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Reviewed, UniProtKB/Swiss-Prot Q1BWM4 (PYRD_BURCA)

Last modified November 25, 2008. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Ordered Locus Names: Bcen_1074
OrganismBurkholderia cenocepacia (strain AU 1054) [Complete proteome] [HAMAP]
Taxonomic identifier331271 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O(2) = orotate + H(2)O(2).

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.

Subunit structure

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane proteinBy similarity.

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Dihydroorotate dehydrogenase
PRO_0000336457

Sites

Active site1781Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1BWM4-1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 48BBC0EDFFFC0917

FASTA34536,756
        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 
IFSGEDAHAK LAAGAALVQL YTGFIYRGPA LVSECVKAIA RERSA 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia AU 1054."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000378 Genomic DNA. Translation: ABF75981.1. Different initiation.
RefSeqYP_620954.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4093165.
GenomeReviewsGene locus Bcen_1074 in contig CP000378_GR.
KEGGbcn:Bcen_1074.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1BWM4.

Enzyme and pathway databases

BioCycBCEN331271:BCEN_1074-MON.

Family and domain databases

HAMAPMF_00225.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. DHO_DHase_1_2.
IPR005719. DHO_DHase_2.
IPR001295. Dihydroorotate_DHase_core.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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_BURCA
AccessionPrimary (citable) accession number: Q1BWM4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: November 25, 2008
This is version 25 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents