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Conserved domains on  [gi|15610855|ref|NP_218236|]
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hypothetical protein Rv3719 [Mycobacterium tuberculosis H37Rv]

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

CATH:  3.30.465.50|3.40.462.20
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02441 super family cl33491
cytokinin dehydrogenase
 82-228 1.06e-15

cytokinin dehydrogenase


The actual alignment was detected with superfamily member PLN02441:

Pssm-ID: 215242 [Multi-domain]  Cd Length: 525  Bit Score: 79.19  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855   82 ADVAGMCTYEDLIAATLHYGLSPlvvpqlRT------ITLGGAVTGLGIESASFRNGlPHES-VLEMDILTGAGELLTVS 154
Cdd:PLN02441 138 VDVSGGELWIDVLKATLKHGLAP------RSwtdylyLTVGGTLSNAGISGQAFRHG-PQISnVLELDVVTGKGEVVTCS 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610855  155 PGQHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFValRHIR--FSSLTAMVAAMERIIdtGGLDGESVDYLDGVVF 228
Cdd:PLN02441 211 PTQNSDLFFAVLGGLGQFGIITRARIALEPAPKRV--RWIRvlYSDFSTFTRDQERLI--SRPPENSFDYVEGFVI 282
 
Name Accession Description Interval E-value
PLN02441 PLN02441
cytokinin dehydrogenase
 82-228 1.06e-15

cytokinin dehydrogenase


Pssm-ID: 215242 [Multi-domain]  Cd Length: 525  Bit Score: 79.19  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855   82 ADVAGMCTYEDLIAATLHYGLSPlvvpqlRT------ITLGGAVTGLGIESASFRNGlPHES-VLEMDILTGAGELLTVS 154
Cdd:PLN02441 138 VDVSGGELWIDVLKATLKHGLAP------RSwtdylyLTVGGTLSNAGISGQAFRHG-PQISnVLELDVVTGKGEVVTCS 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610855  155 PGQHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFValRHIR--FSSLTAMVAAMERIIdtGGLDGESVDYLDGVVF 228
Cdd:PLN02441 211 PTQNSDLFFAVLGGLGQFGIITRARIALEPAPKRV--RWIRvlYSDFSTFTRDQERLI--SRPPENSFDYVEGFVI 282
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
64-213 1.18e-14

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 75.70  E-value: 1.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855  64 LDASGLTGVIGIDPEARTADV-AGmCTYEDLIAATLHYGLSPLVVPQ-LRTITLGGAVTGLGIESASFRNGLPHESVLEM 141
Cdd:COG0277  88 LDLSRMNRILEVDPEDRTATVeAG-VTLADLNAALAPHGLFFPPDPSsQGTATIGGNIATNAGGPRSLKYGLTRDNVLGL 166

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610855 142 DILTGAGELLTVSPG-----QHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFVALRHIRFSSLTAMVAAMERIIDTG 213
Cdd:COG0277 167 EVVLADGEVVRTGGRvpknvTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAG 243
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 50-154 1.73e-10

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: 58.75  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855    50 SNLFRARVKHDARGLDASGLTGVIGIDPEARTADVAGMCTYEDLIAATLHYGLSPLVVPQ-LRTITLGGAVTGLGIESAS 128
Cdd:pfam01565  34 SSLLGGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRALAAKGLLLGLDPGsGIPGTVGGAIATNAGGYGS 113

                          90       100
                  ....*....|....*....|....*.
gi 15610855   129 FRNGLPHESVLEMDILTGAGELLTVS 154
Cdd:pfam01565 114 EKYGLTRDNVLGLEVVLADGEVVRLG 139
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 69-184 6.34e-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: 45.24  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855    69 LTGVIGIDPEARTADVAGMCTYEDLIAATLHYGLSPLVVPQLRTITLGGAV-TGLGIESASFRNGLPHESVLEMDILTGA 147
Cdd:TIGR01677  88 LNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAPYWWGLTVGGMMgTGAHGSSLWGKGSAVHDYVVGIRLVVPA 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15610855   148 G------ELLTVSPGQHSDLYRAFPNSYGTLGYSTRLRIQLEP 184
Cdd:TIGR01677 168 SaaegfaKVRILSEGDTPNEFNAAKVSLGVLGVISQVTLALQP 210
 
