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Q1CTU5 (PYRC_HELPH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:HPAG1_0560
OrganismHelicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP]
Taxonomic identifier357544 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceInferred 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 processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Dihydroorotase HAMAP MF_00219
PRO_1000024017

Sites

Metal binding121Zinc 1 By similarity
Metal binding141Zinc 1 By similarity
Metal binding941Zinc 1; via carbamate group By similarity
Metal binding941Zinc 2; via carbamate group By similarity
Metal binding1331Zinc 2 By similarity
Metal binding1671Zinc 2 By similarity
Metal binding2391Zinc 1 By similarity

Amino acid modifications

Modified residue941N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CTU5 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: E8FC35F5706158CA

FASTA33938,044
        10         20         30         40         50         60 
MEITLFDPID AHLHVRENAL LKAVLRYSSE PFSAAVIMPN LSKPLIDTPT TLEYEEEILK 

        70         80         90        100        110        120 
NSSNFKPLMS LYFNDDLTLE ELQRAHEKGV RFLKLYPKGM TTNAQNGTSD LLDEKTLEIL 

       130        140        150        160        170        180 
ENAQKLGFIL CIHAEQAGFC LDKEFLCHSV LETFALSFPK LKIIIEHLSD WRSIALIEKH 

       190        200        210        220        230        240 
DNLYATLTLH HISMTLDDLL GGSLNPHCFC KPLIKTKKDQ ERLLSLALKA HPKISFGSDS 

       250        260        270        280        290        300 
APHFVSKKHS ANIPAGIFSA PILLPALCEL FEKHNALENL QAFISNNAKT IYGLDNLPSK 

       310        320        330 
KARLSKKPFI VPTHALCLNE KIAILRGGET LSWNLQEIA

« Hide

References

[1]"The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression."
Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed: 16788065] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HPAG1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000241 Genomic DNA. Translation: ABF84627.1.
RefSeqYP_627301.1. NC_008086.1.

3D structure databases

ProteinModelPortalQ1CTU5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1CTU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4099416.
GenomeReviewsGene locus HPAG1_0560 in contig CP000241_GR.
KEGGhpa:HPAG1_0560.
PATRIC20602463. VBIHelPyl56048_0580.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHBG628648.
OMACLPVAKR.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycHPYL357544:HPAG1_0560-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006992. Amidohydro_2.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF04909. Amidohydro_2. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. PyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_HELPH
AccessionPrimary (citable) accession number: Q1CTU5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: January 25, 2012
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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