Reviewed, UniProtKB/Swiss-Prot Q2NCC9 (PYRC_ERYLH)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	ELI_02850

Organism

Erythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]

Taxonomic identifier

314225 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter

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 + H(2)O = N-carbamoyl-L-aspartate.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.
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		PRO_1000024014
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)
	Q2NCC9-1 [UniParc]. Last modified February 7, 2006. Version 1. Checksum: A0E7989C2B46FD83	FASTA	344	37,576
	10 20 30 40 50 60 MTETLTIRRP DDWHLHFRDG AMMRGVVPYT ARQFARAIVM PNLTPPVTTT ALGAAYRERI 70 80 90 100 110 120 LAAVPEGVDF RPLMTAYLTD ETDADDLIDG YTHGVFTAAK LYPANATTNS ASGVTDVEAL 130 140 150 160 170 180 YPVFERMAAA GMVLCIHGEV TDADVDVFDR EKEFIERTMA PLHAAIPALK IAFEHITTSD 190 200 210 220 230 240 AVDFVVGAND NIGATITPQH LHINRNAMLV GGIQPHNYCL PVAKRETHRL ALRQAATSGP 250 260 270 280 290 300 PKFFLGTDSA PHEKHTKESA CGCAGIFGAP YALESYLAVF EEEDALDKFE AFASLNGPAF 310 320 330 340 YGLPVNDETI TLERVPHNVP DSLETEGGKV VPFHAGQELN WRLK

References

[1]	Giovannoni S.J., Cho J.-C., Ferriera S., Johnson J., Kravits S., Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000157 Genomic DNA. Translation: ABC62662.1.
RefSeq	YP_457459.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3869096.
GenomeReviews	Gene locus ELI_02850 in contig CP000157_GR.
KEGG	eli:ELI_02850.
NMPDR	fig|314225.3.peg.2511.
Organism-specific databases
CMR	Search...
Enzyme and pathway databases
BioCyc	ELIT314225:ELI_02850-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_ERYLH

Accession

Primary (citable) accession number: Q2NCC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	February 7, 2006
Last modified:	November 25, 2008
This is version 18 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)