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Conserved domains on  [gi|528471683|ref|XP_005168474|]
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D-2-hydroxyglutarate dehydrogenase, mitochondrial isoform X1 [Danio rerio]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 11416043)

FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor

EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-531 7.22e-137

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


:

Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 404.28  E-value: 7.22e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  73 VTQEDLSFFRALLPGRTITDPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVP 152
Cdd:COG0277    2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 153 VFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRG 232
Cdd:COG0277   82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 233 TVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSI-LCPrKPKAVNVAFLGCSSFQQLLETFQCCR 311
Cdd:COG0277  162 NVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLrLHP-LPEAVATALVAFPDLEAAAAAVRALL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMlGEILSAFEFLDASCMNLLEKHLKLTNPiTECPFYIVIETAGSNATHDEEKLHQfLEEVMTSSLVTDGTVATEATKIK 391
Cdd:COG0277  241 AA-GIAPAALELMDRAALALVEAAPPLGLP-EDGGALLLVEFDGDDAEEVEAQLAR-LRAILEAGGATDVRVAADGAERE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 392 ALWSLRERVTEALTHE--GYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNITSPSKDFALLAAIE 469
Cdd:COG0277  318 RLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERAR 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528471683 470 PY---VYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDN 531
Cdd:COG0277  398 AAaeeIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-531 7.22e-137

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 404.28  E-value: 7.22e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  73 VTQEDLSFFRALLPGRTITDPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVP 152
Cdd:COG0277    2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 153 VFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRG 232
Cdd:COG0277   82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 233 TVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSI-LCPrKPKAVNVAFLGCSSFQQLLETFQCCR 311
Cdd:COG0277  162 NVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLrLHP-LPEAVATALVAFPDLEAAAAAVRALL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMlGEILSAFEFLDASCMNLLEKHLKLTNPiTECPFYIVIETAGSNATHDEEKLHQfLEEVMTSSLVTDGTVATEATKIK 391
Cdd:COG0277  241 AA-GIAPAALELMDRAALALVEAAPPLGLP-EDGGALLLVEFDGDDAEEVEAQLAR-LRAILEAGGATDVRVAADGAERE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 392 ALWSLRERVTEALTHE--GYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNITSPSKDFALLAAIE 469
Cdd:COG0277  318 RLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERAR 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528471683 470 PY---VYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDN 531
Cdd:COG0277  398 AAaeeIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
286-526 6.03e-64

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 208.71  E-value: 6.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  286 KPKAVNVAFLGCSSFQQLLETFQCCRGMlGEILSAFEFLDASCMNLLEKHLKLTN-PITECPFYIVIETAGSNATHDEEK 364
Cdd:pfam02913   1 LPEVRAVALVGFPSFEAAVKAVREIARA-GIIPAALELMDNDALDLVEATLGFPKgLPRDAAALLLVEFEGDDEETAEEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  365 LhQFLEEVMTSSLVTDGTVATEATKIKALWSLRERVTE----ALTHEGYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNV 440
Cdd:pfam02913  80 L-EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  441 VGYGHVGDGNLHLNITSPSKDFALLAAIEPYVYEW---TSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLD 517
Cdd:pfam02913 159 CLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEImdlALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFD 238

                  ....*....
gi 528471683  518 PKGILNPYK 526
Cdd:pfam02913 239 PKGILNPGK 247
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
112-532 3.75e-46

