Reviewed, UniProtKB/Swiss-Prot Q7VTR9 (PYRD_BORPE)

Names and origin

Protein names

Recommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.5.2
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD

Gene names

Name:	pyrD
Ordered Locus Names:	BP3442

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	349 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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	Homodimer 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 process	Pyrimidine biosynthesis
Cellular component	Cell membrane Membrane
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete 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 component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotate oxidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 349	349	Dihydroorotate dehydrogenase HAMAP MF_00225		PRO_0000148425
Sites
	Active site	183	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7VTR9-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 5097A29FD68EB850	FASTA	349	37,116
	10 20 30 40 50 60 MSILFHAYPL ARPALFAMDA ETAHEVTLAQ LQRAYDCGLT RKLLHAQPEA PATLMGLSLR 70 80 90 100 110 120 NPVGLAAGLD KNGAHIDALG NLGFGFVEVG TVTPRAQPGN PKPRMFRLPR ANALINRLGF 130 140 150 160 170 180 NNQGLDAFIA NVQRSQWRSQ GRILGLNIGK NADTPIERAA EDYLIGLAGV YPHADYVTVN 190 200 210 220 230 240 ISSPNTKNLR ALQGGDELSA LLGQLQERRL ALADQHQRHV PLAVKIAPDL SDDQIDAIAE 250 260 270 280 290 300 ILPRHGIDGV IATNTTLARD AVQGLPHAEE AGGVSGAPVH ELSLRVIERL RSRLGDAVAI 310 320 330 340 IGVGGILSGR QASEKMAAGA QAVQLYTGLI YRGPALVGEC VRALAQGSR

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640421 Genomic DNA. Translation: CAE43705.1.
RefSeq	NP_881968.1.
3D structure databases
SMR	Q7VTR9. Positions 8-344.
ModBase	Search...
Genome annotation databases
GeneID	2666939.
KEGG	bpe:BP3442.
NMPDR	fig|257313.1.peg.3038.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG351027.
OMA	AALNRMG.
PhylomeDB	Q7VTR9.
Enzyme and pathway databases
BioCyc	BPER257313:BP3442-MONOMER.
BRENDA	1.3.3.1. 21511.
Family and domain databases
HAMAP	MF_00225. DHO_dh_type2. [Tree]
InterPro	IPR013785. Aldolase_TIM. IPR012135. Dihydroorotate_DH_1_2. IPR005719. Dihydroorotate_DH_2. IPR001295. Dihydroorotate_DH_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
Pfam	PF01180. DHO_dh. 1 hit. [Graphical view]
PIRSF	PIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMs	TIGR01036. pyrD_sub2. 1 hit.
PROSITE	PS00911. DHODEHASE_1. 1 hit. PS00912. DHODEHASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRD_BORPE

Accession

Primary (citable) accession number: Q7VTR9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 1, 2003
Last modified:	February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)