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Q7VIJ1 (PYRC_HELHP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:HH_0614
OrganismHelicobacter hepaticus (strain ATCC 51449 / 3B1) [Complete proteome] [HAMAP]
Taxonomic identifier235279 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter

Protein attributes

Sequence length343 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 – 343343Dihydroorotase HAMAP MF_00219
PRO_0000325572

Sites

Metal binding141Zinc 1 By similarity
Metal binding161Zinc 1 By similarity
Metal binding971Zinc 1; via carbamate group By similarity
Metal binding971Zinc 2; via carbamate group By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1701Zinc 2 By similarity
Metal binding2421Zinc 1 By similarity

Amino acid modifications

Modified residue971N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VIJ1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D11C3F0BA743F204

FASTA34338,495
        10         20         30         40         50         60 
MPQTLQLTNP MDMHLHLREG EMLSAILPFS ANPFSAAVVM PNLKTPITTT AQALAYKRQI 

        70         80         90        100        110        120 
LSLCSTSFEP LMSIFLTPDL DKQELIRAKE AGIHILKLYP KGSTTGSEKG VKEMLCEKTL 

       130        140        150        160        170        180 
HIFEIAQELG FILSIHGESN GFCMEREYEF LPIFAHIAQH FPRLRIIIEH MSDRRSLELI 

       190        200        210        220        230        240 
EQYPNLYATL TLHHITMNLD DVLGGGINPH HFCKPMLKTK KDQQALLQAA LNAHPKVSFG 

       250        260        270        280        290        300 
SDSAPHLESA KLNSKGAAGI FSAPILLPAL AEVFAFHNAL DCLQTFISNR AIANYKLKHF 

       310        320        330        340 
PIKTITLERV ENPVPPYINT PLGHIIPLRA QTNLSWRIKE ENR

« Hide

References

[1]"The complete genome sequence of the carcinogenic bacterium Helicobacter hepaticus."
Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M., Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R., Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B. expand/collapse author list , Shen Z., Weber J., Frosch M., Fox J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003) [PubMed: 12810954] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51449 / 3B1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017125 Genomic DNA. Translation: AAP77211.1.
RefSeqNP_860145.1. NC_004917.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
ProteinModelPortalQ7VIJ1.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1493668.
GenomeReviewsGene locus HH_0614 in contig AE017125_GR.
KEGGhhe:HH0614.
NMPDRfig|235279.1.peg.614.
PATRIC20588684. VBIHelHep90276_0616.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628648.
OMAMEREYEF.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycHHEP235279:HH_0614-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_HELHP
AccessionPrimary (citable) accession number: Q7VIJ1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 52 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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