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 169.80  E-value: 3.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 112 DVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHY 191
Cdd:PLN02805 135 DVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEY 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 192 LEERDFIMPLDLGAKGSchIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEG 271
Cdd:PLN02805 215 LEPYGLFFPLDPGPGAT--IGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEG 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 272 TLGVITAVSILCPRKPKAVNVAFLGCSSFQQLLETfqCCRGMLGEI-LSAFEFLDascmnllEKHLKLTN-----PITEC 345
Cdd:PLN02805 293 TLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADV--AIATMLSGIqVSRVELLD-------EVQIRAINmangkNLPEA 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 346 PfYIVIETAGSNATHDEEKLhqFLEEVMTSSLVTDGTVATEATKIKALWSLRErvtEAL--------THEGYTykYDISL 417
Cdd:PLN02805 364 P-TLMFEFIGTEAYAREQTL--IVQKIASKHNGSDFVFAEEPEAKKELWKIRK---EALwacfamepKYEAMI--TDVCV 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 418 PVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNIT-SPSKDFALLAA--IEPYVYEWTSQWKGSISAEHGLGLKKR 494
Cdd:PLN02805 436 PLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILfDPSQEDQRREAerLNHFMVHTALSMEGTCTGEHGVGTGKM 515
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 528471683 495 NYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDNI 532
Cdd:PLN02805 516 KYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHV 553
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
102-283 3.47e-13

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 71.47  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  102 DWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGntGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQA 181
Cdd:TIGR01678   6 NWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGG--GHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQITVEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  182 GCVLENLSHYLEERDFIMPlDLGAKGSCHIGGNVSTNAGGLRlLRYGSLRGTVLGLEVVLADGRVLNCLATLRKdntgyD 261
Cdd:TIGR01678  84 GIRLYQLHEQLDEHGYSMS-NLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLECSEERNA-----D 156
                         170       180
                  ....*....|....*....|..
gi 528471683  262 LKQLFIGSEGTLGVITAVSILC 283
Cdd:TIGR01678 157 VFQAARVSLGCLGIIVTVTIQV 178
 
Name Accession Description Interval E-value
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
73-531 7.22e-137

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 404.28  E-value: 7.22e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  73 VTQEDLSFFRALLPGRTITDPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVP 152
Cdd:COG0277    2 LTAALLAALRAILAGRVLTDPADRAAYARDGNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGGAVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 153 VFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRG 232
Cdd:COG0277   82 LDGGVVLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSQGTATIGGNIATNAGGPRSLKYGLTRD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 233 TVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEGTLGVITAVSI-LCPrKPKAVNVAFLGCSSFQQLLETFQCCR 311
Cdd:COG0277  162 NVLGLEVVLADGEVVRTGGRVPKNVTGYDLFWLLVGSEGTLGVITEATLrLHP-LPEAVATALVAFPDLEAAAAAVRALL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMlGEILSAFEFLDASCMNLLEKHLKLTNPiTECPFYIVIETAGSNATHDEEKLHQfLEEVMTSSLVTDGTVATEATKIK 391
Cdd:COG0277  241 AA-GIAPAALELMDRAALALVEAAPPLGLP-EDGGALLLVEFDGDDAEEVEAQLAR-LRAILEAGGATDVRVAADGAERE 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 392 ALWSLRERVTEALTHE--GYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNITSPSKDFALLAAIE 469
Cdd:COG0277  318 RLWKARKAALPALGRLdgGAKLLEDVAVPPSRLPELLRELGALAAKYGLRATAFGHAGDGNLHVRILFDPADPEEVERAR 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528471683 470 PY---VYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDN 531
Cdd:COG0277  398 AAaeeIFDLVAELGGSISGEHGIGRLKAEFLPAEYGPAALALLRRIKAAFDPDGILNPGKILPPP 462
FAD-oxidase_C pfam02913
FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.
286-526 6.03e-64

FAD linked oxidases, C-terminal domain; This domain has a ferredoxin-like fold.


Pssm-ID: 397178  Cd Length: 248  Bit Score: 208.71  E-value: 6.03e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  286 KPKAVNVAFLGCSSFQQLLETFQCCRGMlGEILSAFEFLDASCMNLLEKHLKLTN-PITECPFYIVIETAGSNATHDEEK 364
Cdd:pfam02913   1 LPEVRAVALVGFPSFEAAVKAVREIARA-GIIPAALELMDNDALDLVEATLGFPKgLPRDAAALLLVEFEGDDEETAEEE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  365 LhQFLEEVMTSSLVTDGTVATEATKIKALWSLRERVTE----ALTHEGYTYKYDISLPVEKIYDLVQDMRRHLGGMAKNV 440
Cdd:pfam02913  80 L-EAVEAILEAGGAGDVVVATDEAEAERLWAARKYALPlrdaLGGAGPAVFSEDVSVPRSRLADLVRDIKELLDKYGLVV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  441 VGYGHVGDGNLHLNITSPSKDFALLAAIEPYVYEW---TSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLD 517
Cdd:pfam02913 159 CLFGHAGDGNLHLYILFDFRDPEQEERAEKLFDEImdlALELGGSISGEHGVGRDKKPYLEREFGEEGLALMRRIKAAFD 238

