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A3N925 (PYRD_BURP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase (quinone)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:BURPS668_1809
OrganismBurkholderia pseudomallei (strain 668) [Complete proteome] [HAMAP]
Taxonomic identifier320373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group ›

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP-Rule MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP-Rule MF_00225

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP-Rule MF_00225

Subunit structure

Monomer By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   LigandFMN
Flavoprotein
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225
PRO_1000024163

Regions

Nucleotide binding65 – 695FMN By similarity
Nucleotide binding321 – 3222FMN By similarity
Region114 – 1185Substrate binding By similarity
Region249 – 2502Substrate binding By similarity

Sites

Active site1781Nucleophile By similarity
Binding site691Substrate By similarity
Binding site891FMN; via amide nitrogen By similarity
Binding site1421FMN By similarity
Binding site1751FMN By similarity
Binding site1751Substrate By similarity
Binding site1801Substrate By similarity
Binding site2201FMN By similarity
Binding site2481FMN; via carbonyl oxygen By similarity
Binding site2711FMN; via amide nitrogen By similarity
Binding site3001FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A3N925 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 5E7244A6476813E7

FASTA34236,305
        10         20         30         40         50         60 
MFSSLYPLAR ASLFKMDAED AHHLTLRMLG AAGRTGLACA LSPRVPDAPR TVMGLSFRNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAAIDGFAAL GFGFIEVGTV TPRAQPGNPR PRLFRLPEAD AIINRMGFNN 

       130        140        150        160        170        180 
SGVDQFVKNV QAARYRGVLG LNIGKNADTP IERAADDYLY CLERVYPFAS YVTINISSPN 

       190        200        210        220        230        240 
TKNLRQLQGA GELDALLAAL KDKQRRLADL HGKLVPLALK IAPDLDDEQV KEIAATLLRH 

       250        260        270        280        290        300 
DIEGVIATNT TLSREAVKGL PHADEAGGLS GRPVFDASNA VIRKLRAELG DAVPIIGVGG 

       310        320        330        340 
IFSGEDARAK LAAGAALVQL YTGFIYRGPA LVAECVKAIA RG

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 668.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000570 Genomic DNA. Translation: ABN82176.1.
RefSeqYP_001058846.1. NC_009074.1.

3D structure databases

ProteinModelPortalA3N925.
SMRA3N925. Positions 5-339.
ModBaseSearch...

Protein-protein interaction databases

STRING320373.BURPS668_1809.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN82176; ABN82176; BURPS668_1809.
GeneID4881949.
KEGGbpd:BURPS668_1809.
PATRIC19249485. VBIBurPse82117_1701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225103.
KOK00226.
OMAALNRMGF.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycBPSE320373:GJ9C-1806-MONOMER.
UniPathwayUPA00070; UER00946.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00225. DHO_dh_type2.
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. pyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_BURP6
AccessionPrimary (citable) accession number: A3N925
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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