|
Name |
Accession |
Description |
Interval |
E-value |
| AKR_AKR13C1_2 |
cd19078 |
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ... |
10-309 |
0e+00 |
|
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: 593.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTFGD 89
Cdd:cd19078 1 GLEVSAIGLGCMGMSHGYGPPPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 90 DNK-QQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAV 168
Cdd:cd19078 81 GKPgPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 169 QPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEANEKLVTLL 248
Cdd:cd19078 161 CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVDLL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 249 GELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEAL 309
Cdd:cd19078 241 KEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
|
|
| AKR_AKR13A_13D |
cd19076 |
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ... |
2-305 |
9.30e-175 |
|
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: 486.34 E-value: 9.30e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 2 QKRYLGKSGLEVSALGLGCMGLSHGYGPAtDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIAT 81
Cdd:cd19076 1 PTRKLGTQGLEVSALGLGCMGMSAFYGPA-DEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIAT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFGDDNKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQT 161
Cdd:cd19076 80 KFGIVRDPGSGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEAN 241
Cdd:cd19076 160 IRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNPRFQGENFDKN 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447095029 242 EKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19076 240 LKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
|
|
| PdxI |
COG0667 |
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ... |
1-312 |
1.60e-147 |
|
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: 417.66 E-value: 1.60e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLSHGYGPaTDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVI 79
Cdd:COG0667 1 MEYRRLGRSGLKVSRLGLGTMTFGGPWGG-VDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRpRDDVVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 80 ATKFGFTFGDDNKQQilNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGA 159
Cdd:COG0667 80 ATKVGRRMGPGPNGR--GLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 160 QTIRRAHAVQ----PVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDyRSTVPRFAA 235
Cdd:COG0667 158 EQLRRALAIAeglpPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGD-RAATNFVQG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 236 QAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEALETI 312
Cdd:COG0667 237 YLTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAAV 313
|
|
| AKR_AKR13D1 |
cd19145 |
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ... |
3-305 |
1.61e-128 |
|
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: 369.07 E-value: 1.61e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 3 KRYLGKSGLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK-PFRDRVVIAT 81
Cdd:cd19145 2 RVKLGSQGLEVSAQGLGCMGLSGDYGAPKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALKdGPREKVQLAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFGDDNKQQIlNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQT 161
Cdd:cd19145 82 KFGIHEIGGSGVEV-RGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEAN 241
Cdd:cd19145 161 IRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSHPRFQGENLEKN 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447095029 242 EKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19145 241 KVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
|
|
| AKR_AKR13A1 |
cd19144 |
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ... |
1-319 |
3.61e-119 |
|
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: 346.35 E-value: 3.61e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALKP---FRDRV 77
Cdd:cd19144 1 IPTRTLGRNGPSVPALGFGAMGLSAFYGPPKPDEERFAVLDAAFELGCTFWDTADIYGD--SEELIGRWFKQnpgKREKI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFTFGDDNKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19144 79 FLATKFGIEKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSEC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQPVTALQSEYSMWW---REPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFA 234
Cdd:cd19144 159 SAETLRRAHAVHPIAAVQIEYSPFSldiERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAPRFQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 235 AQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEALETIKI 314
Cdd:cd19144 239 AENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAEV 318
|
....*
gi 447095029 315 VGERY 319
Cdd:cd19144 319 VGERY 323
|
|
| AKR_AKR11B1-like |
cd19084 |
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ... |
10-305 |
2.34e-114 |
|
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: 332.95 E-value: 2.34e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTFgD 89
Cdd:cd19084 1 DLKVSRIGLGTWAIGGTWWGEVDDQESIEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRW-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 90 DNKQQILNSRPEHIREAVEGSLRRLKTDVIDlLYQ-HRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAV 168
Cdd:cd19084 80 GGKGVTKDLSPESIRKEVEQSLRRLQTDYID-LYQiHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 169 QPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEANEKLVTLL 248
Cdd:cd19084 159 GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFFRGENFEKNLEIVDKL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 249 GELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19084 239 KEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEI 295
|
|
| AKR_AKR8A1-2 |
cd19077 |
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ... |
9-305 |
4.38e-100 |
|
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: 296.84 E-value: 4.38e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYG---PYLNEEVVGEALK---PFRDRVVIATK 82
Cdd:cd19077 1 NGKLVGPIGLGLMGLTWRPNPTPD-EEAFETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFRkypEYADKVVLSVK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTFGDDnkqqILNSRPEHIREAVEGSLRRLK-TDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQT 161
Cdd:cd19077 80 GGLDPDTL----RPDGSPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IRRAHAVQPVTALQSEYSMWWREPEQ-EILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEA 240
Cdd:cd19077 156 IRRAHAVHPIAAVEVEYSLFSREIEEnGVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFNGENFEK 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 241 NEKLVTLLGELAAEKGVTSAQIALAWLLAQ-KPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19077 236 NLKLVDALQELAEKKGCTPAQLALAWILAQsGPKIIPIPGSTTLERVEENLKAANVELTDEELKEI 301
|
|
| AKR_AKR13B1 |
cd19088 |
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ... |
13-298 |
4.54e-96 |
|
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: 284.88 E-value: 4.54e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCMGLS--HGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTFGDD 90
Cdd:cd19088 1 VSRLGYGAMRLTgpGIWGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLVRTGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 91 NKQQIlNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAVQP 170
Cdd:cd19088 81 GWWGP-DGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 171 VTALQSEYSMWWREPEqEILPLLEELGIGFVPFSPLGKGFLTgaiKPGttfgkddyrstvprfaaqaieaneklvTLLGE 250
Cdd:cd19088 160 IVSVQNRYNLANRDDE-GVLDYCEAAGIAFIPWFPLGGGDLA---QPG---------------------------GLLAE 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 447095029 251 LAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLS 298
Cdd:cd19088 209 VAARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
|
|
| AKR_AKR11B3 |
cd19085 |
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ... |
13-312 |
3.04e-93 |
|
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: 279.09 E-value: 3.04e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCMGLSHGY-GPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTfgddn 91
Cdd:cd19085 1 VSRLGLGCWQFGGGYwWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPD----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 92 kqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAVQPV 171
Cdd:cd19085 76 -----NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 172 TALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPR-FAAQAIEANEKLVTLLGE 250
Cdd:cd19085 151 DSNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFRhFEPGAEEETFEALEKLKE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 251 LAAEKGVTSAQIALAWLLAQkPWIV-PIPGTTKLNRLEENLAAADIVLSQKDTQQITEALETI 312
Cdd:cd19085 231 IADELGVTMAQLALAWVLQQ-PGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDEISDPL 292
|
|
| Aldo_ket_red |
pfam00248 |
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ... |
16-309 |
1.43e-92 |
|
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: 277.27 E-value: 1.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 16 LGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK---PFRDRVVIATKFGFtfGDDNK 92
Cdd:pfam00248 1 IGLGTWQLGGGWGPISK-EEALEALRAALEAGINFIDTAEVYGDGKSEELLGEALKdypVKRDKVVIATKVPD--GDGPW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 QQilNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRA--HAVQP 170
Cdd:pfam00248 78 PS--GGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAltKGKIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 171 VTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRstvpRFAAQAIEANEKLVTLLGE 250
Cdd:pfam00248 156 IVAVQVEYNLLRRRQEEELLEYCKKNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERR----RLLKKGTPLNLEALEALEE 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 251 LAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEAL 309
Cdd:pfam00248 232 IAKEHGVSPAQVALRWALSKPGVTIPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
|
|
| AKR_EcYajO-like |
cd19079 |
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ... |
6-305 |
1.89e-92 |
|
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: 277.54 E-value: 1.89e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 6 LGKSGLEVSALGLGCMGL-SHGYGPAT-DTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF--RDRVVIAT 81
Cdd:cd19079 5 LGNSGLKVSRLCLGCMSFgDPKWRPWVlDEEESRPIIKRALDLGINFFDTANVYSGGASEEILGRALKEFapRDEVVIAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFGDDNKQQILnSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE----- 156
Cdd:cd19079 85 KVYFPMGDGPNGRGL-SR-KHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGASSmyawq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 -AGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAA 235
Cdd:cd19079 163 fAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTDTAKLKYDY 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 236 QAiEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19079 243 FT-EADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYL 311
|
|
| AKR_AKR11B2 |
cd19149 |
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ... |
3-307 |
1.15e-89 |
|
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: 270.68 E-value: 1.15e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 3 KRYLGKSGLEVSALGLGCMGLshGYGPA---TDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVI 79
Cdd:cd19149 1 YRKLGKSGIEASVIGLGTWAI--GGGPWwggSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 80 ATKFG---------FTFGDDNKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVK 150
Cdd:cd19149 79 ATKCGlrwdreggsFFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 151 HFGLSEAGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTV 230
Cdd:cd19149 159 AIGASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDARSGI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 231 PRFaaqAIEANEKLVTLLGE---LAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19149 239 PWF---SPENREKVLALLEKwkpLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
|
|
| AKR_AKR12A1_B1_C1 |
cd19087 |
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ... |
1-307 |
3.60e-88 |
|
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: 266.75 E-value: 3.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGlshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIA 80
Cdd:cd19087 1 MEYRTLGRTGLKVSRLCLGTMN----FGGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGFTFGDDNKQQILNSRpeHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE---- 156
Cdd:cd19087 77 TKVFGPMGDDPNDRGLSRR--HIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLEETLRALDDLVRQGKIRYIGVSNfaaw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 --AGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTtfgKDDYRSTVPRFA 234
Cdd:cd19087 155 qiAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGK---RPESGRLVERAR 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 235 AQAIEANEKLVTLLGE---LAAEKGVTSAQIALAWLLAQkPWIV-PIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19087 232 YQARYGLEEYRDIAERfeaLAAEAGLTPASLALAWVLSH-PAVTsPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
|
|
| AKR_AKR11A1_11D1 |
cd19083 |
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ... |
3-305 |
6.16e-88 |
|
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: 266.21 E-value: 6.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 3 KRYLGKSGLEVSALGLGCMGLS-HGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIA 80
Cdd:cd19083 1 KVKLGKSDIDVNPIGLGTNAVGgHNLYPNLDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKEYnRNEVVIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGFTFGDDNkqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQ 160
Cdd:cd19083 81 TKGAHKFGGDG--SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNFSLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 161 TIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFAAQAIEA 240
Cdd:cd19083 159 QLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPLFKGERFSE 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447095029 241 NEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19083 239 NLDKVDKLKSIADEKGVTVAHLALAWYLTRPAIDVVIPGAKRAEQVIDNLKALDVTLTEEEIAFI 303
|
|
| AKR_AKR9A_9B |
cd19080 |
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ... |
4-298 |
1.54e-84 |
|
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: 257.53 E-value: 1.54e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKF 83
Cdd:cd19080 1 RLLGRSGLRVSPLALGTMTFGTEWGWGADREEARAMFDAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLATKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 84 GFTF--GDDNKQQilNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE----- 156
Cdd:cd19080 81 TMNRrpGDPNAGG--NHR-KNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDtpawv 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 -AGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTfGKDDYRSTVPRFAA 235
Cdd:cd19080 158 vARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEE-GRAGEAKGVTVGFG 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 236 QAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLS 298
Cdd:cd19080 237 KLTERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLS 299
|
|
| AKR_unchar |
cd19102 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
13-309 |
1.08e-82 |
|
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: 252.59 E-value: 1.08e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCM-----GLSHGYGPAtDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTf 87
Cdd:cd19102 1 LTTIGLGTWaigggGWGGGWGPQ-DDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 88 GDDNKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHA 167
Cdd:cd19102 79 WDEEGRIRRSLKPASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 168 VQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGT--TFGKDDYRSTVPRFAAQAIEANEKLV 245
Cdd:cd19102 159 IHPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPERvaSLPADDWRRRSPFFQEPNLARNLALV 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447095029 246 TLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEAL 309
Cdd:cd19102 239 DALRPIAERHGRTVAQLAIAWVLRRPEVTSAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
|
|
| AKR_AKR9C1 |
cd19081 |
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ... |
5-306 |
1.77e-82 |
|
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: 252.14 E-value: 1.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 5 YLGKSGLEVSALGLGCMGlshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLN-------EEVVGEALK--PFRD 75
Cdd:cd19081 1 PLGRTGLSVSPLCLGTMV----FGWTADEETSFALLDAFVDAGGNFIDTADVYSAWVPgnaggesETIIGRWLKsrGKRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 76 RVVIATKFGFTFGDDNKQqiLNsrPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLS 155
Cdd:cd19081 77 RVVIATKVGFPMGPNGPG--LS--RKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 156 E------AGAQTIRRAHAVQPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKddyRS 228
Cdd:cd19081 153 NysawrlQEALELSRQHGLPRYVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPG---ST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 229 TVPRFAAQAI-EANEKLVTLLGELAAEKGVTSAQIALAWLLAQkPWI-VPIPGTTKLNRLEENLAAADIVLSQKDTQQIT 306
Cdd:cd19081 230 RRGEAAKRYLnERGLRILDALDEVAAEHGATPAQVALAWLLAR-PGVtAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
|
|
| AKR_SF |
cd06660 |
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ... |
14-291 |
4.13e-82 |
|
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: 248.59 E-value: 4.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLshgyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK--PFRDRVVIATKFGFTFGDDN 91
Cdd:cd06660 1 SRLGLGTMTF----GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKgrGNRDDVVIATKGGHPPGGDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 92 KQQILNsrPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAV--- 168
Cdd:cd06660 77 SRSRLS--PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYaka 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 169 ---QPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaaqaieanekl 244
Cdd:cd06660 155 hglPGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLARG----------------------------------- 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447095029 245 vtllgelaaekgvtSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLA 291
Cdd:cd06660 200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEENLA 232
|
|
| AKR_PsAKR |
cd19091 |
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ... |
1-308 |
1.03e-81 |
|
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an uncharacterized aldo-keto reductase from Polaromonas sp.
Pssm-ID: 381317 [Multi-domain] Cd Length: 319 Bit Score: 250.61 E-value: 1.03e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLSHGYGP-----ATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRD 75
Cdd:cd19091 1 MEYRTLGRSGLKVSELALGTMTFGGGGGFfgawgGVDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 76 RVVIATKFGFTFGDdNKQQILNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLS 155
Cdd:cd19091 81 DVLIATKVRGRMGE-GPNDVGLSR-HHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 156 E------AGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAI-----KPGTTFGKD 224
Cdd:cd19091 159 NfsawqiMKALGISERRGLARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYrrgqpAPEGSRLRR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 225 DYRSTVPRFAAQAieanEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQ 304
Cdd:cd19091 239 TGFDFPPVDRERG----YDVVDALREIAKETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIAR 314
|
....
gi 447095029 305 ITEA 308
Cdd:cd19091 315 LDKV 318
|
|
| Aldo_ket_red_shaker-like |
cd19074 |
Shaker potassium channel beta subunit family and similar proteins; This family includes ... |
10-299 |
3.05e-79 |
|
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: 243.65 E-value: 3.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMgLSHGYGpaTDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFGFTFG 88
Cdd:cd19074 1 GLKVSELSLGTW-LTFGGQ--VDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWpRESYVISTKVFWPTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 89 DDNKQQILnSRPeHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHAV 168
Cdd:cd19074 78 PGPNDRGL-SRK-HIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 169 Q------PVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDyRSTVPRFAAQA----I 238
Cdd:cd19074 156 ArqfgliPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGKYRDGIPPPSRS-RATDEDNRDKKrrllT 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 239 EANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQ 299
Cdd:cd19074 235 DENLEKVKKLKPIADELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSP 295
|
|
| AKR_AKR11C1 |
cd19086 |
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ... |
11-292 |
2.29e-72 |
|
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: 223.89 E-value: 2.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 11 LEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTFgDD 90
Cdd:cd19086 1 LEVSEIGFGTWGLGGDWWGDVDDAEAIRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRF-DG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 91 NKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDV-PIEDVAGTVKDLIAEGKVKHFGLS----EAGAQTIRRA 165
Cdd:cd19086 80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVlDNDELFEALEKLKQEGKIRAYGVSvgdpEEALAALRRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 HavqpVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIkpgttfgkddyrstvprfaaqaieaneklv 245
Cdd:cd19086 160 G----IDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTGKL------------------------------ 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447095029 246 tllgelaaekgvtsAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAA 292
Cdd:cd19086 206 --------------AQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
|
|
| AKR_AKR6C1_2 |
cd19143 |
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ... |
1-312 |
4.03e-72 |
|
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: 225.94 E-value: 4.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMgLShgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF---RDRV 77
Cdd:cd19143 1 MEYRRLGRSGLKVSALSFGSW-VT--FGNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwpRSDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFTFGDDNKQQILNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19143 78 VVSTKIFWGGGGPPPNDRGLSR-KHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIEETVRAMNDLIDQGKAFYWGTSEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAV------QPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPLGKGFLTG----AIKPGTTFGKDDY 226
Cdd:cd19143 157 SAQQIEEAHEIadrlglIPPVMEQPQYNLFHRERvEVEYAPLYEKYGLGTTTWSPLASGLLTGkynnGIPEGSRLALPGY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 227 RSTVPRFAAQAIEANEKlVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVlsQKDTQQIT 306
Cdd:cd19143 237 EWLKDRKEELGQEKIEK-VRKLKPIAEELGCSLAQLAIAWCLKNPNVSTVITGATKVEQLEENLKALEVL--PKLTPEVM 313
|
....*.
