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Conserved domains on  [gi|490304600|ref|WP_004199885|]
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MULTISPECIES: aldo/keto reductase [Klebsiella]

Protein Classification

aldo/keto reductase( domain architecture ID 14442375)

aldo/keto reductase (AKR) is a soluble NAD(P)(H) oxidoreductase that catalyzes the reduction of aldehydes and/or ketones to their corresponding primary and/or secondary alcohols

CATH:  3.20.20.100
EC:  1.-.-.-
Gene Ontology:  GO:0016491

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
74-372 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: 507.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYGGgPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVEE 153
Cdd:cd19078    2 LEVSAIGLGCMGMSHGYGP-PPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 154 GKPTS--LNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV 231
Cdd:cd19078   81 GKPGPlgLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEFA 311
Cdd:cd19078  161 CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVDLL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304600 312 QSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19078  241 KEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
 
Name Accession Description Interval E-value
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
74-372 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: 507.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYGGgPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVEE 153
Cdd:cd19078    2 LEVSAIGLGCMGMSHGYGP-PPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 154 GKPTS--LNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV 231
Cdd:cd19078   81 GKPGPlgLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEFA 311
Cdd:cd19078  161 CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVDLL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304600 312 QSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19078  241 KEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
67-376 3.12e-121

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: 353.71  E-value: 3.12e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  67 TTRKLGS--LEVSSMGLGCLPMVGYYGggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVI 143
Cdd:COG0667    2 EYRRLGRsgLKVSRLGLGTMTFGGPWG--GVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRpRDDVVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASAR 223
Cdd:COG0667   80 ATKVGRRMGPG-PNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 224 TIRRAHAVL----PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRhNLPRFQPD 299
Cdd:COG0667  159 QLRRALAIAeglpPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRA-ATNFVQGY 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 300 ALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAALAKIP 376
Cdd:COG0667  238 LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAAVP 314
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
103-372 4.95e-79

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: 244.91  E-value: 4.95e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  103 LIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVIATKFGFGVEEGKPtslNSHPDHIRRAVEGSLKRLKT 179
Cdd:pfam00248  23 ALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpvkRDKVVIATKVPDGDGPWPS---GGSKENIRKSLEESLKRLGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  180 DHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRA--HAVLPVTAVQSEYAMWWREPETRIFPTLE 257
Cdd:pfam00248 100 DYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAltKGKIPIVAVQVEYNLLRRRQEEELLEYCK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  258 ELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPdalaKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWI 337
Cdd:pfam00248 180 KNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTP----LNLEALEALEEIAKEHGVSPAQVALRWALSKPGVT 255
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490304600  338 VPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:pfam00248 256 IPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
PRK10376 PRK10376
putative oxidoreductase; Provisional
68-370 1.70e-41

putative oxidoreductase; Provisional


Pssm-ID: 236676 [Multi-domain]  Cd Length: 290  Bit Score: 147.81  E-value: 1.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGSLEVSSMGLGCLPMVG-YYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATK 146
Cdd:PRK10376   9 TFTLGGRSVNRLGYGAMQLAGpGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FGF--GVEEGKPTSLNshPDHIRRAVEGSLKRLKTDHIDLLY------QHRPDPNvPIEDVAETVKALILEGKVKHWGLS 218
Cdd:PRK10376  89 VGArrGEDGSWLPAFS--PAELRRAVHDNLRNLGLDVLDVVNlrlmgdGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 219 EASARTIRRAHAVLPVTAVQSEYAMWWREPETRIfPTLEELGIGFVPYCPTarsflaGAVNPsqrfdstdrrhnlprFQP 298
Cdd:PRK10376 166 NVTPTQVAEARKIAEIVCVQNHYNLAHRADDALI-DALARDGIAYVPFFPL------GGFTP---------------LQS 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 299 DALAknmvllefaqSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:PRK10376 224 STLS----------DVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDG 285
 
Name Accession Description Interval E-value
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
74-372 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: 507.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYGGgPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVEE 153
Cdd:cd19078    2 LEVSAIGLGCMGMSHGYGP-PPDKEEMIELIRKAVELGITFFDTAEVYGPYTNEELVGEALKPFRDQVVIATKFGFKIDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 154 GKPTS--LNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV 231
Cdd:cd19078   81 GKPGPlgLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDPNVPIEEVAGTMKELIKEGKIRHWGLSEAGVETIRRAHAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEFA 311
Cdd:cd19078  161 CPVTAVQSEYSMMWREPEKEVLPTLEELGIGFVPFSPLGKGFLTGKIDENTKFDEGDDRASLPRFTPEALEANQALVDLL 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304600 312 QSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19078  241 KEFAEEKGATPAQIALAWLLAKKPWIVPIPGTTKLSRLEENIGAADIELTPEELREIEDAL 301
AKR_AKR13A_13D cd19076
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...
68-368 1.37e-146

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: 417.39  E-value: 1.37e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMVGYYGggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIAT 145
Cdd:cd19076    2 TRKLGTqgLEVSALGLGCMGMSAFYG--PADEEESIATLHRALELGVTFLDTADMYGPGTNEELLGKALKDRRDEVVIAT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFGFGVEEG-KPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASART 224
Cdd:cd19076   80 KFGIVRDPGsGFRGVDGRPEYVRAACEASLKRLGTDVIDLYYQHRVDPNVPIEETVGAMAELVEEGKVRYIGLSEASADT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 225 IRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKN 304
Cdd:cd19076  160 IRRAHAVHPITAVQSEYSLWTRDIEDEVLPTCRELGIGFVAYSPLGRGFLTGAIKSPEDLPEDDFRRNNPRFQGENFDKN 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304600 305 MVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREI 368
Cdd:cd19076  240 LKLVEKLEAIAAEKGCTPAQLALAWVLAQGDDIVPIPGTKRIKYLEENVGALDVVLTPEELAEI 303
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
67-376 3.12e-121

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: 353.71  E-value: 3.12e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  67 TTRKLGS--LEVSSMGLGCLPMVGYYGggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVI 143
Cdd:COG0667    2 EYRRLGRsgLKVSRLGLGTMTFGGPWG--GVDEAEAIAILDAALDAGINFFDTADVYGPGRSEELLGEALKGRpRDDVVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASAR 223
Cdd:COG0667   80 ATKVGRRMGPG-PNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPDTPIEETLGALDELVREGKIRYIGVSNYSAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 224 TIRRAHAVL----PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRhNLPRFQPD 299
Cdd:COG0667  159 QLRRALAIAeglpPIVAVQNEYSLLDRSAEEELLPAARELGVGVLAYSPLAGGLLTGKYRRGATFPEGDRA-ATNFVQGY 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 300 ALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAALAKIP 376
Cdd:COG0667  238 LTERNLALVDALRAIAAEHGVTPAQLALAWLLAQPGVTSVIPGARSPEQLEENLAAADLELSAEDLAALDAALAAVP 314
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
68-368 1.95e-116

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: 340.95  E-value: 1.95e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMVGYYGGgPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEAL-APVRDRVVIA 144
Cdd:cd19145    2 RVKLGSqgLEVSAQGLGCMGLSGDYGA-PKPEEEGIALIHHAFNSGVTFLDTSDIYGPNTNEVLLGKALkDGPREKVQLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFGFGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASART 224
Cdd:cd19145   81 TKFGIHEIGGSGVEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRIDTTVPIEITMGELKKLVEEGKIKYIGLSEASADT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 225 IRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKN 304
Cdd:cd19145  161 IRRAHAVHPITAVQLEWSLWTRDIEEEIIPTCRELGIGIVPYSPLGRGFFAGKAKLEELLENSDVRKSHPRFQGENLEKN 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304600 305 MVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREI 368
Cdd:cd19145  241 KVLYERVEALAKKKGCTPAQLALAWVLHQGEDVVPIPGTTKIKNLNQNIGALSVKLTKEDLKEI 304
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
73-369 1.16e-106

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: 315.62  E-value: 1.16e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  73 SLEVSSMGLGCLPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVE 152
Cdd:cd19084    1 DLKVSRIGLGTWAIGGTWWGEVDDQES-IEAIKAAIDLGINFFDTAPVYGFGHSEEILGKALKGRRDDVVIATKCGLRWD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 EGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDlLYQ-HRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV 231
Cdd:cd19084   80 GGKGVTKDLSPESIRKEVEQSLRRLQTDYID-LYQiHWPDPNTPIEETAEALEKLKKEGKIRYIGVSNFSVEQLEEARKY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEFA 311
Cdd:cd19084  159 GPIVSLQPPYSMLEREIEEELLPYCRENGIGVLPYGPLAQGLLTGKYKKEPTFPPDDRRSRFPFFRGENFEKNLEIVDKL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 312 QSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19084  239 KEIAEKYGKSLAQLAIAWTLAQPGVTSAIVGAKNPEQLEENAGALDWELTEEELKEID 296
AKR_AKR13A1 cd19144
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...
66-381 2.83e-94

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: 285.11  E-value: 2.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  66 LTTRKLGSL--EVSSMGLGCLPMVGYYGGGPRDRKAMvSLIRAAFEQGITFFDTAEVYGPHlsEEFVGE--ALAP-VRDR 140
Cdd:cd19144    1 IPTRTLGRNgpSVPALGFGAMGLSAFYGPPKPDEERF-AVLDAAFELGCTFWDTADIYGDS--EELIGRwfKQNPgKREK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 141 VVIATKFGF-GVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSE 219
Cdd:cd19144   78 IFLATKFGIeKNVETGEYSVDGSPEYVKKACETSLKRLGVDYIDLYYQHRVDGKTPIEKTVAAMAELVQEGKIKHIGLSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 220 ASARTIRRAHAVLPVTAVQSEYAMW---WREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRF 296
Cdd:cd19144  158 CSAETLRRAHAVHPIAAVQIEYSPFsldIERPEIGVLDTCRELGVAIVAYSPLGRGFLTGAIRSPDDFEEGDFRRMAPRF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 297 QPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAALAKIP 376
Cdd:cd19144  238 QAENFPKNLELVDKIKAIAKKKNVTAGQLTLAWLLAQGDDIIPIPGTTKLKRLEENLGALKVKLTEEEEKEIREIAEEAE 317

                 ....*
gi 490304600 377 LQGGR 381
Cdd:cd19144  318 VVGER 322
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
76-371 4.29e-87

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: 265.60  E-value: 4.29e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  76 VSSMGLGCLPMVGYYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGveegk 155
Cdd:cd19085    1 VSRLGLGCWQFGGGYWWGDQDDEESIATIHAALDAGINFFDTAEAYGDGHSEEVLGKALKGRRDDVVIATKVSPD----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 ptslNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVLPVT 235
Cdd:cd19085   76 ----NLTPEDVRKSCERSLKRLGTDYIDLYQIHWPSSDVPLEETMEALEKLKEEGKIRAIGVSNFGPAQLEEALDAGRID 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 236 AVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPR-FQPDALAKNMVLLEFAQSW 314
Cdd:cd19085  152 SNQLPYNLLWRAIEYEILPFCREHGIGVLAYSPLAQGLLTGKFSSAEDFPPGDARTRLFRhFEPGAEEETFEALEKLKEI 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 315 ARRKNTTPVQFALAWVMaQRPWIV-PIPGTTQYPHLIENSGAPQVRLTDRELREIDAA 371
Cdd:cd19085  232 ADELGVTMAQLALAWVL-QQPGVTsVIVGARNPEQLEENAAAVDLELSPSVLERLDEI 288
AKR_AKR8A1-2 cd19077
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ...
72-369 9.26e-85

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: 260.25  E-value: 9.26e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  72 GSLEVSSMGLGCLPMVGyyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYG---PHLSEEFVGEALA---PVRDRVVIAT 145
Cdd:cd19077    1 NGKLVGPIGLGLMGLTW--RPNPTPDEEAFETMKAALDAGSNLWNGGEFYGppdPHANLKLLARFFRkypEYADKVVLSV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFGFGVEEGKPTSlnsHPDHIRRAVEGSLKRLK-TDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASART 224
Cdd:cd19077   79 KGGLDPDTLRPDG---SPEAVRKSIENILRALGgTKKIDIFEPARVDPNVPIEETIKALKELVKEGKIRGIGLSEVSAET 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 225 IRRAHAVLPVTAVQSEYAMWWREPETR-IFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAK 303
Cdd:cd19077  156 IRRAHAVHPIAAVEVEYSLFSREIEENgVLETCAELGIPIIAYSPLGRGLLTGRIKSLADIPEGDFRRHLDRFNGENFEK 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 304 NMVLLEFAQSWARRKNTTPVQFALAWVMAQ-RPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19077  236 NLKLVDALQELAEKKGCTPAQLALAWILAQsGPKIIPIPGSTTLERVEENLKAANVELTDEELKEIN 302
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
68-370 8.30e-80

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: 247.96  E-value: 8.30e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMVGYYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIAT 145
Cdd:cd19149    1 YRKLGKsgIEASVIGLGTWAIGGGPWWGGSDDNESIRTIHAALDLGINLIDTAPAYGFGHSEEIVGKAIKGRRDKVVLAT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFG----------FGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHW 215
Cdd:cd19149   81 KCGlrwdreggsfFFVRDGVTVYKNLSPESIREEVEQSLKRLGTDYIDLYQTHWQDVETPIEETMEALEELKRQGKIRAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 216 GLSEASARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPR 295
Cdd:cd19149  161 GASNVSVEQIKEYVKAGQLDIIQEKYSMLDRGIEKELLPYCKKNNIAFQAYSPLEQGLLTGKITPDREFDAGDARSGIPW 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304600 296 FQPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19149  241 FSPENREKVLALLEKWKPLCEKYGCTLAQLVIAWTLAQPGITSALCGARKPEQAEENAKAGDIRLSAEDIATMRS 315
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
103-372 4.95e-79

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: 244.91  E-value: 4.95e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  103 LIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVIATKFGFGVEEGKPtslNSHPDHIRRAVEGSLKRLKT 179
Cdd:pfam00248  23 ALRAALEAGINFIDTAEVYGDGKSEELLGEALKDYpvkRDKVVIATKVPDGDGPWPS---GGSKENIRKSLEESLKRLGT 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  180 DHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRA--HAVLPVTAVQSEYAMWWREPETRIFPTLE 257
Cdd:pfam00248 100 DYIDLYYLHWPDPDTPIEETWDALEELKKEGKIRAIGVSNFDAEQIEKAltKGKIPIVAVQVEYNLLRRRQEEELLEYCK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  258 ELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPdalaKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWI 337
Cdd:pfam00248 180 KNGIPLIAYSPLGGGLLTGKYTRDPDKGPGERRRLLKKGTP----LNLEALEALEEIAKEHGVSPAQVALRWALSKPGVT 255
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 490304600  338 VPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:pfam00248 256 IPIPGASNPEQLEDNLGALEFPLSDEEVARIDELL 290
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
76-361 2.53e-76

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: 236.73  E-value: 2.53e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  76 VSSMGLGCLPMVGYYG-GGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVEEG 154
Cdd:cd19088    1 VSRLGYGAMRLTGPGIwGPPADREEAIAVLRRALELGVNFIDTADSYGPDVNERLIAEALHPYPDDVVIATKGGLVRTGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 155 KPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVLPV 234
Cdd:cd19088   81 GWWGPDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDPKVPFEEQLGALAELQDEGLIRHIGLSNVTVAQIEEARAIVRI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 235 TAVQSEYAMWWREPETrIFPTLEELGIGFVPYCPtarsfLAGAvnpsqrfdstdrrhnlprfqpdALAKNMVLLefaQSW 314
Cdd:cd19088  161 VSVQNRYNLANRDDEG-VLDYCEAAGIAFIPWFP-----LGGG----------------------DLAQPGGLL---AEV 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490304600 315 ARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLT 361
Cdd:cd19088  210 AARLGATPAQVALAWLLARSPVMLPIPGTSSVEHLEENLAAAGLRLS 256
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
76-372 1.11e-74

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: 234.10  E-value: 1.11e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  76 VSSMGLGCLPMVG---YYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFG-FGV 151
Cdd:cd19102    1 LTTIGLGTWAIGGggwGGGWGPQDDRDSIAAIRAALDLGINWIDTAAVYGLGHSEEVVGRALKGLRDRPIVATKCGlLWD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 152 EEGKPTSLNShPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV 231
Cdd:cd19102   81 EEGRIRRSLK-PASIRAECEASLRRLGVDVIDLYQIHWPDPDEPIEEAWGALAELKEEGKVRAIGVSNFSVDQMKRCQAI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPS--QRFDSTDRRHNLPRFQPDALAKNMVLLE 309
Cdd:cd19102  160 HPIASLQPPYSLLRRGIEAEILPFCAEHGIGVIVYSPMQSGLLTGKMTPErvASLPADDWRRRSPFFQEPNLARNLALVD 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304600 310 FAQSWARRKNTTPVQFALAWVMAqRPWIV-PIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19102  240 ALRPIAERHGRTVAQLAIAWVLR-RPEVTsAIVGARRPDQIDETVGAADLRLTPEELAEIEALL 302
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
77-352 4.71e-70

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: 220.08  E-value: 4.71e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  77 SSMGLGCLPMvgyygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA--PVRDRVVIATKFGFGVEEG 154
Cdd:cd06660    1 SRLGLGTMTF-----GGDGDEEEAFALLDAALEAGGNFFDTADVYGDGRSERLLGRWLKgrGNRDDVVIATKGGHPPGGD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 155 KPTSLNShPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVL-- 232
Cdd:cd06660   76 PSRSRLS-PEHIRRDLEESLRRLGTDYIDLYYLHRDDPSTPVEETLEALNELVREGKIRYIGVSNWSAERLAEALAYAka 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 233 ----PVTAVQSEYAMWWREP-ETRIFPTLEELGIGFVPYCPTARsflaGavnpsqrfdstdrrhnlprfqpdalaknmvl 307
Cdd:cd06660  155 hglpGFAAVQPQYSLLDRSPmEEELLDWAEENGLPLLAYSPLAR----G------------------------------- 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490304600 308 lefaqswarrknttPVQFALAWVMAQRPWIVPIPGTTQYPHLIEN 352
Cdd:cd06660  200 --------------PAQLALAWLLSQPFVTVPIVGARSPEQLEEN 230
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
68-371 1.60e-69

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: 221.14  E-value: 1.60e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLG--SLEVSSMGLGclpmVGYYGGG---PR-DRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA-PVRDR 140
Cdd:cd19083    1 KVKLGksDIDVNPIGLG----TNAVGGHnlyPNlDEEEGKDLVREALDNGVNLLDTAFIYGLGRSEELVGEVLKeYNRNE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 141 VVIATKFGFGVEEGKpTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEA 220
Cdd:cd19083   77 VVIATKGAHKFGGDG-SVLNNSPEFLRSAVEKSLKRLNTDYIDLYYIHFPDGETPKAEAVGALQELKDEGKIRAIGVSNF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 221 SARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDA 300
Cdd:cd19083  156 SLEQLKEANKDGYVDVLQGEYNLLQREAEEDILPYCVENNISFIPYFPLASGLLAGKYTKDTKFPDNDLRNDKPLFKGER 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 301 LAKNMVLLEFAQSWARRKNTTPVQFALAWVMAqRPWI-VPIPGTTQYPHLIENSGAPQVRLTDRELREIDAA 371
Cdd:cd19083  236 FSENLDKVDKLKSIADEKGVTVAHLALAWYLT-RPAIdVVIPGAKRAEQVIDNLKALDVTLTEEEIAFIDAL 306
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
69-370 3.15e-67

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: 215.51  E-value: 3.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLG--SLEVSSMGLGCLPMvgyygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATK 146
Cdd:cd19087    4 RTLGrtGLKVSRLCLGTMNF-----GGRTDEETSFAIMDRALDAGINFFDTADVYGGGRSEEIIGRWIAGRRDDIVLATK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FGFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEdvaETVKA---LILEGKVKHWGLSE---- 219
Cdd:cd19087   79 VFGPMGDD-PNDRGLSRRHIRRAVEASLRRLQTDYIDLYQMHHFDRDTPLE---ETLRAlddLVRQGKIRYIGVSNfaaw 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 220 --ASARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQ 297
Cdd:cd19087  155 qiAKAQGIAARRGLLRFVSEQPMYNLLKRQAELEILPAARAYGLGVIPYSPLAGGLLTGKYGKGKRPESGRLVERARYQA 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304600 298 PDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQrPWIV-PIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19087  235 RYGLEEYRDIAERFEALAAEAGLTPASLALAWVLSH-PAVTsPIIGPRTLEQLEDSLAALEITLTPELLAEIDE 307
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
74-355 3.15e-65

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: 207.72  E-value: 3.15e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATKFGFGVEE 153
Cdd:cd19086    1 LEVSEIGFGTWGLGGDWWGDVDDAEA-IRALRAALDLGINFFDTADVYGDGHSERLLGKALKGRRDKVVIATKFGNRFDG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 154 GKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNV-PIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVL 232
Cdd:cd19086   80 GPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHNPPDEVlDNDELFEALEKLKQEGKIRAYGVSVGDPEEALAALRRG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 233 PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGavnpsqrfdstdrrhnlprfqpdalaknmvllefaq 312
Cdd:cd19086  160 GIDVVQVIYNLLDQRPEEELFPLAEEHGVGVIARVPLASGLLTG------------------------------------ 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 490304600 313 swarrkntTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGA 355
Cdd:cd19086  204 --------KLAQAALRFILSHPAVSTVIPGARSPEQVEENAAA 238
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
70-369 6.38e-65

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: 209.36  E-value: 6.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  70 KLGS--LEVSSMGLGClpmVGYygGGPRDRKAMV------SLIRAAFEQGITFFDTAEVYGPHLSEEFVGEAL---APvR 138
Cdd:cd19079    4 RLGNsgLKVSRLCLGC---MSF--GDPKWRPWVLdeeesrPIIKRALDLGINFFDTANVYSGGASEEILGRALkefAP-R 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 139 DRVVIATKFGFGVEEGKPTSLNSHpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLS 218
Cdd:cd19079   78 DEVVIATKVYFPMGDGPNGRGLSR-KHIMAEVDASLKRLGTDYIDLYQIHRWDYETPIEETLEALHDVVKSGKVRYIGAS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 219 E------ASARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRhn 292
Cdd:cd19079  157 SmyawqfAKALHLAEKNGWTKFVSMQNHYNLLYREEEREMIPLCEEEGIGVIPWSPLARGRLARPWGDTTERRRSTTD-- 234
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 293 LPRFQPDALA-KNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19079  235 TAKLKYDYFTeADKEIVDRVEEVAKERGVSMAQVALAWLLSKPGVTAPIVGATKLEHLEDAVAALDIKLSEEEIKYLE 312
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
75-369 2.26e-64

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: 206.31  E-value: 2.26e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  75 EVSSMGLGCLPMVGYYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFgfgvee 153
Cdd:cd19072    3 EVPVLGLGTWGIGGGMSKDYSDDKKAIEALRYAIELGINLIDTAEMYGGGHAEELVGKAIKGFdREDLFITTKV------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 154 gkpTSLNSHPDHIRRAVEGSLKRLKTDHIDlLYQ-HRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVL 232
Cdd:cd19072   77 ---SPDHLKYDDVIKAAKESLKRLGTDYID-LYLiHWPNPSIPIEETLRAMEELVEEGKIRYIGVSNFSLEELEEAQSYL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 233 ---PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAvnpsqrfdstdrrhnlprfqpdalaknmVLLE 309
Cdd:cd19072  153 kkgPIVANQVEYNLFDREEESGLLPYCQKNGIAIIAYSPLEKGKLSNA----------------------------KGSP 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 310 FAQSWARRKNTTPVQFALAWVMaQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19072  205 LLDEIAKKYGKTPAQIALNWLI-SKPNVIAIPKASNIEHLEENAGALGWELSEEDLQRLD 263
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
74-362 5.74e-63

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: 203.98  E-value: 5.74e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGyyggGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFGFGVE 152
Cdd:cd19074    2 LKVSELSLGTWLTFG----GQVDDEDAKACVRKAYDLGINFFDTADVYAAGQAEEVLGKALKGWpRESYVISTKVFWPTG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 EGKPTSLNSHPdHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV- 231
Cdd:cd19074   78 PGPNDRGLSRK-HIFESIHASLKRLQLDYVDIYYCHRYDPETPLEETVRAMDDLIRQGKILYWGTSEWSAEQIAEAHDLa 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 -----LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAG-----AVNPSQRF--DSTDRRHNLPRFQPD 299
Cdd:cd19074  157 rqfglIPPVVEQPQYNMLWREIEEEVIPLCEKNGIGLVVWSPLAQGLLTGkyrdgIPPPSRSRatDEDNRDKKRRLLTDE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490304600 300 ALAKNMVLLEFAQswarRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTD 362
Cdd:cd19074  237 NLEKVKKLKPIAD----ELGLTLAQLALAWCLRNPAVSSAIIGASRPEQLEENVKASGVKLSP 295
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
74-372 7.13e-62

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: 201.38  E-value: 7.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA--PVRDRVVIATKFGFGV 151
Cdd:cd19148    2 LPVSRIALGTWAIGGWMWGGTDEKEA-IETIHKALDLGINLIDTAPVYGFGLSEEIVGKALKeyGKRDRVVIATKVGLEW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 152 EEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDlLYQ-HRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHA 230
Cdd:cd19148   81 DEGGEVVRNSSPARIRKEVEDSLRRLQTDYID-LYQvHWPDPLVPIEETAEALKELLDEGKIRAIGVSNFSPEQMETFRK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 231 VLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEF 310
Cdd:cd19148  160 VAPLHTVQPPYNLFEREIEKDVLPYARKHNIVTLAYGALCRGLLSGKMTKDTKFEGDDLRRTDPKFQEPRFSQYLAAVEE 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490304600 311 AQSWARRKNTTPV-QFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19148  240 LDKLAQERYGKSViHLAVRWLLDQPGVSIALWGARKPEQLDAVDEVFGWSLNDEDMKEIDAIL 302
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
69-369 3.60e-61

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: 199.75  E-value: 3.60e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMVGYYGGG--PRDRKAMVsliRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIA 144
Cdd:cd19080    1 RLLGRsgLRVSPLALGTMTFGTEWGWGadREEARAMF---DAYVEAGGNFIDTANNYTNGTSERLLGEFIAGNRDRIVLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFGFGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSE----- 219
Cdd:cd19080   78 TKYTMNRRPGDPNAGGNHRKNLRRSVEASLRRLQTDYIDLLYVHAWDFTTPVEEVMRALDDLVRAGKVLYVGISDtpawv 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 220 -ASARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRfdSTDRRHNLPRFQP 298
Cdd:cd19080  158 vARANTLAELRGWSPFVALQIEYSLLERTPERELLPMARALGLGVTPWSPLGGGLLTGKYQRGEE--GRAGEAKGVTVGF 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 299 DAL-AKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19080  236 GKLtERNWAIVDVVAAVAEELGRSAAQVALAWVRQKPGVVIPIIGARTLEQLKDNLGALDLTLSPEQLARLD 307
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
75-369 2.05e-57

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: 189.36  E-value: 2.05e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  75 EVSSMGLGCLPM--VGYYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA--PVRDRVVIATKFGfg 150
Cdd:cd19093    1 EVSPLGLGTWQWgdRLWWGYGEYGDEDLQAAFDAALEAGVNLFDTAEVYGTGRSERLLGRFLKelGDRDEVVIATKFA-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 151 veegkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVP-IEDVAETVKALILEGKVKHWGLSEASARTIRRAH 229
Cdd:cd19093   79 -----PLPWRLTRRSVVKALKASLERLGLDSIDLYQLHWPGPWYSqIEALMDGLADAVEEGLVRAVGVSNYSADQLRRAH 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 230 AVL-----PVTAVQSEYAMWWREPETR-IFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLPRFqpdaLAK 303
Cdd:cd19093  154 KALkergvPLASNQVEYSLLYRDPEQNgLLPACDELGITLIAYSPLAQGLLTGKYSPENPPPGGRRRLFGRKN----LEK 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 304 NMVLLEFAQSWARRKNTTPVQFALAWVMAQrpWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19093  230 VQPLLDALEEIAEKYGKTPAQVALNWLIAK--GVVPIPGAKNAEQAEENAGALGWRLSEEEVAELD 293
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
74-369 1.16e-56

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: 187.81  E-value: 1.16e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGClpMVGyygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPH-------LSEEFVGEALA--PVRDRVVIA 144
Cdd:cd19081    7 LSVSPLCLGT--MVF---GWTADEETSFALLDAFVDAGGNFIDTADVYSAWvpgnaggESETIIGRWLKsrGKRDRVVIA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFGFGVEEGKPtslNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASART 224
Cdd:cd19081   82 TKVGFPMGPNGP---GLSRKHIRRAVEASLRRLQTDYIDLYQAHWDDPATPLEETLGALNDLIRQGKVRYIGASNYSAWR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 225 IRRA------HAVLPVTAVQSEYAMWWREP-ETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRH-NLPRF 296
Cdd:cd19081  159 LQEAlelsrqHGLPRYVSLQPEYNLVDRESfEGELLPLCREEGIGVIPYSPLAGGFLTGKYRSEADLPGSTRRGeAAKRY 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490304600 297 QPDalaKNMVLLEFAQSWARRKNTTPVQFALAWVMAqRPWI-VPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19081  239 LNE---RGLRILDALDEVAAEHGATPAQVALAWLLA-RPGVtAPIAGARTVEQLEDLLAAAGLRLTDEEVARLD 308
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
69-371 4.21e-56

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: 186.66  E-value: 4.21e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCL------PMVGYYGGgpRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDR 140
Cdd:cd19091    4 RTLGRsgLKVSELALGTMtfggggGFFGAWGG--VDQEEADRLVDIALDAGINFFDTADVYSEGESEEILGKALKGRRDD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 141 VVIATKFGFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEA 220
Cdd:cd19091   82 VLIATKVRGRMGEG-PNDVGLSRHHIIRAVEASLKRLGTDYIDLYQLHGFDALTPLEETLRALDDLVRQGKVRYIGVSNF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 221 SARTIRRAHAV------LPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRRHNLP 294
Cdd:cd19091  161 SAWQIMKALGIserrglARFVALQAYYSLLGRDLEHELMPLALDQGVGLLVWSPLAGGLLSGKYRRGQPAPEGSRLRRTG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 295 RFQP---DALAKNMV--LLEFAQswarRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19091  241 FDFPpvdRERGYDVVdaLREIAK----ETGATPAQVALAWLLSRPTVSSVIIGARNEEQLEDNLGAAGLSLTPEEIARLD 316

                 ..
gi 490304600 370 AA 371
Cdd:cd19091  317 KV 318
AKR_AKR6C1_2 cd19143
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...
69-371 7.32e-50

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: 170.47  E-value: 7.32e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGClpMVGYygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVI 143
Cdd:cd19143    4 RRLGRsgLKVSALSFGS--WVTF--GNQVDVDEAKECMKAAYDAGVNFFDNAEVYANGQSEEIMGQAIKELgwpRSDYVV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEdvaETVKA---LILEGKVKHWGLSEA 220
Cdd:cd19143   80 STKIFWGGGGPPPNDRGLSRKHIVEGTKASLKRLQLDYVDLVFCHRPDPATPIE---ETVRAmndLIDQGKAFYWGTSEW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 221 SARTIRRAHAV------LPVTAVQSEYAMWWREP-ETRIFPTLEELGIGFVPYCPTARSFLAGAVN----PSQRFDSTDR 289
Cdd:cd19143  157 SAQQIEEAHEIadrlglIPPVMEQPQYNLFHRERvEVEYAPLYEKYGLGTTTWSPLASGLLTGKYNngipEGSRLALPGY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 290 RHNLPRFQPDALAKNMVLLEFAQSwARRKNTTPVQFALAWVmAQRPWI--VpIPGTTQYPHLIENSGAPQV--RLTDREL 365
Cdd:cd19143  237 EWLKDRKEELGQEKIEKVRKLKPI-AEELGCSLAQLAIAWC-LKNPNVstV-ITGATKVEQLEENLKALEVlpKLTPEVM 313

                 ....*.
gi 490304600 366 REIDAA 371
Cdd:cd19143  314 EKIEAI 319
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
74-364 3.14e-47

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: 162.73  E-value: 3.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMvgyyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA---PVRDRVVIATK---- 146
Cdd:cd19092    4 LEVSRLVLGCMRL----ADWGESAEELLSLIEAALELGITTFDHADIYGGGKCEELFGEALAlnpGLREKIEIQTKcgir 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FGFGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIR 226
Cdd:cd19092   80 LGDDPRPGRIKHYDTSKEHILASVEGSLKRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELVKSGKVRYFGVSNFTPSQIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 227 --RAHAVLPVTAVQSEYAMWWREP-ETRIFPTLEELGIGFVPYCPTARSFLAGAvnpsqrfdstdrrhNLPRFQPdalak 303
Cdd:cd19092  160 llQSYLDQPLVTNQIELSLLHTEAiDDGTLDYCQLLDITPMAWSPLGGGRLFGG--------------FDERFQR----- 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304600 304 nmvLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTdRE 364
Cdd:cd19092  221 ---LRAALEELAEEYGVTIEAIALAWLLRHPARIQPILGTTNPERIRSAVKALDIELT-RE 277
AKR_YeaE cd19138
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...
68-369 2.40e-46

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: 2.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGSLE-VSSMGLGCLPMvgyyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATK 146
Cdd:cd19138    2 TVTLPDGTkVPALGQGTWYM----GEDPAKRAQEIEALRAGIDLGMTLIDTAEMYGDGGSEELVGEAIRGRRDKVFLVSK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FgfgveegKPTslNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDpNVPIEDVAETVKALILEGKVKHWGLSEASARTIR 226
Cdd:cd19138   78 V-------LPS--NASRQGTVRACERSLRRLGTDYLDLYLLHWRG-GVPLAETVAAMEELKKEGKIRAWGVSNFDTDDME 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 227 RAHAVL---PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSflagavnpsqrfdstdrrhnlpRFQPDALAK 303
Cdd:cd19138  148 ELWAVPgggNCAANQVLYNLGSRGIEYDLLPWCREHGVPVMAYSPLAQG----------------------GLLRRGLLE 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 304 NMVLlefaQSWARRKNTTPVQFALAWVMAQrPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19138  206 NPTL----KEIAARHGATPAQVALAWVLRD-GNVIAIPKSGSPEHARENAAAADLELTEEDLAELD 266
AKR_Tas-like cd19094
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...
107-370 5.72e-45

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: 157.73  E-value: 5.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 107 AFEQGITFFDTAEVY-------GPHLSEEFVGEALA--PVRDRVVIATKF-----GFGVEEGKPTSLNshPDHIRRAVEG 172
Cdd:cd19094   27 AFDEGVNFIDTAEMYpvppspeTQGRTEEIIGSWLKkkGNRDKVVLATKVagpgeGITWPRGGGTRLD--RENIREAVEG 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 173 SLKRLKTDHIDLLYQHRPDPNVP------------------IEDVAETVKALILEGKVKHWGLSEASA----RTIR--RA 228
Cdd:cd19094  105 SLKRLGTDYIDLYQLHWPDRYTPlfgggyytepseeedsvsFEEQLEALGELVKAGKIRHIGLSNETPwgvmKFLElaEQ 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 229 HAVLPVTAVQSEYAMWWREPETrifpTLEEL----GIGFVPYCPTARSFLAGAVNPSQRFDSTDR----RHNLPRF-QPD 299
Cdd:cd19094  185 LGLPRIVSIQNPYSLLNRNFEE----GLAEAchreNVGLLAYSPLAGGVLTGKYLDGAARPEGGRlnlfPGYMARYrSPQ 260
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 300 ALAKNMVLLEFAQSWarrkNTTPVQFALAWVmAQRPWIVP-IPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19094  261 ALEAVAEYVKLARKH----GLSPAQLALAWV-RSRPFVTStIIGATTLEQLKENIDAFDVPLSDELLAEIDA 327
AKR_AKR14A1_2 cd19089
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...
74-365 2.04e-44

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: 155.88  E-value: 2.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPmvgyygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPH--LSEEFVGEAL----APVRDRVVIATKF 147
Cdd:cd19089   11 LPAISLGLWHNF------GDYTSPEEARELLRTAFDLGITHFDLANNYGPPpgSAEENFGRILkrdlRPYRDELVISTKA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 148 GFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRR 227
Cdd:cd19089   85 GYGMWPG-PYGDGGSRKYLLASLDQSLKRMGLDYVDIFYHHRYDPDTPLEETMTALADAVRSGKALYVGISNYPGAKARR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 228 AHAVL-----PVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAvnPSQRFDSTDRRHNLPRFQPDAL- 301
Cdd:cd19089  164 AIALLrelgvPLIIHQPRYSLLDRWAEDGLLEVLEEAGIGFIAFSPLAQGLLTDK--YLNGIPPDSRRAAESKFLTEEAl 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490304600 302 --AKNMVLLEFAQsWARRKNTTPVQFALAWVMaQRPWI--VPIpGTTQYPHLIENSGA-PQVRLTDREL 365
Cdd:cd19089  242 tpEKLEQLRKLNK-IAAKRGQSLAQLALSWVL-RDPRVtsVLI-GASSPSQLEDNVAAlKNLDFSEEEL 307
YdhF COG4989
Predicted oxidoreductase YdhF [General function prediction only];
74-364 1.23e-43

Predicted oxidoreductase YdhF [General function prediction only];


Pssm-ID: 444013 [Multi-domain]  Cd Length: 299  Bit Score: 153.38  E-value: 1.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMvgyyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA--PV-RDRVVIATKFG-- 148
Cdd:COG4989   11 LSVSRIVLGCMRL----GEWDLSPAEAAALIEAALELGITTFDHADIYGGYTCEALFGEALKlsPSlREKIELQTKCGir 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 149 --FGVEEGKPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIR 226
Cdd:COG4989   87 lpSEARDNRVKHYDTSKEHIIASVEGSLRRLGTDYLDLLLLHRPDPLMDPEEVAEAFDELKASGKVRHFGVSNFTPSQFE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 227 --RAHAVLPVTAVQSEYAMWWREPetrIFP-TLEelgigfvpYC------PTARSFLAGAvnpsqRFDSTDRrhnlprfq 297
Cdd:COG4989  167 llQSALDQPLVTNQIELSLLHTDA---FDDgTLD--------YCqlngitPMAWSPLAGG-----RLFGGFD-------- 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 298 PDALAKNMVLLEFAQswarRKNTTPVQFALAWVM---AQrpwIVPIPGTTQYPHLIENSGAPQVRLTdRE 364
Cdd:COG4989  223 EQFPRLRAALDELAE----KYGVSPEAIALAWLLrhpAG---IQPVIGTTNPERIKAAAAALDIELT-RE 284
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
81-331 2.08e-43

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: 153.10  E-value: 2.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  81 LGCLPMvGYYGG--GPRDRKAMVSLIRAAfeqGITFFDTAEVYGPHLSEEFVGEALAPVRdRVVIATKFGFGVeegkPTS 158
Cdd:cd19075    5 LGTMTF-GSQGRftTAEAAAELLDAFLER---GHTEIDTARVYPDGTSEELLGELGLGER-GFKIDTKANPGV----GGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 159 LNshPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHA-------V 231
Cdd:cd19075   76 LS--PENVRKQLETSLKRLKVDKVDVFYLHAPDRSTPLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVEickengwV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 232 LPvTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGavnpsqRFDSTDRRHNLPRFQPD-ALAKNM----- 305
Cdd:cd19075  154 LP-TVYQGMYNAITRQVETELFPCLRKLGIRFYAYSPLAGGFLTG------KYKYSEDKAGGGRFDPNnALGKLYrdryw 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 490304600 306 --VLLEFAQSW---ARRKNTTPVQFALAWVM 331
Cdd:cd19075  227 kpSYFEALEKVeeaAEKEGISLAEAALRWLY 257
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
77-356 1.36e-42

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: 150.56  E-value: 1.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  77 SSMGLGCLpmvgyYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHL-------SEEFVGEALA--PVRDRVVIATKF 147
Cdd:cd19752    1 SELCLGTM-----YFGTRTDEETSFAILDRYVAAGGNFLDTANNYAFWTeggvggeSERLIGRWLKdrGNRDDVVIATKV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 148 GFGVEE--GKPTSLNS-HPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSE----- 219
Cdd:cd19752   76 GAGPRDpdGGPESPEGlSAETIEQEIDKSLRRLGTDYIDLYYAHVDDRDTPLEETLEAFNELVKAGKVRAIGASNfaawr 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 220 -ASARTIRRAHAVLPVTAVQSEYAMWWREPETRI---FPTLEEL--------GIGFVPYCPTarsfLAGAvnpsqrFDST 287
Cdd:cd19752  156 lERARQIARQQGWAEFSAIQQRHSYLRPRPGADFgvqRIVTDELldyassrpDLTLLAYSPL----LSGA------YTRP 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490304600 288 DRRHNLPRFQPDALAKNMVLLEFAQswarRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAP 356
Cdd:cd19752  226 DRPLPEQYDGPDSDARLAVLEEVAG----ELGATPNQVVLAWLLHRTPAIIPLLGASTVEQLEENLAAL 290
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
103-352 5.88e-42

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: 148.86  E-value: 5.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 103 LIRAAFEQGITFFDTAEVYG----PHLSEEFVGEALA--PVRDRVVIATKFGFGVEEGKPTSlNSHPDHIRRAVEGSLKR 176
Cdd:cd19082   22 LLDAFVELGGNFIDTARVYGdwveRGASERVIGEWLKsrGNRDKVVIATKGGHPDLEDMSRS-RLSPEDIRADLEESLER 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 177 LKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSE------ASARTIRRAHAVLPVTAVQSEY-------AM 243
Cdd:cd19082  101 LGTDYIDLYFLHRDDPSVPVGEIVDTLNELVRAGKIRAFGASNwsteriAEANAYAKAHGLPGFAASSPQWslarpnePP 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 244 W------WREPETRIFptLEELGIGFVPYCPTARSFLAGAVNPSQRFDSTDRR-----HNLPRfqpdalaknmvlLEFAQ 312
Cdd:cd19082  181 WpgptlvAMDEEMRAW--HEENQLPVFAYSSQARGFFSKRAAGGAEDDSELRRvyyseENFER------------LERAK 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490304600 313 SWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIEN 352
Cdd:cd19082  247 ELAEEKGVSPTQIALAYVLNQPFPTVPIIGPRTPEQLRDS 286
PRK10376 PRK10376
putative oxidoreductase; Provisional
68-370 1.70e-41

putative oxidoreductase; Provisional


Pssm-ID: 236676 [Multi-domain]  Cd Length: 290  Bit Score: 147.81  E-value: 1.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGSLEVSSMGLGCLPMVG-YYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVIATK 146
Cdd:PRK10376   9 TFTLGGRSVNRLGYGAMQLAGpGVFGPPKDRDAAIAVLREAVALGVNHIDTSDFYGPHVTNQLIREALHPYPDDLTIVTK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FGF--GVEEGKPTSLNshPDHIRRAVEGSLKRLKTDHIDLLY------QHRPDPNvPIEDVAETVKALILEGKVKHWGLS 218
Cdd:PRK10376  89 VGArrGEDGSWLPAFS--PAELRRAVHDNLRNLGLDVLDVVNlrlmgdGHGPAEG-SIEEPLTVLAELQRQGLVRHIGLS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 219 EASARTIRRAHAVLPVTAVQSEYAMWWREPETRIfPTLEELGIGFVPYCPTarsflaGAVNPsqrfdstdrrhnlprFQP 298
Cdd:PRK10376 166 NVTPTQVAEARKIAEIVCVQNHYNLAHRADDALI-DALARDGIAYVPFFPL------GGFTP---------------LQS 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 299 DALAknmvllefaqSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:PRK10376 224 STLS----------DVAASLGATPMQVALAWLLQRSPNILLIPGTSSVAHLRENLAAAELVLSEEVLAELDG 285
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
84-371 3.47e-41

Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 145.97  E-value: 3.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGY--YGGGPRDRKAMVsliRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgfgveegkpts 158
Cdd:COG0656    5 IPALGLgtWQLPGEEAAAAV---RTALEAGYRHIDTAAMYG---NEEGVGEAIAASgvpREELFVTTKV----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 159 LNSH--PDHIRRAVEGSLKRLKTDHIDLLYQHRPDPnvpiEDVAETVKALI-L--EGKVKHWGLSEASARTIRRAHAVLP 233
Cdd:COG0656   68 WNDNhgYDDTLAAFEESLERLGLDYLDLYLIHWPGP----GPYVETWRALEeLyeEGLIRAIGVSNFDPEHLEELLAETG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 234 VT--AVQSEYAMWWREPETRifPTLEELGIGFVPYCPTARSflagavnpsqrfdstdrrhnlprfqpdALAKNMVLLEFA 311
Cdd:COG0656  144 VKpaVNQVELHPYLQQRELL--AFCREHGIVVEAYSPLGRG---------------------------KLLDDPVLAEIA 194
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 312 QswarRKNTTPVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAA 371
Cdd:COG0656  195 E----KHGKTPAQVVLRWHLQRG--VVVIPKSVTPERIRENLDAFDFELSDEDMAAIDAL 248
AKR_PA4992-like cd19095
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ...
80-355 3.50e-40

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: 143.14  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  80 GLGCLpmvGYYGG-GPRDRKAMVSLIRAAFEQGITFFDTAEVYGphLSEEFVGEALAPV-RDRVVIATKFGFGVEEGKPT 157
Cdd:cd19095    4 GLGTS---GIGRVwGVPSEAEAARLLNTALDLGINLIDTAPAYG--RSEERLGRALAGLrRDDLFIATKVGTHGEGGRDR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 158 SLNShPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSeASARTIRRAHAVLPVTAV 237
Cdd:cd19095   79 KDFS-PAAIRASIERSLRRLGTDYIDLLQLHGPSDDELTGEVLETLEDLKAAGKVRYIGVS-GDGEELEAAIASGVFDVV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 238 QSEYAMWWREpETRIFPTLEELGIGFVpycptARSFLAGAVNPSQRFDSTDRRHNLPRFQPDALAKnmvllefAQSWArr 317
Cdd:cd19095  157 QLPYNVLDRE-EEELLPLAAEAGLGVI-----VNRPLANGRLRRRVRRRPLYADYARRPEFAAEIG-------GATWA-- 221
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490304600 318 knttpvQFALAWVMAQRPWIVPIPGTTQYPHLIENSGA 355
Cdd:cd19095  222 ------QAALRFVLSHPGVSSAIVGTTNPEHLEENLAA 253
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
71-372 4.17e-40

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: 144.87  E-value: 4.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  71 LGSLEVSSMGLGCLPMVGYYGG--GPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAP--VRDRVVIATK 146
Cdd:cd19146    6 TAGVRVSPLCLGAMSFGEAWKSmmGECDKETAFKLLDAFYEQGGNFIDTANNYQGEESERWVGEWMASrgNRDEMVLATK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 147 FGFGVEEGKPTSLNS-----HPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEAS 221
Cdd:cd19146   86 YTTGYRRGGPIKIKSnyqgnHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTTSIPELMQSLNHLVAAGKVLYLGVSDTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 222 ARTIR------RAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRfdSTDRRHNLPR 295
Cdd:cd19146  166 AWVVSkanayaRAHGLTQFVVYQGHWSAAFRDFERDILPMCEAEGMALAPWGVLGQGQFRTEEEFKRR--GRSGRKGGPQ 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 296 FQPDALAkNMVLLEFAQswarRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19146  244 TEKERKV-SEKLEKVAE----EKGTAITSVALAYVMHKAPYVFPIVGGRKVEHLKGNIEALGISLSDEEIQEIEDAY 315
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
75-369 4.88e-39

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: 140.40  E-value: 4.88e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  75 EVSSMGLGCLPMVGY-YGGGPRDRKaMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFgfgve 152
Cdd:cd19137    3 KIPALGLGTWGIGGFlTPDYSRDEE-MVELLKTAIELGYTHIDTAEMYGGGHTEELVGKAIKDFpREDLFIVTKV----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 egKPTSLNShpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVL 232
Cdd:cd19137   77 --WPTNLRY--DDLLRSLQNSLRRLDTDYIDLYLIHWPNPNIPLEETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 233 --PVTAVQSEYAMWWREPETR-IFPTLEELGIGFVPYCPTARSflagavnpsqrfdstdrrhnlprfqpdALAKNMVLLE 309
Cdd:cd19137  153 qtPIVCNQVKYNLEDRDPERDgLLEYCQKNGITVVAYSPLRRG---------------------------LEKTNRTLEE 205
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 310 FAQSWARrkntTPVQFALAWVMaQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19137  206 IAKNYGK----TIAQIALAWLI-QKPNVVAIPKAGRVEHLKENLKATEIKLSEEEMKLLD 260
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
84-369 2.59e-38

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: 137.79  E-value: 2.59e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKfgfgVEEGkptslN 160
Cdd:cd19073    1 IPALGLGTWQLRGDDC-ANAVKEALELGYRHIDTAEIYN---NEAEVGEAIAESgvpREDLFITTK----VWRD-----H 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 161 SHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAV--LPVTAVQ 238
Cdd:cd19073   68 LRPEDLKKSVDRSLEKLGTDYVDLLLIHWPNPTVPLEETLGALKELKEAGKVKSIGVSNFTIELLEEALDIspLPIAVNQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 239 SEYAMWWREPETRIFptLEELGIGFVPYCPTARsflaGAVnpsqrfdstdrrhnlprfqpdalAKNMVLLEFAQswarRK 318
Cdd:cd19073  148 VEFHPFLYQAELLEY--CRENDIVITAYSPLAR----GEV-----------------------LRDPVIQEIAE----KY 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490304600 319 NTTPVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19073  195 DKTPAQVALRWLVQKG--IVVIPKASSEDHLKENLAIFDWELTSEDVAKID 243
AKR_unchar cd19105
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
68-228 1.08e-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: 381331 [Multi-domain]  Cd Length: 250  Bit Score: 131.17  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLG--SLEVSSMGLGClpmvgyyGGGPRDRkamVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALA-PVRDRVVIA 144
Cdd:cd19105    3 YRTLGktGLKVSRLGFGG-------GGLPRES---PELLRRALDLGINYFDTAEGYGNGNSEEIIGEALKgLRRDKVFLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFGFGVEEGKptslnshPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALI-L--EGKVKHWGLSEAS 221
Cdd:cd19105   73 TKASPRLDKKD-------KAELLKSVEESLKRLQTDYIDIYQLHGVDTPEERLLNEELLEALEkLkkEGKVRFIGFSTHD 145

                 ....*....
gi 490304600 222 --ARTIRRA 228
Cdd:cd19105  146 nmAEVLQAA 154
AKR_AKR14A2 cd19151
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ...
92-366 2.64e-35

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: 131.76  E-value: 2.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  92 GGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHL--SEEFVG----EALAPVRDRVVIATKFGFGVEEGKPTSLNSHpDH 165
Cdd:cd19151   24 GDVDRYENSRAMLRRAFDLGITHFDLANNYGPPPgsAEENFGrilkEDLKPYRDELIISTKAGYTMWPGPYGDWGSK-KY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 166 IRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEdvaETVKAL---ILEGKVKHWGLSEASARTIRRAHAVL-----PVTAV 237
Cdd:cd19151  103 LIASLDQSLKRMGLDYVDIFYHHRPDPETPLE---ETMGALdqiVRQGKALYVGISNYPPEEAREAAAILkdlgtPCLIH 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 238 QSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLA----GAVNPSQRFDSTDRRHNLPRFQPDALAKNMVLLEFAQs 313
Cdd:cd19151  180 QPKYSMFNRWVEEGLLDVLEEEGIGCIAFSPLAQGLLTdrylNGIPEDSRAAKGSSFLKPEQITEEKLAKVRRLNEIAQ- 258
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490304600 314 warRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGA-PQVRLTDRELR 366
Cdd:cd19151  259 ---ARGQKLAQMALAWVLRNKRVTSVLIGASKPSQIEDAVGAlDNREFSEEELA 309
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
84-369 7.65e-35

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: 128.75  E-value: 7.65e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALA---PVRDRVVIATKFgfgveegkpTSLN 160
Cdd:cd19071    1 MPLIGL-GTYKLKPEETAEAVLAALEAGYRHIDTAAAYG---NEAEVGEAIResgVPREELFITTKL---------WPTD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 161 SHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPI---EDVAETVKALI---LEGKVKHWGLSEASARTIRR--AHAVL 232
Cdd:cd19071   68 HGYERVREALEESLKDLGLDYLDLYLIHWPVPGKEGgskEARLETWRALEelvDEGLVRSIGVSNFNVEHLEEllAAARI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 233 PVTAVQSEYAMWWREPETRIFptLEELGIGFVPYCPtarsfLAGAVNPsqrfdstdrrhnlprfqpdaLAKNMVLLEFAQ 312
Cdd:cd19071  148 KPAVNQIELHPYLQQKELVEF--CKEHGIVVQAYSP-----LGRGRRP--------------------LLDDPVLKEIAK 200
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 313 swarRKNTTPVQFALAWVMaQRPwIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19071  201 ----KYGKTPAQVLLRWAL-QRG-VVVIPKSSNPERIKENLDVFDFELSEEDMAAID 251
AKR_unchar cd19100
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
68-264 1.96e-34

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: 127.21  E-value: 1.96e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMvgyyggGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPhlSEEFVGEALAPVRDRVVIAT 145
Cdd:cd19100    1 YRRLGRtgLKVSRLGFGGGPL------GRLSQEEAAAIIRRALDLGINYFDTAPSYGD--SEEKIGKALKGRRDKVFLAT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFGfgveegkptslNSHPDHIRRAVEGSLKRLKTDHIDLLYQH----RPDPNVPIED--VAETVKALILEGKVKHWGLS- 218
Cdd:cd19100   73 KTG-----------ARDYEGAKRDLERSLKRLGTDYIDLYQLHavdtEEDLDQVFGPggALEALLEAKEEGKIRFIGISg 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490304600 219 ---EASARTIRRAH--AVL-PVTAVQSEYamwwREPETRIFPTLEELGIGFV 264
Cdd:cd19100  142 hspEVLLRALETGEfdVVLfPINPAGDHI----DSFREELLPLAREKGVGVI 189
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
79-370 1.36e-33

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: 125.45  E-value: 1.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  79 MGLGCLPMVGyygggprdrKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALA--PV-RDRVVIATKFGFgveegk 155
Cdd:cd19140   11 LGLGTYPLTG---------EECTRAVEHALELGYRHIDTAQMYG---NEAQVGEAIAasGVpRDELFLTTKVWP------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 ptsLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRA--HAVLP 233
Cdd:cd19140   73 ---DNYSPDDFLASVEESLRKLRTDYVDLLLLHWPNKDVPLAETLGALNEAQEAGLARHIGVSNFTVALLREAveLSEAP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 234 VTAVQSEYamwwrEP---ETRIFPTLEELGIGFVPYCPTARsflaGAVnpsqrfdstdrrhnlprfqpdalAKNMVLLEF 310
Cdd:cd19140  150 LFTNQVEY-----HPyldQRKLLDAAREHGIALTAYSPLAR----GEV-----------------------LKDPVLQEI 197
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 311 aqswARRKNTTPVQFALAWVMaQRPWIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19140  198 ----GRKHGKTPAQVALRWLL-QQEGVAAIPKATNPERLEENLDIFDFTLSDEEMARIAA 252
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
68-279 2.55e-33

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: 126.61  E-value: 2.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLG--SLEVSSMGLGClpmvGYYGG--GPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPVRDRVVI 143
Cdd:cd19104    2 YRRFGrtGLKVSELTFGG----GGIGGlmGRTTREEQIAAVRRALDLGINFFDTAPSYGDGKSEENLGRALKGLPAGPYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGveegkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQH---------RPDPNVPIED------VAETVKALIL 208
Cdd:cd19104   78 TTKVRLD-----PDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHnrigderdkPVGGTLSTTDvlglggVADAFERLRS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 209 EGKVKHWGLSEAS-ARTIRRAHAVLPVTAVQSEY------------AMWWREPETRIFPTLEELGIGFVPYCPTARSFLA 275
Cdd:cd19104  153 EGKIRFIGITGLGnPPAIRELLDSGKFDAVQVYYnllnpsaaearpRGWSAQDYGGIIDAAAEHGVGVMGIRVLAAGALT 232

                 ....
gi 490304600 276 GAVN 279
Cdd:cd19104  233 TSLD 236
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
68-371 1.81e-31

Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 122.62  E-value: 1.81e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMvgyygggPR-DRKAMVSLIRAAFEQGITFFDTAEVYgpHLSEEFVGEALAPVRDRVVIA 144
Cdd:COG1453    3 YRRLGKtgLEVSVLGFGGMRL-------PRkDEEEAEALIRRAIDNGINYIDTARGY--GDSEEFLGKALKGPRDKVILA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFgfgveegkPTSLNShPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIE------DVAETVKALILEGKVKHWGLS 218
Cdd:COG1453   74 TKL--------PPWVRD-PEDMRKDLEESLKRLQTDYIDLYLIHGLNTEEDLEkvlkpgGALEALEKAKAEGKIRHIGFS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 219 easartirrAHAVLPV--TAVQS---EYAM-------WWREPETRIFPTLEELGIGFV---PycptarsfLAGA--VNPS 281
Cdd:COG1453  145 ---------THGSLEVikEAIDTgdfDFVQlqynyldQDNQAGEEALEAAAEKGIGVIimkP--------LKGGrlANPP 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 282 QRFdstdrrhnlprfqpdalaknMVLLEfaqswarrKNTTPVQFALAWVmAQRPWI-VPIPGTTQYPHLIEN--SGAPQV 358
Cdd:COG1453  208 EKL--------------------VELLC--------PPLSPAEWALRFL-LSHPEVtTVLSGMSTPEQLDENlkTADNLE 258
                        330
                 ....*....|...
gi 490304600 359 RLTDRELREIDAA 371
Cdd:COG1453  259 PLTEEELAILERL 271
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
77-276 2.52e-31

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: 120.35  E-value: 2.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  77 SSMGLGCLPMVGYYGGGPRDRKamVSLIRAAFEQGITFFDTAEVYGPhlSEEFVGEALA-PVRDRVVIATKFGFGVEEGK 155
Cdd:cd19090    1 SALGLGTAGLGGVFGGVDDDEA--VATIRAALDLGINYIDTAPAYGD--SEERLGLALAeLPREPLVLSTKVGRLPEDTA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 PTSlnshPDHIRRAVEGSLKRLKTDHIDLLYQHRPD--PNVPIEDVAETVKALIL---EGKVKHWGLS----EASARTIR 226
Cdd:cd19090   77 DYS----ADRVRRSVEESLERLGRDRIDLLMIHDPErvPWVDILAPGGALEALLElkeEGLIKHIGLGggppDLLRRAIE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490304600 227 RAH--AVLPVtavqSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAG 276
Cdd:cd19090  153 TGDfdVVLTA----NRYTLLDQSAADELLPAAARHGVGVINASPLGMGLLAG 200
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
69-376 3.58e-31

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: 120.86  E-value: 3.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMvgyYGGGPRDRKAMvSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVI 143
Cdd:cd19160    6 RNLGKsgLRVSCLGLGTWVT---FGSQISDETAE-DLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKgwrRSSYVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGKPTSLNShpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASAR 223
Cdd:cd19160   82 TTKIYWGGQAETERGLSR--KHIIEGLRGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGMAMYWGTSRWSAM 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 224 TIRRAHAV------LPVTAVQSEYAMWWREP-ETRIFPTLEELGIGFVPYCPTARSFLAGAVN---PSQRFDSTDRRHNL 293
Cdd:cd19160  160 EIMEAYSVarqfnlIPPVCEQAEYHLFQREKvEMQLPELYHKIGVGSVTWSPLACGLITGKYDgrvPDTCRAAVKGYQWL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 294 P-RFQPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQV--RLTDRELREIDA 370
Cdd:cd19160  240 KeKVQSEEGKKQQAKVKELHPIADRLGCTVAQLAIAWCLRSEGVSSVLLGVSSAEQLIENLGSIQVlsQLTPQTVMEIDA 319

                 ....*.
gi 490304600 371 ALAKIP 376
Cdd:cd19160  320 LLGNKP 325
AKR_KCAB1B_AKR6A3-like cd19159
voltage-gated potassium channel subunit beta-1 (KCAB1B) and similar proteins; KCAB1B from Homo ...
69-376 3.70e-31

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: 120.92  E-value: 3.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMvgyYGGGPRDRKAMvSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVI 143
Cdd:cd19159    4 RNLGKsgLRVSCLGLGTWVT---FGGQISDEVAE-RLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKgwrRSSLVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGKPTSLNSHpdHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASAR 223
Cdd:cd19159   80 TTKLYWGGKAETERGLSRK--HIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 224 TIRRAHAV------LPVTAVQSEYAMWWREPETRIFPTL-EELGIGFVPYCPTARSFLAGAVNPSQRfDSTdrRHNLPRF 296
Cdd:cd19159  158 EIMEAYSVarqfnmIPPVCEQAEYHLFQREKVEVQLPELyHKIGVGAMTWSPLACGIISGKYGNGVP-ESS--RASLKCY 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 297 QpdALAKNMVLLEFAQSWARRKNTTPV---------QFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQV--RLTDREL 365
Cdd:cd19159  235 Q--WLKERIVSEEGRKQQNKLKDLSPIaerlgctlpQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVlpKMTSHVV 312
                        330
                 ....*....|.
gi 490304600 366 REIDAALAKIP 376
Cdd:cd19159  313 NEIDNILRNKP 323
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
70-369 9.95e-31

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: 119.54  E-value: 9.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  70 KLGSLEVSSMGLGCLPMVGYYGG--GPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGE--ALAPVRDRVVIAT 145
Cdd:cd19147    4 KTAGIRVSPLILGAMSIGDAWSGfmGSMDKEQAFELLDAFYEAGGNFIDTANNYQDEQSETWIGEwmKSRKNRDQIVIAT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFGF---GVEEGKPTSLNSHPDHIRR---AVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSE 219
Cdd:cd19147   84 KFTTdykAYEVGKGKAVNYCGNHKRSlhvSVRDSLRKLQTDWIDILYVHWWDYTTSIEEVMDSLHILVQQGKVLYLGVSD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 220 ------ASARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPY---------CPTARSFLAGAVNPSQRF 284
Cdd:cd19147  164 tpawvvSAANYYATAHGKTPFSVYQGRWNVLNRDFERDIIPMARHFGMALAPWdvlgggkfqSKKAVEERKKNGEGLRSF 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 285 DSTDRRHNLPRFQPDALAKnmvllefaqsWARRKNTTPVQ-FALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVRLTDR 363
Cdd:cd19147  244 VGGTEQTPEEVKISEALEK----------VAEEHGTESVTaIALAYVRSKAPNVFPLVGGRKIEHLKDNIEALSIKLTPE 313

                 ....*.
gi 490304600 364 ELREID 369
Cdd:cd19147  314 EIEYLE 319
AKR_KCAB2B_AKR6A1-like cd19158
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ...
69-376 2.13e-30

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: 119.03  E-value: 2.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMvgyYGGGPRDRKAMvSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVI 143
Cdd:cd19158    4 RNLGKsgLRVSCLGLGTWVT---FGGQITDEMAE-HLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKgwrRSSLVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGVEEGKPTSLNShpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASAR 223
Cdd:cd19158   80 TTKIFWGGKAETERGLSR--KHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 224 TIRRAHAV------LPVTAVQSEYAMWWREPETRIFPTL-EELGIGFVPYCPTARSFLAGAVN----PSQRFDSTDRRHN 292
Cdd:cd19158  158 EIMEAYSVarqfnlIPPICEQAEYHMFQREKVEVQLPELfHKIGVGAMTWSPLACGIVSGKYDsgipPYSRASLKGYQWL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 293 LPRFQPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQV--RLTDRELREIDA 370
Cdd:cd19158  238 KDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSVLLGASNAEQLMENIGAIQVlpKLSSSIVHEIDS 317

                 ....*.
gi 490304600 371 ALAKIP 376
Cdd:cd19158  318 ILGNKP 323
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
69-359 3.60e-30

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: 117.93  E-value: 3.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMvgyYGGGPRDRKAMvSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVVI 143
Cdd:cd19141    3 RNLGKsgLRVSCLGLGTWVT---FGSQISDEVAE-ELVTLAYENGINLFDTAEVYAAGKAEIVLGKILKKKgwrRSSYVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGFGveeGKP-TSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASA 222
Cdd:cd19141   79 TTKIFWG---GKAeTERGLSRKHIIEGLKASLERLQLEYVDIVFANRPDPNTPMEEIVRAFTHVINQGMAMYWGTSRWSA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 223 RTIRRAHAV------LPVTAVQSEYAMWWREPETRIFPTL-EELGIGFVPYCPTARSFLAG----AVNPSQRFDSTDRRH 291
Cdd:cd19141  156 MEIMEAYSVarqfnlIPPIVEQAEYHLFQREKVEMQLPELfHKIGVGAMTWSPLACGILSGkyddGVPEYSRASLKGYQW 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 292 NLPRFQPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQVR 359
Cdd:cd19141  236 LKEKILSEEGRRQQAKLKELQIIADRLGCTLPQLAIAWCLKNEGVSSVLLGASSTEQLYENLQAIQVL 303
AKR_unchar cd19103
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
106-371 8.76e-29

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381329 [Multi-domain]  Cd Length: 299  Bit Score: 113.97  E-value: 8.76e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 106 AAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFgfgveegKPTSLNSHPDHIRRAVEGSLKRLKTDHIDL 184
Cdd:cd19103   40 KAMAAGLNLWDTAAVYGMGASEKILGEFLKRYpREDYIISTKF-------TPQIAGQSADPVADMLEGSLARLGTDYIDI 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 185 LYQHRPDpnvpieDVAETVKALIL---EGKVKHWGLSEASARTIRRAHAVL-----PVTAVQSEYAMWWREPET-RIFPT 255
Cdd:cd19103  113 YWIHNPA------DVERWTPELIPllkSGKVKHVGVSNHNLAEIKRANEILakagvSLSAVQNHYSLLYRSSEEaGILDY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 256 LEELGIGFVPYCPTARSFLAGAvnpsqrfdsTDRRHNLPRFQPDALAKNMVLLEFA------QSWARRKNTTPVQFALAW 329
Cdd:cd19103  187 CKENGITFFAYMVLEQGALSGK---------YDTKHPLPEGSGRAETYNPLLPQLEeltavmAEIGAKHGASIAQVAIAW 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 490304600 330 VMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAA 371
Cdd:cd19103  258 AIAKG--TTPIIGVTKPHHVEDAARAASITLTDDEIKELEQL 297
AKR_unchar cd19101
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
92-372 2.37e-28

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: 112.69  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  92 GGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPhlSEEFVGEALAPVR------DRVVIATKFGFGVEEGKPTslnshPDH 165
Cdd:cd19101   17 GGIRDEDAAVRAMAAYVDAGLTTFDCADIYGP--AEELIGEFRKRLRrerdaaDDVQIHTKWVPDPGELTMT-----RAY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 166 IRRAVEGSLKRLKTDHIDLLYQHRPDPNVP-IEDVAETVKALILEGKVKHWGLSEASARTIRRA-HAVLPVTAVQSEYAM 243
Cdd:cd19101   90 VEAAIDRSLKRLGVDRLDLVQFHWWDYSDPgYLDAAKHLAELQEEGKIRHLGLTNFDTERLREIlDAGVPIVSNQVQYSL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 244 WWREPETRIFPTLEELGIGFVPYCPTARSFLagavnpSQRF----DSTDRRHNLPRfqpdaLAKNMVLLEFAQSW----- 314
Cdd:cd19101  170 LDRRPENGMAALCEDHGIKLLAYGTLAGGLL------SEKYlgvpEPTGPALETRS-----LQKYKLMIDEWGGWdlfqe 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 315 --------ARRKNTTPVQFALAWVMaQRPWIV-PIPGTTQYPHLIENSGAPQVRLTDRELREIDAAL 372
Cdd:cd19101  239 llrtlkaiADKHGVSIANVAVRWVL-DQPGVAgVIVGARNSEHIDDNVRAFSFRLDDEDRAAIDAVL 304
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
58-373 3.48e-28

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 113.16  E-value: 3.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  58 AAPVRKETLTTRKLGS--LEVSSMGLGCLPMVGYYGGGPRDRkamvSLIRAAFEQGITFFDTAEVYGP--HLSEEFVG-- 131
Cdd:PRK09912   5 ANPERYGQMQYRYCGKsgLRLPALSLGLWHNFGHVNALESQR----AILRKAFDLGITHFDLANNYGPppGSAEENFGrl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 132 --EALAPVRDRVVIATKFGFGVEEGkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILE 209
Cdd:PRK09912  81 lrEDFAAYRDELIISTKAGYDMWPG-PYGSGGSRKYLLASLDQSLKRMGLEYVDIFYSHRVDENTPMEETASALAHAVQS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 210 GKVKHWGLSEAS-ARTIRRAHAV----LPVTAVQSEYAMW--WREpETRIFPTLEELGIGFVPYCPTARSFLAGA-VNPS 281
Cdd:PRK09912 160 GKALYVGISSYSpERTQKMVELLrewkIPLLIHQPSYNLLnrWVD-KSGLLDTLQNNGVGCIAFTPLAQGLLTGKyLNGI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 282 QRFDSTDRRHNLPR-FQPDALAK-NMVLLEFAQSWARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGA-PQV 358
Cdd:PRK09912 239 PQDSRMHREGNKVRgLTPKMLTEaNLNSLRLLNEMAQQRGQSMAQMALSWLLKDERVTSVLIGASRAEQLEENVQAlNNL 318
                        330
                 ....*....|....*
gi 490304600 359 RLTDRELREIDAALA 373
Cdd:PRK09912 319 TFSTEELAQIDQHIA 333
AKR_galDH cd19163
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...
69-218 6.70e-28

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: 111.10  E-value: 6.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMVGYYGggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIAT 145
Cdd:cd19163    4 RKLGKtgLKVSKLGFGASPLGGVFG--PVDEEEAIRTVHEALDSGINYIDTAPWYGQGRSETVLGKALKGIpRDSYYLAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 146 KFG-FGVEEgkPTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHrpDPN-VPIED--VAETVKAL---ILEGKVKHWGLS 218
Cdd:cd19163   82 KVGrYGLDP--DKMFDFSAERITKSVEESLKRLGLDYIDIIQVH--DIEfAPSLDqiLNETLPALqklKEEGKVRFIGIT 157
AKR_AKR6B1 cd19142
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...
69-376 1.13e-25

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: 106.01  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMVGYygggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEAL---APVRDRVVI 143
Cdd:cd19142    4 RNLGKsgLRVSNVGLGTWSTFST----AISEEQAEEIVTLAYENGINYFDTSDAFTSGQAETELGRILkkkGWKRSSYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATK-FGFGVEEGKPTSLNshpdHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEAS- 221
Cdd:cd19142   80 STKiYWSYGSEERGLSRK----HIIESVRASLRRLQLDYIDIVIIHKADPMCPMEEVVRAMSYLIDNGLIMYWGTSRWSp 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 222 -----ARTIRRAHAVLPVTAVQSEYAMWWREPETRIFPTL-EELGIGFVPYCPTARSFLAGaVNPSQRFDSTDRRHNLPR 295
Cdd:cd19142  156 veimeAFSIARQFNCPTPICEQSEYHMFCREKMELYMPELyNKVGVGLITWSPLSLGLDPG-ISEETRRLVTKLSFKSSK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 296 FQPDALAKNMVLLEFAQS--------WARRKNTTPVQFALAWVMAQRPWIVPIPGTTQYPHLIENSGAPQV--RLTDREL 365
Cdd:cd19142  235 YKVGSDGNGIHEETRRAShklrelslIAERLGCDLTQLLIAWSLKNENVQCVLIGASSLEQLYSQLNSLQLlpKLNSAVM 314
                        330
                 ....*....|.
gi 490304600 366 REIDAALAKIP 376
Cdd:cd19142  315 EELERILDNKP 325
AKR_AKR14A1 cd19150
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ...
103-365 2.23e-25

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: 104.84  E-value: 2.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 103 LIRAAFEQGITFFDTAEVYGPHL--SEEFVGEAL----APVRDRVVIATKFGFGVEEGKPTSLNSHpDHIRRAVEGSLKR 176
Cdd:cd19150   35 ILRTAFDLGITHFDLANNYGPPPgsAEENFGRILredfAGYRDELIISTKAGYDMWPGPYGEWGSR-KYLLASLDQSLKR 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 177 LKTDHIDLLYQHRPDPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHAVL-----PVTAVQSEYAMW--WREpE 249
Cdd:cd19150  114 MGLDYVDIFYSHRFDPDTPLEETMGALDHAVRSGKALYVGISSYSPERTREAAAILrelgtPLLIHQPSYNMLnrWVE-E 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 250 TRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDStdRRHNLPRFQPDAL-AKNMVLLEFAQSWARRKNTTPVQFALA 328
Cdd:cd19150  193 SGLLDTLQELGVGCIAFTPLAQGLLTDKYLNGIPEGS--RASKERSLSPKMLtEANLNSIRALNEIAQKRGQSLAQMALA 270
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490304600 329 WVMAQRPWIVPIPGTTQYPHLIENSGA-PQVRLTDREL 365
Cdd:cd19150  271 WVLRDGRVTSALIGASRPEQLEENVGAlDNLTFSADEL 308
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
80-218 3.93e-25

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: 102.64  E-value: 3.93e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  80 GLGC--LPMVGyygGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFgfgveegkP 156
Cdd:cd19096    4 GFGTmrLPESD---DDSIDEEKAIEMIRYAIDAGINYFDTAYGYGGGKSEEILGEALKEGpREKFYLATKL--------P 72
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 157 TSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQH---RPD--PNVPIEDVAETVKALILEGKVKHWGLS 218
Cdd:cd19096   73 PWSVKSAEDFRRILEESLKRLGVDYIDFYLLHglnSPEwlEKARKGGLLEFLEKAKKEGLIRHIGFS 139
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
96-337 4.67e-24

uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of uncharacterized AKR superfamily proteins. Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. AKRs are present in all phyla and are of importance in both health and industrial applications.


Pssm-ID: 381323 [Multi-domain]  Cd Length: 267  Bit Score: 99.91  E-value: 4.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  96 DRKAMVSLIRAAFEQGITFFDTAEVYGphLSEEFVGEALAPvRDRVVIATKFGFGVEEGKptslnSHPDHIRRAVEGSLK 175
Cdd:cd19097   24 SEKEAKKILEYALKAGINTLDTAPAYG--DSEKVLGKFLKR-LDKFKIITKLPPLKEDKK-----EDEAAIEASVEASLK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 176 RLKTDHIDLLYQHRPDpNVPI--EDVAETVKALILEGKVKHWGLSEASARTIRRAHAVLPVTAVQSEYAMW-WREPETRI 252
Cdd:cd19097   96 RLKVDSLDGLLLHNPD-DLLKhgGKLVEALLELKKEGLIRKIGVSVYSPEELEKALESFKIDIIQLPFNILdQRFLKSGL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 253 FPTLEELGIGFVpycptARS-FLAGAVnpsqrFDSTDRRhnlprfqPDALAKNMVLLEFAQSWARRKNTTPVQFALAWVM 331
Cdd:cd19097  175 LAKLKKKGIEIH-----ARSvFLQGLL-----LMEPDKL-------PAKFAPAKPLLKKLHELAKKLGLSPLELALGFVL 237

                 ....*.
gi 490304600 332 AQrPWI 337
Cdd:cd19097  238 SL-PEI 242
AKR_unchar cd19099
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
74-352 1.34e-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: 99.70  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGClpmvgyYGGGPRD--RKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-------RDRVVIA 144
Cdd:cd19099    1 LTLSSLGLGT------YRGDSDDetDEEYREALKAALDSGINVIDTAINYRGGRSERLIGKALRELiekggikRDEVVIV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 145 TKFGF-------------GVEEGKPTSLNS-----------HPDHIRRAVEGSLKRLKTDHIDLLYQHRP-------DPN 193
Cdd:cd19099   75 TKAGYipgdgdeplrplkYLEEKLGRGLIDvadsaglrhciSPAYLEDQIERSLKRLGLDTIDLYLLHNPeeqllelGEE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 194 VPIEDVAETVKAL---ILEGKVKHWGLS--------EASARTI------RRAHAV-----------LPVTAVQSE-YAMW 244
Cdd:cd19099  155 EFYDRLEEAFEALeeaVAEGKIRYYGIStwdgfrapPALPGHLsleklvAAAEEVggdnhhfkviqLPLNLLEPEaLTEK 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 245 WREPE--TRIFPTLEELGIGFVpycpTARSFLAGAVNPSQRFdstDRRHNLPRFQPDAlaknmvllefaqswarrknttp 322
Cdd:cd19099  235 NTVKGeaLSLLEAAKELGLGVI----ASRPLNQGQLLGELRL---ADLLALPGGATLA---------------------- 285
                        330       340       350
                 ....*....|....*....|....*....|
gi 490304600 323 vQFALAWVMAQRPWIVPIPGTTQYPHLIEN 352
Cdd:cd19099  286 -QRALQFARSTPGVDSALVGMRRPEHVDEN 314
AKR_FDH cd19162
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...
77-286 9.04e-21

D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381388 [Multi-domain]  Cd Length: 290  Bit Score: 91.27  E-value: 9.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  77 SSMGLGCLPMVGYYGGGPRDRKAMVSlirAAFEQGITFFDTAEVYGPHLSEEFVGEALAP-VRDRVVIATKFGFGVEEGK 155
Cdd:cd19162    1 PRLGLGAASLGNLARAGEDEAAATLD---AAWDAGIRYFDTAPLYGLGLSERRLGAALARhPRAEYVVSTKVGRLLEPGA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 PTSLNSHP-------DHIRRAVEGSLKRLKTDHIDLLYQHRPDP--NVPIEDVAETVKALILEGKVKHWGLSEASARTIR 226
Cdd:cd19162   78 AGRPAGADrrfdfsaDGIRRSIEASLERLGLDRLDLVFLHDPDRhlLQALTDAFPALEELRAEGVVGAIGVGVTDWAALL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 227 RA--HAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRFDS 286
Cdd:cd19162  158 RAarRADVDVVMVAGRYTLLDRRAATELLPLCAAKGVAVVAAGVFNSGILATDDPAGDRYDY 219
AKR_galDH-like cd19153
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...
68-239 2.03e-20

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: 90.67  E-value: 2.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  68 TRKLGS--LEVSSMGLGCLPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV---RDRVV 142
Cdd:cd19153    2 GETLEIalGNVSPVGLGTAALGGVYGDGLEQDEA-VAIVAEAFAAGINHFDTSPYYGAESSEAVLGKALAALqvpRSSYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 143 IATKFGFGVEEGKPTSlnshPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALIL---EGKVKHWGLS- 218
Cdd:cd19153   81 VATKVGRYRDSEFDYS----AERVRASVATSLERLHTTYLDVVYLHDIEFVDYDTLVDEALPALRTlkdEGVIKRIGIAg 156
                        170       180
                 ....*....|....*....|....
gi 490304600 219 ---EASARTIRRAhAVLPVTAVQS 239
Cdd:cd19153  157 yplDTLTRATRRC-SPGSLDAVLS 179
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
73-218 6.26e-20

