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Conserved domains on  [gi|315040732|ref|XP_003169743|]
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FAD binding domain-containing protein [Nannizzia gypsea CBS 118893]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 10481000)

FAD-dependent oxidoreductase is an FAD/FMN-binding enzyme that catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to Cercospora nicotianae FAD-dependent monooxygenase CTB5

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 ...
 89-224 1.76e-17

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: 79.17  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732   89 SVAIEVTVAQDVVETVKFANNKNVPFLAFNSAHGaLTTLGKMDSGIEIFMKQLNSV-EIAQDGKSVKAGGGINSKYLADK 167
Cdd:pfam01565   2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSS-LLGGAVQTGGIVLDLSRLNGIlEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315040732  168 LWDANKQA--VTGTCECVSYLGPALGGGHGWLQGHHGLIADQFLSMDVVLADGTLKTIT 224
Cdd:pfam01565  81 LAAKGLLLglDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
 
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 ...
 89-224 1.76e-17

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: 79.17  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732   89 SVAIEVTVAQDVVETVKFANNKNVPFLAFNSAHGaLTTLGKMDSGIEIFMKQLNSV-EIAQDGKSVKAGGGINSKYLADK 167
Cdd:pfam01565   2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSS-LLGGAVQTGGIVLDLSRLNGIlEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315040732  168 LWDANKQA--VTGTCECVSYLGPALGGGHGWLQGHHGLIADQFLSMDVVLADGTLKTIT 224
Cdd:pfam01565  81 LAAKGLLLglDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
43-253 2.09e-15

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 78.40  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732  43 MDTSWVDAIKTELVPKLSPEAKVYLPGSRDfdnasvrWSALDKPMVSVAIEVTVAQDVVETVKFANNKNVPFLAFNSAH- 121
Cdd:COG0277    2 LTAALLAALRAILAGRVLTDPADRAAYARD-------GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732 122 ---GALTTlgkmDSGIEIFMKQLNSV-EIAQDGKSVKAGGGInskyladKLWDANKQA---------VTGTCECVSYLGP 188
Cdd:COG0277   75 lagGAVPL----DGGVVLDLSRMNRIlEVDPEDRTATVEAGV-------TLADLNAALaphglffppDPSSQGTATIGGN 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315040732 189 ALGGGHGWLQGHHGLIADQFLSMDVVLADGTLKTITPST-------DLFWAMKGAGHNFGIVTSVTLKIYDI 253
Cdd:COG0277  144 IATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRTGGRVpknvtgyDLFWLLVGSEGTLGVITEATLRLHPL 215
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
98-249 3.82e-03

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 39.32  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732  98 QDVVETVKFANNKNVPFLAFnsahGALTTLGKMDSGIEIFM----KQLNSVEIaqDGKSVKAGGGINSKYLADKLWDANK 173
Cdd:PRK13905  41 EDLQEFLKLLKENNIPVTVL----GNGSNLLVRDGGIRGVVirlgKGLNEIEV--EGNRITAGAGAPLIKLARFAAEAGL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732 174 Q----AVT--GTcecvsyLGPAL---GGGHGwlqghhGLIADQFLSMDVVLADGTLKTITPStDLfwamkgaghNFG--- 241
Cdd:PRK13905 115 SglefAAGipGT------VGGAVfmnAGAYG------GETADVLESVEVLDRDGEIKTLSNE-EL---------GFGyrh 172

                        170
                 ....*....|....*.
gi 315040732 242 --------IVTSVTLK 249
Cdd:PRK13905 173 salqeeglIVLSATFQ 188
 
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 ...
 89-224 1.76e-17

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: 79.17  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732   89 SVAIEVTVAQDVVETVKFANNKNVPFLAFNSAHGaLTTLGKMDSGIEIFMKQLNSV-EIAQDGKSVKAGGGINSKYLADK 167
Cdd:pfam01565   2 AAVVLPESEEEVAAIVRLANENGLPVLPRGGGSS-LLGGAVQTGGIVLDLSRLNGIlEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 315040732  168 LWDANKQA--VTGTCECVSYLGPALGGGHGWLQGHHGLIADQFLSMDVVLADGTLKTIT 224
Cdd:pfam01565  81 LAAKGLLLglDPGSGIPGTVGGAIATNAGGYGSEKYGLTRDNVLGLEVVLADGEVVRLG 139
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
43-253 2.09e-15

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 78.40  E-value: 2.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732  43 MDTSWVDAIKTELVPKLSPEAKVYLPGSRDfdnasvrWSALDKPMVSVAIEVTVAQDVVETVKFANNKNVPFLAFNSAH- 121
Cdd:COG0277    2 LTAALLAALRAILAGRVLTDPADRAAYARD-------GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTg 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732 122 ---GALTTlgkmDSGIEIFMKQLNSV-EIAQDGKSVKAGGGInskyladKLWDANKQA---------VTGTCECVSYLGP 188
Cdd:COG0277   75 lagGAVPL----DGGVVLDLSRMNRIlEVDPEDRTATVEAGV-------TLADLNAALaphglffppDPSSQGTATIGGN 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 315040732 189 ALGGGHGWLQGHHGLIADQFLSMDVVLADGTLKTITPST-------DLFWAMKGAGHNFGIVTSVTLKIYDI 253
Cdd:COG0277  144 IATNAGGPRSLKYGLTRDNVLGLEVVLADGEVVRTGGRVpknvtgyDLFWLLVGSEGTLGVITEATLRLHPL 215
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
98-249 3.82e-03

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 39.32  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732  98 QDVVETVKFANNKNVPFLAFnsahGALTTLGKMDSGIEIFM----KQLNSVEIaqDGKSVKAGGGINSKYLADKLWDANK 173
Cdd:PRK13905  41 EDLQEFLKLLKENNIPVTVL----GNGSNLLVRDGGIRGVVirlgKGLNEIEV--EGNRITAGAGAPLIKLARFAAEAGL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315040732 174 Q----AVT--GTcecvsyLGPAL---GGGHGwlqghhGLIADQFLSMDVVLADGTLKTITPStDLfwamkgaghNFG--- 241
Cdd:PRK13905 115 SglefAAGipGT------VGGAVfmnAGAYG------GETADVLESVEVLDRDGEIKTLSNE-EL---------GFGyrh 172

                        170
                 ....*....|....*.
gi 315040732 242 --------IVTSVTLK 249
Cdd:PRK13905 173 salqeeglIVLSATFQ 188
 
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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