gi 447095029 307 EALETI 312
Cdd:cd19143 314 EKIEAI 319
|
|
| YdhF |
COG4989 |
Predicted oxidoreductase YdhF [General function prediction only]; |
1-301 |
3.36e-71 |
|
Predicted oxidoreductase YdhF [General function prediction only];
Pssm-ID: 444013 [Multi-domain] Cd Length: 299 Bit Score: 223.10 E-value: 3.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLShgyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK--PF-RDRV 77
Cdd:COG4989 1 MKRIKLGASGLSVSRIVLGCMRLG---EWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKlsPSlREKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFTFGDDNKQQIL---NSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGL 154
Cdd:COG4989 78 ELQTKCGIRLPSEARDNRVkhyDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 155 SEAGAQTIR--RAHAVQPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPLGKGFLTGAikpgttfgkddyrstvp 231
Cdd:COG4989 158 SNFTPSQFEllQSALDQPLVTNQIELSLLHTDAfDDGTLDYCQLNGITPMAWSPLAGGRLFGG----------------- 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 232 rFAAQAIEANEKlvtlLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKD 301
Cdd:COG4989 221 -FDEQFPRLRAA----LDELAEKYGVSPEAIALAWLLRHPAGIQPVIGTTNPERIKAAAAALDIELTREE 285
|
|
| AKR_AKR3F1-like |
cd19072 |
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ... |
10-305 |
1.14e-70 |
|
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: 220.56 E-value: 1.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGY-GPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFgftf 87
Cdd:cd19072 1 GEEVPVLGLGTWGIGGGMsKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFdREDLFITTKV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 88 gddnkqQILNSRPEHIREAVEGSLRRLKTDVIDlLYQ-HRVDPDVPIEDVAGTVKDLIAEGKVKHFGLS--------EAG 158
Cdd:cd19072 77 ------SPDHLKYDDVIKAAKESLKRLGTDYID-LYLiHWPNPSIPIEETLRAMEELVEEGKIRYIGVSnfsleeleEAQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 159 AQTIRrahavQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAikpgttfgkddyrstvprfaaqai 238
Cdd:cd19072 150 SYLKK-----GPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNA------------------------ 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 239 eaneKLVTLLGELAAEKGVTSAQIALAWLLaQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19072 201 ----KGSPLLDEIAKKYGKTPAQIALNWLI-SKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRL 262
|
|
| AKR_BsYcsN_EcYdhF-like |
cd19092 |
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ... |
8-308 |
1.46e-69 |
|
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: 218.19 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 8 KSGLEVSALGLGCMGLShgyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK---PFRDRVVIATKFG 84
Cdd:cd19092 1 PEGLEVSRLVLGCMRLA---DWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALAlnpGLREKIEIQTKCG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 85 FTFGDDN---KQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQT 161
Cdd:cd19092 78 IRLGDDPrpgRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IR--RAHAVQPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPLGKGFLtgaikpgttFGKDDyrstvprfaaqai 238
Cdd:cd19092 158 IEllQSYLDQPLVTNQIELSLLHTEAiDDGTLDYCQLLDITPMAWSPLGGGRL---------FGGFD------------- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 239 EANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEA 308
Cdd:cd19092 216 ERFQRLRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELTREEWYEIYEA 285
|
|
| AKR_AKR11B1 |
cd19148 |
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ... |
10-305 |
1.91e-63 |
|
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: 203.31 E-value: 1.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLG--CMGLSHGYGpaTDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF--RDRVVIATKFGF 85
Cdd:cd19148 1 DLPVSRIALGtwAIGGWMWGG--TDEKEAIETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKEYgkRDRVVIATKVGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 TFgDDNKQQILNSRPEHIREAVEGSLRRLKTDVIDlLYQ-HRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRR 164
Cdd:cd19148 79 EW-DEGGEVVRNSSPARIRKEVEDSLRRLQTDYID-LYQvHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 165 AHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTVPRFA----AQAIEA 240
Cdd:cd19148 157 FRKVAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKFQeprfSQYLAA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 241 NEKlvtlLGELAAEKGVTS-AQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19148 237 VEE----LDKLAQERYGKSvIHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEI 298
|
|
| AKR_AKR14A1_2 |
cd19089 |
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ... |
4-294 |
4.13e-62 |
|
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: 199.79 E-value: 4.13e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGcmgLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLN--EEVVGEALK----PFRDRV 77
Cdd:cd19089 2 RRCGRSGLHLPAISLG---LWHNFGDYTSPEEARELLRTAFDLGITHFDLANNYGPPPGsaEENFGRILKrdlrPYRDEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFT-----FGDdnkqqiLNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHF 152
Cdd:cd19089 79 VISTKAGYGmwpgpYGD------GGSR-KYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 153 GLSEAGAQTIRRAHAV-----QPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYR 227
Cdd:cd19089 152 GISNYPGAKARRAIALlrelgVPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDKYLNGIPPDSRRAA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 228 STVPRFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLaQKPWI--VPIpGTTKLNRLEENLAAAD 294
Cdd:cd19089 232 ESKFLTEEALTPEKLEQLRKLNKIAAKRGQSLAQLALSWVL-RDPRVtsVLI-GASSPSQLEDNVAALK 298
|
|
| AKR_AtPLR-like |
cd19093 |
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ... |
12-301 |
2.40e-61 |
|
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: 197.45 E-value: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 12 EVSALGLGCMGLSH---GYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK--PFRDRVVIATKFGFT 86
Cdd:cd19093 1 EVSPLGLGTWQWGDrlwWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKelGDRDEVVIATKFAPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 FGDDNKQQILNsrpehireAVEGSLRRLKTDVIDLLYQHRVDPDVP-IEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRA 165
Cdd:cd19093 81 PWRLTRRSVVK--------ALKASLERLGLDSIDLYQLHWPGPWYSqIEALMDGLADAVEEGLVRAVGVSNYSADQLRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 HA------VQPVTaLQSEYSMWWREPEQ-EILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRstvpRFAAQAI 238
Cdd:cd19093 153 HKalkergVPLAS-NQVEYSLLYRDPEQnGLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRR----LFGRKNL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 239 EANEKLVTLLGELAAEKGVTSAQIALAWLLAQkpWIVPIPGTTKLNRLEENLAAADIVLSQKD 301
Cdd:cd19093 228 EKVQPLLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEEE 288
|
|
| AKR_AKR10A1_2 |
cd19082 |
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ... |
14-294 |
3.37e-61 |
|
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: 197.00 E-value: 3.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLshgyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYL----NEEVVGEALK--PFRDRVVIATKFGFTF 87
Cdd:cd19082 1 SRIVLGTADF----GTRIDEEEAFALLDAFVELGGNFIDTARVYGDWVergaSERVIGEWLKsrGNRDKVVIATKGGHPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 88 GDDNKQQILNsrPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLS-------EAgAQ 160
Cdd:cd19082 77 LEDMSRSRLS--PEDIRADLEESLERLGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASnwsteriAE-AN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 161 TIRRAHAVQPVTALQSEYSM-WWREP----------EQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRst 229
Cdd:cd19082 154 AYAKAHGLPGFAASSPQWSLaRPNEPpwpgptlvamDEEMRAWHEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRR-- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447095029 230 vpRFAAqaiEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD 294
Cdd:cd19082 232 --VYYS---EENFERLERAKELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDSLAAAD 291
|
|
| AKR_Tas-like |
cd19094 |
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ... |
13-300 |
2.78e-52 |
|
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: 175.06 E-value: 2.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCMGlshgYGPATDTRQAIELIRAAVERGVTFFDTAEVY---------GpyLNEEVVGEALK--PFRDRVVIAT 81
Cdd:cd19094 1 VSEICLGTMT----WGEQNTEAEAHEQLDYAFDEGVNFIDTAEMYpvppspetqG--RTEEIIGSWLKkkGNRDKVVLAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KF----GFTFGDDNKQQILNsrPEHIREAVEGSLRRLKTDVIDLL------------------YQHRVDPDVPIEDVAGT 139
Cdd:cd19094 75 KVagpgEGITWPRGGGTRLD--RENIREAVEGSLKRLGTDYIDLYqlhwpdrytplfgggyytEPSEEEDSVSFEEQLEA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 140 VKDLIAEGKVKHFGLSEAGA-------QTIRRAHAVQPVTaLQSEYSMWWREPEQEilplLEEL----GIGFVPFSPLGK 208
Cdd:cd19094 153 LGELVKAGKIRHIGLSNETPwgvmkflELAEQLGLPRIVS-IQNPYSLLNRNFEEG----LAEAchreNVGLLAYSPLAG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 209 GFLTGAIKPGTTFGK----DDYRSTVPRFA-AQAIEANEKLVtllgELAAEKGVTSAQIALAWLLaQKPWIVP-IPGTTK 282
Cdd:cd19094 228 GVLTGKYLDGAARPEggrlNLFPGYMARYRsPQALEAVAEYV----KLARKHGLSPAQLALAWVR-SRPFVTStIIGATT 302
|
330
....*....|....*...
gi 447095029 283 LNRLEENLAAADIVLSQK 300
Cdd:cd19094 303 LEQLKENIDAFDVPLSDE 320
|
|
| AKR_AKR7A1-5 |
cd19075 |
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ... |
18-292 |
2.77e-51 |
|
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: 171.97 E-value: 2.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 18 LGCMGLSHGyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRdRVVIATKFGFTFGDDNKqqiln 97
Cdd:cd19075 5 LGTMTFGSQ-GRFTTAEAAAELLDAFLERGHTEIDTARVYPDGTSEELLGELGLGER-GFKIDTKANPGVGGGLS----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 98 srPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHA-------VQP 170
Cdd:cd19075 78 --PENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 171 vTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGaikpgtTFGKDDYRSTVPRFAAQAI-----------E 239
Cdd:cd19075 156 -TVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTG------KYKYSEDKAGGGRFDPNNAlgklyrdrywkP 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 240 ANEKLVTLLGELAAEKGVTSAQIALAWLL------AQKPWIVpIPGTTKLNRLEENLAA 292
Cdd:cd19075 229 SYFEALEKVEEAAEKEGISLAEAALRWLYhhsaldGEKGDGV-ILGASSLEQLEENLAA 286
|
|
| AKR_unchar |
cd19752 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-294 |
5.77e-51 |
|
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: 170.59 E-value: 5.77e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLshgyGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYL-------NEEVVGEALK--PFRDRVVIATKFG 84
Cdd:cd19752 1 SELCLGTMYF----GTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTeggvggeSERLIGRWLKdrGNRDDVVIATKVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 85 FTFGDDNkqQILNSR----PEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE---- 156
Cdd:cd19752 77 AGPRDPD--GGPESPeglsAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNfaaw 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 --AGAQTIRRAHAVQPVTALQSEYSMWWREP----------EQEILPLLEELG-IGFVPFSPLGKGFLTGAIKPgttfGK 223
Cdd:cd19752 155 rlERARQIARQQGWAEFSAIQQRHSYLRPRPgadfgvqrivTDELLDYASSRPdLTLLAYSPLLSGAYTRPDRP----LP 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 224 DDYRStvprfaaqaiEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD 294
Cdd:cd19752 231 EQYDG----------PDSDARLAVLEEVAGELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAALD 291
|
|
| AKR_AKR14A2 |
cd19151 |
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ... |
4-294 |
4.32e-50 |
|
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: 168.74 E-value: 4.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGcmgLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLN--EEVVG----EALKPFRDRV 77
Cdd:cd19151 3 NRCGRSGLKLPAISLG---LWHNFGDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPGsaEENFGrilkEDLKPYRDEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFT-----FGDdnkqqiLNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHF 152
Cdd:cd19151 80 IISTKAGYTmwpgpYGD------WGSK-KYLIASLDQSLKRMGLDYVDIFYHHRPDPETPLEETMGALDQIVRQGKALYV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 153 GLSEAGAQTIRRAHAV-----QPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkDDYR 227
Cdd:cd19151 153 GISNYPPEEAREAAAIlkdlgTPCLIHQPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLT-----------DRYL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447095029 228 STVP---RFAAQAIEANEKLVT--------LLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD 294
Cdd:cd19151 222 NGIPedsRAAKGSSFLKPEQITeeklakvrRLNEIAQARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGALD 299
|
|
| AKR_AKR9A1-2 |
cd19146 |
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ... |
10-310 |
6.40e-50 |
|
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: 169.14 E-value: 6.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCM--GLSHGYG-PATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGE--ALKPFRDRVVIATKF- 83
Cdd:cd19146 8 GVRVSPLCLGAMsfGEAWKSMmGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEwmASRGNRDEMVLATKYt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 84 -GFTFGDDNKQQIlNSRPEH---IREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGA 159
Cdd:cd19146 88 tGYRRGGPIKIKS-NYQGNHaksLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 160 QTIR------RAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKG-FLTGAikpgttfgKDDYRSTVPR 232
Cdd:cd19146 167 WVVSkanayaRAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGqFRTEE--------EFKRRGRSGR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447095029 233 FAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEALE 310
Cdd:cd19146 239 KGGPQTEKERKVSEKLEKVAEEKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAYP 316
|
|
| AKR_unchar |
cd19105 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
1-293 |
1.24e-49 |
|
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: 165.84 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLShgygpatdtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVI 79
Cdd:cd19105 1 MPYRTLGKTGLKVSRLGFGGGGLP---------RESPELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKGLrRDKVFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 80 ATKFGFTFGDDNKQQILNSrpehireaVEGSLRRLKTDVIDLLYQHRVDPDVPI---EDVAGTVKDLIAEGKVKHFGLSE 156
Cdd:cd19105 72 ATKASPRLDKKDKAELLKS--------VEESLKRLQTDYIDIYQLHGVDTPEERllnEELLEALEKLKKEGKVRFIGFST 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 AGAQ--TIRRAHAVQPVTALQSEYSMW-WREPEQEILPLLEELGIGFVpfsplgkgfltgAIKPgttfgkddyrstvprf 233
Cdd:cd19105 144 HDNMaeVLQAAIESGWFDVIMVAYNFLnQPAELEEALAAAAEKGIGVV------------AMKT---------------- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 234 AAQAIEANEKLVTLLGelaaeKGVTSAQIALAWLLaQKPWI-VPIPGTTKLNRLEENLAAA 293
Cdd:cd19105 196 LAGGYLQPALLSVLKA-----KGFSLPQAALKWVL-SNPRVdTVVPGMRNFAELEENLAAA 250
|
|
| ARA1 |
COG0656 |
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ... |
9-321 |
4.45e-49 |
|
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440421 [Multi-domain] Cd Length: 259 Bit Score: 164.84 E-value: 4.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLshgygpatDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKfgf 85
Cdd:COG0656 1 NGVEIPALGLGTWQL--------PGEEAAAAVRTALEAGYRHIDTAAMYG---NEEGVGEAIAASgvpREELFVTTK--- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 tfgddnkqqILNS--RPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDvpieDVAGTVK---DLIAEGKVKHFGLS---EA 157
Cdd:COG0656 67 ---------VWNDnhGYDDTLAAFEESLERLGLDYLDLYLIHWPGPG----PYVETWRaleELYEEGLIRAIGVSnfdPE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQPVTaLQSEYSMWWREPeqEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaaqA 237
Cdd:COG0656 134 HLEELLAETGVKPAV-NQVELHPYLQQR--ELLAFCREHGIVVEAYSPLGRG---------------------------K 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 238 IEANEklvtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITeALETikivGE 317
Cdd:COG0656 184 LLDDP----VLAEIAEKHGKTPAQVVLRWHLQRG--VVVIPKSVTPERIRENLDAFDFELSDEDMAAID-ALDR----GE 252
|
....
gi 447095029 318 RYSP 321
Cdd:COG0656 253 RLGP 256
|
|
| COG1453 |
COG1453 |
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only]; |
1-313 |
4.99e-48 |
|
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
Pssm-ID: 441062 [Multi-domain] Cd Length: 365 Bit Score: 164.99 E-value: 4.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLshgygPATDTRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALKPFRDRVVIA 80
Cdd:COG1453 1 MQYRRLGKTGLEVSVLGFGGMRL-----PRKDEEEAEALIRRAIDNGINYIDTARGYGD--SEEFLGKALKGPRDKVILA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFgftfgddnkqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIE------DVAGTVKDLIAEGKVKHFGL 154
Cdd:COG1453 74 TKL----------PPWVRDPEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEkvlkpgGALEALEKAKAEGKIRHIGF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 155 S-EAGAQTIRRAHAVQPVTALQSEYSMWWRE--PEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkddyrsTVP 231
Cdd:COG1453 144 StHGSLEVIKEAIDTGDFDFVQLQYNYLDQDnqAGEEALEAAAEKGIGVIIMKPLKGGRLA----------------NPP 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 232 rfaaqaieanEKLVTLLgelaaEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD--IVLSQKDTQQITEAL 309
Cdd:COG1453 208 ----------EKLVELL-----CPPLSPAEWALRFLLSHPEVTTVLSGMSTPEQLDENLKTADnlEPLTEEELAILERLA 272
|
....
gi 447095029 310 ETIK 313
Cdd:COG1453 273 EELG 276
|
|
| PRK10376 |
PRK10376 |
putative oxidoreductase; Provisional |
10-301 |
1.02e-47 |
|
putative oxidoreductase; Provisional
Pssm-ID: 236676 [Multi-domain] Cd Length: 290 Bit Score: 162.06 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLS--HGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKFGFTF 87
Cdd:PRK10376 14 GRSVNRLGYGAMQLAgpGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTKVGARR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 88 GDDNKQQILNSrPEHIREAVEGSLRRLKTDVIDLLyQHRVDPDV------PIEDVAGTVKDLIAEGKVKHFGLSEAGAQT 161
Cdd:PRK10376 94 GEDGSWLPAFS-PAELRRAVHDNLRNLGLDVLDVV-NLRLMGDGhgpaegSIEEPLTVLAELQRQGLVRHIGLSNVTPTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IRRAHAVQPVTALQSEYSMWWREPEQEILPLLEElGIGFVPFSPLGkGFLtgaikpgttfgkddyrstvprfAAQAiean 241
Cdd:PRK10376 172 VAEARKIAEIVCVQNHYNLAHRADDALIDALARD-GIAYVPFFPLG-GFT----------------------PLQS---- 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 242 eklvTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKD 301
Cdd:PRK10376 224 ----STLSDVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEV 279
|
|
| AKR_PA4992-like |
cd19095 |
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ... |
14-292 |
1.58e-47 |
|
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: 160.48 E-value: 1.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLsHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGpyLNEEVVGEALK-PFRDRVVIATKFGfTFGDDNK 92
Cdd:cd19095 1 SVLGLGTSGI-GRVWGVPSEAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAgLRRDDLFIATKVG-THGEGGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 QQILNSrPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSeAGAQTIRRAHAVQPVT 172
Cdd:cd19095 77 DRKDFS-PAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS-GDGEELEAAIASGVFD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 173 ALQSEYSMWWREpEQEILPLLEELGIGFVPFSPLGKGFLTGAIkpgttFGKDDYRSTVPRFAAqaieaneklvtllgeLA 252
Cdd:cd19095 155 VVQLPYNVLDRE-EEELLPLAAEAGLGVIVNRPLANGRLRRRV-----RRRPLYADYARRPEF---------------AA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 447095029 253 AEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAA 292
Cdd:cd19095 214 EIGGATWAQAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
|
|
| AKR_YeaE |
cd19138 |
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ... |
9-305 |
4.99e-47 |
|
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: 159.72 E-value: 4.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLshGYGPATdTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIATKfgftfg 88
Cdd:cd19138 7 DGTKVPALGQGTWYM--GEDPAK-RAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 89 ddnkqqIL--NSRPEHIREAVEGSLRRLKTDVIDL-LYQHRvdPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRA 165
Cdd:cd19138 78 ------VLpsNASRQGTVRACERSLRRLGTDYLDLyLLHWR--GGVPLAETVAAMEELKKEGKIRAWGVSNFDTDDMEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 HAV---QPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLtgaikpgttFGKDDYRSTVprfaaqaieane 242
Cdd:cd19138 150 WAVpggGNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQGGL---------LRRGLLENPT------------ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 243 klvtlLGELAAEKGVTSAQIALAWLLAQkPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19138 209 -----LKEIAARHGATPAQVALAWVLRD-GNVIAIPKSGSPEHARENAAAADLELTEEDLAEL 265
|
|
| AKR_unchar |
cd19100 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
3-291 |
9.57e-45 |
|
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: 152.64 E-value: 9.57e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 3 KRYLGKSGLEVSALGLGCMGLSHGygpatDTRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALKPFRDRVVIATK 82
Cdd:cd19100 1 YRRLGRTGLKVSRLGFGGGPLGRL-----SQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKGRRDKVFLATK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTfgddnkqqilnsRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAG------TVKDLIAEGKVKHFGLSE 156
Cdd:cd19100 74 TGAR------------DYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEDLDQVFGpggaleALLEAKEEGKIRFIGISG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 AGAQTIRRA------HAVQ-PVTALQSEYsmwwREPEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkddyrst 229
Cdd:cd19100 142 HSPEVLLRAletgefDVVLfPINPAGDHI----DSFREELLPLAREKGVGVIAMKVLAGGRLL----------------- 200
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447095029 230 vprfaaqaieaneklvtllgelaaEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLA 291
Cdd:cd19100 201 ------------------------SGDPLDPEQALRYALSLPPVDVVIVGMDSPEELDENLA 238
|
|
| AKR_AKR14A1 |
cd19150 |
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ... |
2-294 |
1.06e-44 |
|
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: 154.92 E-value: 1.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 2 QKRYLGKSGLEVSALGLGcmgLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLN--EEVVGEALK----PFRD 75
Cdd:cd19150 1 QYRRCGKSGLKLPALSLG---LWHNFGDDTPLETQRAILRTAFDLGITHFDLANNYGPPPGsaEENFGRILRedfaGYRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 76 RVVIATKFGFT-----FGddnkqqILNSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVK 150
Cdd:cd19150 78 ELIISTKAGYDmwpgpYG------EWGSR-KYLLASLDQSLKRMGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 151 HFGLSEAGAQTIRRAHAV-----QPVTALQSEYSMW--WREpEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTtfgK 223
Cdd:cd19150 151 YVGISSYSPERTREAAAIlrelgTPLLIHQPSYNMLnrWVE-ESGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGI---P 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 224 DDYRSTVPRFAAQAI--EANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD 294
Cdd:cd19150 227 EGSRASKERSLSPKMltEANLNSIRALNEIAQKRGQSLAQMALAWVLRDGRVTSALIGASRPEQLEENVGALD 299
|
|
| PRK09912 |
PRK09912 |
L-glyceraldehyde 3-phosphate reductase; Provisional |
1-305 |
5.53e-43 |
|
L-glyceraldehyde 3-phosphate reductase; Provisional
Pssm-ID: 182140 [Multi-domain] Cd Length: 346 Bit Score: 151.30 E-value: 5.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGcmgLSHGYG--PATDTRQAieLIRAAVERGVTFFDTAEVYGPYLN--EEVVG----EALKP 72
Cdd:PRK09912 13 MQYRYCGKSGLRLPALSLG---LWHNFGhvNALESQRA--ILRKAFDLGITHFDLANNYGPPPGsaEENFGrllrEDFAA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 73 FRDRVVIATKFGFT-----FGDDNKQQILNSrpehireAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEG 147
Cdd:PRK09912 88 YRDELIISTKAGYDmwpgpYGSGGSRKYLLA-------SLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 148 KVKHFGLSE-AGAQTIRRAHAVQ----PVTALQSEYSMWWREPEQE-ILPLLEELGIGFVPFSPLGKGFLTG----AIKP 217
Cdd:PRK09912 161 KALYVGISSySPERTQKMVELLRewkiPLLIHQPSYNLLNRWVDKSgLLDTLQNNGVGCIAFTPLAQGLLTGkylnGIPQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 218 GTTFGKD--DYRSTVPRFAAqaiEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAA-AD 294
Cdd:PRK09912 241 DSRMHREgnKVRGLTPKMLT---EANLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAlNN 317
|
330
....*....|.
gi 447095029 295 IVLSQKDTQQI 305
Cdd:PRK09912 318 LTFSTEELAQI 328
|
|
| AKR_AKR3F1 |
cd19137 |
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ... |
10-305 |
8.92e-43 |
|
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: 148.49 E-value: 8.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGYGPA-TDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFGFTf 87
Cdd:cd19137 1 GEKIPALGLGTWGIGGFLTPDySRDEEMVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFpREDLFIVTKVWPT- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 88 gddnkqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHA 167
Cdd:cd19137 80 ---------NLRYDDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 168 V--QPVTALQSEYSMWWREPEQE-ILPLLEELGIGFVPFSPLGKGFltgaikpgttfgkddyrstvprfaaqaieanEKL 244
Cdd:cd19137 151 KsqTPIVCNQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRGL-------------------------------EKT 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 245 VTLLGELAAEKGVTSAQIALAWLLaQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19137 200 NRTLEEIAKNYGKTIAQIALAWLI-QKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLL 259
|
|
| AKR_galDH |
cd19163 |
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ... |
1-294 |
1.03e-42 |
|
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: 149.24 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLSHGYGPaTDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVI 79
Cdd:cd19163 1 MKYRKLGKTGLKVSKLGFGASPLGGVFGP-VDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIpRDSYYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 80 ATKFGfTFGDDNKqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRV----DPDVPIEDVAGTVKDLIAEGKVKHFGLS 155
Cdd:cd19163 80 ATKVG-RYGLDPD-KMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIefapSLDQILNETLPALQKLKEEGKVRFIGIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 156 EAGAQTIRR--AHAVQPVTALQS--EYSMWWREPEqEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYRSTvp 231
Cdd:cd19163 158 GYPLDVLKEvlERSPVKIDTVLSycHYTLNDTSLL-ELLPFFKEKGVGVINASPLSMGLLTERGPPDWHPASPEIKEA-- 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 232 rfAAQAIeaneklvtllgELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAAD 294
Cdd:cd19163 235 --CAKAA-----------AYCKSRGVDISKLALQFALSNPDIATTLVGTASPENLRKNLEAAE 284
|
|
| AKR_AKR3F2_3 |
cd19073 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ... |
15-305 |
1.23e-42 |
|
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: 147.42 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 15 ALGLGCMGLSHgygpatdtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFgftfgddn 91
Cdd:cd19073 3 ALGLGTWQLRG--------DDCANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESgvpREDLFITTKV-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 92 kqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAgaqTIR-----RAH 166
Cdd:cd19073 64 --WRDHLRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNF---TIElleeaLDI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 167 AVQPVTALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrsTVPRfaaqaieaneklVT 246
Cdd:cd19073 139 SPLPIAVNQVEFHPFL--YQAELLEYCRENDIVITAYSPLARG-------------------EVLR------------DP 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 247 LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19073 186 VIQEIAEKYDKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDWELTSEDVAKI 242
|
|
| AKR_AKR1-5-like |
cd19071 |
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ... |
15-305 |
1.41e-42 |
|
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: 147.63 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 15 ALGLGCMGLSHGygpatdtrQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGFTfgddn 91
Cdd:cd19071 3 LIGLGTYKLKPE--------ETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIRESgvpREELFITTKLWPT----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 92 kqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQH------RVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRR- 164
Cdd:cd19071 67 -----DHGYERVREALEESLKDLGLDYLDLYLIHwpvpgkEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEEl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 165 -AHA-VQPVtALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkddyrstvprfaaqaIEANE 242
Cdd:cd19071 142 lAAArIKPA-VNQIELHPYL--QQKELVEFCKEHGIVVQAYSPLGRGRRP-------------------------LLDDP 193
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 243 KLVtllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19071 194 VLK----EIAKKYGKTPAQVLLRWALQRG--VVVIPKSSNPERIKENLDVFDFELSEEDMAAI 250
|
|
| AKR_AKR15A-like |
cd19090 |
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ... |
14-293 |
6.64e-41 |
|
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: 143.85 E-value: 6.64e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALK-PFRDRVVIATKFGFTFGDDNK 92
Cdd:cd19090 1 SALGLGTAGLGGVFGGVDD-DEAVATIRAALDLGINYIDTAPAYGD--SEERLGLALAeLPREPLVLSTKVGRLPEDTAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 QQilnsrPEHIREAVEGSLRRLKTDVIDLLYQHrvDPD-VPIEDVAG------TVKDLIAEGKVKHFGLS----EAGAQT 161
Cdd:cd19090 78 YS-----ADRVRRSVEESLERLGRDRIDLLMIH--DPErVPWVDILApggaleALLELKEEGLIKHIGLGggppDLLRRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 162 IRRAHAVQPVTALqsEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGaikpgttfGKDDYRSTVPRFAAQaiEAN 241
Cdd:cd19090 151 IETGDFDVVLTAN--RYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAG--------RPPERVRYTYRWLSP--ELL 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447095029 242 EKLVTLLgELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAA 293
Cdd:cd19090 219 DRAKRLY-ELCDEHGVPLPALALRFLLRDPRISTVLVGASSPEELEQNVAAA 269
|
|
| AKR_unchar |
cd19101 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
12-309 |
1.11e-40 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381327 [Multi-domain] Cd Length: 304 Bit Score: 144.27 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 12 EVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALKPFR------DRVVIATKFGF 85
Cdd:cd19101 1 TISRVINGMWQLSGGHGGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRrerdaaDDVQIHTKWVP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 tfgDDNKQQILnsrPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVP-IEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRR 164
Cdd:cd19101 79 ---DPGELTMT---RAYVEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLRE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 165 A-HAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLT----GAIKPG----TTFGKDDYRSTVPRFAA 235
Cdd:cd19101 153 IlDAGVPIVSNQVQYSLLDRRPENGMAALCEDHGIKLLAYGTLAGGLLSekylGVPEPTgpalETRSLQKYKLMIDEWGG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447095029 236 QaiEANEKLVTLLGELAAEKGVTSAQIALAWLLaQKPWIV-PIPGTTKLNRLEENLAAADIVLSQKDTQQITEAL 309
Cdd:cd19101 233 W--DLFQELLRTLKAIADKHGVSIANVAVRWVL-DQPGVAgVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
|
|
| AKR_AKR3F3 |
cd19140 |
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ... |
10-305 |
1.17e-39 |
|
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: 140.09 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHgygpatdtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALK----PfRDRVVIATKFGF 85
Cdd:cd19140 5 GVRIPALGLGTYPLTG--------EECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAasgvP-RDELFLTTKVWP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 TfgddnkqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRA 165
Cdd:cd19140 73 D----------NYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 --HAVQPVTALQSEYSMWWRepEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkDDYrstvprfaaqaieanek 243
Cdd:cd19140 143 veLSEAPLFTNQVEYHPYLD--QRKLLDAAREHGIALTAYSPLARGEVL-----------KDP----------------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447095029 244 lvtLLGELAAEKGVTSAQIALAWLLaQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19140 193 ---VLQEIGRKHGKTPAQVALRWLL-QQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARI 250
|
|
| AKR_AKR9A3_9B1-4 |
cd19147 |
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ... |
9-305 |
2.31e-39 |
|
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: 141.12 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGL----SHGYGPaTDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGE--ALKPFRDRVVIATK 82
Cdd:cd19147 6 AGIRVSPLILGAMSIgdawSGFMGS-MDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIATK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTF--GDDNKQQILNSRPEHIRE---AVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE- 156
Cdd:cd19147 85 FTTDYkaYEVGKGKAVNYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSDt 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 -----AGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKG-FLTGAIKPGTTFGKDDYRSTV 230
Cdd:cd19147 165 pawvvSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWDVLGGGkFQSKKAVEERKKNGEGLRSFV 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 231 prFAAQAIEANEKLVTLLGELAAEKGVTS-AQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19147 245 --GGTEQTPEEVKISEALEKVAEEHGTESvTAIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPEEIEYL 318
|
|
| AKR_KCAB3B_AKR6A9-like |
cd19160 |
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ... |
1-307 |
2.63e-39 |
|
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: 141.28 E-value: 2.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKP---FRDRV 77
Cdd:cd19160 3 MKYRNLGKSGLRVSCLGLGTWVT---FGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSkgwRRSSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFgFTFGDDNKQQILNSRpeHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19160 80 VVTTKI-YWGGQAETERGLSRK--HIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQ------PVTALQSEYSMWWREPEQEILP-LLEELGIGFVPFSPLGKGFLTGaikpgttfgkdDYRSTV 230
Cdd:cd19160 157 SAMEIMEAYSVArqfnliPPVCEQAEYHLFQREKVEMQLPeLYHKIGVGSVTWSPLACGLITG-----------KYDGRV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 231 PRFAAQAIEA----NEKL-----------VTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADi 295
Cdd:cd19160 226 PDTCRAAVKGyqwlKEKVqseegkkqqakVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQ- 304
|
330
....*....|..
