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Reviewed, UniProtKB/Swiss-Prot Q2KW44 (PYRD_BORA1)

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: BAV2753
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length349 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 – 349349Dihydroorotate dehydrogenase
PRO_1000024154

Sites

Active site1831Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KW44-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 2B79F6391D1BAF15

FASTA34937,027
        10         20         30         40         50         60 
MSILFNAYPL ARPALFAMDA ETAHEVTLAS LQRAYDCGTT RRWLHDQPQL PTTLMGMTLR 

        70         80         90        100        110        120 
NPVGLAAGLD KNGAFIDALG NLGFGFVEVG TVTPRAQSGN PKPRMFRLPK ANALINRLGF 

       130        140        150        160        170        180 
NNQGLDAFLA NVTRSRFRSQ GGILGLNIGK NADTPIERAA DDYLIGLAGV YPHADYVTVN 

       190        200        210        220        230        240 
ISSPNTKNLR ALQGGDELSQ LLAALRDKRA ELAQQHARQV PLVVKIAPDL SQEQIDIIAD 

       250        260        270        280        290        300 
TLLSNGVDGV IATNTTLSRE AVQGMPHAAE TGGLSGAPVH ELSLAVIERL RQRVGSALAI 

       310        320        330        340 
IGVGGILSGQ QAREKIAAGA DAVQLYTGLI YRGPALVGEC VGTLKNTAR 

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM167904 Genomic DNA. Translation: CAJ50364.1.
RefSeqYP_787251.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6266676.
GenomeReviewsGene locus BAV2753 in contig AM167904_GR.
KEGGbav:BAV2753.
NMPDRfig|521.1.peg.356.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ2KW44.

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_BORA1
AccessionPrimary (citable) accession number: Q2KW44
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: November 25, 2008
This is version 25 of the entry and version 1 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