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Conserved domains on  [gi|670476429|ref|WP_031424938|]
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MULTISPECIES: FAD-binding oxidoreductase [Xanthomonas]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 10481000)

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

CATH:  3.40.462.10
Gene Ontology:  GO:0050660|GO:0016491
SCOP:  3001317

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 35-140 4.78e-19

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: 83.02  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   35 LPRGNGRSYGDSCLNPDGALLCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRY-VTVAGAIAND 113
Cdd:pfam01565  28 LPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRALAAKGLLLGLDPGSGIpGTVGGAIATN 107

                          90       100
                  ....*....|....*....|....*..
gi 670476429  114 VHGKNHHRTGNFGHHVRAFELLRSDGE 140
Cdd:pfam01565 108 AGGYGSEKYGLTRDNVLGLEVVLADGE 134
 
Name Accession Description Interval E-value
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 35-140 4.78e-19

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: 83.02  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   35 LPRGNGRSYGDSCLNPDGALLCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRY-VTVAGAIAND 113
Cdd:pfam01565  28 LPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRALAAKGLLLGLDPGSGIpGTVGGAIATN 107

                          90       100
                  ....*....|....*....|....*..
gi 670476429  114 VHGKNHHRTGNFGHHVRAFELLRSDGE 140
Cdd:pfam01565 108 AGGYGSEKYGLTRDNVLGLEVVLADGE 134
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
36-204 3.64e-15

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 77.24  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429  36 PRGNGRSYGDSCLNPDGAL-LCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGT-RYVTVAGAIAND 113
Cdd:COG0277   68 PRGGGTGLAGGAVPLDGGVvLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSqGTATIGGNIATN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429 114 VHGKNHHRTGNFGHHVRAFELLRSDGERRLCTPDEADR-----WFAATVGGLGLTGLITWAEIQLRrvggPMLEAE---N 185
Cdd:COG0277  148 AGGPRSLKYGLTRDNVLGLEVVLADGEVVRTGGRVPKNvtgydLFWLLVGSEGTLGVITEATLRLH----PLPEAVataL 223

                        170
                 ....*....|....*....
gi 670476429 186 IRFGSLDEFFALSAAAAES 204
Cdd:COG0277  224 VAFPDLEAAAAAVRALLAA 242
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 38-172 1.49e-07

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: 53.36  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   38 GNGRSYGDSCLNpDGALLCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRYVTVAGAIANDVHGK 117
Cdd:TIGR01678  45 GGGHSPSDIACT-DGFLIHLDKMNKVLQFDKEKKQITVEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGS 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 670476429  118 N-HHrtGNFGHHVRAFELLRSDGERRLCTPDEADRWFAATVGGLGLTGLITWAEIQ 172
Cdd:TIGR01678 124 SiKH--GILATQVVALTIMTADGEVLECSEERNADVFQAARVSLGCLGIIVTVTIQ 177
 
Name Accession Description Interval E-value
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 35-140 4.78e-19

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: 83.02  E-value: 4.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   35 LPRGNGRSYGDSCLNPDGALLCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRY-VTVAGAIAND 113
Cdd:pfam01565  28 LPRGGGSSLLGGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRALAAKGLLLGLDPGSGIpGTVGGAIATN 107

                          90       100
                  ....*....|....*....|....*..
gi 670476429  114 VHGKNHHRTGNFGHHVRAFELLRSDGE 140
Cdd:pfam01565 108 AGGYGSEKYGLTRDNVLGLEVVLADGE 134
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
36-204 3.64e-15

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 77.24  E-value: 3.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429  36 PRGNGRSYGDSCLNPDGAL-LCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGT-RYVTVAGAIAND 113
Cdd:COG0277   68 PRGGGTGLAGGAVPLDGGVvLDLSRMNRILEVDPEDRTATVEAGVTLADLNAALAPHGLFFPPDPSSqGTATIGGNIATN 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429 114 VHGKNHHRTGNFGHHVRAFELLRSDGERRLCTPDEADR-----WFAATVGGLGLTGLITWAEIQLRrvggPMLEAE---N 185
Cdd:COG0277  148 AGGPRSLKYGLTRDNVLGLEVVLADGEVVRTGGRVPKNvtgydLFWLLVGSEGTLGVITEATLRLH----PLPEAVataL 223

                        170
                 ....*....|....*....
gi 670476429 186 IRFGSLDEFFALSAAAAES 204
Cdd:COG0277  224 VAFPDLEAAAAAVRALLAA 242
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 38-172 1.49e-07

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: 53.36  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   38 GNGRSYGDSCLNpDGALLCARGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRYVTVAGAIANDVHGK 117
Cdd:TIGR01678  45 GGGHSPSDIACT-DGFLIHLDKMNKVLQFDKEKKQITVEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGS 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 670476429  118 N-HHrtGNFGHHVRAFELLRSDGERRLCTPDEADRWFAATVGGLGLTGLITWAEIQ 172
Cdd:TIGR01678 124 SiKH--GILATQVVALTIMTADGEVLECSEERNADVFQAARVSLGCLGIIVTVTIQ 177
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 51-167 8.09e-05

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 44.85  E-value: 8.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 670476429   51 DGALLCA-RGLDRFIAFDPGNGVLRCEAGVTLAEIIELVLPQGWFLPVTPGTRYVTVAGAIANDVHGKNHHRTGNFGH-H 128
Cdd:TIGR01677  78 DGALLIStKRLNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAPYWWGLTVGGMMGTGAHGSSLWGKGSAVHdY 157

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 670476429  129 VRAFELL----RSDG--ERRLCTPDEADRWFAATVGGLGLTGLIT 167
Cdd:TIGR01677 158 VVGIRLVvpasAAEGfaKVRILSEGDTPNEFNAAKVSLGVLGVIS 202
 
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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