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Conserved domains on  [gi|6323684|ref|NP_013755|]
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D-arabinose 1-dehydrogenase (NAD(P)(+)) ARA2 [Saccharomyces cerevisiae S288C]

Protein Classification

aldo/keto reductase family protein( domain architecture ID 14442776)

aldo/keto reductase (AKR) family protein such as Saccharomyces cerevisiae D-arabinose 1-dehydrogenase, also called NAD(+)-specific D-arabinose dehydrogenase, which catalyzes the the oxidation of D-arabinose to D-arabinono-1,4-lactone in the presence of NAD(+)

CATH:  3.20.20.100
EC:  1.1.1.-
Gene Ontology:  GO:0016616
PubMed:  25304492|19706366|9307009|12663943|16970545

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
 2-301 1.29e-165

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: 463.29  E-value: 1.29e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    2 VNEKVNPFDLASVSPLVLGGAILNQQYTDEPESIPLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLRNEFPRDTY 81
Cdd:cd19164   1 PVPKPVALSLAGLPPLIFGAATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIILGRALKALRDEFPRDTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   82 FICTKVGRIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19164  81 FIITKVGRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVLEALKELFKLKDEGKIRNVGISGYPLP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  162 FITWLAEYCSTEesDIGSLDAVLSYCNLNLQNNKLLNFRERLLRNAKLKMVCNASILSMSLLRSQETRQFHPCSHELREC 241
Cdd:cd19164 161 VLLRLAELARTT--AGRPLDAVLSYCHYTLQNTTLLAYIPKFLAAAGVKVVLNASPLSMGLLRSQGPPEWHPASPELRAA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  242 ASQAAKYCQEQNVDLADLATRYAISEWVGKGPVVLGVSSMEELKLALDNYEIVKSNGNRL 301
Cdd:cd19164 239 AAKAAEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDELEEAVEAYWSVLAGASEE 298
 
Name Accession Description Interval E-value
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
 2-301 1.29e-165

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: 463.29  E-value: 1.29e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    2 VNEKVNPFDLASVSPLVLGGAILNQQYTDEPESIPLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLRNEFPRDTY 81
Cdd:cd19164   1 PVPKPVALSLAGLPPLIFGAATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIILGRALKALRDEFPRDTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   82 FICTKVGRIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19164  81 FIITKVGRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVLEALKELFKLKDEGKIRNVGISGYPLP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  162 FITWLAEYCSTEesDIGSLDAVLSYCNLNLQNNKLLNFRERLLRNAKLKMVCNASILSMSLLRSQETRQFHPCSHELREC 241
Cdd:cd19164 161 VLLRLAELARTT--AGRPLDAVLSYCHYTLQNTTLLAYIPKFLAAAGVKVVLNASPLSMGLLRSQGPPEWHPASPELRAA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  242 ASQAAKYCQEQNVDLADLATRYAISEWVGKGPVVLGVSSMEELKLALDNYEIVKSNGNRL 301
Cdd:cd19164 239 AAKAAEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDELEEAVEAYWSVLAGASEE 298
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
 17-314 7.93e-43

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: 149.77  E-value: 7.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684     17 LVLGGAILNQQYT--DEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLrnEFPRDTYFICTKVG-RIG 91
Cdd:pfam00248   1 IGLGTWQLGGGWGpiSKEEAL---EALRAALEAGINFIDTAEVYgdGKSEELLGEALKDY--PVKRDKVVIATKVPdGDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684     92 AEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKfpDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEycs 171
Cdd:pfam00248  76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDT--PIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALT--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    172 TEESDIGSLDAVLSYCNLNLQnnkllnfrERLLRNAKLKMV--CNASILSMSLLRSQETRQFHPCSHELR---------- 239
Cdd:pfam00248 151 KGKIPIVAVQVEYNLLRRRQE--------EELLEYCKKNGIplIAYSPLGGGLLTGKYTRDPDKGPGERRrllkkgtpln 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323684    240 -ECASQAAKYCQEQNVDLADLATRYAISEwVGKGPVVLGVSSMEELKlaldnyEIVKSNGNRLSSKDgqlVEYIQK 314
Cdd:pfam00248 223 lEALEALEEIAKEHGVSPAQVALRWALSK-PGVTIPIPGASNPEQLE------DNLGALEFPLSDEE---VARIDE 288
PLN02587 PLN02587
L-galactose dehydrogenase
 14-330 3.88e-41

L-galactose dehydrogenase


Pssm-ID: 178198 [Multi-domain]  Cd Length: 314  Bit Score: 145.69  E-value: 3.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    14 VSPLVLGGAILNQQYTDEPESIPLEDIiKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnEFPRDTYFICTKVGRIG 91
Cdd:PLN02587  11 VSSVGFGASPLGSVFGPVSEEDAIASV-REAFRLGINFFDTSPYYGGtlSEKVLGKALKAL--GIPREKYVVSTKCGRYG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    92 aEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDIL-EALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:PLN02587  88 -EGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVnETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   171 STeesdiGSLDAVLSYCNLNLQNNKLlnfrERLLRNAKLKMV--CNASILSMSLLRSQETRQFHPCSHELRECASQAAKY 248
Cdd:PLN02587 167 PP-----GTVDVILSYCHYSLNDSSL----EDLLPYLKSKGVgvISASPLAMGLLTENGPPEWHPAPPELKSACAAAATH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   249 CQEQNVDLADLATRYAISEwVGKGPVVLGVSSMEELK---LALDNYEIvksngnrlSSKDGQLVEYIqKNIFKEHFNEEW 325
Cdd:PLN02587 238 CKEKGKNISKLALQYSLSN-KDISTTLVGMNSVQQVEenvAAATELET--------SGIDEELLSEV-EAILAPVKNKTW 307


                 ....*
gi 6323684   326 SSGIP 330
Cdd:PLN02587 308 PSGIQ 312
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
 13-161 1.34e-32

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: 123.36  E-value: 1.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGGAILNQQY--TDEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSnlrnEFPRDTYFICTKVG 88
Cdd:COG0667  12 KVSRLGLGTMTFGGPWggVDEAEAI---AILDAALDAGINFFDTADVYGPgrSEELLGEALK----GRPRDDVVIATKVG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323684   89 RI---GAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEF-VKFPDILEALKELRTlknKGVIKNFGISGYPID 161
Cdd:COG0667  85 RRmgpGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPdTPIEETLGALDELVR---EGKIRYIGVSNYSAE 158
 
Name Accession Description Interval E-value
AKR_ARA2 cd19164
D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ARA2 (EC1.1.1.116), also called NAD(+) ...
 2-301 1.29e-165

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: 463.29  E-value: 1.29e-165
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    2 VNEKVNPFDLASVSPLVLGGAILNQQYTDEPESIPLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLRNEFPRDTY 81
Cdd:cd19164   1 PVPKPVALSLAGLPPLIFGAATFSYQYTTDPESIPPVDIVRRALELGIRAFDTSPYYGPSEIILGRALKALRDEFPRDTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   82 FICTKVGRIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19164  81 FIITKVGRYGPDDFDYSPEWIRASVERSLRRLHTDYLDLVYLHDVEFVADEEVLEALKELFKLKDEGKIRNVGISGYPLP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  162 FITWLAEYCSTEesDIGSLDAVLSYCNLNLQNNKLLNFRERLLRNAKLKMVCNASILSMSLLRSQETRQFHPCSHELREC 241
Cdd:cd19164 161 VLLRLAELARTT--AGRPLDAVLSYCHYTLQNTTLLAYIPKFLAAAGVKVVLNASPLSMGLLRSQGPPEWHPASPELRAA 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  242 ASQAAKYCQEQNVDLADLATRYAISEWVGKGPVVLGVSSMEELKLALDNYEIVKSNGNRL 301
Cdd:cd19164 239 AAKAAEYCQAKGTDLADVALRYALREWGGEGPTVVGCSNVDELEEAVEAYWSVLAGASEE 298
AKR_galDH-like cd19153
L-galactose dehydrogenase (L-galDH), D-arabinose 1-dehydrogenase (ARA2) and similar proteins; ...
 2-301 2.78e-160

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: 449.68  E-value: 2.78e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    2 VNEKVNPFdLASVSPLVLGGAILNQQYTDEPESIPLEDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnEFPRD 79
Cdd:cd19153   1 FGETLEIA-LGNVSPVGLGTAALGGVYGDGLEQDEAVAIVAEAFAAGINHFDTSPYYGAesSEAVLGKALAAL--QVPRS 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   80 TYFICTKVGRIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVK-FPDILEALKELRTLKNKGVIKNFGISGY 158
Cdd:cd19153  78 SYTVATKVGRYRDSEFDYSAERVRASVATSLERLHTTYLDVVYLHDIEFVDyDTLVDEALPALRTLKDEGVIKRIGIAGY 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  159 PIDFITWLAEYCSteesdIGSLDAVLSYCNLNLQNNKLLnFRERLLRNAKLKMVCNASILSMSLLRSQETRQFHPCSHEL 238
Cdd:cd19153 158 PLDTLTRATRRCS-----PGSLDAVLSYCHLTLQDARLE-SDAPGLVRGAGPHVINASPLSMGLLTSQGPPPWHPASGEL 231

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684  239 RECASQAAKYCQEQNVDLADLATRYAISEWVGKGPVVLGVSSMEELKLALDNYEIVKSNGNRL 301
Cdd:cd19153 232 RHYAAAADAVCASVEASLPDLALQYSLAAHAGVGTVLLGPSSLAQLRSMLAAVDAVASLGAAI 294
AKR_galDH cd19163
L-galactose dehydrogenase (L-galDH) and similar proteins; L-galDH (EC 1.1.1.316), also called ...
 14-292 4.13e-71

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: 222.81  E-value: 4.13e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQY--TDEPESIpleDIIKYAFSHGINAIDTSPYYG--PSEVLYGRALSNLrnefPRDTYFICTKVGR 89
Cdd:cd19163  13 VSKLGFGASPLGGVFgpVDEEEAI---RTVHEALDSGINYIDTAPWYGqgRSETVLGKALKGI----PRDSYYLATKVGR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   90 IGA---EEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDIL--EALKELRTLKNKGVIKNFGISGYPIDFIT 164
Cdd:cd19163  86 YGLdpdKMFDFSAERITKSVEESLKRLGLDYIDIIQVHDIEFAPSLDQIlnETLPALQKLKEEGKVRFIGITGYPLDVLK 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  165 WLAEYCSTEesdigsLDAVLSYCnlnlqnnkllnfRERLLRNAKLKM----------VCNASILSMSLLRSQETRQFHPC 234
Cdd:cd19163 166 EVLERSPVK------IDTVLSYC------------HYTLNDTSLLELlpffkekgvgVINASPLSMGLLTERGPPDWHPA 227

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323684  235 SHELRECASQAAKYCQEQNVDLADLATRYAISEwvGKGPVVL-GVSSMEELKLALDNYE 292
Cdd:cd19163 228 SPEIKEACAKAAAYCKSRGVDISKLALQFALSN--PDIATTLvGTASPENLRKNLEAAE 284
AKR_AKR15A-like cd19090
AKR15A family of aldo-keto reductase and similar proteins; The AKR15 family includes ...
 15-292 1.61e-50

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: 169.27  E-value: 1.61e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILnqqyTDEPESIPLE---DIIKYAFSHGINAIDTSPYYGPSEVLYGRALsnlrNEFPRDTYFICTKVGRIG 91
Cdd:cd19090   1 SALGLGTAGL----GGVFGGVDDDeavATIRAALDLGINYIDTAPAYGDSEERLGLAL----AELPREPLVLSTKVGRLP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   92 AEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDIL---EALKELRTLKNKGVIKNFGISGYPIDFitwLAE 168
Cdd:cd19090  73 EDTADYSADRVRRSVEESLERLGRDRIDLLMIHDPERVPWVDILapgGALEALLELKEEGLIKHIGLGGGPPDL---LRR 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  169 YCSTeesdiGSLDAVLSYCNLNLQNNKLlnfRERLLRNAK-LKM-VCNASILSMSLL--RSQETRQFHPcSHELRECASQ 244
Cdd:cd19090 150 AIET-----GDFDVVLTANRYTLLDQSA---ADELLPAAArHGVgVINASPLGMGLLagRPPERVRYTY-RWLSPELLDR 220

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6323684  245 AAKY---CQEQNVDLADLATRYAISEwvgkgP----VVLGVSSMEELKlalDNYE 292
Cdd:cd19090 221 AKRLyelCDEHGVPLPALALRFLLRD-----PristVLVGASSPEELE---QNVA 267
Aldo_ket_red pfam00248
Aldo/keto reductase family; This family includes a number of K+ ion channel beta chain ...
 17-314 7.93e-43

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: 149.77  E-value: 7.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684     17 LVLGGAILNQQYT--DEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLrnEFPRDTYFICTKVG-RIG 91
Cdd:pfam00248   1 IGLGTWQLGGGWGpiSKEEAL---EALRAALEAGINFIDTAEVYgdGKSEELLGEALKDY--PVKRDKVVIATKVPdGDG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684     92 AEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKfpDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEycs 171
Cdd:pfam00248  76 PWPSGGSKENIRKSLEESLKRLGTDYIDLYYLHWPDPDT--PIEETWDALEELKKEGKIRAIGVSNFDAEQIEKALT--- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    172 TEESDIGSLDAVLSYCNLNLQnnkllnfrERLLRNAKLKMV--CNASILSMSLLRSQETRQFHPCSHELR---------- 239
Cdd:pfam00248 151 KGKIPIVAVQVEYNLLRRRQE--------EELLEYCKKNGIplIAYSPLGGGLLTGKYTRDPDKGPGERRrllkkgtpln 222

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323684    240 -ECASQAAKYCQEQNVDLADLATRYAISEwVGKGPVVLGVSSMEELKlaldnyEIVKSNGNRLSSKDgqlVEYIQK 314
Cdd:pfam00248 223 lEALEALEEIAKEHGVSPAQVALRWALSK-PGVTIPIPGASNPEQLE------DNLGALEFPLSDEE---VARIDE 288
PLN02587 PLN02587
L-galactose dehydrogenase
 14-330 3.88e-41

L-galactose dehydrogenase


Pssm-ID: 178198 [Multi-domain]  Cd Length: 314  Bit Score: 145.69  E-value: 3.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    14 VSPLVLGGAILNQQYTDEPESIPLEDIiKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnEFPRDTYFICTKVGRIG 91
Cdd:PLN02587  11 VSSVGFGASPLGSVFGPVSEEDAIASV-REAFRLGINFFDTSPYYGGtlSEKVLGKALKAL--GIPREKYVVSTKCGRYG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    92 aEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDIL-EALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:PLN02587  88 -EGFDFSAERVTKSVDESLARLQLDYVDILHCHDIEFGSLDQIVnETIPALQKLKESGKVRFIGITGLPLAIFTYVLDRV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   171 STeesdiGSLDAVLSYCNLNLQNNKLlnfrERLLRNAKLKMV--CNASILSMSLLRSQETRQFHPCSHELRECASQAAKY 248
Cdd:PLN02587 167 PP-----GTVDVILSYCHYSLNDSSL----EDLLPYLKSKGVgvISASPLAMGLLTENGPPEWHPAPPELKSACAAAATH 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   249 CQEQNVDLADLATRYAISEwVGKGPVVLGVSSMEELK---LALDNYEIvksngnrlSSKDGQLVEYIqKNIFKEHFNEEW 325
Cdd:PLN02587 238 CKEKGKNISKLALQYSLSN-KDISTTLVGMNSVQQVEenvAAATELET--------SGIDEELLSEV-EAILAPVKNKTW 307


                 ....*
gi 6323684   326 SSGIP 330
Cdd:PLN02587 308 PSGIQ 312
PdxI COG0667
Pyridoxal reductase PdxI or related oxidoreductase, aldo/keto reductase family [Coenzyme ...
 13-161 1.34e-32

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: 123.36  E-value: 1.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGGAILNQQY--TDEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSnlrnEFPRDTYFICTKVG 88
Cdd:COG0667  12 KVSRLGLGTMTFGGPWggVDEAEAI---AILDAALDAGINFFDTADVYGPgrSEELLGEALK----GRPRDDVVIATKVG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323684   89 RI---GAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEF-VKFPDILEALKELRTlknKGVIKNFGISGYPID 161
Cdd:COG0667  85 RRmgpGPNGRGLSREHIRRAVEASLRRLGTDYIDLYQLHRPDPdTPIEETLGALDELVR---EGKIRYIGVSNYSAE 158
AKR_AKR11C1 cd19086
AKR11C family of aldo-keto reductase (AKR); Bacillus subtilis uncharacterized oxidoreductase ...
 13-156 6.35e-28

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: 108.72  E-value: 6.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGG-AILNQQY--TDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNlrnefPRDTYFICTKV 87
Cdd:cd19086   2 EVSEIGFGTwGLGGDWWgdVDDAEAI---RALRAALDLGINFFDTADVYgdGHSERLLGKALKG-----RRDKVVIATKF 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   88 GRI----GAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLH--DVEFVKFPDILEALKElrtLKNKGVIKNFGIS 156
Cdd:cd19086  74 GNRfdggPERPQDFSPEYIREAVEASLKRLGTDYIDLYQLHnpPDEVLDNDELFEALEK---LKQEGKIRAYGVS 145
AKR_PA4992-like cd19095
Pseudomona aeruginosa PA4992 and similar proteins; Pseudomona aeruginosa PA4992 is the ...
 15-158 1.19e-26

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: 105.78  E-value: 1.19e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILNQQYTDEPESiPLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLRnefpRDTYFICTKVG---RIG 91
Cdd:cd19095   1 SVLGLGTSGIGRVWGVPSEA-EAARLLNTALDLGINLIDTAPAYGRSEERLGRALAGLR----RDDLFIATKVGthgEGG 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323684   92 AEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLH-DVEFVKFPDILEALKELRTlknKGVIKNFGISGY 158
Cdd:cd19095  76 RDRKDFSPAAIRASIERSLRRLGTDYIDLLQLHgPSDDELTGEVLETLEDLKA---AGKVRYIGVSGD 140
AKR_unchar cd19100
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 14-157 3.15e-26

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: 104.10  E-value: 3.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILnqQYTDEPESiplEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNlrnefPRDTYFICTKVGrigae 93
Cdd:cd19100  11 VSRLGFGGGPL--GRLSQEEA---AAIIRRALDLGINYFDTAPSYGDSEEKIGKALKG-----RRDKVFLATKTG----- 75

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323684   94 efNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVK-FPDIL---EALKELRTLKNKGVIKNFGISG 157
Cdd:cd19100  76 --ARDYEGAKRDLERSLKRLGTDYIDLYQLHAVDTEEdLDQVFgpgGALEALLEAKEEGKIRFIGISG 141
AKR_SF cd06660
Aldo-keto reductase (AKR) superfamily; Aldo-keto reductases (AKRs) are a superfamily of ...
 15-161 5.08e-26

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: 103.37  E-value: 5.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILNQQyTDEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLRNefpRDTYFICTKVG---R 89
Cdd:cd06660   1 SRLGLGTMTFGGD-GDEEEAF---ALLDAALEAGGNFFDTADVYGDgrSERLLGRWLKGRGN---RDDVVIATKGGhppG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684   90 IGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLH-DVEFVKFPDILEALKELRtlkNKGVIKNFGISGYPID 161
Cdd:cd06660  74 GDPSRSRLSPEHIRRDLEESLRRLGTDYIDLYYLHrDDPSTPVEETLEALNELV---REGKIRYIGVSNWSAE 143
AKR_unchar cd19097
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 15-296 1.34e-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: 100.68  E-value: 1.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGA-------ILNQQY-TDEPEsipLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLrnefprDTYFICTK 86
Cdd:cd19097   1 SKLALGTAqfgldygIANKSGkPSEKE---AKKILEYALKAGINTLDTAPAYGDSEKVLGKFLKRL------DKFKIITK 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   87 VGRIGAEEFNySRDFVRFSVHRSCERLHTTYLDLVYLHDVE--FVKFPDILEALKElrtLKNKGVIKNFGISGY-PIDFI 163
Cdd:cd19097  72 LPPLKEDKKE-DEAAIEASVEASLKRLKVDSLDGLLLHNPDdlLKHGGKLVEALLE---LKKEGLIRKIGVSVYsPEELE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  164 TWLAEYCsteesdigsLDAV---LSYcnlnlqnnkllnFRERLLRNAKLKMVCNASI------------LSMSLLRSQE- 227
Cdd:cd19097 148 KALESFK---------IDIIqlpFNI------------LDQRFLKSGLLAKLKKKGIeiharsvflqglLLMEPDKLPAk 206

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  228 TRQFHPCSHELREcasqaakYCQEQNVDLADLATRYAIS-EWVGKgpVVLGVSSMEELKLALDNYEIVKS 296
Cdd:cd19097 207 FAPAKPLLKKLHE-------LAKKLGLSPLELALGFVLSlPEIDK--IVVGVDSLEQLKEIIAAFKKPPL 267
AKR_unchar cd19105
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 14-156 2.43e-22