                  ....*....
gi 528471683  518 PKGILNPYK 526
Cdd:pfam02913 239 PKGILNPGK 247
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
112-532 3.75e-46

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 169.80  E-value: 3.75e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 112 DVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHY 191
Cdd:PLN02805 135 DVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGATSIEGHTLAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLELNEY 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 192 LEERDFIMPLDLGAKGSchIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNCLATLRKDNTGYDLKQLFIGSEG 271
Cdd:PLN02805 215 LEPYGLFFPLDPGPGAT--IGGMCATRCSGSLAVRYGTMRDNVISLKVVLPNGDVVKTASRARKSAAGYDLTRLVIGSEG 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 272 TLGVITAVSILCPRKPKAVNVAFLGCSSFQQLLETfqCCRGMLGEI-LSAFEFLDascmnllEKHLKLTN-----PITEC 345
Cdd:PLN02805 293 TLGVITEVTLRLQKIPQHSVVAMCNFPTIKDAADV--AIATMLSGIqVSRVELLD-------EVQIRAINmangkNLPEA 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 346 PfYIVIETAGSNATHDEEKLhqFLEEVMTSSLVTDGTVATEATKIKALWSLRErvtEAL--------THEGYTykYDISL 417
Cdd:PLN02805 364 P-TLMFEFIGTEAYAREQTL--IVQKIASKHNGSDFVFAEEPEAKKELWKIRK---EALwacfamepKYEAMI--TDVCV 435
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 418 PVEKIYDLVQDMRRHLGGMAKNVVGYGHVGDGNLHLNIT-SPSKDFALLAA--IEPYVYEWTSQWKGSISAEHGLGLKKR 494
Cdd:PLN02805 436 PLSHLAELISRSKKELDASPLVCTVIAHAGDGNFHTIILfDPSQEDQRREAerLNHFMVHTALSMEGTCTGEHGVGTGKM 515
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 528471683 495 NYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLPDNI 532
Cdd:PLN02805 516 KYLEKELGIEALQTMKRIKKALDPNNIMNPGKLIPPHV 553
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
112-249 6.50e-40

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 141.18  E-value: 6.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  112 DVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPvFDEIILSTSLMNQVFAFDNISGILTCQAGCVLENLSHY 191
Cdd:pfam01565   2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVQ-TGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 528471683  192 LEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNC 249
Cdd:pfam01565  81 LAAKGLLLGLDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRL 138
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
78-529 3.94e-35

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 137.99  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  78 LSFFRALLPGRTIT-DPDLLKSSNVDWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDE 156
Cdd:PRK11230  22 LMALREHLPGLEILhTDEELIPYECDGLSAYRTRPLLVVLPKQMEQVQALLAVCHRLRVPVVARGAGTGLSGGALPLEKG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 157 IILSTSLMNQVFAFDNISGILTCQAGcvLENL--SHYLEERDFIMPLDLGAKGSCHIGGNVSTNAGGLRLLRYGSLRGTV 234
Cdd:PRK11230 102 VLLVMARFNRILDINPVGRRARVQPG--VRNLaiSQAAAPHGLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNL 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 235 LGLEVVLADGRVLNcLATLRKDNTGYDLKQLFIGSEGTLGVITAVSILCPRKPKAVNVaflgcssfqqLLETFQCCR--- 311
Cdd:PRK11230 180 LKVEILTLDGEALT-LGSDALDSPGFDLLALFTGSEGMLGVVTEVTVKLLPKPPVARV----------LLASFDSVEkag 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 312 GMLGEILSA------FEFLDASCMNLLEKHLKLTNPItECPFYIVIETAGSNATHDEEKLHqfLEEVMTSSLVTDGTVAT 385
Cdd:PRK11230 249 LAVGDIIAAgiipggLEMMDNLSIRAAEDFIHAGYPV-DAEAILLCELDGVESDVQEDCER--VNDILLKAGATDVRLAQ 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 386 EATKIKALWSLRERVTEAL--THEGYtYKYDISLP---VEKIYDLVQDMRRHLGGMAKNVVgygHVGDGNLH----LNIT 456
Cdd:PRK11230 326 DEAERVRFWAGRKNAFPAVgrISPDY-YCMDGTIPrreLPGVLEGIARLSQQYGLRVANVF---HAGDGNMHplilFDAN 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528471683 457 SPSkDFALLAAIEPYVYEWTSQWKGSISAEHGLGLKKRNYIYYSKPSEAVALMGSIKAMLDPKGILNPYKTLP 529
Cdd:PRK11230 402 EPG-ELERAEALGGKILELCVEVGGSITGEHGVGREKINQMCAQFNSDEITLFHAVKAAFDPDGLLNPGKNIP 473
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
102-283 3.47e-13

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 71.47  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  102 DWLKTVQGSSDVLLRPKTTEEVSQILRYCNERNLAVCPQGGntGLVGGSVPVFDEIILSTSLMNQVFAFDNISGILTCQA 181
Cdd:TIGR01678   6 NWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGG--GHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQITVEA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683  182 GCVLENLSHYLEERDFIMPlDLGAKGSCHIGGNVSTNAGGLRlLRYGSLRGTVLGLEVVLADGRVLNCLATLRKdntgyD 261
Cdd:TIGR01678  84 GIRLYQLHEQLDEHGYSMS-NLGSISEVSVAGIISTGTHGSS-IKHGILATQVVALTIMTADGEVLECSEERNA-----D 156
                         170       180
                  ....*....|....*....|..
gi 528471683  262 LKQLFIGSEGTLGVITAVSILC 283
Cdd:TIGR01678 157 VFQAARVSLGCLGIIVTVTIQV 178
glcE PRK11282
glycolate oxidase FAD binding subunit; Provisional
176-281 2.59e-05

glycolate oxidase FAD binding subunit; Provisional


Pssm-ID: 236893 [Multi-domain]  Cd Length: 352  Bit Score: 46.37  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 176 ILTCQAGCVLENLSHYLEERDFIMPL---DLGAKGSchIGGNVSTNAGGLRLLRYGSLRGTVLGLEVVLADGRVLNCLAT 252
Cdd:PRK11282  58 VITARAGTPLAELEAALAEAGQMLPFeppHFGGGAT--LGGMVAAGLSGPRRPWAGAVRDFVLGTRLINGRGEHLRFGGQ 135
                         90       100
                 ....*....|....*....|....*....
gi 528471683 253 LRKDNTGYDLKQLFIGSEGTLGVITAVSI 281
Cdd:PRK11282 136 VMKNVAGYDVSRLMAGSLGTLGVLLEVSL 164
PRK11183 PRK11183
D-lactate dehydrogenase; Provisional
109-221 6.28e-05

D-lactate dehydrogenase; Provisional


Pssm-ID: 236872 [Multi-domain]  Cd Length: 564  Bit Score: 45.60  E-value: 6.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528471683 109 GSSDVL--LRPKTTEEVSQILRYCNERNLAVCPQGGNTGLVGGSVPVFDE-----IILSTSLMNQVFAFDNISGILtCQA 181
Cdd:PRK11183  35 GQGDALavVFPGTLLELWRVLQACVAADKIIIMQAANTGLTGGSTPNGNDydrdiVIISTLRLDKIQLLNNGKQVL-ALP 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 528471683 182 GCVLENLSHYLeerdfimpLDLGAK-----GSCHIG----GNVSTNAGG 221
Cdd:PRK11183 114 GTTLYQLEKAL--------KPLGREphsviGSSCIGasviGGICNNSGG 154
 
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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