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B4E8N4 (PYRD_BURCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:BceJ2315_15750
ORF Names:BCAL1611
OrganismBurkholderia cepacia (strain J2315 / LMG 16656) (Burkholderia cenocepacia (strain J2315)) [Complete proteome] [HAMAP]
Taxonomic identifier216591 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length345 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 – 345345Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000100252

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
B4E8N4 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: CABFD0EDFFE8B65C

FASTA34536,789
        10         20         30         40         50         60 
MFSSLYPLAR ASLFKMDAED AHHLTLRALG AAGRTGLACA LSARVPDAPR TVMGLTFRNP 

        70         80         90        100        110        120 
VGLAAGLDKD GAAIDGLAAL GFGFIEVGTV TPRPQPGNPR PRMFRLPQAE ALINRMGFNN 

       130        140        150        160        170        180 
HGVDQFVKNV QAARYRGILG LNIGKNADTP IERAAEDYLY CLERVYPFAS YVTINISSPN 

       190        200        210        220        230        240 
TKNLRQLQGA GELDALLAAL KDKQQRLADL HGKLVPLALK IAPDLDDEQV KEIGDTLLRH 

       250        260        270        280        290        300 
KIEAVIATNT TLSRAAVQGL PHADEAGGLS GRPVFDASNE VIRKLHAEVG NDVPIIGVGG 

       310        320        330        340 
IFSGEDARAK LAAGAALVQL YTGFIYRGPA LVSECVKAIA RERTA

« Hide

References

[1]"Genomic analysis of Burkholderia cenocepacia J2315, an epidemic cystic fibrosis pathogen."
Holden M.T.G.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J2315 / LMG 16656.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM747720 Genomic DNA. Translation: CAR51909.1.
RefSeqYP_002230739.1. NC_011000.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4E8N4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6931882.
GenomeReviewsGene locus BceJ2315_15750 in contig AM747720_GR.
KEGGbcj:BCAL1611.
PATRIC19075009. VBIBurCen118154_1666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
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_BURCJ
AccessionPrimary (citable) accession number: B4E8N4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 27 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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