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: 89.26  E-value: 6.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  73 SLEVSSMGLGCLPMVGYYGGGPRDRKAmVSLIRAAFEQGITFFDTAEVYGPhlSEEFVGEALAPV-----RDRVVIATKF 147
Cdd:cd19164   10 LAGLPPLIFGAATFSYQYTTDPESIPP-VDIVRRALELGIRAFDTSPYYGP--SEIILGRALKALrdefpRDTYFIITKV 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 148 G-FGVEEgkptsLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHrpDPN-VPIEDVAETVKALIL---EGKVKHWGLS 218
Cdd:cd19164   87 GrYGPDD-----FDYSPEWIRASVERSLRRLHTDYLDLVYLH--DVEfVADEEVLEALKELFKlkdEGKIRNVGIS 155
AKR_AKR3F2 cd19139
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...
104-370 1.06e-19

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: 87.41  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALA--PV-RDRVVIATKFGFGveegkptslNSHPDHIRRAVEGSLKRLKTD 180
Cdd:cd19139   20 VRTALELGYRHIDTAQIYD---NEAAVGQAIAesGVpRDELFITTKIWID---------NLSKDKLLPSLEESLEKLRTD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 181 HIDLLYQHRPDPNVPIEdVAETVKALIL---EGKVKHWGLSEASARTIRRAHAVL---PVTAVQSEyamwwrepetrIFP 254
Cdd:cd19139   88 YVDLTLIHWPSPNDEVP-VEEYIGALAEakeQGLTRHIGVSNFTIALLDEAIAVVgagAIATNQIE-----------LSP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 255 TLEELGIgfVPYCptarsflagavnpsqrfdstdRRHNLP--RFQPdaLAKNMVL-LEFAQSWARRKNTTPVQFALAWVM 331
Cdd:cd19139  156 YLQNRKL--VAHC---------------------KQHGIHvtSYMT--LAYGKVLdDPVLAAIAERHGATPAQIALAWAM 210
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 490304600 332 aQRPWIVpIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19139  211 -ARGYAV-IPSSTKREHLRSNLLALDLTLDADDMAAIAA 247
AKR_AKR15A1 cd19161
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ...
77-288 4.64e-19

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: 87.00  E-value: 4.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  77 SSMGLGCLPMVGYYGggPRDRKAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFG---FGVE 152
Cdd:cd19161    1 SELGLGTAGLGNLYT--AVSNADADATLDAAWDSGIRYFDTAPMYGHGLAEHRLGDFLREKpRDEFVLSTKVGrllKPAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 EG---------KPTSLNSHPDH----IRRAVEGSLKRLKTDHIDLLYQHRPDPnVPIEDVAETV----------KA---L 206
Cdd:cd19161   79 EGsvpdpngfvDPLPFEIVYDYsydgIMRSFEDSLQRLGLNRIDILYVHDIGV-YTHGDRKERHhfaqlmsggfKAleeL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 207 ILEGKVKHWGLSEASARTIRRA--HAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAGAVNPSQRF 284
Cdd:cd19161  158 KKAGVIKAFGLGVNEVQICLEAldEADLDCFLLAGRYSLLDQSAEEEFLPRCEQRGTSLVIGGVFNSGILATGTKSGAKF 237

                 ....
gi 490304600 285 DSTD 288
Cdd:cd19161  238 NYGD 241
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
83-376 5.89e-19

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: 85.75  E-value: 5.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  83 CLPMVGY------YGGGPRDR-KAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFGFGVe 152
Cdd:cd19120    3 KIPAIAFgtgtawYKSGDDDIqRDLVDSVKLALKAGFRHIDTAEMYG---NEKEVGEALKESgvpREDLFITTKVSPGI- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 egkptslnshpDHIRRAVEGSLKRLKTDHIDLLYQHRP----DPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRR- 227
Cdd:cd19120   79 -----------KDPREALRKSLAKLGVDYVDLYLIHSPffakEGGPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEEl 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 228 -AHAVLPVTAVQSEYamwwrepetriFPTLEELGIGFVPYCptarsflagavnpsqrfdstdRRHN-----------LPR 295
Cdd:cd19120  148 lDTAKIKPAVNQIEF-----------HPYLYPQQPALLEYC---------------------REHGivvsaysplspLTR 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 296 FQPDALAKnmVLLEFAQswarRKNTTPVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDAALAKI 375
Cdd:cd19120  196 DAGGPLDP--VLEKIAE----KYGVTPAQVLLRWALQKG--IVVVTTSSKEERMKEYLEAFDFELTEEEVEEIDKAGKQK 267

                 .
gi 490304600 376 P 376
Cdd:cd19120  268 H 268
PLN02587 PLN02587
L-galactose dehydrogenase
69-218 3.52e-18

L-galactose dehydrogenase


Pssm-ID: 178198 [Multi-domain]  Cd Length: 314  Bit Score: 84.44  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  69 RKLGS--LEVSSMGLGCLPMVGYYGGGPRDrkAMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEAL--APV-RDRVVI 143
Cdd:PLN02587   2 RELGStgLKVSSVGFGASPLGSVFGPVSEE--DAIASVREAFRLGINFFDTSPYYGGTLSEKVLGKALkaLGIpREKYVV 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 144 ATKFGFGVEegkptSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDVAETVKALIL---EGKVKHWGLS 218
Cdd:PLN02587  80 STKCGRYGE-----GFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVNETIPALQKlkeSGKVRFIGIT 152
AKR_AKR15A cd19152
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...
79-276 6.95e-18

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: 83.43  E-value: 6.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  79 MGLGCLPMVGYYGGGPRDRkaMVSLIRAAFEQGITFFDTAEVYGPHLSEEFVGEALAPV-RDRVVIATKFGF------GV 151
Cdd:cd19152    3 LGFGTAPLGNLYEAVSDEE--AKATLVAAWDLGIRYFDTAPWYGAGLSEERLGAALRELgREDYVISTKVGRllvplqEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 152 EEGKPTSLNSHPDH----------IRRAVEGSLKRLKTDHIDLLYQHRPDPNVPI--------EDVAETVKALIL---EG 210
Cdd:cd19152   81 EPTFEPGFWNPLPFdavfdysydgILRSIEDSLQRLGLSRIDLLSIHDPDEDLAGaesdehfaQAIKGAFRALEElreEG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 211 KVKHWGLSEASARTIRRA--HAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFLAG 276
Cdd:cd19152  161 VIKAIGLGVNDWEVILRIleEADLDWVMLAGRYTLLDHSAARELLPECEKRGVKVVNAGPFNSGFLAG 228
AKR_AKR1G1_CeAKR cd19154
Caenorhabditis elegans aldo-keto reductase (CeAKR) and similar proteins; CeAKR is a founding ...
84-370 1.23e-16

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: 79.76  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGY--YGGGPRDrkaMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGFGVEEg 154
Cdd:cd19154   12 MPLIGLgtWQSKGAE---GITAVRTALKAGYRLIDTAFLYQ---NEEAIGEALAELleegvvkREDLFITTKLWTHEHA- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 155 kptslnshPDHIRRAVEGSLKRLKTDHIDLLYQHRP-------------------DPNVPIEDVAETVKALILEGKVKHW 215
Cdd:cd19154   85 --------PEDVEEALRESLKKLQLEYVDLYLIHAPaafkddegesgtmengmsiHDAVDVEDVWRGMEKVYDEGLTKAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 216 GLSEASARTIRRAHAV--LPVTAVQSEYAMWWREPETRIFptLEELGIGFVPYCPTARsflAGAVNPsqrfDSTDRRHNL 293
Cdd:cd19154  157 GVSNFNNDQIQRILDNarVKPHNNQVECHLYFPQKELVEF--CKKHNISVTSYATLGS---PGRANF----TKSTGVSPA 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490304600 294 PRFQPDALAKNMvllefaqswARRKNTTPVQFALAWVMaQRPWIVpIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19154  228 PNLLQDPIVKAI---------AEKHGKTPAQVLLRYLL-QRGIAV-IPKSATPSRIKENFNIFDFSLSEEDMATLEE 293
tas PRK10625
putative aldo-keto reductase; Provisional
73-371 2.16e-16

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 79.51  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  73 SLEVSSMGLGCLPmvgyYGGGPRDRKAMVSLiRAAFEQGITFFDTAEVYG--PH-----LSEEFVGEALAPV--RDRVVI 143
Cdd:PRK10625  10 SLEVSTLGLGTMT----FGEQNSEADAHAQL-DYAVAQGINLIDVAEMYPvpPRpetqgLTETYIGNWLAKRgsREKLII 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 144 ATKFGfGVEEGKPTSLNSHP----DHIRRAVEGSLKRLKTDHIDLLYQHRPD--------------PNVPIEDVAETVKA 205
Cdd:PRK10625  85 ASKVS-GPSRNNDKGIRPNQaldrKNIREALHDSLKRLQTDYLDLYQVHWPQrptncfgklgyswtDSAPAVSLLETLDA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 206 L---ILEGKVKHWGLSEASARTIRR------AHAVLPVTAVQSEYAMWWREPETRIFPTLEELGIGFVPYCPTARSFL-- 274
Cdd:PRK10625 164 LaeqQRAGKIRYIGVSNETAFGVMRylhlaeKHDLPRIVTIQNPYSLLNRSFEVGLAEVSQYEGVELLAYSCLAFGTLtg 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 275 --------AGAVNP-SQRFDstdrRHNLPRFQpDALAKNMVLlefaqswARRKNTTPVQFALAWVmAQRPWIVP-IPGTT 344
Cdd:PRK10625 244 kylngakpAGARNTlFSRFT----RYSGEQTQ-KAVAAYVDI-------AKRHGLDPAQMALAFV-RRQPFVAStLLGAT 310
                        330       340
                 ....*....|....*....|....*..
gi 490304600 345 QYPHLIENSGAPQVRLTDRELREIDAA 371
Cdd:PRK10625 311 TMEQLKTNIESLHLTLSEEVLAEIEAV 337
AKR_CeZK1290-like cd19135
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...
74-370 3.38e-16

Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the prototype of this family. It is an uncharacterized aldo/keto reductase family oxidoreductase.


Pssm-ID: 381361 [Multi-domain]  Cd Length: 265  Bit Score: 77.75  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGCLPMVGYYgggprdRKAMVSLIRaafEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgFG 150
Cdd:cd19135   11 VEMPILGLGTSHSGGYS------HEAVVYALK---ECGYRHIDTAKRYG---CEELLGKAIKESgvpREDLFLTTKL-WP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 151 VEEGKPTSlnshpdhiRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDV----AETVKALIL---EGKVKHWGLSEASA- 222
Cdd:cd19135   78 SDYGYEST--------KQAFEASLKRLGVDYLDLYLLHWPDCPSSGKNVketrAETWRALEElydEGLCRAIGVSNFLIe 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 223 --RTIRRAHAVLPVtAVQSEYAMWWREPETRIFptLEELGIGFVPYCPtarsflagavnpsqrfdstdrrhnlprfqpda 300
Cdd:cd19135  150 hlEQLLEDCSVVPH-VNQVEFHPFQNPVELIEY--CRDNNIVFEGYCP-------------------------------- 194
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490304600 301 LAKNMVLLEFA-QSWARRKNTTPVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19135  195 LAKGKALEEPTvTELAKKYQKTPAQILIRWSIQNG--VVTIPKSTKEERIKENCQVFDFSLSEEDMATLDS 263
AKR_DrGR-like cd19136
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ...
84-370 4.92e-15

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: 74.21  E-value: 4.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYyggGP---RDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAP-------VRDRVVIATKFG---FG 150
Cdd:cd19136    1 MPILGL---GTfrlRGEEEVRQAVDAALKAGYRLIDTASVYR---NEADIGKALRDllpkyglSREDIFITSKLApkdQG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 151 VEEGkptslnshpdhiRRAVEGSLKRLKTDHIDLLYQHRPDP-NVPIEDVA------ETVKAL---ILEGKVKHWGLSEA 220
Cdd:cd19136   75 YEKA------------RAACLGSLERLGTDYLDLYLIHWPGVqGLKPSDPRnaelrrESWRALedlYKEGKLRAIGVSNY 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 221 SARTIR--RAHAVLPVTAVQSEYAMWWREPETRIFptLEELGIGFVPYCPTARSflagavnpsqrfdstdrrhnlprfqP 298
Cdd:cd19136  143 TVRHLEelLKYCEVPPAVNQVEFHPHLVQKELLKF--CKDHGIHLQAYSSLGSG-------------------------D 195
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 299 DALAKNMVLLEFAQSWARrkntTPVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19136  196 LRLLEDPTVLAIAKKYGR----TPAQVLLRWALQQG--IGVIPKSTNPERIAENIKVFDFELSEEDMAELNA 261
AKR_AKR1G1_1I cd19111
Caenorhabditis elegans aldo-keto reductase (CeAKR), Coptotermes gestroi aldo-keto reductase ...
104-369 1.10e-14

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: 73.69  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFgfgveegkPTSLNShPDHIRRAVEGSLKR 176
Cdd:cd19111   23 VDYALFVGYRHIDTALSYQ---NEKAIGEALKWWlkngklkREEVFITTKL--------PPVYLE-FKDTEKSLEKSLEN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 177 LKTDHIDLLYQHRPDPNV-------------PIEDVAETVKALILEGKVKHWGLSEASARTIRR--AHAVLPVTAVQSEY 241
Cdd:cd19111   91 LKLPYVDLYLIHHPCGFVnkkdkgerelassDVTSVWRAMEALVSEGKVKSIGLSNFNPRQINKilAYAKVKPSNLQLEC 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 242 AMWWREPETRIFptLEELGIGFVPYCPTARSFLAGAVNPSQrfdstdrrhnlprfQPDALAKNMVLlefaqSWARRKNTT 321
Cdd:cd19111  171 HAYLQQRELRKF--CNKKNIVVTAYAPLGSPGRANQSLWPD--------------QPDLLEDPTVL-----AIAKELDKT 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 490304600 322 PVQFALAWVMAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19111  230 PAQVLLRFVLQRG--TGVLPKSTNKERIEENFEVFDFELTEEHFKKLK 275
AKR_AKR2E1-5 cd19116
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ...
83-370 4.51e-14

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: 71.93  E-value: 4.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  83 CLPMVGYYGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGfgveegk 155
Cdd:cd19116   10 EIPAIALGTWKLKDDEGVRQAVKHAIEAGYRHIDTAYLYG---NEAEVGEAIREKiaegvvkREDLFITTKLW------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 ptslNSHPDH--IRRAVEGSLKRLKTDHIDLLYQHRP-------DPNVPIE------DVAETVKA---LILEGKVKHWGL 217
Cdd:cd19116   80 ----NSYHEReqVEPALRESLKRLGLDYVDLYLIHWPvafkennDSESNGDgslsdiDYLETWRGmedLVKLGLTRSIGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 218 SEASARTIRR--AHAVLPVTAVQSEyamwwrepetrIFPTL---------EELGIGFVPYCPTARSFLAGAVNPSQRFDS 286
Cdd:cd19116  156 SNFNSEQINRllSNCNIKPAVNQIE-----------VHPTLtqeklvaycQSNGIVVMAYSPFGRLVPRGQTNPPPRLDD 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 287 tdrrhnlprfqpdalaknmvllEFAQSWARRKNTTPVQFALAWVMaQRPwIVPIPGTTQYPHLIENSGAPQVRLTDRELR 366
Cdd:cd19116  225 ----------------------PTLVAIAKKYGKTTAQIVLRYLI-DRG-VVPIPKSSNKKRIKENIDIFDFQLTPEEVA 280

                 ....
gi 490304600 367 EIDA 370
Cdd:cd19116  281 ALNS 284
dkgB PRK11172
2,5-didehydrogluconate reductase DkgB;
76-384 1.00e-13

2,5-didehydrogluconate reductase DkgB;


Pssm-ID: 183012 [Multi-domain]  Cd Length: 267  Bit Score: 70.82  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  76 VSSMGLGCLPMVGyygggprdrKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAP---VRDRVVIATKFGfgVE 152
Cdd:PRK11172   3 IPAFGLGTFRLKD---------QVVIDSVKTALELGYRAIDTAQIYD---NEAAVGQAIAEsgvPRDELFITTKIW--ID 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 egkptslNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPN--VPiedVAETVKALIlegKVKHWGLSEA---SARTI-- 225
Cdd:PRK11172  69 -------NLAKDKLIPSLKESLQKLRTDYVDLTLIHWPSPNdeVS---VEEFMQALL---EAKKQGLTREigiSNFTIal 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 226 -RRAHAVLPVTAV---QSEYAMWWREPETRIFptLEELGIGFVPYCPTArsflAGAVnpsqrfdstdrrhnlprfqpdal 301
Cdd:PRK11172 136 mKQAIAAVGAENIatnQIELSPYLQNRKVVAF--AKEHGIHVTSYMTLA----YGKV----------------------- 186
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 302 AKNMVLLEFAQswarRKNTTPVQFALAWVMaQRPWIVpIPGTTQYPHLIENSGAPQVRLTDRELREIdAALAKiplqGGR 381
Cdd:PRK11172 187 LKDPVIARIAA----KHNATPAQVILAWAM-QLGYSV-IPSSTKRENLASNLLAQDLQLDAEDMAAI-AALDR----NGR 255

                 ....
gi 490304600 382 -ADP 384
Cdd:PRK11172 256 lVSP 259
AKR_AKR5D1_E1 cd19132
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...
80-370 3.50e-13

AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B (DkgB) from Corynebacterium sp. and 2,5-diketo-D-gluconic acid reductase Zymomonas mobilis are founding members of aldo-keto reductase family 5 member D1 (AKR5D1) and E1 (AKR5E1), respectively. DkgB (EC 1.1.1.274), also called 2,5-didehydrogluconate reductase (2-dehydro-D-gluconate-forming), or 2,5-DKG reductase B, or 2,5-DKGR B, or 25DKGR-B, catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG).


Pssm-ID: 381358 [Multi-domain]  Cd Length: 255  Bit Score: 68.84  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  80 GLGCLPMVGYYGggprdrkamVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALA----PvRDRVVIATKFGfGVEEGK 155
Cdd:cd19132   11 GFGTYPLKGDEG---------VEAVVAALQAGYRLLDTAFNYE---NEGAVGEAVRrsgvP-REELFVTTKLP-GRHHGY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 156 ptslnshpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVpieDV-AETVKALI---LEGKVKHWGLS---EASARTIRRA 228
Cdd:cd19132   77 --------EEALRTIEESLYRLGLDYVDLYLIHWPNPSR---DLyVEAWQALIearEEGLVRSIGVSnflPEHLDRLIDE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 229 HAVLPVTAvQSEYAMWWREPETRIFptLEELGIGFVPYCPTARsflagavnpsqrfdstdrrhnlprfqPDALAKNMVLL 308
Cdd:cd19132  146 TGVTPAVN-QIELHPYFPQAEQRAY--HREHGIVTQSWSPLGR--------------------------GSGLLDEPVIK 196
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490304600 309 EFAQswarRKNTTPVQFALAWvMAQRPwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19132  197 AIAE----KHGKTPAQVVLRW-HVQLG-VVPIPKSANPERQRENLAIFDFELSDEDMAAIAA 252
AKR_BaDH-like cd19129
Bradyrhizobium diazoefficiens dehydrogenase (DH) and similar proteins; Bradyrhizobium ...
80-334 2.32e-11

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: 64.02  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  80 GLGCLPMVGYyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYgphLSEEFVGEALAPV-------RDRVVIATKFgfgve 152
Cdd:cd19129    2 GSGAIPALGF-GTLIPDPSATRNAVKAALEAGFRHFDCAERY---RNEAEVGEAMQEVfkagkirREDLFVTTKL----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 egkpTSLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRP--------------------DPNVPIEDVAETVKALILEGKV 212
Cdd:cd19129   73 ----WNTNHRPERVKPAFEASLKRLQLDYLDLYLIHTPfafqpgdeqdprdangnviyDDGVTLLDTWRAMERLVDEGRC 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 213 KHWGLSEAS---ARTIRRAHAVLPVtAVQSEYAMWWrePETRIFPTLEELGIGFVPYCPTArsflagavnpsqrfdstdr 289
Cdd:cd19129  149 KAIGLSDVSlekLREIFEAARIKPA-VVQVESHPYL--PEWELLDFCKNHGIVLQAFAPLG------------------- 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490304600 290 rHNLprfQPDALAKNMVLlefaqSWARRKNTTPVQFALAWVMaQR 334
Cdd:cd19129  207 -HGM---EPKLLEDPVIT-----AIARRVNKTPAQVLLAWAI-QR 241
AKR_AKR5C2 cd19131
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...
101-218 2.71e-11

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: 63.16  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 101 VSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgfgveegkptsLNSHPDH--IRRAVEGSLK 175
Cdd:cd19131   26 ASAVREALEVGYRSIDTAAIYG---NEEGVGKAIRASgvpREELFITTKL-----------WNSDQGYdsTLRAFDESLR 91
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490304600 176 RLKTDHIDLLYQHRPdpnVPIED-VAETVKALI---LEGKVKHWGLS 218
Cdd:cd19131   92 KLGLDYVDLYLIHWP---VPAQDkYVETWKALIelkKEGRVKSIGVS 135
AKR_AKR2B1-10 cd19113
AKR2B family of aldo-keto reductase (AKR); The AKR2B family of AKR includes NAD(P)H-dependent ...
70-370 6.59e-11

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: 62.85  E-value: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  70 KLGS-LEVSSMGLGCLPMvgyygggprDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRV 141
Cdd:cd19113    4 KLNSgYKMPSVGFGCWKL---------DNATAADQIYQAIKAGYRLFDGAEDYG---NEKEVGEGVNRAideglvkREEL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 142 VIATKFgfgveegkptsLNS--HPDHIRRAVEGSLKRLKTDHIDLLYQHRP--------------------DPNVPIEDV 199
Cdd:cd19113   72 FLTSKL-----------WNNfhDPKNVETALNKTLSDLKLDYVDLFLIHFPiafkfvpieekyppgfycgdGDNFVYEDV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 200 --AETVKA---LILEGKVKHWGLSEASARTIR---RAHAVLPVtAVQSEYAMWWREPetRIFPTLEELGIGFVPYCPTA- 270
Cdd:cd19113  141 piLDTWKAlekLVDAGKIKSIGVSNFPGALILdllRGATIKPA-VLQIEHHPYLQQP--KLIEYAQKAGITITAYSSFGp 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 271 RSFLagavnpsqrfdstdrRHNLPRfqpdalAKNMVLL---EFAQSWARRKNTTPVQFALAWVmAQRPwIVPIPGTTQYP 347
Cdd:cd19113  218 QSFV---------------ELNQGR------ALNTPTLfehDTIKSIAAKHNKTPAQVLLRWA-TQRG-IAVIPKSNLPE 274
                        330       340
                 ....*....|....*....|...
gi 490304600 348 HLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19113  275 RLLQNLSVNDFDLTKEDFEEIAK 297
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
107-370 8.64e-11

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: 61.82  E-value: 8.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 107 AFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFGFGveegkptslNSHPDHIRRAVEGSLKRLKTDHID 183
Cdd:cd19133   32 AIKAGYRLIDTAAAYG---NEEAVGRAIKKSgipREELFITTKLWIQ---------DAGYEKAKKAFERSLKRLGLDYLD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 184 LLYQHRpdpnvPIEDVAETVKA---LILEGKVKHWGLSEASARTIRR---AHAVLPvtAV-QSEYAMWWREPETRIFptL 256
Cdd:cd19133  100 LYLIHQ-----PFGDVYGAWRAmeeLYKEGKIRAIGVSNFYPDRLVDlilHNEVKP--AVnQIETHPFNQQIEAVEF--L 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 257 EELGIGFVPYCPTARSflagavnpsqrfdstdrRHNlprfqpdaLAKNMVLLEFAQswarRKNTTPVQFALAWVMaQRPw 336
Cdd:cd19133  171 KKYGVQIEAWGPFAEG-----------------RNN--------LFENPVLTEIAE----KYGKSVAQVILRWLI-QRG- 219
                        250       260       270
                 ....*....|....*....|....*....|....
gi 490304600 337 IVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19133  220 IVVIPKSVRPERIAENFDIFDFELSDEDMEAIAA 253
AKR_unchar cd19098
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
106-376 3.52e-10

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: 60.82  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 106 AAFEQGITFFDTAEVYGphLSEEFVG---EALAPVRDRVVIATKFGF----------GVEEGKPTSLnshpDHIRRAVEG 172
Cdd:cd19098   43 AAWAAGVRYFDAARSYG--RAEEFLGswlRSRNIAPDAVFVGSKWGYtytadwqvdaAVHEVKDHSL----ARLLKQWEE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 173 SLKRLKtDHIDlLYQ-HRPDPNVPIEDVAETVKALIlEGKVKHW--GLSEAS---ARTIRRAHAVLP-----VTAVQSEy 241
Cdd:cd19098  117 TRSLLG-KHLD-LYQiHSATLESGVLEDADVLAALA-ELKAEGVkiGLSLSGpqqAETLRRALEIEIdgarlFDSVQAT- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 242 amwWREPETRIFPTLEEL---GIGFVpycptARSFLA-GAVnpsqrfdstdrrhnLPRFQPDALAKNMVLLEFAqswARR 317
Cdd:cd19098  193 ---WNLLEQSAGEALEEAheaGMGVI-----VKEALAnGRL--------------TDRNPSPELAPLMAVLKAV---ADR 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 318 KNTTPVQFALAWVMAQrPWI-VPIPGTTQYPHLIENSGAPQVRLtDRELREIDAALAKIP 376
Cdd:cd19098  248 LGVTPDALALAAVLAQ-PFVdVVLSGAATPEQLRSNLRALDVSL-DLELLAALADLAEPP 305
AKR_AKR3G1 cd19123
AKR3G family of aldo-keto reductase (AKR); Synechocystis sp. aldo/keto reductase slr0942 is a ...
104-370 5.25e-10

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: 60.12  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGFgveegkptslNSH-PDHIRRAVEGSLK 175
Cdd:cd19123   31 VKQALEAGYRHIDCAAIYG---NEAEIGAALAEVfkegkvkREDLWITSKLWN----------NSHaPEDVLPALEKTLA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 176 RLKTDHIDLLYQHRP------------------DPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRRAHA---VLPV 234
Cdd:cd19123   98 DLQLDYLDLYLMHWPvalkkgvgfpesgedllsLSPIPLEDTWRAMEELVDKGLCRHIGVSNFSVKKLEDLLAtarIKPA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 235 TAvQSEYAMWWREPETRIFptLEELGIGFVPYCPtarsflagavnpsqrFDSTDRRHNLPRFQPDALAKNMVLLEFAQsw 314
Cdd:cd19123  178 VN-QVELHPYLQQPELLAF--CRDNGIHLTAYSP---------------LGSGDRPAAMKAEGEPVLLEDPVINKIAE-- 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 315 arRKNTTPVQFALAWVMaQRPWIVpIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19123  238 --KHGASPAQVLIAWAI-QRGTVV-IPKSVNPERIQQNLEAAEVELDASDMATIAA 289
AKR_AKR5B1 cd19127
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...
101-370 2.31e-09

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: 57.80  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 101 VSLIRAAFEQGITFFDTAEVYGphlSEEFVGEAL---APVRDRVVIATKFgFGVEEGKptslnshpDHIRRAVEGSLKRL 177
Cdd:cd19127   25 ADAVATALADGYRLIDTAAAYG---NEREVGEGIrrsGVDRSDIFVTTKL-WISDYGY--------DKALRGFDASLRRL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 178 KTDHIDLLYQHRPDPNVpIEDVAETVKAL---ILEGKVKHWGLSEASARTIRR---AHAVLPvtAV-QSEYAMWWREPET 250
Cdd:cd19127   93 GLDYVDLYLLHWPVPND-FDRTIQAYKALeklLAEGRVRAIGVSNFTPEHLERlidATTVVP--AVnQVELHPYFSQKDL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 251 RIFPTleELGIGFVPYCPTarsflaGAVNPSQRFDSTDRRHNLprfqpdalaKNMVLLEFAQSWARrkntTPVQFALAWV 330
Cdd:cd19127  170 RAFHR--RLGIVTQAWSPI------GGVMRYGASGPTGPGDVL---------QDPTITGLAEKYGK----TPAQIVLRWH 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490304600 331 MAQRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19127  229 LQNG--VSAIPKSVHPERIAENIDIFDFALSAEDMAAIDA 266
AKR_AKR4A_4B cd19124
AKR4A and AKR4B families of aldo-keto reductase (AKR); The AKR4A family of AKR includes ...
94-333 8.28e-09

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: 56.12  E-value: 8.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  94 PRDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPVRDRVVIATKFGFGVEEgKPTSLNSHPDHIRRAVEGS 173
Cdd:cd19124   16 PPSPEDIKAAVLEAIEVGYRHFDTAAAYG---TEEALGEALAEALRLGLVKSRDELFVTS-KLWCSDAHPDLVLPALKKS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 174 LKRLKTDHIDLLYQHRP---DP---NVPIEDvaETVKALILEG------KVKHWGLSEA------SARTIRR--AHAVLP 233
Cdd:cd19124   92 LRNLQLEYVDLYLIHWPvslKPgkfSFPIEE--EDFLPFDIKGvweameECQRLGLTKAigvsnfSCKKLQEllSFATIP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 234 VTAVQSEYAMWWREPETRIFptLEELGIGFVPYCPtarsfLAGAVNPsqrfdstdrrhnlprFQPDALAKNMVLLEFAQS 313
Cdd:cd19124  170 PAVNQVEMNPAWQQKKLREF--CKANGIHVTAYSP-----LGAPGTK---------------WGSNAVMESDVLKEIAAA 227
                        250       260
                 ....*....|....*....|
gi 490304600 314 warrKNTTPVQFALAWVMAQ 333
Cdd:cd19124  228 ----KGKTVAQVSLRWVYEQ 243
AKR_AKR2A1-2 cd19112
AKR2A family of aldo-keto reductase (AKR); The AKR2A family of AKR includes AKR2A1 ...
84-370 8.33e-09

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: 56.34  E-value: 8.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYyGGGPRDRKAMVSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFgfgveegkp 156
Cdd:cd19112   11 MPVIGL-GVWRMEPGEIKELILNAIKIGYRHFDCAADYK---NEKEVGEALAEAfktglvkREDLFITTKL--------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 157 tsLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRP-----------------------DPNVPIEDVAETVKALILEGKVK 213
Cdd:cd19112   78 --WNSDHGHVIEACKDSLKKLQLDYLDLYLVHFPvatkhtgvgttgsalgedgvldiDVTISLETTWHAMEKLVSAGLVR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 214 HWGLSEASARTIRRAHAvlpvtavQSEYAMWWREPETRIFPTLEELgigfVPYC------PTARSFLAGAVNPSQRFDST 287
Cdd:cd19112  156 SIGISNYDIFLTRDCLA-------YSKIKPAVNQIETHPYFQRDSL----VKFCqkhgisVTAHTPLGGAAANAEWFGSV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 288 DrrhnlPRFQPdalaknmVLLEFAQSWarrkNTTPVQFALAWVMaQRPWIVpIPGTTQYPHLIENSGAPQVRLTDRELRE 367
Cdd:cd19112  225 S-----PLDDP-------VLKDLAKKY----GKSAAQIVLRWGI-QRNTAV-IPKSSKPERLKENIDVFDFQLSKEDMKL 286

