Reviewed, UniProtKB/Swiss-Prot B7NL72 (PYRC_ECO7I)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	ECIAI39_2101

Organism

Escherichia coli O7:K1 (strain IAI39 / ExPEC) [Complete proteome] [HAMAP]

Taxonomic identifier

585057 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
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. HAMAP MF_00219
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219
Subunit structure	Homodimer By similarity. HAMAP MF_00219
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 HAMAP MF_00219		PRO_1000193074
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)
	B7NL72-1 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: E59FA63A66341047	FASTA	348	38,843
	10 20 30 40 50 60 MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 70 80 90 100 110 120 QRILDTVPAG 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 TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ

References

[1]

"Organised genome dynamics in the Escherichia coli species results in highly diverse adaptive paths." Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P., Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E. , Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C., Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E. PLoS Genet. 5:E1000344-E1000344(2009) [PubMed: 19165319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU928164 Genomic DNA. Translation: CAR18228.1.
RefSeq	YP_002408064.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	7153440.
GenomeReviews	Gene locus ECIAI39_2101 in contig CU928164_GR.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG628648.
OMA	CLPVAKR.
Family and domain databases
HAMAP	MF_00219. PyrC_type1. [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_ECO7I

Accession

Primary (citable) accession number: B7NL72

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 10, 2009
Last modified:	February 9, 2010
This is version 12 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)