gi 447095029 296 VLSQKDTQQITE 307
Cdd:cd19160 305 VLSQLTPQTVME 316
|
|
| Aldo_ket_red_shaker |
cd19141 |
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ... |
4-305 |
5.08e-38 |
|
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: 137.19 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGCMGLshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKP---FRDRVVIA 80
Cdd:cd19141 3 RNLGKSGLRVSCLGLGTWVT---FGSQISDEVAEELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKkgwRRSSYVIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFgFTFGDDNKQQILnSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQ 160
Cdd:cd19141 80 TKI-FWGGKAETERGL-SR-KHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSAM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 161 TIRRAHAVQ------PVTALQSEYSMWWREPEQEILP-LLEELGIGFVPFSPLGKGFLTGaikpgttfgkdDYRSTVPRF 233
Cdd:cd19141 157 EIMEAYSVArqfnliPPIVEQAEYHLFQREKVEMQLPeLFHKIGVGAMTWSPLACGILSG-----------KYDDGVPEY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 234 AAQAI------------EANEKLVTLLGELA--AEK-GVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVls 298
Cdd:cd19141 226 SRASLkgyqwlkekilsEEGRRQQAKLKELQiiADRlGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVL-- 303
|
....*..
gi 447095029 299 QKDTQQI 305
Cdd:cd19141 304 PKLTPNI 310
|
|
| AKR_AKR6B1 |
cd19142 |
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ... |
1-312 |
2.78e-36 |
|
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: 132.97 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMglsHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF---RDRV 77
Cdd:cd19142 1 LKYRNLGKSGLRVSNVGLGTW---STFSTAISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILKKKgwkRSSY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFGFTFGDDNKQQilnSRpEHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSE- 156
Cdd:cd19142 78 IVSTKIYWSYGSEERGL---SR-KHIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 157 -----AGAQTIRRAHAVQPVTALQSEYSMWWREP-EQEILPLLEELGIGFVPFSPL------GKGFLTGAIKPGTTFGKD 224
Cdd:cd19142 154 spveiMEAFSIARQFNCPTPICEQSEYHMFCREKmELYMPELYNKVGVGLITWSPLslgldpGISEETRRLVTKLSFKSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 225 DYR-STVPRFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAadIVLSQKDTQ 303
Cdd:cd19142 234 KYKvGSDGNGIHEETRRASHKLRELSLIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNS--LQLLPKLNS 311
|
....*....
gi 447095029 304 QITEALETI 312
Cdd:cd19142 312 AVMEELERI 320
|
|
| AKR_unchar |
cd19104 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
2-294 |
1.51e-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: 381330 [Multi-domain] Cd Length: 321 Bit Score: 131.23 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 2 QKRYLGKSGLEVSALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPFRDRVVIAT 81
Cdd:cd19104 1 KYRRFGRTGLKVSELTFGGGGIGGLMGRTTR-EEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYITT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGftFGDDNkqqiLNSRPEHIREAVEGSLRRLKTDVIDLLYQH-------RVDPDVPI--------EDVAGTVKDLIAE 146
Cdd:cd19104 80 KVR--LDPDD----LGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderDKPVGGTLsttdvlglGGVADAFERLRSE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 147 GKVKHFGLSEAG-AQTIRRAHAVQPVTALQSEY------------SMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTG 213
Cdd:cd19104 154 GKIRFIGITGLGnPPAIRELLDSGKFDAVQVYYnllnpsaaearpRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALTT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 214 AIK-----PGTTFGKD--DYRSTVPrFAAqaieaneklvtllgeLAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRL 286
Cdd:cd19104 234 SLDrgreaPPTSDSDVaiDFRRAAA-FRA---------------LAREWGETLAQLAHRFALSNPGVSTVLVGVKNREEL 297
|
....*...
gi 447095029 287 EENLAAAD 294
Cdd:cd19104 298 EEAVAAEA 305
|
|
| AKR_unchar |
cd19103 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
42-308 |
2.43e-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: 381329 [Multi-domain] Cd Length: 299 Bit Score: 130.15 E-value: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 42 AAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFgftfgddnKQQILNSRPEHIREAVEGSLRRLKTDVID 120
Cdd:cd19103 40 KAMAAGLNLWDTAAVYGMGASEKILGEFLKRYpREDYIISTKF--------TPQIAGQSADPVADMLEGSLARLGTDYID 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 121 LLYQHrvDPDvpieDVAGTVKDLIA---EGKVKHFGLSEAGAQTIRRAHAVQ-----PVTALQSEYSMWWREPEQE-ILP 191
Cdd:cd19103 112 IYWIH--NPA----DVERWTPELIPllkSGKVKHVGVSNHNLAEIKRANEILakagvSLSAVQNHYSLLYRSSEEAgILD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 192 LLEELGIGFVPFSPLGKGFLTGA-----IKPGTTFGKDDYRSTVPRFaaqaieanEKLVTLLGELAAEKGVTSAQIALAW 266
Cdd:cd19103 186 YCKENGITFFAYMVLEQGALSGKydtkhPLPEGSGRAETYNPLLPQL--------EELTAVMAEIGAKHGASIAQVAIAW 257
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 447095029 267 LLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEA 308
Cdd:cd19103 258 AIAKG--TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
|
|
| AKR_KCAB1B_AKR6A3-like |
cd19159 |
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ... |
1-312 |
8.33e-35 |
|
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: 129.39 E-value: 8.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGLshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKP---FRDRV 77
Cdd:cd19159 1 MKYRNLGKSGLRVSCLGLGTWVT---FGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKkgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFgFTFGDDNKQQILNSRpeHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19159 78 VITTKL-YWGGKAETERGLSRK--HIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQ------PVTALQSEYSMWWREPEQEILP-LLEELGIGFVPFSPLGKGFLTGAIKPGTtfgKDDYRSTV 230
Cdd:cd19159 155 SAMEIMEAYSVArqfnmiPPVCEQAEYHLFQREKVEVQLPeLYHKIGVGAMTWSPLACGIISGKYGNGV---PESSRASL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 231 P-------RFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIVlsQKDTQ 303
Cdd:cd19159 232 KcyqwlkeRIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVL--PKMTS 309
|
....*....
gi 447095029 304 QITEALETI 312
Cdd:cd19159 310 HVVNEIDNI 318
|
|
| AKR_AKR3C2-3 |
cd19120 |
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ... |
10-308 |
1.31e-31 |
|
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: 119.26 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKfgft 86
Cdd:cd19120 1 GSKIPAIAFGTGTAWYKSGDDDIQRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESgvpREDLFITTK---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 fgddnkqqiLNSRPEHIREAVEGSLRRLKTDVIDLLYQH---RVDPDVPieDVAGTVKDLIA---EGKVKHFGLSEAGAQ 160
Cdd:cd19120 74 ---------VSPGIKDPREALRKSLAKLGVDYVDLYLIHspfFAKEGGP--TLAEAWAELEAlkdAGLVRSIGVSNFRIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 161 TIRR--AHAVQPVTALQSEYSMWWREPEQEILPLLEELGI---GFVPFSPLGKGfltgaikpgttfgkddyrstvprfaa 235
Cdd:cd19120 143 DLEEllDTAKIKPAVNQIEFHPYLYPQQPALLEYCREHGIvvsAYSPLSPLTRD-------------------------- 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 236 qaieANEKLVTLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITEA 308
Cdd:cd19120 197 ----AGGPLDPVLEKIAEKYGVTPAQVLLRWALQKG--IVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKA 263
|
|
| AKR_KCAB2B_AKR6A1-like |
cd19158 |
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ... |
1-296 |
2.70e-31 |
|
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: 119.80 E-value: 2.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMgLSHGyGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKP---FRDRV 77
Cdd:cd19158 1 QFYRNLGKSGLRVSCLGLGTW-VTFG-GQITD-EMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKkgwRRSSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 78 VIATKFgFTFGDDNKQQILNSRpeHIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19158 78 VITTKI-FWGGKAETERGLSRK--HIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQ------PVTALQSEYSMWWREPEQEILP-LLEELGIGFVPFSPLGKGFLTG----AIKPGTTFGKDDY 226
Cdd:cd19158 155 SSMEIMEAYSVArqfnliPPICEQAEYHMFQREKVEVQLPeLFHKIGVGAMTWSPLACGIVSGkydsGIPPYSRASLKGY 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 227 RSTVPRFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIV 296
Cdd:cd19158 235 QWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVL 304
|
|
| AKR_Fe-S_oxidoreductase |
cd19096 |
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ... |
14-294 |
6.35e-31 |
|
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: 116.89 E-value: 6.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFGFTfgddnk 92
Cdd:cd19096 1 SVLGFGTMRLPESDDDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGpREKFYLATKLPPW------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 qqiLNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVD-PDVPIEDVAGTVKDLI----AEGKVKHFGLS-EAGAQTIRRA- 165
Cdd:cd19096 75 ---SVKSAEDFRRILEESLKRLGVDYIDFYLLHGLNsPEWLEKARKGGLLEFLekakKEGLIRHIGFSfHDSPELLKEIl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 --HAVQPVTaLQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkddyrstvprfaaqaiEANEK 243
Cdd:cd19096 152 dsYDFDFVQ-LQYNYLDQENQAGRPGIEYAAKKGMGVIIMEPLKGGGLA--------------------------NNPPE 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447095029 244 LVTLLgelaAEKGVTSAQIALAWLLAQkPWI-VPIPGTTKLNRLEENLAAAD 294
Cdd:cd19096 205 ALAIL----CGAPLSPAEWALRFLLSH-PEVtTVLSGMSTPEQLDENIAAAD 251
|
|
| AKR_AKR1G1_CeAKR |
cd19154 |
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ... |
8-307 |
1.20e-28 |
|
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: 112.12 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 8 KSGLEVSALGLGCMGLShgygPATdtrqAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIA 80
Cdd:cd19154 7 SNGVKMPLIGLGTWQSK----GAE----GITAVRTALKAGYRLIDTAFLYQ---NEEAIGEALAELleegvvkREDLFIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGFTFgddnkqqilnSRPEHIREAVEGSLRRLKTDVIDLL-------------------YQHRVDPDVPIEDVAGTVK 141
Cdd:cd19154 76 TKLWTHE----------HAPEDVEEALRESLKKLQLEYVDLYlihapaafkddegesgtmeNGMSIHDAVDVEDVWRGME 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 142 DLIAEGKVKHFGLSEAGAQTIRRAHAVQ--PVTALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGkgfltgaiKPGt 219
Cdd:cd19154 146 KVYDEGLTKAIGVSNFNNDQIQRILDNArvKPHNNQVECHLYF--PQKELVEFCKKHNISVTSYATLG--------SPG- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 220 tfgkddyRSTVPRFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQ 299
Cdd:cd19154 215 -------RANFTKSTGVSPAPNLLQDPIVKAIAEKHGKTPAQVLLRYLLQRG--IAVIPKSATPSRIKENFNIFDFSLSE 285
|
....*...
gi 447095029 300 KDTQQITE 307
Cdd:cd19154 286 EDMATLEE 293
|
|
| AKR_ARA2 |
cd19164 |
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ... |
11-300 |
2.54e-28 |
|
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: 111.21 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 11 LEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPylNEEVVGEALK----PF-RDRVVIATKFGF 85
Cdd:cd19164 11 AGLPPLIFGAATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGP--SEIILGRALKalrdEFpRDTYFIITKVGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 TFGDDnkqqiLNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDpDVPIEDVAGTVK---DLIAEGKVKHFGLSEAGAQTI 162
Cdd:cd19164 89 YGPDD-----FDYSPEWIRASVERSLRRLHTDYLDLVYLHDVE-FVADEEVLEALKelfKLKDEGKIRNVGISGYPLPVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 163 RR-AHAV-----QPVTALQSeYSMWwrEPEQEILPLLEE--LGIGFVPF----SPLGKGFLTGAIKPGTTFGKDDYRSTV 230
Cdd:cd19164 163 LRlAELArttagRPLDAVLS-YCHY--TLQNTTLLAYIPkfLAAAGVKVvlnaSPLSMGLLRSQGPPEWHPASPELRAAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 231 PRFAaqaieaneklvtllgELAAEKGVTSAQIALAWLLAQKPWIVP-IPGTTKLNRLEENLAAADIVLSQK 300
Cdd:cd19164 240 AKAA---------------EYCQAKGTDLADVALRYALREWGGEGPtVVGCSNVDELEEAVEAYWSVLAGA 295
|
|
| AKR_AKR15A |
cd19152 |
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ... |
14-293 |
2.54e-27 |
|
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: 108.85 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF-RDRVVIATKFGFTFGDDNK 92
Cdd:cd19152 1 PKLGFGTAPLGNLYEAVSD-EEAKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELgREDYVISTKVGRLLVPLQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 QQ-----ILNSRPEH----------IREAVEGSLRRLKTDVIDLLYQHRVDPDVPI--------EDVAGTVKDLI---AE 146
Cdd:cd19152 80 VEptfepGFWNPLPFdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGaesdehfaQAIKGAFRALEelrEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 147 GKVKHFGLSEAGAQTIRRAHAVQPVTA--LQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGaikpGTTFGKD 224
Cdd:cd19152 160 GVIKAIGLGVNDWEVILRILEEADLDWvmLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAG----GDNFDYY 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 225 DYRSTVPRFAAQAIEaneklvtlLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAA 293
Cdd:cd19152 236 EYGPAPPELIARRDR--------IEALCEQHGVSLAAAALQFALAPPAVASVAPGASSPERVEENVALL 296
|
|
| AKR_FDH |
cd19162 |
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ... |
14-294 |
1.92e-25 |
|
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: 103.21 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLshGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEAL--KPfRDRVVIATKFG--FTFGD 89
Cdd:cd19162 1 PRLGLGAASL--GNLARAGEDEAAATLDAAWDAGIRYFDTAPLYGLGLSERRLGAALarHP-RAEYVVSTKVGrlLEPGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 90 DNKQQILNSRP----EHIREAVEGSLRRLKTDVIDLLYQHRVDP--DVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIR 163
Cdd:cd19162 78 AGRPAGADRRFdfsaDGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGVTDWAALL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 164 RAHAVQPVTA--LQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFgkdDYRSTVPRFAAQAIEan 241
Cdd:cd19162 158 RAARRADVDVvmVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRY---DYRPATPEVLARARR-- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 447095029 242 eklvtlLGELAAEKGVTSAQIALAWLLaQKPWIVPI-PGTTKLNRLEENLAAAD 294
Cdd:cd19162 233 ------LAAVCRRYGVPLPAAALQFPL-RHPAVASVvVGAASPAELRDNLALLR 279
|
|
| tas |
PRK10625 |
putative aldo-keto reductase; Provisional |
1-320 |
2.14e-25 |
|
putative aldo-keto reductase; Provisional
Pssm-ID: 236727 [Multi-domain] Cd Length: 346 Bit Score: 104.17 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 1 MQKRYLGKSGLEVSALGLGCMGlshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYgPY--------LNEEVVGEALKP 72
Cdd:PRK10625 1 MQYHRIPHSSLEVSTLGLGTMT----FGEQNSEADAHAQLDYAVAQGINLIDVAEMY-PVpprpetqgLTETYIGNWLAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 73 F--RDRVVIATKF-GFTFGDDNK---QQILNSRpeHIREAVEGSLRRLKTDVIDLL----------------YQHRVD-P 129
Cdd:PRK10625 76 RgsREKLIIASKVsGPSRNNDKGirpNQALDRK--NIREALHDSLKRLQTDYLDLYqvhwpqrptncfgklgYSWTDSaP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 130 DVPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRR------AHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPF 203
Cdd:PRK10625 154 AVSLLETLDALAEQQRAGKIRYIGVSNETAFGVMRylhlaeKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 204 SPLGKGFLTG----AIKPGttfgkdDYRSTV-PRFAAQAIEANEKLVTLLGELAAEKGVTSAQIALAWlLAQKPWIVP-I 277
Cdd:PRK10625 234 SCLAFGTLTGkylnGAKPA------GARNTLfSRFTRYSGEQTQKAVAAYVDIAKRHGLDPAQMALAF-VRRQPFVAStL 306
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 447095029 278 PGTTKLNRLEENLAAADIVLSQkdtqqitEALETIKIVGERYS 320
Cdd:PRK10625 307 LGATTMEQLKTNIESLHLTLSE-------EVLAEIEAVHQVYT 342
|
|
| AKR_AKR15A1 |
cd19161 |
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ... |
14-296 |
1.30e-24 |
|
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: 101.25 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEAL--KPfRDRVVIATKFGFTFGDDN 91
Cdd:cd19161 1 SELGLGTAGLGNLYTAVSN-ADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLreKP-RDEFVLSTKVGRLLKPAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 92 KQQILNSRPEH---------------IREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVA---------GTVK---DLI 144
Cdd:cd19161 79 EGSVPDPNGFVdplpfeivydysydgIMRSFEDSLQRLGLNRIDILYVHDIGVYTHGDRKErhhfaqlmsGGFKaleELK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 145 AEGKVKHFGLSEAGAQTIRRAHAVQPVTA--LQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFg 222
Cdd:cd19161 159 KAGVIKAFGLGVNEVQICLEALDEADLDCflLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGAKF- 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447095029 223 kdDYRSTVPRFAAQAIEaneklvtlLGELAAEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIV 296
Cdd:cd19161 238 --NYGDAPAEIISRVME--------IEKICDAYNVPLAAAALQFPLRHPAVASVLTGARNPAQLRQNVEAFQTD 301
|
|
| PLN02587 |
PLN02587 |
L-galactose dehydrogenase |
4-313 |
2.35e-24 |
|
L-galactose dehydrogenase
Pssm-ID: 178198 [Multi-domain] Cd Length: 314 Bit Score: 100.62 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGCMGLSHGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF---RDRVVIA 80
Cdd:PLN02587 2 RELGSTGLKVSSVGFGASPLGSVFGPVSE-EDAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALKALgipREKYVVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKF-----GFTFGddnkqqilnsrPEHIREAVEGSLRRLKTDVIDLLYQHRV---DPDVPIEDVAGTVKDLIAEGKVKHF 152
Cdd:PLN02587 81 TKCgrygeGFDFS-----------AERVTKSVDESLARLQLDYVDILHCHDIefgSLDQIVNETIPALQKLKESGKVRFI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 153 GLSEAGAQTIRRA-HAVQP----VTALQSEYSMWWREPEqEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFGKDDYR 227
Cdd:PLN02587 150 GITGLPLAIFTYVlDRVPPgtvdVILSYCHYSLNDSSLE-DLLPYLKSKGVGVISASPLAMGLLTENGPPEWHPAPPELK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 228 StvprfAAQAIEANEKlvtllgelaaEKGVTSAQIALAWLLAQKPWIVPIPGTTKLNRLEENLAAADIV----LSQKDTQ 303
Cdd:PLN02587 229 S-----ACAAAATHCK----------EKGKNISKLALQYSLSNKDISTTLVGMNSVQQVEENVAAATELetsgIDEELLS 293
|
330
....*....|
gi 447095029 304 QITEALETIK 313
Cdd:PLN02587 294 EVEAILAPVK 303
|
|
| AKR_AKR3F2 |
cd19139 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ... |
13-305 |
7.25e-24 |
|
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: 97.81 E-value: 7.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCMGLShgygpATDTRQAIeliRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFgftfgd 89
Cdd:cd19139 1 IPAFGLGTFRLK-----DDVVIDSV---RTALELGYRHIDTAQIYD---NEAAVGQAIAESgvpRDELFITTKI------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 90 dnkqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPD--VPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHA 167
Cdd:cd19139 64 ----WIDNLSKDKLLPSLEESLEKLRTDYVDLTLIHWPSPNdeVPVEEYIGALAEAKEQGLTRHIGVSNFTIALLDEAIA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 168 V---QPVTALQSEYSMWWREPeqEILPLLEELGIGFVPFSPLGKGFLtgaikpgttfGKDDyrstvprfaaqaieanekl 244
Cdd:cd19139 140 VvgaGAIATNQIELSPYLQNR--KLVAHCKQHGIHVTSYMTLAYGKV----------LDDP------------------- 188
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 245 vtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19139 189 --VLAAIAERHGATPAQIALAWAMARG--YAVIPSSTKREHLRSNLLALDLTLDADDMAAI 245
|
|
| AKR_unchar |
cd19099 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
11-291 |
1.12e-23 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381325 [Multi-domain] Cd Length: 316 Bit Score: 98.93 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 11 LEVSALGLGC-MGlshGYGPATDtRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALK-------PFRDRVVIATK 82
Cdd:cd19099 1 LTLSSLGLGTyRG---DSDDETD-EEYREALKAALDSGINVIDTAINYRGGRSERLIGKALReliekggIKRDEVVIVTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTFGD--------DNKQQILNS---------------RPEHIREAVEGSLRRLKTDVIDLLYQHrvDPDVP-IEDVAG 138
Cdd:cd19099 77 AGYIPGDgdeplrplKYLEEKLGRglidvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLH--NPEEQlLELGEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 139 TVKDLI-----------AEGKVKHFGLS---------------------EAGAQTIRRAH---AVQ-PVTALQSEYSMWW 182
Cdd:cd19099 155 EFYDRLeeafealeeavAEGKIRYYGIStwdgfrappalpghlsleklvAAAEEVGGDNHhfkVIQlPLNLLEPEALTEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 183 REPEQEILPLLE---ELGIGFVPFSPLGKGFLTGaikpgttfgkddyrstvprfaaqaieanekLVTLLGELAAEKGVTS 259
Cdd:cd19099 235 NTVKGEALSLLEaakELGLGVIASRPLNQGQLLG------------------------------ELRLADLLALPGGATL 284
|
330 340 350
....*....|....*....|....*....|..
gi 447095029 260 AQIALAWLLAQKPWIVPIPGTTKLNRLEENLA 291
Cdd:cd19099 285 AQRALQFARSTPGVDSALVGMRRPEHVDENLA 316
|
|
| AKR_galDH-like |
cd19153 |
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ... |
4-298 |
1.07e-22 |
|
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; L-galDH (EC 1.1.1.316), also called L-galactose 1-dehydrogenase, catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). It uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+). ARA2 (EC1.1.1.116), also called NAD(+)-specific D-arabinose dehydrogenase, catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+).
Pssm-ID: 381379 [Multi-domain] Cd Length: 294 Bit Score: 95.68 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 4 RYLGKSGLEVSALGLGCMGLSHGYGPATDTRQAIELIRAAVERGVTFFDTAEVYGPYLNEEVVGEALKPF---RDRVVIA 80
Cdd:cd19153 3 ETLEIALGNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqvpRSSYTVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGftfgdDNKQQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRV---DPDVPIEDVAGTVKDLIAEGKVKHFGLSEA 157
Cdd:cd19153 83 TKVG-----RYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIefvDYDTLVDEALPALRTLKDEGVIKRIGIAGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRA---HAVQPVTALQSEYSMWWREPEQE-ILPLLEE-LGIGFVPFSPLGKGFLTG----AIKPGttfgkddyrS 228
Cdd:cd19153 158 PLDTLTRAtrrCSPGSLDAVLSYCHLTLQDARLEsDAPGLVRgAGPHVINASPLSMGLLTSqgppPWHPA---------S 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447095029 229 TVPRFAAQAIEAneklvtllgeLAAEKGVTSAQIALAWLLAQKPWIVP-IPGTTKLNRLEENLAAADIVLS 298
Cdd:cd19153 229 GELRHYAAAADA----------VCASVEASLPDLALQYSLAAHAGVGTvLLGPSSLAQLRSMLAAVDAVAS 289
|
|
| AKR_AKR2E1-5 |
cd19116 |
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ... |
9-305 |
4.44e-22 |
|
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: 93.89 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGcmglSHGYGPATDTRQAIeliRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIAT 81
Cdd:cd19116 7 DGNEIPAIALG----TWKLKDDEGVRQAV---KHAIEAGYRHIDTAYLYG---NEAEVGEAIREKiaegvvkREDLFITT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFgddnkqqilnSRPEHIREAVEGSLRRLKTDVIDLLYQH----------------RVDPDVPIEDVAGTVKDLIA 145
Cdd:cd19116 77 KLWNSY----------HEREQVEPALRESLKRLGLDYVDLYLIHwpvafkenndsesngdGSLSDIDYLETWRGMEDLVK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 146 EGKVKHFGLSEAGAQTIRRAHA---VQPVtALQSEYSmwwrePEQEILPLLE---ELGIGFVPFSPLGKGFLTGAIKPGT 219
Cdd:cd19116 147 LGLTRSIGVSNFNSEQINRLLSncnIKPA-VNQIEVH-----PTLTQEKLVAycqSNGIVVMAYSPFGRLVPRGQTNPPP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 220 TFgkddyrstvprfaaqaieANEKLVtllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQ 299
Cdd:cd19116 221 RL------------------DDPTLV----AIAKKYGKTTAQIVLRYLIDRG--VVPIPKSSNKKRIKENIDIFDFQLTP 276
|
....*.
gi 447095029 300 KDTQQI 305
Cdd:cd19116 277 EEVAAL 282
|
|
| AKR_DrGR-like |
cd19136 |
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ... |
32-305 |
6.53e-22 |
|
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: 93.08 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 32 DTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATKFGftfgdDNKQQIlnsrpEHIR 104
Cdd:cd19136 16 EVRQAVD---AALKAGYRLIDTASVYR---NEADIGKALRDLlpkyglsREDIFITSKLA-----PKDQGY-----EKAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 105 EAVEGSLRRLKTDVIDLLYQH-----RVDPDVP--IEDVAGTVK---DLIAEGKVKHFGLSEagaQTIR-----RAHAVQ 169
Cdd:cd19136 80 AACLGSLERLGTDYLDLYLIHwpgvqGLKPSDPrnAELRRESWRaleDLYKEGKLRAIGVSN---YTVRhleelLKYCEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 170 PVTALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkDDYRSTVPRFAAqaieaneklvtllg 249
Cdd:cd19136 157 PPAVNQVEFHPHL--VQKELLKFCKDHGIHLQAYSSLGSG--------------DLRLLEDPTVLA-------------- 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 250 eLAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19136 207 -IAKKYGRTPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFELSEEDMAEL 259
|
|
| AKR_unchar |
cd19097 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
14-295 |
1.23e-21 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381323 [Multi-domain] Cd Length: 267 Bit Score: 92.21 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 14 SALGLGCMGLSHGYGPA-----TDTRQAIELIRAAVERGVTFFDTAEVYGpyLNEEVVGEALKPfRDRVVIATKFGFTFG 88
Cdd:cd19097 1 SKLALGTAQFGLDYGIAnksgkPSEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKR-LDKFKIITKLPPLKE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 89 DDNKqqilnsRPEHIREAVEGSLRRLKTDVIDLLYQHRVDpDVPI--EDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAH 166
Cdd:cd19097 78 DKKE------DEAAIEASVEASLKRLKVDSLDGLLLHNPD-DLLKhgGKLVEALLELKKEGLIRKIGVSVYSPEELEKAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 167 AVQPVTALQSEYSMW-WREPEQEILPLLEELGIGFVPFSPLGKGFLTgaIKPgttfgkddyrSTVPRFAAQAieanEKLV 245
Cdd:cd19097 151 ESFKIDIIQLPFNILdQRFLKSGLLAKLKKKGIEIHARSVFLQGLLL--MEP----------DKLPAKFAPA----KPLL 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 447095029 246 TLLGELAAEKGVTSAQIALAWLLAQkPWI--VPIpGTTKLNRLEENLAAADI 295
Cdd:cd19097 215 KKLHELAKKLGLSPLELALGFVLSL-PEIdkIVV-GVDSLEQLKEIIAAFKK 264
|
|
| AKR_AKR5F1 |
cd19133 |
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ... |
10-305 |
3.33e-20 |
|
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: 88.02 E-value: 3.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLShgygPATDTRQAIeliRAAVERGVTFFDTAEVYGpylNEEVVGEALK----PfRDRVVIATKFGF 85
Cdd:cd19133 6 GVEMPILGFGVFQIP----DPEECERAV---LEAIKAGYRLIDTAAAYG---NEEAVGRAIKksgiP-REELFITTKLWI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 TFGDDNKQqilnsrpehiREAVEGSLRRLKTDVIDLLYQHRvdpdvPIEDVAGTVK---DLIAEGKVKHFGLSEAGAQTI 162
Cdd:cd19133 75 QDAGYEKA----------KKAFERSLKRLGLDYLDLYLIHQ-----PFGDVYGAWRameELYKEGKIRAIGVSNFYPDRL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 163 RR---AHAVQPVTaLQSE-YSMWWREPEQEIlplLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaAQAI 238
Cdd:cd19133 140 VDlilHNEVKPAV-NQIEtHPFNQQIEAVEF---LKKYGVQIEAWGPFAEG-------------------------RNNL 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 239 EANEklvtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19133 191 FENP----VLTEIAEKYGKSVAQVILRWLIQRG--IVVIPKSVRPERIAENFDIFDFELSDEDMEAI 251
|
|
| AKR_BaDH-like |
cd19129 |
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ... |
10-311 |
3.43e-20 |
|
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: 89.05 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMglshgYGPATDTRQAIeliRAAVERGVTFFDTAEvygPYLNEEVVGEALKPF-------RDRVVIATK 82
Cdd:cd19129 3 SGAIPALGFGTL-----IPDPSATRNAV---KAALEAGFRHFDCAE---RYRNEAEVGEAMQEVfkagkirREDLFVTTK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTfgddnkqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQHR--------------------VDPDVPIEDVAGTVKD 142
Cdd:cd19129 72 LWNT----------NHRPERVKPAFEASLKRLQLDYLDLYLIHTpfafqpgdeqdprdangnviYDDGVTLLDTWRAMER 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 143 LIAEGKVKHFGLSE---AGAQTIRRAHAVQPVtALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGfltgaIKPGT 219
Cdd:cd19129 142 LVDEGRCKAIGLSDvslEKLREIFEAARIKPA-VVQVESHPYL--PEWELLDFCKNHGIVLQAFAPLGHG-----MEPKL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 220 TfgkDDyrstvprfaaqaieaneklvTLLGELAAEKGVTSAQIALAWllAQKPWIVPIPGTTKLNRLEENLaaaDI-VLS 298
Cdd:cd19129 214 L---ED--------------------PVITAIARRVNKTPAQVLLAW--AIQRGTALLTTSKTPSRIRENF---DIsTLP 265
|
330
....*....|...
gi 447095029 299 QKDTQQITEALET 311
Cdd:cd19129 266 EDAMREINEGIKT 278
|
|
| AKR_AKR5D1_E1 |
cd19132 |
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ... |
10-311 |
9.34e-19 |
|
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: 84.24 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLshgygpatDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALK----PfRDRVVIATKFgf 85
Cdd:cd19132 4 GTQIPAIGFGTYPL--------KGDEGVEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRrsgvP-REELFVTTKL-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 tfgdDNKQQilnsRPEHIREAVEGSLRRLKTDVIDLLYQHRVDP--DVPIEdvagTVKDLIA---EGKVKHFGLS---EA 157
Cdd:cd19132 70 ----PGRHH----GYEEALRTIEESLYRLGLDYVDLYLIHWPNPsrDLYVE----AWQALIEareEGLVRSIGVSnflPE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHAVQPVTAlQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaaqa 237
Cdd:cd19132 138 HLDRLIDETGVTPAVN-QIELHPYF--PQAEQRAYHREHGIVTQSWSPLGRG---------------------------- 186
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 238 ieanEKLVT--LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITeALET 311
Cdd:cd19132 187 ----SGLLDepVIKAIAEKHGKTPAQVVLRWHVQLG--VVPIPKSANPERQRENLAIFDFELSDEDMAAIA-ALDR 255
|
|
| AKR_CeZK1290-like |
cd19135 |
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ... |
9-303 |
1.15e-18 |
|
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: 83.91 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGcmgLSHGYGPATDTrqaieLIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGF 85
Cdd:cd19135 9 NGVEMPILGLG---TSHSGGYSHEA-----VVYALKECGYRHIDTAKRYG---CEELLGKAIKESgvpREDLFLTTKLWP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 86 T-FGDDNkqqilnsrpehIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGT-------VKDLIAEGKVKHFGLSEA 157
Cdd:cd19135 78 SdYGYES-----------TKQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVKETraetwraLEELYDEGLCRAIGVSNF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 158 GAQTIRRAHA---VQPVtALQSEYSMWwrEPEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfa 234
Cdd:cd19135 147 LIEHLEQLLEdcsVVPH-VNQVEFHPF--QNPVELIEYCRDNNIVFEGYCPLAKG------------------------- 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 235 aQAIeaNEKLVTllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQ 303
Cdd:cd19135 199 -KAL--EEPTVT---ELAKKYQKTPAQILIRWSIQNG--VVTIPKSTKEERIKENCQVFDFSLSEEDMA 259
|
|
| AKR_AKR1G1_1I |
cd19111 |
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ... |
10-307 |
1.16e-18 |
|
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: 84.47 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLShgygpatdTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATK 82
Cdd:cd19111 1 GFPMPVIGLGTYQSP--------PEEVRAAVDYALFVGYRHIDTALSYQ---NEKAIGEALKWWlkngklkREEVFITTK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTFgddnkqqilnSRPEHIREAVEGSLRRLKTDVIDLLYQH-------------RVDPDVPIEDVAGTVKDLIAEGKV 149
Cdd:cd19111 70 LPPVY----------LEFKDTEKSLEKSLENLKLPYVDLYLIHhpcgfvnkkdkgeRELASSDVTSVWRAMEALVSEGKV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 150 KHFGLSEAGAQTIRR--AHAVQPVTALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKgfltgaikPGttfgkddyR 227
Cdd:cd19111 140 KSIGLSNFNPRQINKilAYAKVKPSNLQLECHAYL--QQRELRKFCNKKNIVVTAYAPLGS--------PG--------R 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 228 STVPRFAAQAIEANEKLVTllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19111 202 ANQSLWPDQPDLLEDPTVL---AIAKELDKTPAQVLLRFVLQRG--TGVLPKSTNKERIEENFEVFDFELTEEHFKKLKT 276
|
|
| AKR_AKR2B1-10 |
cd19113 |
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ... |
9-307 |
2.24e-18 |
|
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: 84.03 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLshgygpatDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIAT 81
Cdd:cd19113 7 SGYKMPSVGFGCWKL--------DNATAADQIYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRAideglvkREELFLTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFGDdnkqqilnsrPEHIREAVEGSLRRLKTDVIDLLYQH------------RVDP-------------DVPIEDV 136
Cdd:cd19113 76 KLWNNFHD----------PKNVETALNKTLSDLKLDYVDLFLIHfpiafkfvpieeKYPPgfycgdgdnfvyeDVPILDT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 137 AGTVKDLIAEGKVKHFGLSE-AGA--QTIRRAHAVQPVtALQSEYSMWWREPEqeILPLLEELGIGFVPFSPLG-KGFLT 212
Cdd:cd19113 146 WKALEKLVDAGKIKSIGVSNfPGAliLDLLRGATIKPA-VLQIEHHPYLQQPK--LIEYAQKAGITITAYSSFGpQSFVE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 213 gaikpgttFGKDDYRSTVPRFAAQAIEAneklvtllgeLAAEKGVTSAQIALAWllAQKPWIVPIPGTTKLNRLEENLAA 292
Cdd:cd19113 223 --------LNQGRALNTPTLFEHDTIKS----------IAAKHNKTPAQVLLRW--ATQRGIAVIPKSNLPERLLQNLSV 282
|
330
....*....|....*
gi 447095029 293 ADIVLSQKDTQQITE 307
Cdd:cd19113 283 NDFDLTKEDFEEIAK 297
|
|
| AKR_AKR3G1 |
cd19123 |
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ... |
10-305 |
3.69e-18 |
|
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a founding member of aldo-keto reductase family 3 member G1 (AKR3G1). It is an aldo/keto reductase that catalyzes the NADPH-dependent reduction of aldehyde- and ketone-groups of different classes of carbonyl compounds to the corresponding alcohols.
Pssm-ID: 381349 [Multi-domain] Cd Length: 297 Bit Score: 83.23 E-value: 3.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGygpatdtrQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEAL-KPF------RDRVVIATK 82
Cdd:cd19123 9 GDLIPALGLGTWKSKPG--------EVGQAVKQALEAGYRHIDCAAIYG---NEAEIGAALaEVFkegkvkREDLWITSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGftfgdDNKQQilnsrPEHIREAVEGSLRRLKTDVIDLL-------YQHRV-----------DPDVPIEDVAGTVKDLI 144
Cdd:cd19123 78 LW-----NNSHA-----PEDVLPALEKTLADLQLDYLDLYlmhwpvaLKKGVgfpesgedllsLSPIPLEDTWRAMEELV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 145 AEGKVKHFGLSEAGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkd 224
Cdd:cd19123 148 DKGLCRHIGVSNFSVKKLEDLLATARIKPAVNQVELHPYLQQPELLAFCRDNGIHLTAYSPLGSG--------------- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 225 dyrstvPRFAAQAIEANEKLVT--LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDT 302
Cdd:cd19123 213 ------DRPAAMKAEGEPVLLEdpVINKIAEKHGASPAQVLIAWAIQRG--TVVIPKSVNPERIQQNLEAAEVELDASDM 284
|
...
gi 447095029 303 QQI 305
Cdd:cd19123 285 ATI 287
|
|
| AKR_AKR5B1 |
cd19127 |
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ... |
10-307 |
1.59e-16 |
|
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: 78.22 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMglshgygpATDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGFT 86
Cdd:cd19127 6 GVEMPALGLGVF--------QTPPEETADAVATALADGYRLIDTAAAYG---NEREVGEGIRRSgvdRSDIFVTTKLWIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 -FGDDNKqqilnsrpehiREAVEGSLRRLKTDVIDLLYQHRVDPDVpIEDVAGTVKDL---IAEGKVKHFGLSEAGAQTI 162
Cdd:cd19127 75 dYGYDKA-----------LRGFDASLRRLGLDYVDLYLLHWPVPND-FDRTIQAYKALeklLAEGRVRAIGVSNFTPEHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 163 RR-AHAVQPVTAL-QSEYSMWWREPeqeilPLLE---ELGIGFVPFSPLGkgfltgaikpgttfgkddyrsTVPRFAAQA 237
Cdd:cd19127 143 ERlIDATTVVPAVnQVELHPYFSQK-----DLRAfhrRLGIVTQAWSPIG---------------------GVMRYGASG 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447095029 238 IEANEKLVT--LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19127 197 PTGPGDVLQdpTITGLAEKYGKTPAQIVLRWHLQNG--VSAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
|
|
| AKR_AKR5C2 |
cd19131 |
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ... |
35-306 |
3.45e-16 |
|
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; Escherichia coli DkgA/YqhE is a founding member of aldo-keto reductase family 5 member C2 (AKR5C2). DkgA/YqhE (EC 1.1.1.274), also called 2,5-DKG reductase A, or 2,5-DKGR A, or 25DKGR-A, or AKR5C, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives.
Pssm-ID: 381357 [Multi-domain] Cd Length: 256 Bit Score: 77.03 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 35 QAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKfgftfgddnkqqILNSRPEH--IREAVEG 109
Cdd:cd19131 24 EAASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASgvpREELFITTK------------LWNSDQGYdsTLRAFDE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 110 SLRRLKTDVIDLLYQHRvdpDVPIED-VAGTVKDLI---AEGKVKHFGLSEAGAQTIRR---AHAVQPVTAlQSEysMWW 182
Cdd:cd19131 89 SLRKLGLDYVDLYLIHW---PVPAQDkYVETWKALIelkKEGRVKSIGVSNFTIEHLQRlidETGVVPVVN-QIE--LHP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 183 REPEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkDDyrstvprfaaqaieaneklvTLLGELAAEKGVTSAQI 262
Cdd:cd19131 163 RFQQRELRAFHAKHGIQTESWSPLGQGGLL-----------SD--------------------PVIGEIAEKHGKTPAQV 211
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 447095029 263 ALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQIT 306
Cdd:cd19131 212 VIRWHLQNG--LVVIPKSVTPSRIAENFDVFDFELDADDMQAIA 253
|
|
| AKR_AKR4C1-15 |
cd19125 |
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ... |
8-307 |
6.32e-16 |
|
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase (ALR) from Hordeum vulgare (AKR4C1), Bromus inermis (AKR4C2), Avena fatua (AKR4C3), and Xerophyta viscosa (AKR4C4), two aldose reductases, DpAR1 (AKR4C5) and DpAR2(AKR4C6), from Digitalis purpurea, aldehyde reductase from Zea mays (AKR4C7), four aldo-keto reductases from Arabidopsis thaliana (AKR4C8-11), and another three aldo-keto reductases from Aloe arborescens (AKR4C12) and Oryza sativa (AKR4C14/15). ALR (EC 1.1.1.21), also called AR, aldehyde reductase, or polyol dehydrogenase (NADP(+)), is a cytosolic NADPH-dependent oxidoreductase that catalyzes the reduction of a variety of aldehydes and carbonyls, including monosaccharides. Both DpAR1 and DpAR2 reduce the ketone group of steroid structures. They may be involved in plant steroid metabolism in general and in cardenolide biosynthesis in particular. Plant aldo-keto reductases of the AKR4C subfamily play key roles during stress and are attractive targets for developing stress-tolerant crops.
Pssm-ID: 381351 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 8 KSGLEVSALGLGCMGLSHGygpatDTRQAIeliRAAVERGVTFFDTAEVYGpylNEEVVGEALKP-FRDRVV------IA 80
Cdd:cd19125 6 NTGAKIPAVGLGTWQADPG-----VVGNAV---KTAIKEGYRHIDCAAIYG---NEKEIGKALKKlFEDGVVkredlfIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGFTfgddnkqqilNSRPEHIREAVEGSLRRLKTDVIDLLYQH---RVD-----------PDVPIEDVAGTVKDLIAE 146
Cdd:cd19125 75 SKLWCT----------DHAPEDVPPALEKTLKDLQLDYLDLYLIHwpvRLKkgahmpepeevLPPDIPSTWKAMEKLVDS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 147 GKVKHFGLSEAGAQTIRR--AHAVQPVTALQSEYSMWWREpeQEILPLLEELGIGFVPFSPLGKgfltgaikPGTTFGKD 224
Cdd:cd19125 145 GKVRAIGVSNFSVKKLEDllAVARVPPAVNQVECHPGWQQ--DKLHEFCKSKGIHLSAYSPLGS--------PGTTWVKK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 225 DYRSTvprfaaqaieaneklvTLLGELAAEKGVTSAQIALAWLLaQKPWIVpIPGTTKLNRLEENLAAADIVLSQKDTQQ 304
Cdd:cd19125 215 NVLKD----------------PIVTKVAEKLGKTPAQVALRWGL-QRGTSV-LPKSTNEERIKENIDVFDWSIPEEDFAK 276
|
...
gi 447095029 305 ITE 307
Cdd:cd19125 277 FSS 279
|
|
| dkgB |
PRK11172 |
2,5-didehydrogluconate reductase DkgB; |
13-310 |
1.50e-15 |
|
2,5-didehydrogluconate reductase DkgB;
Pssm-ID: 183012 [Multi-domain] Cd Length: 267 Bit Score: 75.45 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 13 VSALGLGCMGLshgygpaTDtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFgftfgd 89
Cdd:PRK11172 3 IPAFGLGTFRL-------KD-QVVIDSVKTALELGYRAIDTAQIYD---NEAAVGQAIAESgvpRDELFITTKI------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 90 dnkqQILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPD--VPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAHA 167
Cdd:PRK11172 66 ----WIDNLAKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVSVEEFMQALLEAKKQGLTREIGISNFTIALMKQAIA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 168 VQPVTAL---QSEYSMWWREpeQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgKDDyrstvprfaaqaieanekl 244
Cdd:PRK11172 142 AVGAENIatnQIELSPYLQN--RKVVAFAKEHGIHVTSYMTLAYGKVL----------KDP------------------- 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447095029 245 vtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITeALE 310
Cdd:PRK11172 191 --VIARIAAKHNATPAQVILAWAMQLG--YSVIPSSTKRENLASNLLAQDLQLDAEDMAAIA-ALD 251
|
|
| AKR_AKR5G1-3 |
cd19157 |
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ... |
10-322 |
2.31e-14 |
|
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: 72.04 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGygpatdtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGft 86
Cdd:cd19157 7 GVKMPWLGLGVFKVEEG-------SEVVNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESgipREELFITSKVW-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 fgddNKQQILNSrpehIREAVEGSLRRLKTDVIDLLYQHRVDPDVPIEDVAGTVKdLIAEGKVKHFGLS---EAGAQTIR 163
Cdd:cd19157 75 ----NADQGYDS----TLKAFEASLERLGLDYLDLYLIHWPVKGKYKETWKALEK-LYKDGRVRAIGVSnfqVHHLEDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 164 RAHAVQPVTAlQSEYSMwwREPEQEILPLLEELGIGFVPFSPLGKGFLtgaikpgttFGKDdyrstvprfaaqaieanek 243
Cdd:cd19157 146 ADAEIVPMVN-QVEFHP--RLTQKELRDYCKKQGIQLEAWSPLMQGQL---------LDNP------------------- 194
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 244 lvtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQItEALETikivGERYSPE 322
Cdd:cd19157 195 ---VLKEIAEKYNKSVAQVILRWDLQNG--VVTIPKSIKEHRIIENADVFDFELSQEDMDKI-DALNE----NLRVGPD 263
|
|
| AKR_unchar |
cd19098 |
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ... |
10-319 |
3.14e-14 |
|
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.
Pssm-ID: 381324 [Multi-domain] Cd Length: 318 Bit Score: 71.99 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGL-GCMGLSH------GYGPATDTRQAIELIRAAVERGVTFFDTAEVYGpyLNEEVVG---EALKPFRDRVVI 79
Cdd:cd19098 4 GLGLAALGRpGYINLGHaadlgsGRSVEAMRAHTHAVLDAAWAAGVRYFDAARSYG--RAEEFLGswlRSRNIAPDAVFV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 80 ATKFGFTF-GDDNKQQILNSRPEH----IREAVEGSLRRLKtDVIDLlYQ-HRVDPDVPIEDVAGTVKDL--IAEGKVKh 151
Cdd:cd19098 82 GSKWGYTYtADWQVDAAVHEVKDHslarLLKQWEETRSLLG-KHLDL-YQiHSATLESGVLEDADVLAALaeLKAEGVK- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 152 FGLSEAG---AQTIRRAHAVQP-----VTALQSEYSMWwrepEQEILPLLEEL---GIGFVPFSPLGKGFLTGaikpgtt 220
Cdd:cd19098 159 IGLSLSGpqqAETLRRALEIEIdgarlFDSVQATWNLL----EQSAGEALEEAheaGMGVIVKEALANGRLTD------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 221 fgkddyRSTVPRFAAqaieanekLVTLLGELAAEKGVTSAQIALAWLLAQkPWI-VPIPGTTKLNRLEENLAAADIVLSq 299
Cdd:cd19098 228 ------RNPSPELAP--------LMAVLKAVADRLGVTPDALALAAVLAQ-PFVdVVLSGAATPEQLRSNLRALDVSLD- 291
|
330 340
....*....|....*....|
gi 447095029 300 kdtQQITEALETIKIVGERY 319
Cdd:cd19098 292 ---LELLAALADLAEPPEDY 308
|
|
| AKR_AKR5A_5G |
cd19126 |
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ... |
10-306 |
3.14e-14 |
|
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes prostaglandin F2-alpha synthase (PGFS) from Leishmania major (AKR5A1) and Trypanosoma brucei (AKR5A2). PGFS, also called 9,11-endoperoxide prostaglandin H2 reductase, catalyzes the NADP-dependent formation of prostaglandin F2-alpha from prostaglandin H2. It has also aldo/ketoreductase activity for synthetic substrates 9,10-phenanthrenequinone and p-nitrobenzaldehyde. The AKR5G family of AKR includes Bacillus subtilis glyoxal reductase (GR), uncharacterized oxidoreductase YtbE, and Bacillus aryabhattai aldo-keto reductase, which corresponds to aldo-keto reductase family 5 member G1-3 (AKR5G1-3), respectively. GR (YvgN, EC 1.1.1.283), also called methylglyoxal reductase, reduces glyoxal and methylglyoxal (2-oxopropanal). It is not involved in vitamin B6 biosynthesis.
Pssm-ID: 381352 [Multi-domain] Cd Length: 254 Bit Score: 71.31 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGygpatdtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFgft 86
Cdd:cd19126 6 GTRMPWLGLGVFQTPDG-------DETERAVQTALENGYRSIDTAAIYK---NEEGVGEAIRESgvpREELFVTTKL--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 FGDDnkqqilnSRPEHIREAVEGSLRRLKTDVIDLLYQHRVDPDvPIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRAH 166
Cdd:cd19126 73 WNDD-------QRARRTEDAFQESLDRLGLDYVDLYLIHWPGKD-KFIDTWKALEKLYASGKVKAIGVSNFQEHHLEELL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 167 AVQPVTAL--QSEYSMWWRepEQEILPLLEELGIGFVPFSPLGKGFLTgaikpgttfgkddyrsTVPRFAAqaieanekl 244
Cdd:cd19126 145 AHADVVPAvnQVEFHPYLT--QKELRGYCKSKGIVVEAWSPLGQGGLL----------------SNPVLAA--------- 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447095029 245 vtllgeLAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQIT 306
Cdd:cd19126 198 ------IGEKYGKSAAQVVLRWDIQHG--VVTIPKSVHASRIKENADIFDFELSEDDMTAID 251
|
|
| AKR_AKR4A_4B |
cd19124 |
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ... |
9-307 |
6.34e-14 |
|
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: 70.76 E-value: 6.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCmglshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALK--------PFRDRVVIA 80
Cdd:cd19124 1 SGQTMPVIGMGT------ASDPPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAealrlglvKSRDELFVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 81 TKFGFTFGDdnkqqilnsrPEHIREAVEGSLRRLKTDVIDLLYQH---RVDPDV---PIE-------DVAGTVKDLiaE- 146
Cdd:cd19124 72 SKLWCSDAH----------PDLVLPALKKSLRNLQLEYVDLYLIHwpvSLKPGKfsfPIEeedflpfDIKGVWEAM--Ee 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 147 ----GKVKHFGLSEAGAQTIRR--AHAVQPVTALQSEYSMWWREpeQEILPLLEELGIGFVPFSPLGKgfltgaikPGTT 220
Cdd:cd19124 140 cqrlGLTKAIGVSNFSCKKLQEllSFATIPPAVNQVEMNPAWQQ--KKLREFCKANGIHVTAYSPLGA--------PGTK 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 221 FGKDdyrstvprfaaqAIEANEklvtLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQK 300
Cdd:cd19124 210 WGSN------------AVMESD----VLKEIAAAKGKTVAQVSLRWVYEQG--VSLVVKSFNKERMKQNLDIFDWELTEE 271
|
....*..
gi 447095029 301 DTQQITE 307
Cdd:cd19124 272 DLEKISE 278
|
|
| AKR_AKR2A1-2 |
cd19112 |
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ... |
9-305 |
1.31e-13 |
|
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: 70.21 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLSHGygpatdtrQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALK-PF------RDRVVIAT 81
Cdd:cd19112 7 SGHKMPVIGLGVWRMEPG--------EIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAeAFktglvkREDLFITT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KfgftfgddnkqqILNSRPEHIREAVEGSLRRLKTDVIDLLYQH-----------------------RVDPDVPIEDVAG 138
Cdd:cd19112 76 K------------LWNSDHGHVIEACKDSLKKLQLDYLDLYLVHfpvatkhtgvgttgsalgedgvlDIDVTISLETTWH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 139 TVKDLIAEGKVKHFGLSEAGAQTIRRAHA---VQPVTALQSEYSMWWREpeqEILPLLEELGIGFVPFSPLGkGFLTGAI 215
Cdd:cd19112 144 AMEKLVSAGLVRSIGISNYDIFLTRDCLAyskIKPAVNQIETHPYFQRD---SLVKFCQKHGISVTAHTPLG-GAAANAE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 216 KPGTTFGKDDyrstvprfaaqaieaneklvTLLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADI 295
Cdd:cd19112 220 WFGSVSPLDD--------------------PVLKDLAKKYGKSAAQIVLRWGIQRN--TAVIPKSSKPERLKENIDVFDF 277
|
330
....*....|
gi 447095029 296 VLSQKDTQQI 305
Cdd:cd19112 278 QLSKEDMKLI 287
|
|
| AKR_AKR5C1 |
cd19130 |
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ... |
26-305 |
1.13e-12 |
|
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: 66.86 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 26 GYG----PATDTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGftfgDDNKqqilns 98
Cdd:cd19130 14 GYGvfkvPPADTQRAVA---TALEVGYRHIDTAAIYG---NEEGVGAAIAASgipRDELFVTTKLW----NDRH------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 99 RPEHIREAVEGSLRRLKTDVIDLLYQHRVDP--DVPIEDVAgTVKDLIAEGKVKHFGLSEAGAQTIRRAHAVQPVTALQS 176
Cdd:cd19130 78 DGDEPAAAFAESLAKLGLDQVDLYLVHWPTPaaGNYVHTWE-AMIELRAAGRTRSIGVSNFLPPHLERIVAATGVVPAVN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 177 EYSMWWREPEQEILPLLEELGIGFVPFSPLGKGFLTGAikpgttfgkddyrstvprfaaqaieaneklvTLLGELAAEKG 256
Cdd:cd19130 157 QIELHPAYQQRTIRDWAQAHDVKIEAWSPLGQGKLLGD-------------------------------PPVGAIAAAHG 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 447095029 257 VTSAQIALAWLLaQKPWIVpIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19130 206 KTPAQIVLRWHL-QKGHVV-FPKSVRRERMEDNLDVFDFDLTDTEIAAI 252
|
|
| AKR_AKR3A1-2 |
cd19117 |
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ... |
9-307 |
1.54e-12 |
|
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: 66.75 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLSHGygpatDTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALK----PfRDRVVIATKFG 84
Cdd:cd19117 10 TGAEIPAVGLGTWQSKPN-----EVAKAVE---AALKAGYRHIDTAAIYG---NEEEVGQGIKdsgvP-REEIFITTKLW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 85 FTFgddnkqqilNSRPEhirEAVEGSLRRLKTDVIDLLYQH---------------------RVDPDVPIEDVAGTVKDL 143
Cdd:cd19117 78 CTW---------HRRVE---EALDQSLKKLGLDYVDLYLMHwpvpldpdgndflfkkddgtkDHEPDWDFIKTWELMQKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 144 IAEGKVKHFGLSEAGAQTIRRAHAVQP--VTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGkgfltgaikpgttf 221
Cdd:cd19117 146 PATGKVKAIGVSNFSIKNLEKLLASPSakIVPAVNQIELHPLLPQPKLVDFCKSKGIHATAYSPLG-------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 222 gkddyrstvprfAAQAIEANEKLVTllgELAAEKGVTSAQIALAWLLaQKPWIVpIPGTTKLNRLEENLAAadIVLSQKD 301
Cdd:cd19117 212 ------------STNAPLLKEPVII---KIAKKHGKTPAQVIISWGL-QRGYSV-LPKSVTPSRIESNFKL--FTLSDEE 272
|
....*.
gi 447095029 302 TQQITE 307
Cdd:cd19117 273 FKEIDE 278
|
|
| AKR_GlAR-like |
cd19128 |
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ... |
26-305 |
4.98e-12 |
|
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), also called aldehyde reductase, is the prototype of this family. It catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Pssm-ID: 381354 [Multi-domain] Cd Length: 277 Bit Score: 65.24 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 26 GYGPATDTRQAI-ELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATKFGFTFgddnkqqiln 97
Cdd:cd19128 5 GFGTYKITESESkEAVKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdggvkREDLFITSKLWPTM---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 98 SRPEHIREAVEGSLRRLKTDVIDLLYQH---RVDPD----------------VPIEDVAGTVKDLIAEGKVKHFGLSEAG 158
Cdd:cd19128 72 HQPENVKEQLLITLQDLQLEYLDLFLIHwplAFDMDtdgdprddnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 159 AQTIR---RAHAVQPVTAlQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGkgfltgaikpgttfGKDDYRSTVPrfaa 235
Cdd:cd19128 152 TKLLTdllNYCKIKPFMN-QIECHPYF--QNDKLIKFCIENNIHVTAYRPLG--------------GSYGDGNLTF---- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447095029 236 QAIEAneklvtlLGELAAEKGVTSAQIALAWLLAQKP--WIVpIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19128 211 LNDSE-------LKALATKYNTTPPQVIIAWHLQKWPknYSV-IPKSANKSRCQQNFDINDLALTKEDMDAI 274
|
|
| AKR_AKR3D1 |
cd19121 |
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ... |
9-295 |
5.09e-12 |
|
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: 65.24 E-value: 5.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLSHGygpatDTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALKPF------RDRVVIATK 82
Cdd:cd19121 8 TGASIPAVGLGTWQAKAG-----EVKAAVA---HALKIGYRHIDGALCYQ---NEDEVGEGIKEAiaggvkREDLFVTTK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 83 FGFTFgddnkqqilNSRPEhirEAVEGSLRRLKTDVIDLLYQH----------------------RVDPDVPIEDVAGTV 140
Cdd:cd19121 77 LWSTY---------HRRVE---LCLDRSLKSLGLDYVDLYLVHwpvllnpngnhdlfptlpdgsrDLDWDWNHVDTWKQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 141 KDLIAEGKVKHFGLSEAG----AQTIRRAHAVQPVTALQSEYSMwwrePEQEILPLLEELGIGFVPFSPLGKgflTGAik 216
Cdd:cd19121 145 EKVLKTGKTKAIGVSNYSipylEELLKHATVVPAVNQVENHPYL----PQQELVDFCKEKGILIEAYSPLGS---TGS-- 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447095029 217 pgttfgkddyrstvPRFAAQAIEaneklvtllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADI 295
Cdd:cd19121 216 --------------PLISDEPVV----------EIAKKHNVGPGTVLISYQVARG--AVVLPKSVTPDRIKSNLEIIDL 268
|
|
| dkgA |
PRK11565 |
2,5-didehydrogluconate reductase DkgA; |
16-307 |
1.30e-11 |
|
2,5-didehydrogluconate reductase DkgA;
Pssm-ID: 183203 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 16 LGLGCMglshgygpATDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKfgftfgddnk 92
Cdd:PRK11565 18 LGLGVW--------QASNEEVITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEAsvaREELFITTK---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 93 qqILNSRPEHIREAVEGSLRRLKTDVIDLLYQHRvdPDVPIEDVAGTVKDLIA---EGKVKHFGLS---EAGAQTIRRAH 166
Cdd:PRK11565 77 --LWNDDHKRPREALEESLKKLQLDYVDLYLMHW--PVPAIDHYVEAWKGMIElqkEGLIKSIGVCnfqIHHLQRLIDET 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 167 AVQPVTAlqseysmwwrepEQEILPLLEEL---------GIGFVPFSPLGKGfltgaikpgttfGKDdyrstvpRFAAQA 237
Cdd:PRK11565 153 GVTPVIN------------QIELHPLMQQRqlhawnathKIQTESWSPLAQG------------GKG-------VFDQKV 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 238 IEaneklvtllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:PRK11565 202 IR----------DLADKYGKTPAQIVIRWHLDSG--LVVIPKSVTPSRIAENFDVFDFRLDKDELGEIAK 259
|
|
| AKR_AKR1I_CgAKR1 |
cd19155 |
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ... |
21-307 |
1.08e-10 |
|
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: 61.77 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 21 MGLSHGYGPATDTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATKFGFTfgddnkq 93
Cdd:cd19155 15 VGLGTWQSSPEEIETAVD---TALEAGYRHIDTAYVYR---NEAAIGNVLKKWidsgkvkREELFIVTKLPPG------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 94 qilNSRPEHIREAVEGSLRRLKTDVIDLLYQH---------------------RVDPDVPIEDVAGTVKDLIAEGKVKHF 152
Cdd:cd19155 82 ---GNRREKVEKFLLKSLEKLQLDYVDLYLIHfpvgslskeddsgkldptgehKQDYTTDLLDIWKAMEAQVDQGLTRSI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 153 GLSEAGAQTIRR---AHAVQPVTaLQSEYSMWWRepEQEILPLLEELGIGFVPFSPLGKGFLTGAIKpgttfGKDDYRST 229
Cdd:cd19155 159 GLSNFNREQMARilkNARIKPAN-LQVELHVYLQ--QKDLVDFCSTHSITVTAYAPLGSPGAAHFSP-----GTGSPSGS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 230 VPrfaaqaieaneKLVT--LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19155 231 SP-----------DLLQdpVVKAIAERHGKSPAQVLLRWLMQRG--VVVIPKSTNAARIKENFQVFDFELTEADMAKLSS 297
|
|
| AKR_AKR1A1-4 |
cd19106 |
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ... |
9-311 |
1.27e-10 |
|
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol dehydrogenase [NADP(+)] (ALR, EC 1.1.1.2) from Homo sapiens (AKR1A1), Sus scrofa (AKR1A2), Rattus norvegicus (liver, AKR1A3), and Mus musculus (AKR1A4). ALR, also known as aldehyde reductase, or ALDR1, catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. In vitro substrates include succinic semialdehyde, 4-nitrobenzaldehyde, 1,2-naphthoquinone, methylglyoxal, and D-glucuronic acid.
Pssm-ID: 381332 [Multi-domain] Cd Length: 305 Bit Score: 61.25 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCMGLSHGygpatdtrQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKpfrdrvviaTKFGFTFG 88
Cdd:cd19106 3 TGQKMPLIGLGTWKSKPG--------QVKAAVKYALDAGYRHIDCAAVYG---NEQEVGEALK---------EKVGPGKA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 89 DDNKQQILNS-------RPEHIREAVEGSLRRLKTDVIDLLYQH------RVD------PD-------VPIEDVAGTVKD 142
Cdd:cd19106 63 VPREDLFVTSklwntkhHPEDVEPALRKTLKDLQLDYLDLYLIHwpyafeRGDnpfpknPDgtirydsTHYKETWKAMEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 143 LIAEGKVKHFGLSEAGAQTIRRAHA---VQPVTaLQSEYSMWWRepEQEILPLLEELGIGFVPFSPLGKGFLTGAiKPGT 219
Cdd:cd19106 143 LVDKGLVKAIGLSNFNSRQIDDILSvarIKPAV-LQVECHPYLA--QNELIAHCKARGLVVTAYSPLGSPDRPWA-KPDE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 220 TFGKDDyrstvPRfaaqaieaneklvtlLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQ 299
Cdd:cd19106 219 PVLLEE-----PK---------------VKALAKKYNKSPAQILLRWQVQRG--VVVIPKSVTPSRIKQNIQVFDFTLSP 276
|
330
....*....|..
gi 447095029 300 KDTQQItEALET 311
Cdd:cd19106 277 EEMKQL-DALNR 287
|
|
| AKR_AKR5A1_2 |
cd19156 |
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ... |
10-322 |
9.07e-10 |
|
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: 58.30 E-value: 9.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 10 GLEVSALGLGCMGLSHGygpatdtRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKFGft 86
Cdd:cd19156 6 GVEMPRLGLGVWRVQDG-------AEAENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESgvpREEVFVTTKLW-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 fgddNKQQILnsrpEHIREAVEGSLRRLKTDVIDLLYQHRvdpdvpieDVAGTVKD-------LIAEGKVKHFGLSEAGA 159
Cdd:cd19156 74 ----NSDQGY----ESTLAAFEESLEKLGLDYVDLYLIHW--------PVKGKFKDtwkafekLYKEKKVRAIGVSNFHE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 160 QTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaaqaie 239
Cdd:cd19156 138 HHLEELLKSCKVAPMVNQIELHPLLTQEPLRKFCKEKNIAVEAWSPLGQG------------------------------ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 240 aneKLVT--LLGELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQItEALETikivGE 317
Cdd:cd19156 188 ---KLLSnpVLKAIGKKYGKSAAQVIIRWDIQHG--IITIPKSVHEERIQENFDVFDFELTAEEIRQI-DGLNT----DH 257
|
....*
gi 447095029 318 RYSPE 322
Cdd:cd19156 258 RYGPD 262
|
|
| AKR_AKR2C1 |
cd19114 |
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ... |
26-307 |
1.01e-09 |
|
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.
Pssm-ID: 381340 [Multi-domain] Cd Length: 302 Bit Score: 58.72 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 26 GYGPA-TDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATKFGFTFgddnkqqiln 97
Cdd:cd19114 8 GFGTAkIKANETEEVIYNAIKVGYRLIDGALLYG---NEAEVGRGIRKAiqeglvkREDLFIVTKLWNNF---------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 98 SRPEHIREAVEGSLRRLKTDVIDLLYQH------RVDP-------------------DVPIEDVAGTVKDLIAEGKVKHF 152
Cdd:cd19114 75 HGKDHVREAFDRQLKDYGLDYIDLYLIHfpipaaYVDPaenypflwkdkelkkfpleQSPMQECWREMEKLVDAGLVRNI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 153 GLSEAGAQTIRR--AHAVQPVTALQSEYSMWWrePEQEILPLLEELGIGFVPFSPLGKGFLTGAIKPGTTFgkddyrstV 230
Cdd:cd19114 155 GIANFNVQLILDllTYAKIKPAVLQIEHHPYL--QQKRLIDWAKKQGIQITAYSSFGNAVYTKVTKHLKHF--------T 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447095029 231 PRFAAQAIEAneklvtllgeLAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19114 225 NLLEHPVVKK----------LADKHKRDTGQVLLRWAVQRN--ITVIPKSVNVERMKTNLDITSYKLDEEDMEALYE 289
|
|
| AKR_AKR2D1 |
cd19115 |
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose ... |
43-307 |
2.12e-09 |
|
AKR2D family of aldo-keto reductase (AKR); Aspergillus niger NAD(P)H-dependent D-xylose reductase xyl1 (XR, EC 1.1.1.307) is a founding member of aldo-keto reductase family 2 member D1 (AKR2D1). It catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol in a NAD(P)H dependent manner.
Pssm-ID: 381341 [Multi-domain] Cd Length: 311 Bit Score: 57.82 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 43 AVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIATKFGFTFGDdnkqqilnsrPEHIREAVEGSLRRLK 115
Cdd:cd19115 35 AIKAGYRLFDGACDYG---NEVEAGQGVARAikegivkREDLFIVSKLWNTFHD----------GERVEPICRKQLADWG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 116 TDVIDLLYQH------RVDPDV------------------PIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIR---RAHAV 168
Cdd:cd19115 102 IDYFDLFLIHfpialkYVDPAVryppgwfydgkkvefsnaPIQETWTAMEKLVDKGLARSIGVSNFSAQLLMdllRYARI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 169 QPVTaLQSEYSMWWREPEqeILPLLEELGIGFVPFSPLG-KGFLTgaikpgttFGKDDYRSTVPRFAAQAIEAneklvtl 247
Cdd:cd19115 182 RPAT-LQIEHHPYLTQPR--LVKYAQKEGIAVTAYSSFGpQSFLE--------LDLPGAKDTPPLFEHDVIKS------- 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 248 lgeLAAEKGVTSAQIALAWllAQKPWIVPIPGTTKLNRLEENLAAADIVLSQKDTQQITE 307
Cdd:cd19115 244 ---IAEKHGKTPAQVLLRW--ATQRGIAVIPKSNNPKRLAQNLDVTGFDLEAEEIKAISA 298
|
|
| AKR_AKR3B1-3 |
cd19118 |
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ... |
40-307 |
2.76e-09 |
|
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: 57.04 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 40 IRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF--------RDRVVIATKFGFTFgddnkqqilnSRPEHIREAVEGSL 111
Cdd:cd19118 26 VKIALKAGYRHLDLAKVYQ---NQHEVGQALKELlkeepgvkREDLFITSKLWNNS----------HRPEYVEPALDDTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 112 RRLKTDVIDLLYQH-----------RVDPDVPIED----------VAGTVKDLIA---EGKVKHFGLSEAGA---QTIRR 164
Cdd:cd19118 93 KELGLDYLDLYLIHwpvafkptgdlNPLTAVPTNGgevdldlsvsLVDTWKAMVElkkTGKVKSIGVSNFSIdhlQAIIE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 165 AHAVQPVTAlQSEYSMwwREPEQEILPLLEELGIGFVPFSPLGkgfltgaikpGTTFGKddyrstvPRfaaqaIEANEKL 244
Cdd:cd19118 173 ETGVVPAVN-QIEAHP--LLLQDELVDYCKSKNIHITAYSPLG----------NNLAGL-------PL-----LVQHPEV 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447095029 245 VtllgELAAEKGVTSAQIALAWllAQKPWIVPIPGTTKLNRLEENLaaADIVLSQKDTQQITE 307
Cdd:cd19118 228 K----AIAAKLGKTPAQVLIAW--GIQRGHSVIPKSVTPSRIRSNF--EQVELSDDEFNAVTA 282
|
|
| AKR_AKR3E1 |
cd19122 |
AKR3E family of aldo-keto reductase (AKR); Trichoderma reesei NADP(+)-dependent glycerol ... |
60-310 |
4.74e-08 |
|
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: 53.39 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 60 YLNEEVVGEALKPF--------RDRVVIATKfgftfgddnkqqILNS--RPEHIREAVEGSLRRLKTDVIDLLYQH---- 125
Cdd:cd19122 47 YLNEDEVGDAVRDFlkenpsvkREDLFICTK------------VWNHlhEPEDVKWSIDNSLKNLKLDYIDLFLVHwpia 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 126 ---------RVDPD---VPIEDVAG-------TVKDLIAEGKVKHFGLSE---AGAQTIRRAHAVQPvTALQSEYSMWWr 183
Cdd:cd19122 115 aekndqrspKLGPDgkyVILKDLTEnpeptwrAMEEIYESGKAKAIGVSNwtiPGLKKLLSFAKVKP-HVNQIEIHPFL- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 184 ePEQEILPLLEELGIGFVPFSPLGKgfltgaikpgttfgkddyRSTVPRfAAQAIEANEklvtLLGELAAEKGVTSAQIA 263
Cdd:cd19122 193 -PNEELVDYCFSNDILPEAYSPLGS------------------QNQVPS-TGERVSENP----TLNEVAEKGGYSLAQVL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 447095029 264 LAWLLaQKPWIVpIPGTTKLNRLEENLAAADivLSQKDTQQITEALE 310
Cdd:cd19122 249 IAWGL-RRGYVV-LPKSSTPSRIESNFKSIE--LSDEDFEAINQVAK 291
|
|
| AKR_AKR3C1 |
cd19119 |
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ... |
9-307 |
4.36e-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: 50.57 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 9 SGLEVSALGLGCmglshgYGPATDTRQAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKPF-------RDRVVIAT 81
Cdd:cd19119 8 TGASIPALGLGT------ASPHEDRAEVKEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgsikREELFITT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 82 KFGFTFGDdnkqqilnsrpeHIREAVEGSLRRLKTDVIDLLYQH-----------------RVDPDVPIEDVAG-----T 139
Cdd:cd19119 79 KVWPTFYD------------EVERSLDESLKALGLDYVDLLLVHwpvcfekdsddsgkpftPVNDDGKTRYAASgdhitT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 140 VKDL---IAEGKVKHFGLSEAGAQTIRRAHAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGfltgaik 216
Cdd:cd19119 147 YKQLekiYLDGRAKAIGVSNYSIVYLERLIKECKVVPAVNQVELHPHLPQMDLRDFCFKHGILVTAYSPLGSH------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 217 pgttfgkddyrstvprfaAQAIEANEKLVtllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAadIV 296
Cdd:cd19119 220 ------------------GAPNLKNPLVK----KIAEKYNVSTGDILISYHVRQG--VIVLPKSLKPVRIVSNGKI--VS 273
|
330
....*....|.
gi 447095029 297 LSQKDTQQITE 307
Cdd:cd19119 274 LTKEDLQKLDD 284
|
|
| AKR_AKR5H1 |
cd19134 |
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ... |
15-305 |
2.01e-06 |
|
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: 48.31 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 15 ALGLGCMGLSHgygpaTDTRQAIElirAAVERGVTFFDTAEVYGpylNEEVVGEALKPF---RDRVVIATKF-----GFT 86
Cdd:cd19134 13 VIGLGVGELSD-----DEAERSVS---AALEAGYRLIDTAAAYG---NEAAVGRAIAASgipRGELFVTTKLatpdqGFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 87 fgddnkqqilnsrpeHIREAVEGSLRRLKTDVIDLLYQHRVDPDV-PIEDVAGTVKDLIAEGKVKHFGLSEAGAQTIRRA 165
Cdd:cd19134 82 ---------------ASQAACRASLERLGLDYVDLYLIHWPAGREgKYVDSWGGLMKLREEGLARSIGVSNFTAEHLENL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 166 HAVQPVTALQSEYSMWWREPEQEILPLLEELGIGFVPFSPLGKGfltgaikpgttfgkddyrstvprfaaQAIEANEklV 245
Cdd:cd19134 147 IDLTFFTPAVNQIELHPLLNQAELRKVNAQHGIVTQAYSPLGVG--------------------------RLLDNPA--V 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 246 TllgELAAEKGVTSAQIALAWLLAQKpwIVPIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19134 199 T---AIAAAHGRTPAQVLLRWSLQLG--NVVISRSSNPERIASNLDVFDFELTADHMDAL 253
|
|
| AKR_AKR1C1-35 |
cd19108 |
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) ... |
35-125 |
2.89e-05 |
|
AKR1C family of aldo-keto reductase (AKR); The AKR1C family of aldo-keto reductase (AKR) includes AKR1C1 (20-alpha-hydroxysteroid dehydrogenase, also known as 20alpha-HSD), AKR1C2 (3alpha-HSD type 3), AKR1C3 (17beta-HSD type 5), and AKR1C4 (3alpha-HSD type 1) from Homo sapiens; AKR1C5 (20alpha-HSD, also known as prostaglandin-E(2) 9-reductase) from Rattus norvegicus (ovary); AKR1C6 (estradiol 17beta-HSD type 5) from Mus musculus; AKR1C7 (prostaglandin F synthase 1 or PGF1) from Bos taurus (lung); AKR1C8 (20alpha-HSD) from Rattus norvegicus (ovary); AKR1C9 (3alpha-HSD) from Rattus norvegicus (liver); AKR1C10a (Rho crystallin) from Rana temporaria and AKR1C10b (Rho crystallin) from Rana catesbeina; AKR1C11 (prostaglandin F synthase 2 or PGF2) from Bos taurus (liver); AKR1C12 (aldo-keto reductase or AKR), AKR1C13 (interleukin-3-regulated AKR), and AKR1C14 (3alpha-HSD) from Mus musculus; AKR1C15 (NADPH-dependent reductase), AKR1C16 (NAD+-preferring 3alpha/17beta/20alpha-HSD), and AKR1C17 (NAD+-dependent 3alpha-HSD) from Rattus norvegicus; AKR1C18 (20alpha-HSD), AKR1C19 (3-hydroxybutyrate dehydrogenase or 3HB dehydrogenase), AKR1C20 (3alpha(17beta)-HSD), AKR1C21 (3(17)alpha-HSD), AKR1C22 (dihydrodiol dehydrogenase or DD) from Mus musculus; AKR1C23 (20alpha-HSD) from Equus caballus; AKR1C24 (NAD+-dependent 17beta-HSD) from Rattus norvegicus; AKR1C25 (3(20)alpha-HSD) from Macaca fuscata; AKR1C26 (identical to morphine 6-dehydrogenase or M6DH, acts as NAD(+)-dependent 3alpha/17beta-HSD), AKR1C27/AKR1C28 (NAD(+)-dependent 3alpha/17beta-HSDs), AKR1C29 (identical to 3-hydroxyhexobarbital dehydrogenase or 3HBD, acts as NADPH-preferring reductase with 3alpha/3beta/17beta/20alpha-HSD activity), AKR1C30 (identical to naloxone reductase type 1 and acts as 17beta-HSD), AKR1C31 (3alpha/17beta/20alpha-HSD), AKR1C32 (identical to loxoprofen reductase and acts as 3alpha/20alpha-HSD), and AKR1C33 (identical to naloxone reductase type 2 and mainly acts as 3alpha-HSD) from Oryctolagus cuniculus; AKR1C34 (NAD+-dependent morphine 6-dehydrogenase or M6DH with 3beta/17beta/20alpha-HSD activity) and AKR1C35 (NAD+-dependent dehydrogenase with 3(17)beta-HSD activity) from Mesocricetus auratus.
Pssm-ID: 381334 [Multi-domain] Cd Length: 303 Bit Score: 44.91 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 35 QAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALKP-------FRDRVVIATKFGFTFgddnkqqilnSRPEHIREAV 107
Cdd:cd19108 28 KALEATKLAIDAGFRHIDSAYLYQ---NEEEVGQAIRSkiadgtvKREDIFYTSKLWCTF----------HRPELVRPAL 94
|
90
....*....|....*...
gi 447095029 108 EGSLRRLKTDVIDLLYQH 125
Cdd:cd19108 95 EKSLKKLQLDYVDLYLIH 112
|
|
| AKR_AKR1B1-19 |
cd19107 |
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase ... |
35-305 |
1.58e-04 |
|
AKR1B family of aldo-keto reductase (AKR); The AKR1B family of AKR includes aldose reductase (AR, EC 1.1.1.21) from Homo sapiens (AKR1B1), Oryctolagus cuniculus (kidney, AKR1B2), Mus musculus (AKR1B3), Rattus norvegicus (lens, AKR1B4), Bos taurus (lens/testis, AKR1B5), and Sus scrofa (lens, AKR1B6), aldose reductase-related protein 1 (ALD1, EC1.1.1.21) from Mus musculus (AKR1B7), Rattus norvegicus (AKR1B14), and Homo sapiens (AKR1B15), Mus musculus fibroblast growth factor induced protein (FR-1 or AKR1B8, EC 1.1.1.21), Cricetulus griseus aldose reductase-related protein 2 (ALD2 or AKR1B9, EC 1.1.1.21), aldose reductase-like from Homo sapiens (ARL-1 or AKR1B10) and Rattus norvegicus (AKR1B13), aldo-keto reductase from Gallus domesticus (eye, tongue, esophagus, AKR1B12), and Oryctolagus cuniculus AR-like protein (3beta-HSD, AKR1B19). AR, also called aldehyde reductase, catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. ALD1 reduces a broad range of aliphatic and aromatic aldehydes to the corresponding alcohols. It may play a role in the metabolism of xenobiotic aromatic aldehydes. FR-1, also called aldose reductase-related protein 2, or fibroblast growth factor-regulated protein (FGFRP), is induced by fibroblast growth factor-1. It may play a role in the regulation of the cell cycle. FR-1 belongs to the NADPH-dependent aldo-keto reductase family. ALD2 is an inducible aldo-keto reductase with a preference for aliphatic substrates. It can also act on small aromatic aldehydes, steroid aldehydes and some ketone substrates. ARL-1, also called aldose reductase-like, or aldose reductase-related protein (ARP), or small intestine reductase, or SI reductase, acts as all-trans-retinaldehyde reductase that can efficiently reduce aliphatic and aromatic aldehydes, and is less active on hexoses (in vitro). It may be responsible for detoxification of reactive aldehydes in the digested food before the nutrients are passed on to other organs. AKR1B15, also called estradiol 17-beta-dehydrogenase AKR1B15, is a mitochondrial aldo-keto reductase that catalyzes the reduction of androgens and estrogens with high positional selectivity (shows 17-beta-hydroxysteroid dehydrogenase activity) as well as 3-keto-acyl-CoAs. It has a strong selectivity towards NADP(H). AKR1B19 is aldose reductase-like that may show 3-beta-hydroxysteroid dehydrogenase (3beta-HSD) activity.
Pssm-ID: 381333 [Multi-domain] Cd Length: 307 Bit Score: 42.79 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 35 QAIELIRAAVERGVTFFDTAEVYGpylNEEVVGEALK-PFRDRVV------IATKFGFTFGDDNKqqilnsrpehIREAV 107
Cdd:cd19107 18 QVTEAVKVAIDAGYRHIDCAYVYQ---NENEVGEAIQeKIKEQVVkredlfIVSKLWCTFHEKGL----------VKGAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 108 EGSLRRLKTDVIDLLYQH-----RVDPDVPIEDVAGTV--------------KDLIAEGKVKHFGLSEAGAQTIRR---- 164
Cdd:cd19107 85 QKTLSDLKLDYLDLYLIHwptgfKPGKELFPLDESGNVipsdttfldtweamEELVDEGLVKAIGVSNFNHLQIERilnk 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447095029 165 -AHAVQPVTAlQSEYSMWWRepEQEILPLLEELGIGFVPFSPLGkgfltgaiKPGTTFGKDDYRSTV--PRfaaqaiean 241
Cdd:cd19107 165 pGLKYKPAVN-QIECHPYLT--QEKLIQYCQSKGIVVTAYSPLG--------SPDRPWAKPEDPSLLedPK--------- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447095029 242 eklvtlLGELAAEKGVTSAQIALAWLLaQKPWIVpIPGTTKLNRLEENLAAADIVLSQKDTQQI 305
Cdd:cd19107 225 ------IKEIAAKHNKTTAQVLIRFPI-QRNLVV-IPKSVTPERIAENFKVFDFELSSEDMATI 280
|
|
| |