                 ...
gi 490304600 368 IDA 370
Cdd:cd19112  287 IKS 289
AKR_AKR4C1-15 cd19125
AKR4C family of aldo-keto reductase (AKR); The AKR4C family of AKR includes aldose reductase ...
82-329 1.50e-08

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: 55.43  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  82 GCLPMVGY--YGGGPRDRKAMVsliRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGfgve 152
Cdd:cd19125    9 AKIPAVGLgtWQADPGVVGNAV---KTAIKEGYRHIDCAAIYG---NEKEIGKALKKLfedgvvkREDLFITSKLW---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 153 egkptsLNSH-PDHIRRAVEGSLKRLKTDHIDLLYQHRP----------DP-NVPIEDVAETVKA---LILEGKVKHWGL 217
Cdd:cd19125   79 ------CTDHaPEDVPPALEKTLKDLQLDYLDLYLIHWPvrlkkgahmpEPeEVLPPDIPSTWKAmekLVDSGKVRAIGV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 218 SEASARTIRRAHAVLPVT-AV-QSEYAMWWRepETRIFPTLEELGIGFVPYCPTARSflagavnpsqrfDSTDRRHNlpr 295
Cdd:cd19125  153 SNFSVKKLEDLLAVARVPpAVnQVECHPGWQ--QDKLHEFCKSKGIHLSAYSPLGSP------------GTTWVKKN--- 215
                        250       260       270
                 ....*....|....*....|....*....|....
gi 490304600 296 fqpdaLAKNMVLLEFAQswarRKNTTPVQFALAW 329
Cdd:cd19125  216 -----VLKDPIVTKVAE----KLGKTPAQVALRW 240
AKR_AKR5G1-3 cd19157
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...
101-370 1.27e-07

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: 52.39  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 101 VSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgFGVEEGKPTSLnshpdhirRAVEGSLKRL 177
Cdd:cd19157   27 VNAVKTALKNGYRSIDTAAIYG---NEEGVGKGIKESgipREELFITSKV-WNADQGYDSTL--------KAFEASLERL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 178 KTDHIDLLYQHRPDPNVpiedVAETVKA---LILEGKVKHWGLSEASARTIRRAHAVLPVTAV--QSEYAMWWREPETRI 252
Cdd:cd19157   95 GLDYLDLYLIHWPVKGK----YKETWKAlekLYKDGRVRAIGVSNFQVHHLEDLLADAEIVPMvnQVEFHPRLTQKELRD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 253 FptLEELGIGFVPYCPtarsFLAGavnpsQRFDstdrrhnlprfqpdalakNMVLLEFAQSWarrkNTTPVQFALAWVMA 332
Cdd:cd19157  171 Y--CKKQGIQLEAWSP----LMQG-----QLLD------------------NPVLKEIAEKY----NKSVAQVILRWDLQ 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 490304600 333 QRpwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19157  218 NG--VVTIPKSIKEHRIIENADVFDFELSQEDMDKIDA 253
AKR_AKR1I_CgAKR1 cd19155
Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi ...
104-369 1.83e-07

Coptotermes gestroi aldo-keto reductase (CgAKR-1) and similar proteins; Coptotermes gestroi aldo-keto reductase (CgAKR-1) is a founding member of aldo-keto reductase family 1 member I (AKR1I). It is a multipurpose enzyme with potential biotechnological applications.


Pssm-ID: 381381 [Multi-domain]  Cd Length: 307  Bit Score: 52.14  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFgfgveegKPTSlnSHPDHIRRAVEGSLKR 176
Cdd:cd19155   31 VDTALEAGYRHIDTAYVYR---NEAAIGNVLKKWidsgkvkREELFIVTKL-------PPGG--NRREKVEKFLLKSLEK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 177 LKTDHIDLLYQHRP---------------------DPNVPIEDVAETVKALILEGKVKHWGLSEASARTIRR--AHAVLP 233
Cdd:cd19155   99 LQLDYVDLYLIHFPvgslskeddsgkldptgehkqDYTTDLLDIWKAMEAQVDQGLTRSIGLSNFNREQMARilKNARIK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 234 VTAVQSEYAMWWREPETRIFptLEELGIGFVPYCPTARSFLAgAVNPSqrfdstdrRHNLPRFQPDaLAKNMVLLEFAQs 313
Cdd:cd19155  179 PANLQVELHVYLQQKDLVDF--CSTHSITVTAYAPLGSPGAA-HFSPG--------TGSPSGSSPD-LLQDPVVKAIAE- 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 314 warRKNTTPVQFALAWVMaQRPwIVPIPGTTQYPHLIENSGAPQVRLTDRELREID 369
Cdd:cd19155  246 ---RHGKSPAQVLLRWLM-QRG-VVVIPKSTNAARIKENFQVFDFELTEADMAKLS 296
AKR_GlAR-like cd19128
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ...
104-365 3.36e-07

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: 51.37  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGfgveegkPTslNSHPDHIRRAVEGSLKR 176
Cdd:cd19128   20 VKNAIKAGYRHIDCAYYYG---NEAFIGIAFSEIfkdggvkREDLFITSKLW-------PT--MHQPENVKEQLLITLQD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 177 LKTDHIDLLYQHRP---DPN----------------VPIEDVAETVKALILEGKVKHWGLSEASARTIRR--AHAVLPVT 235
Cdd:cd19128   88 LQLEYLDLFLIHWPlafDMDtdgdprddnqiqslskKPLEDTWRAMEQCVDEKLTKNIGVSNYSTKLLTDllNYCKIKPF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 236 AVQSEYAMWWrePETRIFPTLEELGIGFVPYCPTARSFLAGAVNPsqrfdstdrrhnlprfQPDALAKNMvllefaqswA 315
Cdd:cd19128  168 MNQIECHPYF--QNDKLIKFCIENNIHVTAYRPLGGSYGDGNLTF----------------LNDSELKAL---------A 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490304600 316 RRKNTTPVQFALAWVMAQRP--WIVpIPGTTQYPHLIENSGAPQVRLTDREL 365
Cdd:cd19128  221 TKYNTTPPQVIIAWHLQKWPknYSV-IPKSANKSRCQQNFDINDLALTKEDM 271
dkgA PRK11565
2,5-didehydrogluconate reductase DkgA;
101-218 3.87e-07

2,5-didehydrogluconate reductase DkgA;


Pssm-ID: 183203 [Multi-domain]  Cd Length: 275  Bit Score: 51.23  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 101 VSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgfgveegkptsLNSHPDHIRRAVEGSLKRL 177
Cdd:PRK11565  31 ITAIHKALEVGYRSIDTAAIYK---NEEGVGKALKEAsvaREELFITTKL-----------WNDDHKRPREALEESLKKL 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490304600 178 KTDHIDLLYQHRPDPnvPIEDVAETVKALIL---EGKVKHWGLS 218
Cdd:PRK11565  97 QLDYVDLYLMHWPVP--AIDHYVEAWKGMIElqkEGLIKSIGVC 138
AKR_AKR1A1-4 cd19106
AKR1A family of aldo-keto reductase (AKR); The AKR1A family of AKR includes alcohol ...
104-370 1.47e-06

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: 49.31  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEAL--------APVRDRVVIATKFgfgveegkptsLNS--HPDHIRRAVEGS 173
Cdd:cd19106   26 VKYALDAGYRHIDCAAVYG---NEQEVGEALkekvgpgkAVPREDLFVTSKL-----------WNTkhHPEDVEPALRKT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 174 LKRLKTDHIDLLYQHRP------------DPNVPIE----DVAETVKA---LILEGKVKHWGLSEASARTI-------RR 227
Cdd:cd19106   92 LKDLQLDYLDLYLIHWPyafergdnpfpkNPDGTIRydstHYKETWKAmekLVDKGLVKAIGLSNFNSRQIddilsvaRI 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 228 AHAVLPVtavqseyamwwrepETRIFPTLEELgigfVPYCpTARSFLAGAVNPsqrFDSTDRrhnlPRFQPDalakNMVL 307
Cdd:cd19106  172 KPAVLQV--------------ECHPYLAQNEL----IAHC-KARGLVVTAYSP---LGSPDR----PWAKPD----EPVL 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490304600 308 LEFA--QSWARRKNTTPVQFALAWVMaQRPwIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19106  222 LEEPkvKALAKKYNKSPAQILLRWQV-QRG-VVVIPKSVTPSRIKQNIQVFDFTLSPEEMKQLDA 284
AKR_AKR3A1-2 cd19117
AKR3A family of aldo-keto reductase (AKR); Saccharomyces cerevisiae Gcy1p and Ypr1p are ...
104-369 1.91e-06

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: 49.03  E-value: 1.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEAL----APvRDRVVIATKFGfgveegkptslNSHPDHIRRAVEGSLKRLKT 179
Cdd:cd19117   33 VEAALKAGYRHIDTAAIYG---NEEEVGQGIkdsgVP-REEIFITTKLW-----------CTWHRRVEEALDQSLKKLGL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 180 DHIDLLYQHRPDPNVP---------------------IEDVAETVKALILEGKVKHWGLSEASARTIRRAHAvlpvtavq 238
Cdd:cd19117   98 DYVDLYLMHWPVPLDPdgndflfkkddgtkdhepdwdFIKTWELMQKLPATGKVKAIGVSNFSIKNLEKLLA-------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 239 seyamwwrEPETRIFPTLEELGI-------GFVPYCpTARSFLAGAVNPsqrFDSTDrrhnlprfqpDALAKNMVLLEFA 311
Cdd:cd19117  170 --------SPSAKIVPAVNQIELhpllpqpKLVDFC-KSKGIHATAYSP---LGSTN----------APLLKEPVIIKIA 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490304600 312 QSwarrKNTTPVQFALAWvMAQRPWIVpIPGTTQyPHLIENSGApQVRLTDRELREID 369
Cdd:cd19117  228 KK----HGKTPAQVIISW-GLQRGYSV-LPKSVT-PSRIESNFK-LFTLSDEEFKEID 277
AKR_AKR3C1 cd19119
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ...
84-211 2.01e-06

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: 49.03  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYYGGGPRDRKAMV-SLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV-------RDRVVIATKFGfgveegk 155
Cdd:cd19119   12 IPALGLGTASPHEDRAEVkEAVEAAIKEGYRHIDTAYAYE---TEDFVGEAIKRAiddgsikREELFITTKVW------- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490304600 156 PTSLnshpDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVPIEDvaETVKALILEGK 211
Cdd:cd19119   82 PTFY----DEVERSLDESLKALGLDYVDLLLVHWPVCFEKDSD--DSGKPFTPVND 131
AKR_AKR5C1 cd19130
Corynebacterium sp. 2,5-diketo-D-gluconic acid reductase A (DkgA) and similar proteins; ...
84-192 7.87e-06

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: 46.83  E-value: 7.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGY--YGGGPRDRKAMVSlirAAFEQGITFFDTAEVYGphlSEEFVGEALAP---VRDRVVIATKFGfgveegkptS 158
Cdd:cd19130   10 IPQLGYgvFKVPPADTQRAVA---TALEVGYRHIDTAAIYG---NEEGVGAAIAAsgiPRDELFVTTKLW---------N 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 490304600 159 LNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDP 192
Cdd:cd19130   75 DRHDGDEPAAAFAESLAKLGLDQVDLYLVHWPTP 108
AKR_AKR3B1-3 cd19118
AKR3B family of aldo-keto reductase (AKR); Sporidiobolus salmonicolor NADPH-dependent aldehyde ...
84-225 9.45e-06

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: 47.02  E-value: 9.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGY--YGGGPRDRKAMVsliRAAFEQGITFFDTAEVYGphlSEEFVGEALAPVRDRVViatkfGFGVEEGKPTSL-- 159
Cdd:cd19118    7 IPAIGLgtWQAEPGEVGAAV---KIALKAGYRHLDLAKVYQ---NQHEVGQALKELLKEEP-----GVKREDLFITSKlw 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 160 -NSH-PDHIRRAVEGSLKRLKTDHIDLLYQHRP------------------------DPNVPIEDVAETVKALILEGKVK 213
Cdd:cd19118   76 nNSHrPEYVEPALDDTLKELGLDYLDLYLIHWPvafkptgdlnpltavptnggevdlDLSVSLVDTWKAMVELKKTGKVK 155
                        170
                 ....*....|..
gi 490304600 214 HWGLSEASARTI 225
Cdd:cd19118  156 SIGVSNFSIDHL 167
AKR_AKR5A_5G cd19126
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...
104-370 4.40e-05

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: 44.74  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 104 IRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgFGVEEGKPTSLNshpdhirrAVEGSLKRLKTD 180
Cdd:cd19126   29 VQTALENGYRSIDTAAIYK---NEEGVGEAIRESgvpREELFVTTKL-WNDDQRARRTED--------AFQESLDRLGLD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 181 HIDLLYQHRPDPnvpiEDVAETVKAL---ILEGKVKHWGLSEASARTIRR--AHAVLPVTAVQSEYAMWWREPETRIFpt 255
Cdd:cd19126   97 YVDLYLIHWPGK----DKFIDTWKALeklYASGKVKAIGVSNFQEHHLEEllAHADVVPAVNQVEFHPYLTQKELRGY-- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 256 LEELGIgfvpyCPTARSFLAGAvnpsqrfdstdrrhnlprfqpdALAKNMVLLEFAQSWARrkntTPVQFALAWVMaQRP 335
Cdd:cd19126  171 CKSKGI-----VVEAWSPLGQG----------------------GLLSNPVLAAIGEKYGK----SAAQVVLRWDI-QHG 218
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 490304600 336 wIVPIPGTTQYPHLIENSGAPQVRLTDRELREIDA 370
Cdd:cd19126  219 -VVTIPKSVHASRIKENADIFDFELSEDDMTAIDA 252
AKR_AKR3D1 cd19121
AKR3D family of aldo-keto reductase (AKR); Trichoderma reesei D-galacturonate reductase (GAR1, ...
74-195 4.47e-04

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: 41.75  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  74 LEVSSMGLGClpmvgYYGGGPRDRKAMVSLIRAafeqGITFFDTAEVYGphlSEEFVG----EALAPV--RDRVVIATKF 147
Cdd:cd19121   10 ASIPAVGLGT-----WQAKAGEVKAAVAHALKI----GYRHIDGALCYQ---NEDEVGegikEAIAGGvkREDLFVTTKL 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490304600 148 gfgveegkptsLNSHPDHIRRAVEGSLKRLKTDHIDLLYQHRPDPNVP 195
Cdd:cd19121   78 -----------WSTYHRRVELCLDRSLKSLGLDYVDLYLVHWPVLLNP 114
AKR_AKR5H1 cd19134
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ...
84-194 1.20e-03

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: 40.22  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600  84 LPMVGYYGGGPRDRKAMVSlIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgfgveegkptsln 160
Cdd:cd19134   11 MPVIGLGVGELSDDEAERS-VSAALEAGYRLIDTAAAYG---NEAAVGRAIAASgipRGELFVTTKL------------- 73
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490304600 161 SHPDH----IRRAVEGSLKRLKTDHIDLLYQHRPDPNV 194
Cdd:cd19134   74 ATPDQgftaSQAACRASLERLGLDYVDLYLIHWPAGRE 111
AKR_AKR5A1_2 cd19156
AKR5A family of aldo-keto reductase (AKR); Prostaglandin F2-alpha synthase (PGFS) from ...
101-218 1.85e-03

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: 39.81  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490304600 101 VSLIRAAFEQGITFFDTAEVYGphlSEEFVGEALAPV---RDRVVIATKFgFGVEEGKPTSLnshpdhirRAVEGSLKRL 177
Cdd:cd19156   26 ENAVKWAIEAGYRHIDTAAIYK---NEEGVGQGIRESgvpREEVFVTTKL-WNSDQGYESTL--------AAFEESLEKL 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490304600 178 KTDHIDLLYQHRPDPNvPIEDVAETVKALILEGKVKHWGLS 218
Cdd:cd19156   94 GLDYVDLYLIHWPVKG-KFKDTWKAFEKLYKEKKVRAIGVS 133
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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