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


Pssm-ID: 381331 [Multi-domain]  Cd Length: 250  Bit Score: 93.80  E-value: 2.43e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAilnqqytdePESIPLEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRnefpRDTYFICTKVGrig 91
Cdd:cd19105  13 VSRLGFGGG---------GLPRESPELLRRALDLGINYFDTAEGYgnGNSEEIIGEALKGLR----RDKVFLATKAS--- 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323684   92 AEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDV----EFVKFPDILEALKElrtLKNKGVIKNFGIS 156
Cdd:cd19105  77 PRLDKKDKAELLKSVEESLKRLQTDYIDIYQLHGVdtpeERLLNEELLEALEK---LKKEGKVRFIGFS 142
AKR_FDH cd19162
D-threo-aldose 1-dehydrogenase (FDH) and similar proteins; FDH (EC1.1.1.122), also called (2S, ...
 40-297 5.74e-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: 90.88  E-value: 5.74e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   40 IIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLrnefPRDTYFICTKVGR---IGAE--------EFNYSRDFVRFSV 106
Cdd:cd19162  24 TLDAAWDAGIRYFDTAPLYglGLSERRLGAALARH----PRAEYVVSTKVGRllePGAAgrpagadrRFDFSADGIRRSI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  107 HRSCERLHTTYLDLVYLHDVEfvkfPDILEALKE----LRTLKNKGVIKNFGISGYPIDFITWLAEycsteesdIGSLDA 182
Cdd:cd19162 100 EASLERLGLDRLDLVFLHDPD----RHLLQALTDafpaLEELRAEGVVGAIGVGVTDWAALLRAAR--------RADVDV 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  183 VLsycnlnlqnnklLNFRERLLRNAKLK-----------MVCNASILSMSLL--RSQETRQFH--PCSHELRECASQAAK 247
Cdd:cd19162 168 VM------------VAGRYTLLDRRAATellplcaakgvAVVAAGVFNSGILatDDPAGDRYDyrPATPEVLARARRLAA 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 6323684  248 YCQEQNVDLADLATRYaisewVGKGP----VVLGVSSMEELklaLDNYEIVKSN 297
Cdd:cd19162 236 VCRRYGVPLPAAALQF-----PLRHPavasVVVGAASPAEL---RDNLALLRTP 281
AKR_AKR11B3 cd19085
Synechococcus sp. aldo-keto reductase (SakR1) and similar proteins; Synechococcus sp. SakR1 is ...
 14-156 1.10e-20

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: 90.34  E-value: 1.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLG----GAILNQQYTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNEfprdtYFICTKV 87
Cdd:cd19085   1 VSRLGLGcwqfGGGYWWGDQDDEESI---ATIHAALDAGINFFDTAEAYgdGHSEEVLGKALKGRRDD-----VVIATKV 72

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   88 griGAEEFNYSRdfVRFSVHRSCERLHTTYLDLVYLH-DVEFVKFPDILEALKELRTlknKGVIKNFGIS 156
Cdd:cd19085  73 ---SPDNLTPED--VRKSCERSLKRLGTDYIDLYQIHwPSSDVPLEETMEALEKLKE---EGKIRAIGVS 134
COG1453 COG1453
Predicted oxidoreductase of the aldo/keto reductase family [General function prediction only];
14-163 1.69e-20

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


Pssm-ID: 441062 [Multi-domain]  Cd Length: 365  Bit Score: 91.03  E-value: 1.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGaiLNQQYTDEPEsipLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNlrnefPRDTYFICTKVGrigae 93
Cdd:COG1453  13 VSVLGFGG--MRLPRKDEEE---AEALIRRAIDNGINYIDTARGYGDSEEFLGKALKG-----PRDKVILATKLP----- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   94 EFNYSRDFVRFSVHRSCERLHTTYLDLVYLHdveFVKFPDILE-------ALKELRTLKNKGVIKNFGIS---------- 156
Cdd:COG1453  78 PWVRDPEDMRKDLEESLKRLQTDYIDLYLIH---GLNTEEDLEkvlkpggALEALEKAKAEGKIRHIGFSthgslevike 154

                       170
                ....*....|
gi 6323684  157 ---GYPIDFI 163
Cdd:COG1453 155 aidTGDFDFV 164
AKR_unchar cd19104
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 14-289 4.32e-20

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


Pssm-ID: 381330 [Multi-domain]  Cd Length: 321  Bit Score: 89.25  E-value: 4.32e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQY--TDEPESIpleDIIKYAFSHGINAIDTSPYYG--PSEVLYGRALSNLRNEFprdtyFICTKVgR 89
Cdd:cd19104  12 VSELTFGGGGIGGLMgrTTREEQI---AAVRRALDLGINFFDTAPSYGdgKSEENLGRALKGLPAGP-----YITTKV-R 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   90 IGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHD----------VEFVKFPDIL---EALKELRTLKNKGVIKNFGIS 156
Cdd:cd19104  83 LDPDDLGDIGGQIERSVEKSLKRLKRDSVDLLQLHNrigderdkpvGGTLSTTDVLglgGVADAFERLRSEGKIRFIGIT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  157 GypidfitwLAEYCSTEES-DIGSLDAVL--------SYCNLNLQNNKLLNFRErLLRNAKLK--MVCNASILSMSLLRS 225
Cdd:cd19104 163 G--------LGNPPAIRELlDSGKFDAVQvyynllnpSAAEARPRGWSAQDYGG-IIDAAAEHgvGVMGIRVLAAGALTT 233

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  226 QETRQFHP----CSHELRECASQAA--KYCQEQNVDLADLATRYAISEwVGKGPVVLGVSSMEELKLALD 289
Cdd:cd19104 234 SLDRGREApptsDSDVAIDFRRAAAfrALAREWGETLAQLAHRFALSN-PGVSTVLVGVKNREELEEAVA 302
AKR_AKR15A1 cd19161
Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD) and similar proteins; Microbacterium ...
 15-155 7.08e-20

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: 88.15  E-value: 7.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILNQQYTDEPESiPLEDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnefPRDTYFICTKVGRI-- 90
Cdd:cd19161   1 SELGLGTAGLGNLYTAVSNA-DADATLDAAWDSGIRYFDTAPMYGHglAEHRLGDFLREK----PRDEFVLSTKVGRLlk 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   91 ------------------GAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDV---------EFVKFPDILE-ALKELR 142
Cdd:cd19161  76 paregsvpdpngfvdplpFEIVYDYSYDGIMRSFEDSLQRLGLNRIDILYVHDIgvythgdrkERHHFAQLMSgGFKALE 155

                       170
                ....*....|...
gi 6323684  143 TLKNKGVIKNFGI 155
Cdd:cd19161 156 ELKKAGVIKAFGL 168
AKR_AKR11B1-like cd19084
AKR11B1/AKR11B2 subfamily of aldo-keto reductase (AKR); Bacillus subtilis YhdN, also called ...
 14-170 8.08e-20

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: 87.97  E-value: 8.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAIL---NQQYTDEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnefpRDTYFICTKVG 88
Cdd:cd19084   4 VSRIGLGTWAIggtWWGEVDDQESI---EAIKAAIDLGINFFDTAPVYGFghSEEILGKALKGR-----RDDVVIATKCG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   89 ----RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHdvefvkFPD----ILEALKELRTLKNKGVIKNFGISGYPI 160
Cdd:cd19084  76 lrwdGGKGVTKDLSPESIRKEVEQSLRRLQTDYIDLYQIH------WPDpntpIEETAEALEKLKKEGKIRYIGVSNFSV 149

                       170
                ....*....|
gi 6323684  161 DFITWLAEYC 170
Cdd:cd19084 150 EQLEEARKYG 159
AKR_AKR15A cd19152
AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum ...
 15-155 2.71e-19

AKR15A family of aldo-keto reductase; The AKR15 family includes Microbacterium luteolum pyridoxal 4-dehydrogenase (PLD), Pseudomonas sp. D-threo-aldose 1-dehydrogenase (FDH), and similar proteins. PLD (EC1.1.1.107) catalyzes irreversible oxidation of pyridoxal. FDH(EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose. FDH (EC1.1.1.122), also called (2S,3R)-aldose dehydrogenase, or L-fucose dehydrogenase, catalyzes the oxidation of L-fucose to L-fuconolactone in the presence of NADP(+). It is also active against L-galactose, and to a much lesser degree, D-arabinose.


Pssm-ID: 381378 [Multi-domain]  Cd Length: 308  Bit Score: 86.51  E-value: 2.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILNQQYTDEPESIPLEDIIKyAFSHGINAIDTSPYYGP--SEVLYGRALSnlrnEFPRDTYFICTKVGRI-- 90
Cdd:cd19152   1 PKLGFGTAPLGNLYEAVSDEEAKATLVA-AWDLGIRYFDTAPWYGAglSEERLGAALR----ELGREDYVISTKVGRLlv 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   91 ---GAEE---------------FNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVE---------FVKFPDILEALKELRT 143
Cdd:cd19152  76 plqEVEPtfepgfwnplpfdavFDYSYDGILRSIEDSLQRLGLSRIDLLSIHDPDedlagaesdEHFAQAIKGAFRALEE 155

                       170
                ....*....|..
gi 6323684  144 LKNKGVIKNFGI 155
Cdd:cd19152 156 LREEGVIKAIGL 167
AKR_Fe-S_oxidoreductase cd19096
Fe-S oxidoreductase and similar proteins; The family includes a group of uncharacterized Fe-S ...
 30-169 9.48e-19

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


Pssm-ID: 381322 [Multi-domain]  Cd Length: 255  Bit Score: 84.15  E-value: 9.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   30 DEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSnlrnEFPRDTYFICTKvgrIGAEEFNYSRDFVRFsVH 107
Cdd:cd19096  19 DEEKAI---EMIRYAIDAGINYFDTAYGYGGgkSEEILGEALK----EGPREKFYLATK---LPPWSVKSAEDFRRI-LE 87

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323684  108 RSCERLHTTYLDLVYLHDVEFVKFPDILE---ALKELRTLKNKGVIKNFGIS--GYPIDFITWLAEY 169
Cdd:cd19096  88 ESLKRLGVDYIDFYLLHGLNSPEWLEKARkggLLEFLEKAKKEGLIRHIGFSfhDSPELLKEILDSY 154
AKR_AKR3F1-like cd19072
Thermotoga maritime Tm1743, Escherichia coli YeaE and similar proteins; Thermotoga maritime ...
 13-161 5.83e-18

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: 82.28  E-value: 5.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLG----GAILNQQYTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNlrneFPRDTYFICTK 86
Cdd:cd19072   3 EVPVLGLGtwgiGGGMSKDYSDDKKAI---EALRYAIELGINLIDTAEMYggGHAEELVGKAIKG----FDREDLFITTK 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   87 VGRIgaeefNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFvkFPDILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19072  76 VSPD-----HLKYDDVIKAAKESLKRLGTDYIDLYLIHWPNP--SIPIEETLRAMEELVEEGKIRYIGVSNFSLE 143
AKR_unchar cd19099
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 38-156 1.30e-17

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


Pssm-ID: 381325 [Multi-domain]  Cd Length: 316  Bit Score: 81.98  E-value: 1.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNL--RNEFPRDTYFICTKVG------------------------- 88
Cdd:cd19099  24 REALKAALDSGINVIDTAINYrgGRSERLIGKALRELieKGGIKRDEVVIVTKAGyipgdgdeplrplkyleeklgrgli 103

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323684   89 ---RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVE-------FVKFPDILE-ALKELRTLKNKGVIKNFGIS 156
Cdd:cd19099 104 dvaDSAGLRHCISPAYLEDQIERSLKRLGLDTIDLYLLHNPEeqllelgEEEFYDRLEeAFEALEEAVAEGKIRYYGIS 182
AKR_BsYcsN_EcYdhF-like cd19092
Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins; Bacillus subtilis YcsN and ...
 13-171 1.55e-17

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: 81.45  E-value: 1.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGG-AILNQQYTDEPesipLEDIIKYAFSHGINAIDTSPYYG--PSEVLYGRALS---NLRNEFprdtyFICTK 86
Cdd:cd19092   5 EVSRLVLGCmRLADWGESAEE----LLSLIEAALELGITTFDHADIYGggKCEELFGEALAlnpGLREKI-----EIQTK 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   87 VG-RIGAEE-------FNYSRDFVRFSVHRSCERLHTTYLDLVYLHDvefvkfPDIL----EALKELRTLKNKGVIKNFG 154
Cdd:cd19092  76 CGiRLGDDPrpgrikhYDTSKEHILASVEGSLKRLGTDYLDLLLLHR------PDPLmdpeEVAEAFDELVKSGKVRYFG 149

                       170
                ....*....|....*..
gi 6323684  155 ISGYPIDFITWLAEYCS 171
Cdd:cd19092 150 VSNFTPSQIELLQSYLD 166
AKR_AKR13B1 cd19088
AKR13B family of aldo-keto reductase (AKR); Xylella fastidiosa phenylacetaldehyde ...
 14-183 1.74e-17

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: 80.72  E-value: 1.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYT-----DEPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNlrneFPRDTYfICTK 86
Cdd:cd19088   1 VSRLGYGAMRLTGPGIwgppaDREEAI---AVLRRALELGVNFIDTADSYGPdvNERLIAEALHP----YPDDVV-IATK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   87 VG--RIGAEEF--NYSRDFVRFSVHRSCERLHTTYLDLVYLHDVE-FVKFPDILEALKELRtlkNKGVIKNFGISGYPID 161
Cdd:cd19088  73 GGlvRTGPGWWgpDGSPEYLRQAVEASLRRLGLDRIDLYQLHRIDpKVPFEEQLGALAELQ---DEGLIRHIGLSNVTVA 149

                       170       180
                ....*....|....*....|..
gi 6323684  162 FItwlaeycsTEESDIGSLDAV 183
Cdd:cd19088 150 QI--------EEARAIVRIVSV 163
AKR_AKR11B2 cd19149
Escherichia coli NADH-specific methylglyoxal reductase (YdjG) and similar proteins; ...
 14-183 4.03e-17

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: 80.39  E-value: 4.03e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLG----GAILNQQYTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNEfprdtYFICTKV 87
Cdd:cd19149  11 ASVIGLGtwaiGGGPWWGGSDDNESI---RTIHAALDLGINLIDTAPAYgfGHSEEIVGKAIKGRRDK-----VVLATKC 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   88 G---RIGAEEFNYSRDFV-----------RFSVHRSCERLHTTYLDLVYLH--DVEfvkFPdILEALKELRTLKNKGVIK 151
Cdd:cd19149  83 GlrwDREGGSFFFVRDGVtvyknlspesiREEVEQSLKRLGTDYIDLYQTHwqDVE---TP-IEETMEALEELKRQGKIR 158

                       170       180       190
                ....*....|....*....|....*....|..
gi 6323684  152 NFGISGYPIDFItwlAEYCSteesdIGSLDAV 183
Cdd:cd19149 159 AIGASNVSVEQI---KEYVK-----AGQLDII 182
AKR_EcYajO-like cd19079
Escherichia coli YajO and similar proteins; Escherichia coli YajO is the prototype of this ...
 14-141 3.36e-16

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: 78.01  E-value: 3.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLG----GAILNQQYT-DEPESIPledIIKYAFSHGINAIDTSPYY--GPSEVLYGRAlsnLRNEFPRDTYFICTK 86
Cdd:cd19079  12 VSRLCLGcmsfGDPKWRPWVlDEEESRP---IIKRALDLGINFFDTANVYsgGASEEILGRA---LKEFAPRDEVVIATK 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   87 VGRIGAEEFN---YSRDFVRFSVHRSCERLHTTYLDLVYLH--DVEfVKFPDILEALKEL 141
Cdd:cd19079  86 VYFPMGDGPNgrgLSRKHIMAEVDASLKRLGTDYIDLYQIHrwDYE-TPIEETLEALHDV 144
AKR_unchar cd19102
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 30-161 4.06e-16

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: 77.33  E-value: 4.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   30 DEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLrnefpRDTYFICTKVGRIGAEEFNYSRDFVRFSVH 107
Cdd:cd19102  24 DDRDSI---AAIRAALDLGINWIDTAAVYglGHSEEVVGRALKGL-----RDRPIVATKCGLLWDEEGRIRRSLKPASIR 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  108 RSCE----RLHTTYLDLVYLH--DVEfvkfPDILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19102  96 AECEaslrRLGVDVIDLYQIHwpDPD----EPIEEAWGALAELKEEGKVRAIGVSNFSVD 151
AKR_AKR11A1_11D1 cd19083
AKR11A and AKR11D families of aldo-keto reductase (AKR); Bacillus subtilis aldo-keto ...
 39-161 6.39e-16

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: 77.07  E-value: 6.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   39 DIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSnlrnEFPRDTYFICTKVGRI---GAEEFNYSRDFVRFSVHRSCERL 113
Cdd:cd19083  37 DLVREALDNGVNLLDTAFIYGLgrSEELVGEVLK----EYNRNEVVIATKGAHKfggDGSVLNNSPEFLRSAVEKSLKRL 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6323684  114 HTTYLDLVYLHdvefvkFPD----ILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19083 113 NTDYIDLYYIH------FPDgetpKAEAVGALQELKDEGKIRAIGVSNFSLE 158
AKR_unchar cd19101
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 37-154 1.73e-15

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


Pssm-ID: 381327 [Multi-domain]  Cd Length: 304  Bit Score: 75.71  E-value: 1.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   37 LEDIIKYAFShGINAIDTSPYYGPSEVLYGRALSNLRNEFPRDTYF-ICTK-VGRIGaeEFNYSRDFVRFSVHRSCERLH 114
Cdd:cd19101  26 VRAMAAYVDA-GLTTFDCADIYGPAEELIGEFRKRLRRERDAADDVqIHTKwVPDPG--ELTMTRAYVEAAIDRSLKRLG 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6323684  115 TTYLDLVYLH--DVEfvkFPDILEALKELRTLKNKGVIKNFG 154
Cdd:cd19101 103 VDRLDLVQFHwwDYS---DPGYLDAAKHLAELQEEGKIRHLG 141
AKR_AKR1-5-like cd19071
AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases ...
 38-170 2.81e-15

AKR1/2/3/4/5 family of aldo-keto reductase (AKR) and similar proteins; Aldo-keto reductases (AKRs) are a superfamily of soluble NAD(P)(H) oxidoreductases whose chief purpose is to reduce aldehydes and ketones to primary and secondary alcohols. The family includes AKR1A/B/C/D/E/G/I, AKR2A/B/C/D/E, AKR3A/B/C/D/E/G, AKR4A/B/C, AKR5A/B/C/D/E/F/G/H, and similar proteins.


Pssm-ID: 381297 [Multi-domain]  Cd Length: 251  Bit Score: 74.44  E-value: 2.81e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNLRneFPRDTYFICTKVGRIgaeefNYSRDFVRFSVHRSCERLHTTY 117
Cdd:cd19071  17 AEAVLAALEAGYRHIDTAAAYG-NEAEVGEAIRESG--VPREELFITTKLWPT-----DHGYERVREALEESLKDLGLDY 88

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323684  118 LDLVYLH----DVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19071  89 LDLYLIHwpvpGKEGGSKEARLETWRALEELVDEGLVRSIGVSNFNVEHLEELLAAA 145
AKR_AKR11B1 cd19148
Bacillus subtilis aldo-keto reductase YhdN and similar proteins; Bacillus subtilis YhdN, also ...
 29-158 1.09e-14

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: 73.50  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   29 TDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRnefPRDTYFICTKVGR--IGAEEF--NYSRDFV 102
Cdd:cd19148  22 TDEKEAI---ETIHKALDLGINLIDTAPVYgfGLSEEIVGKALKEYG---KRDRVVIATKVGLewDEGGEVvrNSSPARI 95

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  103 RFSVHRSCERLHTTYLDLVYLHdvefvkFPDILEALKE----LRTLKNKGVIKNFGISGY 158
Cdd:cd19148  96 RKEVEDSLRRLQTDYIDLYQVH------WPDPLVPIEEtaeaLKELLDEGKIRAIGVSNF 149
AKR_AKR13A_13D cd19076
AKR13A and AKR13D families of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto ...
 13-156 2.29e-14

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: 72.63  E-value: 2.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGGAILNQQY--TDEPESIPLediIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNlrnefPRDTYFICTKVG 88
Cdd:cd19076  11 EVSALGLGCMGMSAFYgpADEEESIAT---LHRALELGVTFLDTADMYGPgtNEELLGKALKD-----RRDEVVIATKFG 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   89 --RIGAEEFNY---SRDFVRFSVHRSCERLHTTYLDLVYLHDVEfVKFP--DILEALKELRTlknKGVIKNFGIS 156
Cdd:cd19076  83 ivRDPGSGFRGvdgRPEYVRAACEASLKRLGTDVIDLYYQHRVD-PNVPieETVGAMAELVE---EGKVRYIGLS 153
AKR_AKR3C2-3 cd19120
Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis ...
 36-171 2.51e-14

Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase, Candida parapsilosis NADPH-dependent conjugated polyketone reductase C2 (CPR), and similar proteins; Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase (EC 1.1.1.190/EC 1.1.1.191) and Candida parapsilosis NADPH-dependent CPR (EC 1.1.1.358/EC 1.1.1.168) are founding members of aldo-keto reductase family 3 member C2 (AKR3C2) and C3 (AKR3C3), respectively. Saccharomyces pombe NAD/NADP-dependent indole-3-acetaldehyde reductase catalyzes the conversion from (Indol-3-yl)ethanol to (indol-3-yl)acetaldehyde in a NAD/NADP-dependent manner. CPR, also called 2-dehydropantolactone reductase, or 2-dehydropantolactone reductase (A-specific), or ketopantoyl-lactone reductase, acts as a NADPH-dependent conjugated polyketone reductase with broad substrate specificity and strict stereospecificity. It reduces ketopantoyl lactone and isatin.


Pssm-ID: 381346 [Multi-domain]  Cd Length: 269  Bit Score: 71.88  E-value: 2.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   36 PLEDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVGRIGAEefnysrdfVRFSVHRSCERLHT 115
Cdd:cd19120  26 DLVDSVKLALKAGFRHIDTAEMYG-NEKEVGEALK--ESGVPREDLFITTKVSPGIKD--------PREALRKSLAKLGV 94

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6323684  116 TYLDLVYLHDVEFVKF--PDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCS 171
Cdd:cd19120  95 DYVDLYLIHSPFFAKEggPTLAEAWAELEALKDAGLVRSIGVSNFRIEDLEELLDTAK 152
Aldo_ket_red_shaker-like cd19074
Shaker potassium channel beta subunit family and similar proteins; This family includes ...
 14-159 2.74e-14

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: 72.24  E-value: 2.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSnlrnEFPRDTYFICTKV-GRI 90
Cdd:cd19074   4 VSELSLGTWLTFGGQVDDEDAK---ACVRKAYDLGINFFDTADVYaaGQAEEVLGKALK----GWPRESYVISTKVfWPT 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684   91 GAEEFNY--SRDFVRFSVHRSCERLHTTYLDLVYLH--DVEfvkfPDILEALKELRTLKNKGVIKNFGISGYP 159
Cdd:cd19074  77 GPGPNDRglSRKHIFESIHASLKRLQLDYVDIYYCHryDPE----TPLEETVRAMDDLIRQGKILYWGTSEWS 145
AKR_AKR13D1 cd19145
AKR13D family of aldo-keto reductase (AKR); Rauvolfia serpentina PR is a founding member of ...
 14-156 4.10e-14

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: 71.69  E-value: 4.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYTD---EPESIpleDIIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLrnefPRDTYFICTKVG 88
Cdd:cd19145  12 VSAQGLGCMGLSGDYGApkpEEEGI---ALIHHAFNSGVTFLDTSDIYGPntNEVLLGKALKDG----PREKVQLATKFG 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684   89 RIGAE----EFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEfVKFPdILEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19145  85 IHEIGgsgvEVRGDPAYVRAACEASLKRLDVDYIDLYYQHRID-TTVP-IEITMGELKKLVEEGKIKYIGLS 154
AKR_PsAKR cd19091
Polaromonas Sp. aldo-keto reductase and similar proteins; The prototype of this family is an ...
 29-159 1.09e-13

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: 70.72  E-value: 1.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   29 TDEPESiplEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNEFprdtyFICTKV-GRIGA--EEFNYSRDFVR 103
Cdd:cd19091  36 VDQEEA---DRLVDIALDAGINFFDTADVYseGESEEILGKALKGRRDDV-----LIATKVrGRMGEgpNDVGLSRHHII 107

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323684  104 FSVHRSCERLHTTYLDLVYLHDVEFVKfPdILEALKELRTLKNKGVIKNFGISGYP 159
Cdd:cd19091 108 RAVEASLKRLGTDYIDLYQLHGFDALT-P-LEETLRALDDLVRQGKVRYIGVSNFS 161
AKR_Tas-like cd19094
Escherichia coli Tas protein and similar proteins; Escherichia coli Tas protein is the ...
 14-294 1.39e-13

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: 70.29  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYTdEPESIpleDIIKYAFSHGINAIDTSPYYG--PSEVLYGRA---LSN-LRNEFPRDTYFICTKV 87
Cdd:cd19094   1 VSEICLGTMTWGEQNT-EAEAH---EQLDYAFDEGVNFIDTAEMYPvpPSPETQGRTeeiIGSwLKKKGNRDKVVLATKV 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   88 -GR------IGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLH-------------------DVEFVKFPDILEALKEl 141
Cdd:cd19094  77 aGPgegitwPRGGGTRLDRENIREAVEGSLKRLGTDYIDLYQLHwpdrytplfgggyytepseEEDSVSFEEQLEALGE- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  142 rtLKNKGVIKNFGIS-----------------GYP-IDFIT------------WLAEYCSTEesDIGSL------DAVLS 185
Cdd:cd19094 156 --LVKAGKIRHIGLSnetpwgvmkflelaeqlGLPrIVSIQnpysllnrnfeeGLAEACHRE--NVGLLaysplaGGVLT 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  186 --YCnlnlqnnkllnfrERLLRNAKLKmvcnasilsMSLLRSQETRQFHPCSHE-LRECASQAAKYcqeqNVDLADLATR 262
Cdd:cd19094 232 gkYL-------------DGAARPEGGR---------LNLFPGYMARYRSPQALEaVAEYVKLARKH----GLSPAQLALA 285

                       330       340       350
                ....*....|....*....|....*....|...
gi 6323684  263 YAIS-EWVGKgpVVLGVSSMEELKLALDNYEIV 294
Cdd:cd19094 286 WVRSrPFVTS--TIIGATTLEQLKENIDAFDVP 316
ARA1 COG0656
Aldo/keto reductase, related to diketogulonate reductase [Secondary metabolites biosynthesis, ...
 38-170 1.69e-13

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


Pssm-ID: 440421 [Multi-domain]  Cd Length: 259  Bit Score: 69.31  E-value: 1.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVgrigaEEFNYSRDFVRFSVHRSCERLHTTY 117
Cdd:COG0656  21 AAAVRTALEAGYRHIDTAAMYG-NEEGVGEAIA--ASGVPREELFVTTKV-----WNDNHGYDDTLAAFEESLERLGLDY 92

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323684  118 LDLVYLHdvefvkFP---DILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:COG0656  93 LDLYLIH------WPgpgPYVETWRALEELYEEGLIRAIGVSNFDPEHLEELLAET 142
AKR_AKR13C1_2 cd19078
AKR13C family of aldo-keto reductase (AKR); The AKR13C family includes Helicobacter pyroli ...
 14-156 1.78e-13

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: 69.95  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQY---TDEPESIPLediIKYAFSHGINAIDTSPYYGP--SEVLYGRALSNLRNEFprdtyFICTKVG 88
Cdd:cd19078   4 VSAIGLGCMGMSHGYgppPDKEEMIEL---IRKAVELGITFFDTAEVYGPytNEELVGEALKPFRDQV-----VIATKFG 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   89 ------RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVE-FVKFPDILEALKElrtLKNKGVIKNFGIS 156
Cdd:cd19078  76 fkidggKPGPLGLDSRPEHIRKAVEGSLKRLQTDYIDLYYQHRVDpNVPIEEVAGTMKE---LIKEGKIRHWGLS 147
AKR_AtPLR-like cd19093
Arabidopsis thaliana pyridoxal reductase (PLR) and similar proteins; Arabidopsis thaliana PLR ...
 14-161 2.14e-13

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: 69.56  E-value: 2.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGG-AILNQQYTDEPESIP--LEDIIKYAFSHGINAIDTSPYYG--PSEVLYGRALSNLRnefPRDTYFICTKVg 88
Cdd:cd19093   2 VSPLGLGTwQWGDRLWWGYGEYGDedLQAAFDAALEAGVNLFDTAEVYGtgRSERLLGRFLKELG---DRDEVVIATKF- 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   89 rIGAEEFNYSRDFVRfSVHRSCERLHTTYLDLVYLHDVEFVKFPD--ILEALKElrtLKNKGVIKNFGISGYPID 161
Cdd:cd19093  78 -APLPWRLTRRSVVK-ALKASLERLGLDSIDLYQLHWPGPWYSQIeaLMDGLAD---AVEEGLVRAVGVSNYSAD 147
AKR_AKR3F2_3 cd19073
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB), Sinorhizobium meliloti ...
 39-170 2.42e-13

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: 68.45  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   39 DIIKYAFSHGINAIDTSPYYGPSEVLyGRALSNLRneFPRDTYFICTKVGRIgaeefNYSRDFVRFSVHRSCERLHTTYL 118
Cdd:cd19073  18 NAVKEALELGYRHIDTAEIYNNEAEV-GEAIAESG--VPREDLFITTKVWRD-----HLRPEDLKKSVDRSLEKLGTDYV 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6323684  119 DLVYLHDVEF-VKFPDILEALKElrtLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19073  90 DLLLIHWPNPtVPLEETLGALKE---LKEAGKVKSIGVSNFTIELLEEALDIS 139
AKR_AKR7A1-5 cd19075
AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1 ...
 17-170 7.83e-13

AKR7A family of aldo-keto reductase (AKR); Aflatoxin B1 aldehyde reductase member 1/3 (AKR7A1/AKR7A3/AFAR) from Rattus norvegicus, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR1/AFAR) and aflatoxin B1 aldehyde reductase member 3 (AKR7A3/AFAR2) from Homo sapiens, aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AFAR2) from Rattus norvegicus, and aflatoxin B1 aldehyde reductase member 2 (AKR7A2/AKR7A5/AFAR) from Mus musculus, are founding members of aldo-keto reductase family 7 member A1-5 (AKR7A1-5), respectively. AKR7A2 (EC 1.1.1.n11), also called AFB1 aldehyde reductase 1, or AFB1-AR 1, or aldoketoreductase 7, or succinic semialdehyde reductase, or SSA reductase, catalyzes the NADPH-dependent reduction of succinic semialdehyde to gamma-hydroxybutyrate (GHB). It has NADPH-dependent aldehyde reductase activity towards 2-carboxybenzaldehyde, 2-nitrobenzaldehyde and pyridine-2-aldehyde (in vitro). AKR7A2, AKR7A3 (also called AFB1 aldehyde reductase 2 or AFB1-AR 2), and AKR7A4 (also called AFB1 aldehyde reductase 3, or AFB1-AR 3, or aldoketoreductase 7-like), may be involved in protection of liver against the toxic and carcinogenic effects of aflatoxin B1 (AFB1), a potent hepatocarcinogen. They can reduce the dialdehyde protein-binding form of AFB1 to the non-binding AFB1 dialcohol.


Pssm-ID: 381301 [Multi-domain]  Cd Length: 304  Bit Score: 67.97  E-value: 7.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   17 LVLGGAILNQQ--YTDEPESIPLEDIIKyafSHGINAIDTSPYYGP--SEVLYGRALSNLRnefprdTYFICTKVgrIGA 92
Cdd:cd19075   3 IILGTMTFGSQgrFTTAEAAAELLDAFL---ERGHTEIDTARVYPDgtSEELLGELGLGER------GFKIDTKA--NPG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   93 EEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHdvefvkFPD----ILEALKELRTLKNKGVIKNFGISGYPIDFITWLAE 168
Cdd:cd19075  72 VGGGLSPENVRKQLETSLKRLKVDKVDVFYLH------APDrstpLEETLAAIDELYKEGKFKEFGLSNYSAWEVAEIVE 145


                ..
gi 6323684  169 YC 170
Cdd:cd19075 146 IC 147
AKR_AKR3F3 cd19140
Sinorhizobium meliloti isatin reductase and similar proteins; Sinorhizobium meliloti isatin ...
 36-160 8.36e-13

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: 67.28  E-value: 8.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   36 PLEDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVGrigaeEFNYSRDFVRFSVHRSCERLHT 115
Cdd:cd19140  22 ECTRAVEHALELGYRHIDTAQMYG-NEAQVGEAIA--ASGVPRDELFLTTKVW-----PDNYSPDDFLASVEESLRKLRT 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 6323684  116 TYLDLVYLH----DVefvkfpDILEALKELRTLKNKGVIKNFGISGYPI 160
Cdd:cd19140  94 DYVDLLLLHwpnkDV------PLAETLGALNEAQEAGLARHIGVSNFTV 136
AKR_AKR9C1 cd19081
AKR9C family of aldo-keto reductase (AKR); Haloferax volcanii aldo-keto reductase is a ...
 13-159 9.65e-13

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: 67.62  E-value: 9.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   13 SVSPLVLGGAILNQQyTDEPESIPLEDiikyAF-SHGINAIDTSPYY---------GPSEVLYGRALSNLRNefpRDTYF 82
Cdd:cd19081   8 SVSPLCLGTMVFGWT-ADEETSFALLD----AFvDAGGNFIDTADVYsawvpgnagGESETIIGRWLKSRGK---RDRVV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   83 ICTKVGR-IGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHdvefvkFPD----ILEALKELRTLKNKGVIKNFGISG 157
Cdd:cd19081  80 IATKVGFpMGPNGPGLSRKHIRRAVEASLRRLQTDYIDLYQAH------WDDpatpLEETLGALNDLIRQGKVRYIGASN 153


                ..
gi 6323684  158 YP 159
Cdd:cd19081 154 YS 155
AKR_AKR13A1 cd19144
AKR13A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe aldo-keto reductase YakC ...
 44-156 7.69e-12

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: 65.16  E-value: 7.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   44 AFSHGINAIDTSPYYGPSEVLYGRALsnLRNEFPRDTYFICTKVG-----RIGAEEFNYSRDFVRFSVHRSCERLHTTYL 118
Cdd:cd19144  43 AFELGCTFWDTADIYGDSEELIGRWF--KQNPGKREKIFLATKFGieknvETGEYSVDGSPEYVKKACETSLKRLGVDYI 120

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6323684  119 DLVYLHDVEfVKFPdILEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19144 121 DLYYQHRVD-GKTP-IEKTVAAMAELVQEGKIKHIGLS 156
AKR_YeaE cd19138
Escherichia coli YeaE and similar proteins; Escherichia coli YeaE is the prototype of this ...
 10-156 1.18e-11

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: 64.19  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   10 DLASVSPLVLGGAILNQQYTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNlrnefPRDTYFICTKV 87
Cdd:cd19138   7 DGTKVPALGQGTWYMGEDPAKRAQEI---EALRAGIDLGMTLIDTAEMYgdGGSEELVGEAIRG-----RRDKVFLVSKV 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6323684   88 grigaEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDILEALKElrtLKNKGVIKNFGIS 156
Cdd:cd19138  79 -----LPSNASRQGTVRACERSLRRLGTDYLDLYLLHWRGGVPLAETVAAMEE---LKKEGKIRAWGVS 139
AKR_AKR10A1_2 cd19082
AKR10A family of aldo-keto reductase (AKR); Streptomyces bluensis aldo-keto reductase (BlmT) ...
 15-156 1.86e-11

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: 63.73  E-value: 1.86e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   15 SPLVLGGAILnQQYTDEPESIPLEDiikYAFSHGINAIDTSPYY------GPSEVLYGRALSNLRNefpRDTYFICTKVG 88
Cdd:cd19082   1 SRIVLGTADF-GTRIDEEEAFALLD---AFVELGGNFIDTARVYgdwverGASERVIGEWLKSRGN---RDKVVIATKGG 73

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684   89 RIGAEEFNYSR---DFVRFSVHRSCERLHTTYLDLVYLH-DVEFVKFPDILEALKElrtLKNKGVIKNFGIS 156
Cdd:cd19082  74 HPDLEDMSRSRlspEDIRADLEESLERLGTDYIDLYFLHrDDPSVPVGEIVDTLNE---LVRAGKIRAFGAS 142
AKR_AKR12A1_B1_C1 cd19087
AKR12A, AKR12B, AKR12C families of aldo-keto reductase (AKR); Streptomyces fradiae TylCII, ...
 14-159 1.31e-10

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: 61.43  E-value: 1.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQyTDEPESIpleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNEFprdtyFICTKVGRIG 91
Cdd:cd19087  13 VSRLCLGTMNFGGR-TDEETSF---AIMDRALDAGINFFDTADVYggGRSEEIIGRWIAGRRDDI-----VLATKVFGPM 83

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684   92 AEEFN---YSRDFVRFSVHRSCERLHTTYLDLVYLHDV-EFVKFPDILEALKELRTlknKGVIKNFGISGYP 159
Cdd:cd19087  84 GDDPNdrgLSRRHIRRAVEASLRRLQTDYIDLYQMHHFdRDTPLEETLRALDDLVR---QGKIRYIGVSNFA 152
AKR_unchar cd19752
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 29-165 2.04e-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: 381391 [Multi-domain]  Cd Length: 291  Bit Score: 60.81  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   29 TDEPESIPLEDIIkyaFSHGINAIDTSPYY---------GPSEVLYGRALSNLRNefpRDTYFICTKVG----RIGAEEF 95
Cdd:cd19752  14 TDEETSFAILDRY---VAAGGNFLDTANNYafwteggvgGESERLIGRWLKDRGN---RDDVVIATKVGagprDPDGGPE 87

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6323684   96 NY---SRDFVRFSVHRSCERLHTTYLDLVYLHdVEFVKFP--DILEALKElrtLKNKGVIKNFGISGYPidfiTW 165
Cdd:cd19752  88 SPeglSAETIEQEIDKSLRRLGTDYIDLYYAH-VDDRDTPleETLEAFNE---LVKAGKVRAIGASNFA----AW 154
AKR_AKR3F1 cd19137
Thermotoga maritime Tm1743 and similar proteins; Thermotoga maritime Tm1743 is a founding ...
 21-172 7.38e-10

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: 58.74  E-value: 7.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   21 GAILNQQYTDEPESIPLediIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNlrneFPRDTYFICTKVGRIgaeefNYS 98
Cdd:cd19137  15 GGFLTPDYSRDEEMVEL---LKTAIELGYTHIDTAEMYggGHTEELVGKAIKD----FPREDLFIVTKVWPT-----NLR 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323684   99 RDFVRFSVHRSCERLHTTYLDLVYLHdvefVKFPDIL--EALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCST 172
Cdd:cd19137  83 YDDLLRSLQNSLRRLDTDYIDLYLIH----WPNPNIPleETLSAMAEGVRQGLIRYIGVSNFNRRLLEEAISKSQT 154
AKR_AKR6B1 cd19142
AKR6B family of aldo-keto reductase (AKR); Drosophila melanogaster Hk protein is a founding ...
 37-124 1.47e-09

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: 58.24  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   37 LEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSnlRNEFPRDTYFICTKV-GRIGAEEFNYSRDFVRFSVHRSCERL 113
Cdd:cd19142  33 AEEIVTLAYENGINYFDTSDAFtsGQAETELGRILK--KKGWKRSSYIVSTKIyWSYGSEERGLSRKHIIESVRASLRRL 110

                        90
                ....*....|.
gi 6323684  114 HTTYLDLVYLH 124
Cdd:cd19142 111 QLDYIDIVIIH 121
AKR_DrGR-like cd19136
Danio rerio glyoxal reductase-like (GR-like) protein and similar proteins; Danio rerio GR-like ...
 44-170 3.01e-09

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: 56.87  E-value: 3.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   44 AFSHGINAIDTSPYYGpSEVLYGRALSNL--RNEFPRDTYFICTKVGRigaeeFNYSRDFVRFSVHRSCERLHTTYLDLV 121
Cdd:cd19136  24 ALKAGYRLIDTASVYR-NEADIGKALRDLlpKYGLSREDIFITSKLAP-----KDQGYEKARAACLGSLERLGTDYLDLY 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323684  122 YLH--DVEFVKFPDI------LEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19136  98 LIHwpGVQGLKPSDPrnaelrRESWRALEDLYKEGKLRAIGVSNYTVRHLEELLKYC 154
AKR_AKR6C1_2 cd19143
AKR6C family of aldo-keto reductase (AKR); Voltage-gated potassium channel subunit beta (KCAB) ...
 14-124 4.49e-09

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: 56.84  E-value: 4.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAIL--NQQYTDEPEsipleDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRneFPRDTYFICTKVGR 89
Cdd:cd19143  13 VSALSFGSWVTfgNQVDVDEAK-----ECMKAAYDAGVNFFDNAEVYanGQSEEIMGQAIKELG--WPRSDYVVSTKIFW 85

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 6323684   90 IGAEEFN----YSRDFVRFSVHRSCERLHTTYLDLVYLH 124
Cdd:cd19143  86 GGGGPPPndrgLSRKHIVEGTKASLKRLQLDYVDLVFCH 124
AKR_AKR9A1-2 cd19146
Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus ...
 14-170 1.23e-08

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: 55.51  E-value: 1.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYT------DEPESIPLEDiikYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNefpRDTYFICT 85
Cdd:cd19146  11 VSPLCLGAMSFGEAWKsmmgecDKETAFKLLD---AFYEQGGNFIDTANNYqgEESERWVGEWMASRGN---RDEMVLAT 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   86 K---VGRIGAEE---FNY---SRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKfpDILEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19146  85 KyttGYRRGGPIkikSNYqgnHAKSLRLSVEASLKKLQTSYIDILYVHWWDYTT--SIPELMQSLNHLVAAGKVLYLGVS 162

                       170
                ....*....|....
gi 6323684  157 GYPidfiTWLAEYC 170
Cdd:cd19146 163 DTP----AWVVSKA 172
AKR_AKR14A1_2 cd19089
AKR14A family of aldo-keto reductase (AKR); Escherichia coli L-glyceraldehyde 3-phosphate ...
 40-171 1.29e-08

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: 55.34  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   40 IIKYAFSHGINAIDTSPYYGPS----EVLYGRALSNLRnEFPRDTYFICTKVGrigaeefnY-----------SRDFVRF 104
Cdd:cd19089  34 LLRTAFDLGITHFDLANNYGPPpgsaEENFGRILKRDL-RPYRDELVISTKAG--------YgmwpgpygdggSRKYLLA 104

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684  105 SVHRSCERLHTTYLDLVYLHDVEfvkfPDI-----LEALKEL-RTLKNKGViknfGISGYPIDFITWLAEYCS 171
Cdd:cd19089 105 SLDQSLKRMGLDYVDIFYHHRYD----PDTpleetMTALADAvRSGKALYV----GISNYPGAKARRAIALLR 169
AKR_AKR3F2 cd19139
Escherichia coli 2,5-diketo-D-gluconic acid reductase B (DkgB/YafB) and similar proteins; ...
 39-160 1.45e-08

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: 54.67  E-value: 1.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   39 DIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNLRneFPRDTYFICTKVgrigaEEFNYSRDFVRFSVHRSCERLHTTYL 118
Cdd:cd19139  18 DSVRTALELGYRHIDTAQIYD-NEAAVGQAIAESG--VPRDELFITTKI-----WIDNLSKDKLLPSLEESLEKLRTDYV 89

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6323684  119 DLVYLH-----DVEfvkfpDILEALKELRTLKNKGVIKNFGISGYPI 160
Cdd:cd19139  90 DLTLIHwpspnDEV-----PVEEYIGALAEAKEQGLTRHIGVSNFTI 131
AKR_AKR2E1-5 cd19116
AKR2E family of aldo-keto reductase (AKR); Bombyx mori 3-dehydroecdysone reductase is a ...
 36-171 1.71e-08

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: 54.98  E-value: 1.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   36 PLEDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNL--RNEFPRDTYFICTKVGRIgaeefNYSRDFVRFSVHRSCERL 113
Cdd:cd19116  26 GVRQAVKHAIEAGYRHIDTAYLYG-NEAEVGEAIREKiaEGVVKREDLFITTKLWNS-----YHEREQVEPALRESLKRL 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684  114 HTTYLDLVYLH---------------DVEFVKFpDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCS 171
Cdd:cd19116 100 GLDYVDLYLIHwpvafkenndsesngDGSLSDI-DYLETWRGMEDLVKLGLTRSIGVSNFNSEQINRLLSNCN 171
Aldo_ket_red_shaker cd19141
Shaker potassium channel beta subunit (AKR6A) family of aldo-keto reductase (AKR); This family ...
 14-122 1.63e-07

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: 52.06  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGG-AILNQQYTDEPEsiplEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSnlRNEFPRDTYFICTKV--G 88
Cdd:cd19141  12 VSCLGLGTwVTFGSQISDEVA----EELVTLAYENGINLFDTAEVYaaGKAEIVLGKILK--KKGWRRSSYVITTKIfwG 85

                        90       100       110
                ....*....|....*....|....*....|....
gi 6323684   89 RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVY 122
Cdd:cd19141  86 GKAETERGLSRKHIIEGLKASLERLQLEYVDIVF 119
AKR_CeZK1290-like cd19135
Caenorhabditis elegans ZK1290.5 and similar proteins; Caenorhabditis elegans ZK1290.5 is the ...
 43-171 2.18e-07

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: 51.17  E-value: 2.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   43 YAFSH-GINAIDTSPYYGpSEVLYGRALSNlrNEFPRDTYFICTKV--GRIGAEEfnysrdfVRFSVHRSCERLHTTYLD 119
Cdd:cd19135  33 YALKEcGYRHIDTAKRYG-CEELLGKAIKE--SGVPREDLFLTTKLwpSDYGYES-------TKQAFEASLKRLGVDYLD 102

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6323684  120 LVYLHdvefvkFPD-----------ILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCS 171
Cdd:cd19135 103 LYLLH------WPDcpssgknvketRAETWRALEELYDEGLCRAIGVSNFLIEHLEQLLEDCS 159
AKR_unchar cd19103
uncharacterized aldo-keto reductase (AKR) superfamily protein; This family includes a group of ...
 37-156 2.84e-07

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


Pssm-ID: 381329 [Multi-domain]  Cd Length: 299  Bit Score: 51.18  E-value: 2.84e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   37 LEDIIKYAFSHGINAIDTSPYY--GPSEvlygRALSNLRNEFPRDTYFICTKVGRIGAEEfnySRDFVRFSVHRSCERLH 114
Cdd:cd19103  34 LKAVFDKAMAAGLNLWDTAAVYgmGASE----KILGEFLKRYPREDYIISTKFTPQIAGQ---SADPVADMLEGSLARLG 106

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 6323684  115 TTYLDLVYLH---DVEfvkfpdilEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19103 107 TDYIDIYWIHnpaDVE--------RWTPELIPLLKSGKVKHVGVS 143
AKR_AKR3C1 cd19119
Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar ...
 38-172 3.11e-07

Saccharomyces cerevisiae D-arabinose dehydrogenase [NAD(P)+] heavy chain (Ara1p) and similar proteins; Saccharomyces cerevisiae Ara1p (EC 1.1.1.117), also called D-arabinose 1-dehydrogenase (NAD(P)(+)), is a founding members of aldo-keto reductase family 3 member C1 (AKR3C1). It catalyzes the oxidation of D-arabinose, L-xylose, L-fucose, and L-galactose in the presence of NADP(+).


Pssm-ID: 381345 [Multi-domain]  Cd Length: 294  Bit Score: 50.96  E-value: 3.11e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNL--RNEFPRDTYFICTKVGRIGAEEFNYSRDfvrfsvhRSCERLHT 115
Cdd:cd19119  30 KEAVEAAIKEGYRHIDTAYAYE-TEDFVGEAIKRAidDGSIKREELFITTKVWPTFYDEVERSLD-------ESLKALGL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  116 TYLDLVYLH----------DVEFVKFP-------------DILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCST 172
Cdd:cd19119 102 DYVDLLLVHwpvcfekdsdDSGKPFTPvnddgktryaasgDHITTYKQLEKIYLDGRAKAIGVSNYSIVYLERLIKECKV 181
AKR_AKR5F1 cd19133
the AKR5F family of aldo-keto reductase (AKR); Klebsiella sp. 2,5-diketo-D-gluconic acid ...
 38-170 4.03e-07

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: 50.27  E-value: 4.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGPSEVLyGRALsnLRNEFPRDTYFICTKVGrigAEEFNYSRdfVRFSVHRSCERLHTTY 117
Cdd:cd19133  26 ERAVLEAIKAGYRLIDTAAAYGNEEAV-GRAI--KKSGIPREELFITTKLW---IQDAGYEK--AKKAFERSLKRLGLDY 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6323684  118 LDLVYLHDvefvKFPDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19133  98 LDLYLIHQ----PFGDVYGAWRAMEELYKEGKIRAIGVSNFYPDRLVDLILHN 146
dkgB PRK11172
2,5-didehydrogluconate reductase DkgB;
36-161 7.59e-07

2,5-didehydrogluconate reductase DkgB;


Pssm-ID: 183012 [Multi-domain]  Cd Length: 267  Bit Score: 49.64  E-value: 7.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    36 PLEDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKvgrIGAEefNYSRDFVRFSVHRSCERLHT 115
Cdd:PRK11172  17 VVIDSVKTALELGYRAIDTAQIYD-NEAAVGQAIA--ESGVPRDELFITTK---IWID--NLAKDKLIPSLKESLQKLRT 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6323684   116 TYLDLVYLH-----DVefVKFPDILEALKElrtLKNKGVIKNFGISGYPID 161
Cdd:PRK11172  89 DYVDLTLIHwpspnDE--VSVEEFMQALLE---AKKQGLTREIGISNFTIA 134
AKR_AKR9A3_9B1-4 cd19147
Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; ...
 14-159 3.70e-06

Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD) and similar proteins; Phanerochaete chrysosporium ADD (EC1.1.1.91) is a founding member of aldo-keto reductase family 9 member A3. It is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). This family also includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.


Pssm-ID: 381373 [Multi-domain]  Cd Length: 319  Bit Score: 47.90  E-value: 3.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQYT------DEPESIPLEDIIkYAFshGINAIDTSPYYG--PSEVLYGRALSNLRNefpRDTYFICT 85
Cdd:cd19147  10 VSPLILGAMSIGDAWSgfmgsmDKEQAFELLDAF-YEA--GGNFIDTANNYQdeQSETWIGEWMKSRKN---RDQIVIAT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   86 KVG------RIG-AEEFNYSRDFVR---FSVHRSCERLHTTYLDLVYLHDVEFVKfpDILEALKELRTLKNKGVIKNFGI 155
Cdd:cd19147  84 KFTtdykayEVGkGKAVNYCGNHKRslhVSVRDSLRKLQTDWIDILYVHWWDYTT--SIEEVMDSLHILVQQGKVLYLGV 161


                ....
gi 6323684  156 SGYP 159
Cdd:cd19147 162 SDTP 165
AKR_KCAB3B_AKR6A9-like cd19160
voltage-gated potassium channel subunit beta-3 (KCAB3B) and similar proteins; KCAB3B from Homo ...
 14-122 8.43e-06

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: 46.90  E-value: 8.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAI-LNQQYTDEPEsiplEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSnlRNEFPRDTYFICTKV--G 88
Cdd:cd19160  15 VSCLGLGTWVtFGSQISDETA----EDLLTVAYEHGVNLFDTAEVYaaGKAERTLGNILK--SKGWRRSSYVVTTKIywG 88

                        90       100       110
                ....*....|....*....|....*....|....
gi 6323684   89 RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVY 122
Cdd:cd19160  89 GQAETERGLSRKHIIEGLRGSLDRLQLEYVDIVF 122
AKR_AKR5G1-3 cd19157
AKR5G family of aldo-keto reductase (AKR); Bacillus subtilis glyoxal reductase (GR), ...
 32-171 2.92e-05

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: 45.07  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   32 PESIPLEDIIKYAFSHGINAIDTSPYYGPSEVLyGRAL--SNLrnefPRDTYFICTKVGRigaEEFNYSRDFVRFSVhrS 109
Cdd:cd19157  21 EEGSEVVNAVKTALKNGYRSIDTAAIYGNEEGV-GKGIkeSGI----PREELFITSKVWN---ADQGYDSTLKAFEA--S 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684  110 CERLHTTYLDLVYLHDVEFVKFPdilEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCS 171
Cdd:cd19157  91 LERLGLDYLDLYLIHWPVKGKYK---ETWKALEKLYKDGRVRAIGVSNFQVHHLEDLLADAE 149
AKR_AKR5B1 cd19127
AKR5B family of aldo-keto reductase (AKR); Pseudomonas putida morphine 6-dehydrogenase (M6DH) ...
 39-171 3.81e-05

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: 44.71  E-value: 3.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   39 DIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVGrigAEEFNYSRDFVRFSvhRSCERLHTTYL 118
Cdd:cd19127  26 DAVATALADGYRLIDTAAAYG-NEREVGEGIR--RSGVDRSDIFVTTKLW---ISDYGYDKALRGFD--ASLRRLGLDYV 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6323684  119 DLVYLHDVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCS 171
Cdd:cd19127  98 DLYLLHWPVPNDFDRTIQAYKALEKLLAEGRVRAIGVSNFTPEHLERLIDATT 150
PRK10376 PRK10376
putative oxidoreductase; Provisional
 44-156 5.48e-05

putative oxidoreductase; Provisional


Pssm-ID: 236676 [Multi-domain]  Cd Length: 290  Bit Score: 44.19  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    44 AFSHGINAIDTSPYYGP--SEVLYGRALsnlrneFP-RDTYFICTKVGRIGAEEFNY----SRDFVRFSVHRSCERLHTT 116
Cdd:PRK10376  49 AVALGVNHIDTSDFYGPhvTNQLIREAL------HPyPDDLTIVTKVGARRGEDGSWlpafSPAELRRAVHDNLRNLGLD 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 6323684   117 YLDLVYLHDVEFVKFPD---ILEALKELRTLKNKGVIKNFGIS 156
Cdd:PRK10376 123 VLDVVNLRLMGDGHGPAegsIEEPLTVLAELQRQGLVRHIGLS 165
AKR_AKR5C2 cd19131
Escherichia coli 2,5-diketo-D-gluconic acid reductase A (DkgA/YqhE) and similar proteins; ...
 38-161 1.38e-04

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: 42.74  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVgrigaeeFN--YSRDFVRFSVHRSCERLHT 115
Cdd:cd19131  26 ASAVREALEVGYRSIDTAAIYG-NEEGVGKAIR--ASGVPREELFITTKL-------WNsdQGYDSTLRAFDESLRKLGL 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6323684  116 TYLDLVYLHdvefvkFP-----DILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19131  96 DYVDLYLIH------WPvpaqdKYVETWKALIELKKEGRVKSIGVSNFTIE 140
AKR_AKR5A_5G cd19126
AKR5A and AKR5G families of aldo-keto reductase (AKR); The AKR5A family of AKR includes ...
 38-170 1.92e-04

