Reviewed, UniProtKB/Swiss-Prot Q834E0 (PYRC_ENTFA)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	EF_1718

Organism

Enterococcus faecalis (Streptococcus faecalis) [Complete proteome] [HAMAP]

Taxonomic identifier

1351 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Lactobacillales › Enterococcaceae › Enterococcus

Protein attributes

Sequence length	427 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_00220
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_00220
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	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 – 427	427	Dihydroorotase HAMAP MF_00220		PRO_1000024082
Sites
	Metal binding	60	1	Zinc 1 By similarity
	Metal binding	62	1	Zinc 1 By similarity
	Metal binding	142	1	Zinc 1; via carbamate group By similarity
	Metal binding	142	1	Zinc 2; via carbamate group By similarity
	Metal binding	179	1	Zinc 2 By similarity
	Metal binding	232	1	Zinc 2 By similarity
	Metal binding	305	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	142	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q834E0-1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D7C715161F315D01	FASTA	427	46,058
	10 20 30 40 50 60 MKTLIKNGKI IKKENQLIEA ALWLENGVIH AIGESFDEAD FEQVFDANGQ LITPGLVDVH 70 80 90 100 110 120 VHFREPGFTY KETIKTGSKA AARGGFTTVC AMPNLNPVPD TAEKLSEVYD LIQKDAVVKV 130 140 150 160 170 180 LQYAPITEEL RSEVLTNQKA LKEAGAFAFT NDGVGVQTAG TMYLAMKEAA ALNMALVAHT 190 200 210 220 230 240 EDESLLFGGV MHEGEVSKKL GLPGILSATE ASQIARDITL AKETGVHYHV CHVSTEESVR 250 260 270 280 290 300 VIRDAKKAGI HVTAEVSPHH LILVDEDIPG DEGFWKMNPP LRGLADRQAL IDGLLDGTID 310 320 330 340 350 360 CIATDHAPHG LEEKQQSFLN APFGIVGSET AFQLIYTNFV ETGIFTLEQV IDWMAVKPAE 370 380 390 400 410 420 IFGLNAGTLT IGAPADIAVF DLATAAPIDA EAFESMAVNT PFTGWTVKGK TLMTFVDGAL AWSEEAQ

References

[1]

"Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus faecalis." Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R., Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin S.A. , Kolonay J.F., Madupu R., Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M. Science 299:2071-2074(2003) [PubMed: 12663927] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: V583 / ATCC 700802.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE016830 Genomic DNA. Translation: AAO81494.1.
RefSeq	NP_815424.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	1200610.
GenomeReviews	Gene locus EF_1718 in contig AE016830_GR.
KEGG	efa:EF1718.
NMPDR	fig|226185.1.peg.1609.
TIGR	EF_1718.
Phylogenomic databases
HOGENOM	Q834E0.
OMA	CDVHPVG.
Enzyme and pathway databases
BioCyc	EFAE226185:EF_1718-MON.
BRENDA	3.5.2.3. 704.
Family and domain databases
HAMAP	MF_00220. [Tree]
InterPro	IPR006680. Amidohydro_1. IPR004722. DHOmult. IPR002195. Dihydroorotase_CS. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
ProDom	PD000518. DHOase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00857. pyrC_multi. 1 hit.
PROSITE	PS00482. DIHYDROOROTASE_1. 1 hit. PS00483. DIHYDROOROTASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PYRC_ENTFA

Accession

Primary (citable) accession number: Q834E0

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	November 3, 2009
This is version 37 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)