Reviewed, UniProtKB/Swiss-Prot Q0VNK6 (PYRC_ALCBS)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	ABO_1794

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the DHOase family. Type 1 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular function	dihydroorotase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Dihydroorotase HAMAP MF_00219		PRO_0000325567
Sites
	Metal binding	14	1	Zinc 1 By similarity
	Metal binding	16	1	Zinc 1 By similarity
	Metal binding	100	1	Zinc 1; via carbamate group By similarity
	Metal binding	100	1	Zinc 2; via carbamate group By similarity
	Metal binding	137	1	Zinc 2 By similarity
	Metal binding	175	1	Zinc 2 By similarity
	Metal binding	248	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	100	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VNK6-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 11BB1FED181C7F0F	FASTA	344	38,001
	10 20 30 40 50 60 MTDSLTIARP DDWHLHFRDG DLLAETVPAT ANVFGRAIVM PNLTPPVNTV AEAAEYRERI 70 80 90 100 110 120 LAQVPAGVNF EPLMVLYLTD STPVQEVERA ANSDFVHALK LYPAGATTNS DSGVTDPGKI 130 140 150 160 170 180 THLYEAMEKH DVPLLVHGEV TDAEVDIFDR ERVFIDRYLA DIRDQFPALR IVFEHVTTAE 190 200 210 220 230 240 GVNFVREANA LTAATVTPQH LLMNRNDLLV GGVRPHNYCL PILKRRQHQE AIQKAVIEGN 250 260 270 280 290 300 SRFFLGTDSA PHARTKKEAA CGCAGCYSAR AALPLYATFL EQHNALDKLE GFASHFGADF 310 320 330 340 YRLPRHTDTV TLVRKPWAVP TVIDAAGEPV VPFFAGEQLP WSLG

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL17242.1.
RefSeq	YP_693514.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0VNK6.
Genome annotation databases
GeneID	4211156.
GenomeReviews	Gene locus ABO_1794 in contig AM286690_GR.
KEGG	abo:ABO_1794.
NMPDR	fig|393595.12.peg.1799.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VNK6.
OMA	IMPNLVP.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1794-MON.
Family and domain databases
HAMAP	MF_00219. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004721. DHOdimr. IPR002195. Dihydroorotase_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
PIRSF	PIRSF001237. DHOdimr. 1 hit.
TIGRFAMs	TIGR00856. pyrC_dimer. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_ALCBS

Accession

Primary (citable) accession number: Q0VNK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 18, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 29 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)