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: 42.42  E-value: 1.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVGRigaEEFNYSRDFVRFsvHRSCERLHTTY 117
Cdd:cd19126  26 ERAVQTALENGYRSIDTAAIYK-NEEGVGEAIR--ESGVPREELFVTTKLWN---DDQRARRTEDAF--QESLDRLGLDY 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 6323684  118 LDLVYLHDVEFVKFPDILEALKELRTlknKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19126  98 VDLYLIHWPGKDKFIDTWKALEKLYA---SGKVKAIGVSNFQEHHLEELLAHA 147
AKR_AKR5D1_E1 cd19132
AKR5D and AKR5E families of aldo-keto reductase (AKR); 2,5-diketo-D-gluconic acid reductase B ...
 44-159 2.63e-04

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: 41.87  E-value: 2.63e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   44 AFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKV-GRigaeefNYSRDFVRFSVHRSCERLHTTYLDLVY 122
Cdd:cd19132  29 ALQAGYRLLDTAFNYE-NEGAVGEAVR--RSGVPREELFVTTKLpGR------HHGYEEALRTIEESLYRLGLDYVDLYL 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 6323684  123 LHdvefvkFPD-----ILEALKELRTLKNKGVIKNFGISGYP 159
Cdd:cd19132 100 IH------WPNpsrdlYVEAWQALIEAREEGLVRSIGVSNFL 135
PRK09912 PRK09912
L-glyceraldehyde 3-phosphate reductase; Provisional
 40-127 3.92e-04

L-glyceraldehyde 3-phosphate reductase; Provisional


Pssm-ID: 182140 [Multi-domain]  Cd Length: 346  Bit Score: 41.90  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    40 IIKYAFSHGINAIDTSPYYGP----SEVLYGRALsnlRNEFP--RDTYFICTKVGR---IGAEEFNYSRDFVRFSVHRSC 110
Cdd:PRK09912  48 ILRKAFDLGITHFDLANNYGPppgsAEENFGRLL---REDFAayRDELIISTKAGYdmwPGPYGSGGSRKYLLASLDQSL 124

                         90
                 ....*....|....*..
gi 6323684   111 ERLHTTYLDLVYLHDVE 127
Cdd:PRK09912 125 KRMGLEYVDIFYSHRVD 141
AKR_AKR8A1-2 cd19077
AKR8A family of aldo-keto reductase (AKR); Schizosaccharomyces pombe PLR and PLR2 are founding ...
 26-156 4.42e-04

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: 41.46  E-value: 4.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   26 QQYTDEpESIPledIIKYAFSHGINAIDTSPYYGPSEvlygrALSNLR------NEFP--RDTYFICTKVGRIGAE-EFN 96
Cdd:cd19077  20 NPTPDE-EAFE---TMKAALDAGSNLWNGGEFYGPPD-----PHANLKllarffRKYPeyADKVVLSVKGGLDPDTlRPD 90

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6323684   97 YSRDFVRFSVHRSCERLHTT-YLDLVYLHDVEfvKFPDILEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19077  91 GSPEAVRKSIENILRALGGTkKIDIFEPARVD--PNVPIEETIKALKELVKEGKIRGIGLS 149
AKR_AKR5H1 cd19134
AKR5H family of aldo-keto reductase (AKR); Mycobacterium smegmatis MSMEG_2407 is a founding ...
 44-158 4.55e-04

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: 41.38  E-value: 4.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   44 AFSHGINAIDTSPYYGpSEVLYGRALSnlRNEFPRDTYFICTKVGRiGAEEFNYSRDFVRfsvhRSCERLHTTYLDLVYL 123
Cdd:cd19134  33 ALEAGYRLIDTAAAYG-NEAAVGRAIA--ASGIPRGELFVTTKLAT-PDQGFTASQAACR----ASLERLGLDYVDLYLI 104

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 6323684  124 H--DVEFVKFPDILEALKELRTLknkGVIKNFGISGY 158
Cdd:cd19134 105 HwpAGREGKYVDSWGGLMKLREE---GLARSIGVSNF 138
AKR_KCAB2B_AKR6A1-like cd19158
voltage-gated potassium channel subunit beta-2 (KCAB2B) and similar proteins; KCAB2B from Bos ...
 14-156 5.08e-04

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: 41.22  E-value: 5.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAI-LNQQYTDEPEsiplEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSnlRNEFPRDTYFICTKV--G 88
Cdd:cd19158  13 VSCLGLGTWVtFGGQITDEMA----EHLMTLAYDNGINLFDTAEVYaaGKAEVVLGNIIK--KKGWRRSSLVITTKIfwG 86

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684   89 RIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVylhdveFVKFPD----ILEALKELRTLKNKGVIKNFGIS 156
Cdd:cd19158  87 GKAETERGLSRKHIIEGLKASLERLQLEYVDVV------FANRPDpntpMEETVRAMTHVINQGMAMYWGTS 152
tas PRK10625
putative aldo-keto reductase; Provisional
 8-156 6.65e-04

putative aldo-keto reductase; Provisional


Pssm-ID: 236727 [Multi-domain]  Cd Length: 346  Bit Score: 40.99  E-value: 6.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684     8 PFDLASVSPLVLGGAILNQQYTDEPESIPLEdiikYAFSHGINAIDTSPYY---------GPSEVLYGRALSNLRNefpR 78
Cdd:PRK10625   7 PHSSLEVSTLGLGTMTFGEQNSEADAHAQLD----YAVAQGINLIDVAEMYpvpprpetqGLTETYIGNWLAKRGS---R 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684    79 DTYFICTKVGriGAEEFNYS---------RDFVRFSVHRSCERLHTTYLDLVYLH------------------DVEFVKF 131
Cdd:PRK10625  80 EKLIIASKVS--GPSRNNDKgirpnqaldRKNIREALHDSLKRLQTDYLDLYQVHwpqrptncfgklgyswtdSAPAVSL 157

                        170       180
                 ....*....|....*....|....*
gi 6323684   132 PDILEALKElrtLKNKGVIKNFGIS 156
Cdd:PRK10625 158 LETLDALAE---QQRAGKIRYIGVS 179
AKR_AKR2C1 cd19114
AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent ...
 38-170 6.70e-04

AKR2C family of aldo-keto reductase (AKR); Mucor mucedo NADP-dependent 4-dihydromethyl-trisporate dehydrogenase (TDH), also called 4-dihydromethyltrisporate dehydrogenase, or 4-dihydromethyl-TA dehydrogenase, is a founding member of aldo-keto reductase family 2 member C1 (AKR2C1). It is involved in the biosynthesis of trisporic acid, the sexual hormone of zygomycetes, which induces the first steps of zygophore development. TDH catalyzes the NADP-dependent oxidation of (+) mating-type specific precursor 4-dihydromethyl-trisporate to methyl-trisporate.


Pssm-ID: 381340 [Multi-domain]  Cd Length: 302  Bit Score: 41.00  E-value: 6.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNLRNE--FPRDTYFICTKVgrigaeeFN--YSRDFVRFSVHRSCERL 113
Cdd:cd19114  20 EEVIYNAIKVGYRLIDGALLYG-NEAEVGRGIRKAIQEglVKREDLFIVTKL-------WNnfHGKDHVREAFDRQLKDY 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684  114 HTTYLDLVYLH-------------------DVEFVKFP----DILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19114  92 GLDYIDLYLIHfpipaayvdpaenypflwkDKELKKFPleqsPMQECWREMEKLVDAGLVRNIGIANFNVQLILDLLTYA 171
AKR_GlAR-like cd19128
Giardia lamblia aldose reductase (AR) and similar proteins; Giardia lamblia AR (EC 1.1.1.21), ...
 38-170 1.01e-03

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: 40.20  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   38 EDIIKYAFSHGINAIDTSPYYGpSEVLYGRALSNLRNE--FPRDTYFICTKVGrigaeEFNYSRDFVRFSVHRSCERLHT 115
Cdd:cd19128  17 KEAVKNAIKAGYRHIDCAYYYG-NEAFIGIAFSEIFKDggVKREDLFITSKLW-----PTMHQPENVKEQLLITLQDLQL 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6323684  116 TYLDLVYLH-DVEFVKFPDILEALKELRT----------------LKNKGVIKNFGISGYPIDFITWLAEYC 170
Cdd:cd19128  91 EYLDLFLIHwPLAFDMDTDGDPRDDNQIQslskkpledtwrameqCVDEKLTKNIGVSNYSTKLLTDLLNYC 162
AKR_AKR14A1 cd19150
Escherichia coli L-glyceraldehyde 3-phosphate reductase (GPR/YghZ/AKR14A1) and similar ...
 39-158 2.03e-03

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: 39.36  E-value: 2.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   39 DIIKYAFSHGINAIDTSPYYGP----SEVLYGRAlsnLRNEFP--RDTYFICTKVG-RIGAEEFNY--SRDFVRFSVHRS 109
Cdd:cd19150  34 AILRTAFDLGITHFDLANNYGPppgsAEENFGRI---LREDFAgyRDELIISTKAGyDMWPGPYGEwgSRKYLLASLDQS 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 6323684  110 CERLHTTYLDLVYLHDVEfvkfPD--ILEALKELRTLKNKGVIKNFGISGY 158
Cdd:cd19150 111 LKRMGLDYVDIFYSHRFD----PDtpLEETMGALDHAVRSGKALYVGISSY 157
AKR_AKR14A2 cd19151
Salmonella enterica aldo-keto reductase (AKR) and similar protein; Salmonella enterica AKR is ...
 40-161 2.45e-03

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: 39.31  E-value: 2.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   40 IIKYAFSHGINAIDTSPYYGP----SEVLYGRAL-SNLRNEfpRDTYFICTKVGRIGAE----EFNySRDFVRFSVHRSC 110
Cdd:cd19151  35 MLRRAFDLGITHFDLANNYGPppgsAEENFGRILkEDLKPY--RDELIISTKAGYTMWPgpygDWG-SKKYLIASLDQSL 111

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6323684  111 ERLHTTYLDLVYLHDvefvkfPD----ILEALKELRTLKNKGVIKNFGISGYPID 161
Cdd:cd19151 112 KRMGLDYVDIFYHHR------PDpetpLEETMGALDQIVRQGKALYVGISNYPPE 160
AKR_AKR9A_9B cd19080
AKR9A and AKR9B families of aldo-keto reductase (AKR); The AKR9A family includes Aspergillus ...
 14-172 2.49e-03

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: 39.12  E-value: 2.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   14 VSPLVLGGAILNQQY---TDEPESiplEDIIKYAFSHGINAIDTSPYY--GPSEVLYGRALSNLRNEFprdtyFICTKVG 88
Cdd:cd19080  10 VSPLALGTMTFGTEWgwgADREEA---RAMFDAYVEAGGNFIDTANNYtnGTSERLLGEFIAGNRDRI-----VLATKYT 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323684   89 rigaeeFNYSRDFV------RFSVHRSCE----RLHTTYLDLVYLHDVEFVKfpDILEALKELRTLKNKGVIKNFGISgy 158
Cdd:cd19080  82 ------MNRRPGDPnaggnhRKNLRRSVEaslrRLQTDYIDLLYVHAWDFTT--PVEEVMRALDDLVRAGKVLYVGIS-- 151

                       170
                ....*....|....
gi 6323684  159 piDFITWLAEYCST 172
Cdd:cd19080 152 --DTPAWVVARANT 163
 
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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