|
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: 47.34 E-value: 6.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 59 EEQSIATVIEAFNQGINFFDTSPYYGAtlSEKVLGKCLKALGASRDEYIVATKCG-RYAEGF----------DFSAERVT 127
Cdd:cd19098 34 RAHTHAVLDAAWAAGVRYFDAARSYGR--AEEFLGSWLRSRNIAPDAVFVGSKWGyTYTADWqvdaavhevkDHSLARLL 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
7SMI_A 128 KSIDESLERLQlEYVDILQCHD--IEFGSLDQivNETIPALQKIKESGktRFIGIT 181
Cdd:cd19098 112 KQWEETRSLLG-KHLDLYQIHSatLESGVLED--ADVLAALAELKAEG--VKIGLS 162
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
42-236 |
9.72e-06 |
|
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: 46.36 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 42 CVGFGASplgnvfgDVSEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKAL----GASRDEYIVATKCGRYae 117
Cdd:cd19128 3 RLGFGTY-------KITESESKEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdgGVKREDLFITSKLWPT-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 118 gfDFSAERVTKSIDESLERLQLEYVDILQCH--------------DIEFGSLDQIV--NETIPALQKIKESGKTRFIGIT 181
Cdd:cd19128 71 --MHQPENVKEQLLITLQDLQLEYLDLFLIHwplafdmdtdgdprDDNQIQSLSKKplEDTWRAMEQCVDEKLTKNIGVS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
7SMI_A 182 GLPLEVYTYVLD--RVPPGTIDVvlsYCH-YCINDSTLEdmlpYFKSKGVGVINASPL 236
Cdd:cd19128 149 NYSTKLLTDLLNycKIKPFMNQI---ECHpYFQNDKLIK----FCIENNIHVTAYRPL 199
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
37-181 |
1.72e-05 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 45.73 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 37 GLNLSCVGFGASPLG--NVFGDVSE-EQSIATVIEAFNQGINFFDTSPYYGATLSEKVLgkcLKALGASRDEYIVATKCG 113
Cdd:PRK10376 14 GRSVNRLGYGAMQLAgpGVFGPPKDrDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLI---REALHPYPDDLTIVTKVG 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
7SMI_A 114 --RYAEGF---DFSAERVTKSIDESLERLQLEYVDILQ------CHDIEFGSLDqivnETIPALQKIKESGKTRFIGIT 181
Cdd:PRK10376 91 arRGEDGSwlpAFSPAELRRAVHDNLRNLGLDVLDVVNlrlmgdGHGPAEGSIE----EPLTVLAELQRQGLVRHIGLS 165
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
35-202 |
2.26e-05 |
|
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: 45.53 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGASplgnvFGDVSEEQSiaTVIEAFNQGINFFDTSPYYgatLSEKVLGKCLKALGAS----RDEYIVAT 110
Cdd:cd19129 1 NGSGAIPALGFGTL-----IPDPSATRN--AVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVFKAgkirREDLFVTT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 111 KCGRYaegfDFSAERVTKSIDESLERLQLEYVDILQCH-----------DIEFGSLDQIVN------ETIPALQKIKESG 173
Cdd:cd19129 71 KLWNT----NHRPERVKPAFEASLKRLQLDYLDLYLIHtpfafqpgdeqDPRDANGNVIYDdgvtllDTWRAMERLVDEG 146
|
170 180 190
....*....|....*....|....*....|.
7SMI_A 174 KTRFIGITGLPLEVYTYVLD--RVPPGTIDV 202
Cdd:cd19129 147 RCKAIGLSDVSLEKLREIFEaaRIKPAVVQV 177
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
58-181 |
4.37e-05 |
|
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: 44.41 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 58 SEEQSIATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALGAS----RDEYIVATKCGRYaegfDFSAERVTKSIDES 133
Cdd:cd19111 15 PPEEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWWLKNgklkREEVFITTKLPPV----YLEFKDTEKSLEKS 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 134 LERLQLEYVDILQCH------------DIEFGSLDqiVNETIPALQKIKESGKTRFIGIT 181
Cdd:cd19111 88 LENLKLPYVDLYLIHhpcgfvnkkdkgERELASSD--VTSVWRAMEALVSEGKVKSIGLS 145
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
35-181 |
8.48e-05 |
|
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol 2-dehydrogenase (GLD2, EC 1.1.1.156), also called dihydroxyacetone reductase, is a founding member of aldo-keto reductase family 3 member E1 (AKR3E1). It acts as a glycerol oxidoreductase probably involved in glycerol synthesis.
Pssm-ID: 381348 [Multi-domain] Cd Length: 291 Bit Score: 43.76 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFGAsplgnVFGDVSEEQSIATVIEAFNQGINFFDTSPYYgatLSEKVLGKCLKAL-----GASRDEYIVA 109
Cdd:cd19122 4 NNGVKIPAVGFGT-----FANEGAKGETYAAVTKALDVGYRHLDCAWFY---LNEDEVGDAVRDFlkenpSVKREDLFIC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 110 TKCGRYAEGFdfsaERVTKSIDESLERLQLEYVDILQCH-----------------DIEFGSLDQIVNETIP---ALQKI 169
Cdd:cd19122 76 TKVWNHLHEP----EDVKWSIDNSLKNLKLDYIDLFLVHwpiaaekndqrspklgpDGKYVILKDLTENPEPtwrAMEEI 151
|
170
....*....|..
7SMI_A 170 KESGKTRFIGIT 181
Cdd:cd19122 152 YESGKAKAIGVS 163
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
35-282 |
8.55e-05 |
|
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde reductase 1 (ARI, EC 1.1.1.2), Trichosporonoides megachilieni NADPH-dependent erthyrose reductase (ER) 1/2 and 3, are founding members of aldo-keto reductase family 3 member B1 (AKR3B1), B2 (AKR3B2), and B3 (AKR3B3), respectively. Sporidiobolus salmonicolor NADPH-ARI, also called alcohol dehydrogenase [NADP(+)], or aldehyde reductase I, or ALR 1, catalyzes the asymmetric reduction of aliphatic and aromatic aldehydes and ketones to an R-enantiomer. It reduces ethyl 4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate. Trichosporonoides megachilieni NADPH-ERs catalyze the reduction of D-erythrose.
Pssm-ID: 381344 [Multi-domain] Cd Length: 283 Bit Score: 43.55 E-value: 8.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 35 NTGLNLSCVGFG---ASPlgnvfGDVSeeqsiATVIEAFNQGINFFDTSPYYGatlSEKVLGKCLKAL-----GASRDEY 106
Cdd:cd19118 2 NTGNKIPAIGLGtwqAEP-----GEVG-----AAVKIALKAGYRHLDLAKVYQ---NQHEVGQALKELlkeepGVKREDL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 107 IVATKcgryAEGFDFSAERVTKSIDESLERLQLEYVDILQCH-------------------DIEFGSLDQIVN--ETIPA 165
Cdd:cd19118 69 FITSK----LWNNSHRPEYVEPALDDTLKELGLDYLDLYLIHwpvafkptgdlnpltavptNGGEVDLDLSVSlvDTWKA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 166 LQKIKESGKTRFIGITGLPLEVYTYVLDR--VPPGTIDVvlSYCHYCINDstleDMLPYFKSKGVgVINA-SPLsmGLHT 242
Cdd:cd19118 145 MVELKKTGKVKSIGVSNFSIDHLQAIIEEtgVVPAVNQI--EAHPLLLQD----ELVDYCKSKNI-HITAySPL--GNNL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|
7SMI_A 243 ENGPPEwhPASPEIKAAckaaadyCKKNGKNISKLALQYS 282
Cdd:cd19118 216 AGLPLL--VQHPEVKAI-------AAKLGKTPAQVLIAWG 246
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
66-341 |
3.54e-04 |
|
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: 41.70 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 66 VIEAFNQGINFFDTSPYYGatlSEKVLGKCLKALG----ASRDEYIVATKCgryaegFDFSAERVTKSIDESLERLQLEY 141
Cdd:cd19112 30 ILNAIKIGYRHFDCAADYK---NEKEVGEALAEAFktglVKREDLFITTKL------WNSDHGHVIEACKDSLKKLQLDY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 142 VDILQCH------DIEFGSLDQIVNE--------TIP------ALQKIKESGKTRFIGITGLPL----EVYTYvlDRVPP 197
Cdd:cd19112 101 LDLYLVHfpvatkHTGVGTTGSALGEdgvldidvTISlettwhAMEKLVSAGLVRSIGISNYDIfltrDCLAY--SKIKP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7SMI_A 198 GtIDVVLSYCHYcindsTLEDMLPYFKSKGVGVINASPLSMGLHTENgppEWHPASPEIKAACKAAAdycKKNGKNISKL 277
Cdd:cd19112 179 A-VNQIETHPYF-----QRDSLVKFCQKHGISVTAHTPLGGAAANAE---WFGSVSPLDDPVLKDLA---KKYGKSAAQI 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
7SMI_A 278 ALQYSLSNKDIstTLVGMNSVKQVEENVGaALELETAGKDEKTFAEIENILKpIKNQSWPSGIQ 341
Cdd:cd19112 247 VLRWGIQRNTA--VIPKSSKPERLKENID-VFDFQLSKEDMKLIKSLDRKYR-TNQPAKFWGID 306
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