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Q1CI09 (PYRC_YERPN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:YPN_2042
ORF Names:YP516_2274
OrganismYersinia pestis bv. Antiqua (strain Nepal516) [Complete proteome] [HAMAP]
Taxonomic identifier377628 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length348 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP-Rule MF_00219

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00219

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP-Rule MF_00219

Subunit structure

Homodimer By similarity. HAMAP-Rule 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_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydroorotase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 348348Dihydroorotase HAMAP-Rule MF_00219
PRO_1000024075

Sites

Metal binding171Zinc 1 By similarity
Metal binding191Zinc 1 By similarity
Metal binding1031Zinc 1; via carbamate group By similarity
Metal binding1031Zinc 2; via carbamate group By similarity
Metal binding1401Zinc 2 By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2511Zinc 1 By similarity

Amino acid modifications

Modified residue1031N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1CI09 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: B9215D6E02697221

FASTA34838,542
        10         20         30         40         50         60 
MTAQPQTLKI RRPDDWHIHL RDDEMLSTVL PYTSEVFARA IVMPNLAQPI TTVASAIAYR 

        70         80         90        100        110        120 
ERILAAVPAG HKFTPLMTCY LTNSLDAKEL TTGFEQGVFT AAKLYPANAT TNSTHGVSDI 

       130        140        150        160        170        180 
PAIYPLFEQM QKIGMPLLIH GEVTDAAVDI FDREARFIDQ ILEPIRQKFP ELKIVFEHIT 

       190        200        210        220        230        240 
TKDAADYVLA GNRFLGATVT PQHLMFNRNH MLVGGIRPHL FCLPILKRST HQQALRAAVA 

       250        260        270        280        290        300 
SGSDRFFLGT DSAPHAKHRK ESSCGCAGVF NAPAALPAYA SVFEELNALQ HLEAFCALNG 

       310        320        330        340 
PRFYGLPVND DVVELVRTPF LQPEEIPLGN ESVIPFLAGQ TLNWSVKR 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nepal516.
[2]"Yersinia pestis Nepal516A whole genome shotgun sequencing project."
Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L., Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R., Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.
Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000305 Genomic DNA. Translation: ABG18371.1.
ACNQ01000012 Genomic DNA. Translation: EEO76520.1.
RefSeqYP_647971.1. NC_008149.1.

3D structure databases

ProteinModelPortalQ1CI09.
SMRQ1CI09. Positions 6-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING377628.YPN_2042.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG18371; ABG18371; YPN_2042.
EEO76520; EEO76520; YP516_2274.
GeneID4126092.
KEGGypn:YPN_2042.
PATRIC18603582. VBIYerPes46733_2451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHOG000256259.
KOK01465.
OMALKRNVHQ.
OrthoDBEOG6TFCMH.

Enzyme and pathway databases

BioCycYPES377628:GIXK-2103-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. pyrC_dimer. 1 hit.
PROSITEPS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_YERPN
AccessionPrimary (citable) accession number: Q1CI09
Secondary accession number(s): C4GU08
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways