Reviewed, UniProtKB/Swiss-Prot Q0TJ12 (PYRC_ECOL5)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	ECP_1054

Organism

Escherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

362663 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	348 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 – 348	348	Dihydroorotase		PRO_1000024010
Sites
	Metal binding	17	1	Zinc 1 By similarity
	Metal binding	19	1	Zinc 1 By similarity
	Metal binding	103	1	Zinc 1; via carbamate group By similarity
	Metal binding	103	1	Zinc 2; via carbamate group By similarity
	Metal binding	140	1	Zinc 2 By similarity
	Metal binding	178	1	Zinc 2 By similarity
	Metal binding	251	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	103	1	N6-carboxylysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0TJ12-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: D64F8849910E3CCC	FASTA	348	38,827
	10 20 30 40 50 60 MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 70 80 90 100 110 120 QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV 130 140 150 160 170 180 DAIMPILERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT 190 200 210 220 230 240 TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVA 250 260 270 280 290 300 SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG 310 320 330 340 PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ

References

[1]

"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536." Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J. Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000247 Genomic DNA. Translation: ABG69067.1.
RefSeq	YP_668968.1.
3D structure databases
SMR	Q0TJ12. Positions 5-347.
ModBase	Search...
Genome annotation databases
GeneID	4189711.
GenomeReviews	Gene locus ECP_1054 in contig CP000247_GR.
KEGG	ecp:ECP_1054.
NMPDR	fig|340197.3.peg.2560.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0TJ12.
Enzyme and pathway databases
BioCyc	ECOL362663:ECP_1054-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_ECOL5

Accession

Primary (citable) accession number: Q0TJ12

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	November 25, 2008
This is version 23 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)