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Q5P6Y5 (PYRC_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. 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:AZOSEA08010
ORF Names:ebA1456
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

Protein attributes

Sequence length344 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 – 344344Dihydroorotase HAMAP MF_00219
PRO_0000325570

Sites

Metal binding131Zinc 1 By similarity
Metal binding151Zinc 1 By similarity
Metal binding991Zinc 1; via carbamate group By similarity
Metal binding991Zinc 2; via carbamate group By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2471Zinc 1 By similarity

Amino acid modifications

Modified residue991N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5P6Y5 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 75E74BD36B3B7FC3

FASTA34437,310
        10         20         30         40         50         60 
MQTISLIRPD DWHLHVRDGA ALATVVPHTA RRFGRALIMP NLRPPVTTAA QALEYRARIL 

        70         80         90        100        110        120 
AAVPPGQHFE PLMSLYLTDN TSPDEIDRAK ASGAVVAVKL YPAGATTNSD AGVTAIEKVH 

       130        140        150        160        170        180 
AVLERMEKLG MVLCVHGEVT HGDVDVFDRE QVFIEQVLAP LVARFPALRV VFEHITTAEA 

       190        200        210        220        230        240 
ARFVQDAGPN VAATVTAHHL LLNRNAIFAG GIRPHHYCLP VLKRETHRRA LVEAATSGNA 

       250        260        270        280        290        300 
KFFLGTDSAP HSRAAKETAC GCAGCYTAHA AIELYAEAFE QAGALDRLEA FASLNGPAFY 

       310        320        330        340 
GLAPNAERIT LAKDAWEVPG EYEYLHDDPL VPLRAGETVA WRVL

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI06926.1.
RefSeqYP_157827.1. NC_006513.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
ProteinModelPortalQ5P6Y5.
SMRQ5P6Y5. Positions 2-343.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P6Y5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3181227.
GenomeReviewsGene locus AZOSEA08010 in contig CR555306_GR.
KEGGeba:ebA1456.
NMPDRfig|76114.4.peg.353.
PATRIC20967695. VBIAroAro98752_0808.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHBG628648.
OMACLPVAKR.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycASP76114:EBA1456-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 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_AROAE
AccessionPrimary (citable) accession number: Q5P6Y5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 47 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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