Dihydroorotase - Escherichia coli O9:H4 (strain HS)

Names and origin

Protein names

Recommended name:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3

Gene names

Name:	pyrC
Ordered Locus Names:	EcHS_A1185

Organism

Escherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]

Taxonomic identifier

331112 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	348 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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; UMP from HCO(3)(-): step 3/6. HAMAP MF_00219
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the DHOase family. Type 1 subfamily.

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Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	3D-structure 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...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 348

348

Dihydroorotase HAMAP MF_00219

PRO_1000058649

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

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Sequences

Sequence

Length

Mass (Da)

Tools

A7ZZ20-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 2EFEA36B232519A0
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FASTA

348

38,813

        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 
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

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References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

+

Additional computationally mapped references.

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Cross-references

Sequence databases

CP000802 Genomic DNA. Translation: ABV05524.1.

RefSeq

YP_001457907.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2Z27	X-ray	1.87	A	2-348	[»]

ModBase

Search...

Genome annotation databases

GeneID

5594408.

GenomeReviews

Gene locus EcHS_A1185 in contig CP000802_GR.

KEGG

ecx:EcHS_A1185.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

A7ZZ20. 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...

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Entry information

Entry name

PYRC_ECOHS

Accession

Primary (citable) accession number: A7ZZ20

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	June 16, 2009
This is version 11 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families