Q8X8N8 (PYRC_ECO57) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	Z1699, ECs1440

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule 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-Rule 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	'de novo' UMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway pyrimidine nucleobase biosynthetic process Inferred from electronic annotation. Source: InterPro
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 348	347	Dihydroorotase HAMAP-Rule MF_00219		PRO_0000147207
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)
	Q8X8N8 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 057D1F6834446CA7	FASTA	348	38,844
	10 20 30 40 50 60 MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 70 80 90 100 110 120 QRILHAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSV 130 140 150 160 170 180 DAIMPVLERM 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 TFIELVREEH QVAESIALTD DTLVPFLAGE TVRWSVKQ

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG55808.1. BA000007 Genomic DNA. Translation: BAB34863.1.
PIR	D85668. H90808.
RefSeq	NP_287196.1. NC_002655.2. NP_309467.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8X8N8.
SMR	Q8X8N8. Positions 4-347.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z1699.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG55808; AAG55808; Z1699. BAB34863; BAB34863; BAB34863.
GeneID	914110. 959400.
KEGG	ece:Z1699. ecs:ECs1440.
PATRIC	18352119. VBIEscCol44059_1286.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0418.
HOGENOM	HOG000256259.
KO	K01465.
OMA	FEHITTE.
ProtClustDB	PRK05451.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-1426-MONOMER.
UniPathway	UPA00070; UER00117.
Family and domain databases
HAMAP	MF_00219. PyrC_type1.
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_ECO57

Accession

Primary (citable) accession number: Q8X8N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program