B3BP79 (B3BP79_ECO57) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Dihydroorotase HAMAP MF_00219
Short name=DHOase HAMAP MF_00219
EC=3.5.2.3 HAMAP MF_00219

Gene names

Name:	pyrC HAMAP MF_00219 EMBL EDU88925.1
ORF Names:	ECH7EC869_2437 EMBL EDU88925.1

Organism

Escherichia coli O157:H7 str. EC869 EMBL EDU88925.1

Taxonomic identifier

478008 [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 SAAS SAAS004721
Cofactor	Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219 SAAS SAAS004721
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219 SAAS SAAS004721
Subunit structure	Homodimer By similarity. HAMAP MF_00219 SAAS SAAS004721
Sequence similarities	Belongs to the DHOase family. Type 1 subfamily. HAMAP MF_00219
Caution	The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. EMBL EDU88925.1

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis HAMAP MF_00219 SAAS SAAS004721
Ligand	Metal-binding HAMAP MF_00219 SAAS SAAS004721 Zinc HAMAP MF_00219 SAAS SAAS004721
Molecular function	Hydrolase HAMAP MF_00219 SAAS SAAS004721 EMBL EDU88925.1
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
Sites
	Metal binding	17	1	Zinc 1 By similarity HAMAP MF_00219
	Metal binding	19	1	Zinc 1 By similarity HAMAP MF_00219
	Metal binding	103	1	Zinc 1; via carbamate group By similarity HAMAP MF_00219
	Metal binding	103	1	Zinc 2; via carbamate group By similarity HAMAP MF_00219
	Metal binding	140	1	Zinc 2 By similarity HAMAP MF_00219
	Metal binding	178	1	Zinc 2 By similarity HAMAP MF_00219
	Metal binding	251	1	Zinc 1 By similarity HAMAP MF_00219
Amino acid modifications
	Modified residue	103	1	N6-carboxylysine By similarity HAMAP MF_00219

Sequences

	Sequence		Length	Mass (Da)
	B3BP79 [UniParc]. Last modified July 22, 2008. Version 1. 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 Signatures of Escherichia coli O157:H7 Isolates from the Bovine Host Reservoir." Eppinger M., Mammel M.K., Leclerc J.E., Ravel J., Cebula T.A. Appl. Environ. Microbiol. 77:2916-2925(2011) [PubMed: 21421787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: EC869 EMBL EDU88925.1.
[2]	Rosovitz M.J., Ravel J. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: EC869 EMBL EDU88925.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	ABHU01000030 Genomic DNA. Translation: EDU88925.1.
3D structure databases
ProteinModelPortal	B3BP79.
SMR	B3BP79. Positions 4-347.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
PATRIC	29373073. VBIEscCol71386_5028.
Phylogenomic databases
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

B3BP79_ECO57

Accession

Primary (citable) accession number: B3BP79

Entry history

Integrated into UniProtKB/TrEMBL:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	December 14, 2011
This is version 23 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)