Name Accession Description Interval E-value
PLN02441 PLN02441
cytokinin dehydrogenase
 82-228 1.06e-15

cytokinin dehydrogenase


Pssm-ID: 215242 [Multi-domain]  Cd Length: 525  Bit Score: 79.19  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855   82 ADVAGMCTYEDLIAATLHYGLSPlvvpqlRT------ITLGGAVTGLGIESASFRNGlPHES-VLEMDILTGAGELLTVS 154
Cdd:PLN02441 138 VDVSGGELWIDVLKATLKHGLAP------RSwtdylyLTVGGTLSNAGISGQAFRHG-PQISnVLELDVVTGKGEVVTCS 210

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15610855  155 PGQHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFValRHIR--FSSLTAMVAAMERIIdtGGLDGESVDYLDGVVF 228
Cdd:PLN02441 211 PTQNSDLFFAVLGGLGQFGIITRARIALEPAPKRV--RWIRvlYSDFSTFTRDQERLI--SRPPENSFDYVEGFVI 282
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
64-213 1.18e-14

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


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 75.70  E-value: 1.18e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855  64 LDASGLTGVIGIDPEARTADV-AGmCTYEDLIAATLHYGLSPLVVPQ-LRTITLGGAVTGLGIESASFRNGLPHESVLEM 141
Cdd:COG0277  88 LDLSRMNRILEVDPEDRTATVeAG-VTLADLNAALAPHGLFFPPDPSsQGTATIGGNIATNAGGPRSLKYGLTRDNVLGL 166

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610855 142 DILTGAGELLTVSPG-----QHSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFVALRHIRFSSLTAMVAAMERIIDTG 213
Cdd:COG0277 167 EVVLADGEVVRTGGRvpknvTGYDLFWLLVGSEGTLGVITEATLRLHPLPEAVATALVAFPDLEAAAAAVRALLAAG 243
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 50-154 1.73e-10

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: 58.75  E-value: 1.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855    50 SNLFRARVKHDARGLDASGLTGVIGIDPEARTADVAGMCTYEDLIAATLHYGLSPLVVPQ-LRTITLGGAVTGLGIESAS 128
Cdd:pfam01565  34 SSLLGGAVQTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRALAAKGLLLGLDPGsGIPGTVGGAIATNAGGYGS 113

                          90       100
                  ....*....|....*....|....*.
gi 15610855   129 FRNGLPHESVLEMDILTGAGELLTVS 154
Cdd:pfam01565 114 EKYGLTRDNVLGLEVVLADGEVVRLG 139
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 69-184 6.34e-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: 45.24  E-value: 6.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855    69 LTGVIGIDPEARTADVAGMCTYEDLIAATLHYGLSPLVVPQLRTITLGGAV-TGLGIESASFRNGLPHESVLEMDILTGA 147
Cdd:TIGR01677  88 LNHVVAVDATAMTVTVESGMSLRELIVEAEKAGLALPYAPYWWGLTVGGMMgTGAHGSSLWGKGSAVHDYVVGIRLVVPA 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 15610855   148 G------ELLTVSPGQHSDLYRAFPNSYGTLGYSTRLRIQLEP 184
Cdd:TIGR01677 168 SaaegfaKVRILSEGDTPNEFNAAKVSLGVLGVISQVTLALQP 210
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 72-238 2.26e-03

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 40.53  E-value: 2.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855   72 VIGIDPEARTADVAGMCTYEDLIAATLHYGL--SPLVVPQLrTITLGGAVTglgiESAS----FRNGLPHESVLEMDILT 145
Cdd:PRK11230 112 ILDINPVGRRARVQPGVRNLAISQAAAPHGLyyAPDPSSQI-ACSIGGNVA----ENAGgvhcLKYGLTVHNLLKVEILT 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610855  146 GAGELLTV------SPGqhSDLYRAFPNSYGTLGYSTRLRIQLEPVRPFVALRHIRFSSLTAMVAAMERIIDTGGLDGeS 219
Cdd:PRK11230 187 LDGEALTLgsdaldSPG--FDLLALFTGSEGMLGVVTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIAAGIIPG-G 263

                        170
                 ....*....|....*....
gi 15610855  220 VDYLDGVVFSADESYLCIG 238
Cdd:PRK11230 264 LEMMDNLSIRAAEDFIHAG 282
 
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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