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Q5HPZ0 (PYRC_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 64. 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:SERP0767
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00220

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-Rule MF_00220

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Dihydroorotase HAMAP-Rule MF_00220
PRO_0000147253

Sites

Metal binding591Zinc 1 By similarity
Metal binding611Zinc 1 By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2311Zinc 2 By similarity
Metal binding3041Zinc 1 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HPZ0 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 95188955DCE466B1

FASTA42546,795
        10         20         30         40         50         60 
MKLIKNGKIL KNGILKDTEI LIDGKRIKQI SSKINASSSN IEVIDAKGNL IAPGFVDVHV 

        70         80         90        100        110        120 
HLREPGGEHK ETIESGTKAA ARGGFTTVCP MPNTRPVPDT VEHVRELRQR ISETAQVRVL 

       130        140        150        160        170        180 
PYAAITKRQA GTELVDFEKL ALEGVFAFTD DGVGVQTASM MYAAMKQAAK VKKPIVAHCE 

       190        200        210        220        230        240 
DNSLIYGGAM HKGKRSEELG IPGIPNIAES VQIARDVLLA EATGCHYHVC HVSTKESVRV 

       250        260        270        280        290        300 
IRDAKKAGIH VTAEVTPHHL LLTENDVPGD DSNYKMNPPL RSNEDREALL EGLLDGTIDC 

       310        320        330        340        350        360 
IATDHAPHAK EEKEQPMTKA PFGIVGSETA FPLLYTHFVR RGNWSLQQLV DYFTIKPATI 

       370        380        390        400        410        420 
FNLNYGKLHK DSYADLTIID LNTEKEIKSE DFLSKADNTP FIGEKVYGNP TLTMLKGEVV 


FEEEK

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References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000029 Genomic DNA. Translation: AAW54170.1.
RefSeqYP_188350.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HPZ0.
ModBaseSearch...

Protein-protein interaction databases

STRING176279.SERP0767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54170; AAW54170; SERP0767.
GeneID3242843.
KEGGser:SERP0767.
PATRIC19612405. VBIStaEpi130894_0745.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHOG000219142.
KOK01465.
OMAGKNSPFI.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-793-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_STAEQ
AccessionPrimary (citable) accession number: Q5HPZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: February 15, 2005
Last modified: May 1, 2013
This is version 64 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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