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A5VNQ1 (PYRD_BRUO2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 39. 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:BOV_0325
OrganismBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512) [Complete proteome] [HAMAP]
Taxonomic identifier444178 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length364 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 MF_00225

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

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

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP 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' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP 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 – 364364Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000024157

Regions

Nucleotide binding61 – 655FMN By similarity
Nucleotide binding316 – 3172FMN By similarity
Region110 – 1145Substrate binding By similarity
Region244 – 2452Substrate binding By similarity

Sites

Active site1731Nucleophile By similarity
Binding site651Substrate By similarity
Binding site851FMN; via amide nitrogen By similarity
Binding site1391FMN By similarity
Binding site1701FMN By similarity
Binding site1701Substrate By similarity
Binding site1751Substrate By similarity
Binding site2151FMN By similarity
Binding site2431FMN; via carbonyl oxygen By similarity
Binding site2661FMN; via amide nitrogen By similarity
Binding site2951FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VNQ1 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 87BA9B721649C6D7

FASTA36439,272
        10         20         30         40         50         60 
MSGLFETLGR RALFTFDAEQ AHGLSITGLK TGIVTCRTPE DPALSVKVAG LKFPNPLGMA 

        70         80         90        100        110        120 
AGYDKNAEVP DALLKLGFGF AEVGTLTPRP QSGNPRPRIF RLVDDKAVIN RLGFNNEGHE 

       130        140        150        160        170        180 
AAFKRLSRRA GKSGIVGVNI GANKDAEDRI ADYVAGIRRF YQLARYFTVN ISSPNTPGLR 

       190        200        210        220        230        240 
NLQAREALHE LLSRVLEARD EEGNMCTLKR PVFLKIAPDL TDEELDDIAA EADAQKLDGI 

       250        260        270        280        290        300 
IVSNTTLSRS GLKNPENSNE TGGLSGAPLF ERSTVVLARM RERVGPDMPL IGVGGIDSAE 

       310        320        330        340        350        360 
TALAKIKAGA DLVQLYTGLI YRGPGLPGEI LRGLSTAIKH EGVSSIAELR DRDTKEWAAR 


KLIS

« Hide

References

[1]Paulsen I.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25840 / 63/290 / NCTC 10512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000708 Genomic DNA. Translation: ABQ61413.1.
RefSeqYP_001258348.1. NC_009505.1.

3D structure databases

ProteinModelPortalA5VNQ1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5VNQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5201581.
GenomeReviewsGene locus BOV_0325 in contig CP000708_GR.
KEGGbov:BOV_0325.
PATRIC17860417. VBIBruOvi136990_1627.
TIGRBOV_0325.

Phylogenomic databases

HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00226.
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_BRUO2
AccessionPrimary (citable) accession number: A5VNQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 39 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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