Dihydroorotase - Escherichia coli (strain SE11)

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Reviewed, UniProtKB/Swiss-Prot B6I9D9 (PYRC_ECOSE)

Last modified November 3, 2009. Version 10. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	ECSE_1125

Organism

Escherichia coli (strain SE11) [Complete proteome] [HAMAP]

Taxonomic identifier

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 + H₂O = N-carbamoyl-L-aspartate. HAMAP 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 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	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

348

Dihydroorotase HAMAP MF_00219

PRO_1000100043

Sites

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1 By similarity

Metal binding

1

Zinc 1; via carbamate group By similarity

Metal binding

1

Zinc 2; via carbamate group By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 2 By similarity

Metal binding

1

Zinc 1 By similarity

Amino acid modifications

Modified residue

1

N6-carboxylysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

B6I9D9-1 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 13357FD2416721F1
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348

38,826

        10         20         30         40         50         60 
MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR 

        70         80         90        100        110        120 
QRILDAVPAG HNFTPLMTCY LTDSLDPNEL ERGFNEGVFT AAKLYPANAT TNSSHGVTSI 

       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]

"Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
DNA Res. 15:375-386(2008) [PubMed: 18931093] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
	AP009240 Genomic DNA. Translation: BAG76649.1.
RefSeq	YP_002292400.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	6999496.
GenomeReviews	Gene locus ECSE_1125 in contig AP009240_GR.
KEGG	ecy:ECSE_1125.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	IMPNLVP.
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_ECOSE

Accession

Primary (citable) accession number: B6I9D9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	December 16, 2008
Last modified:	November 3, 2009
This is version 10 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)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents