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Reviewed, UniProtKB/Swiss-Prot Q9RVC3 (PYRC_DEIRA)

Last modified June 16, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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: DR_1106
OrganismDeinococcus radiodurans [Complete proteome] [HAMAP]
Taxonomic identifier1299 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

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Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6. HAMAP MF_00220

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Dihydroorotase HAMAP MF_00220
PRO_0000147233

Regions

Compositional bias200 – 2056Poly-Ala HAMAP MF_00220

Sites

Metal binding531Zinc 1 By similarity
Metal binding551Zinc 1 By similarity
Metal binding1351Zinc 1; via carbamate group By similarity
Metal binding1351Zinc 2; via carbamate group By similarity
Metal binding1721Zinc 2 By similarity
Metal binding2251Zinc 2 By similarity
Metal binding2981Zinc 1 By similarity

Amino acid modifications

Modified residue1351N6-carboxylysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9RVC3-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 087BCD29EA156BE7

FASTA41644,917
        10         20         30         40         50         60 
MTITITNIKR VGSEQTESLT IENGLIKGWN LPAEGEIFDG QGGTLAPALI ELHAHLREPG 

        70         80         90        100        110        120 
QTEKEDLASG LAAASAGGYG TVVCMPNTRP VIDDPALVRS LIEKARGLGF ARLRPAAAVT 

       130        140        150        160        170        180 
KGEKGEQLTE MSYLKEAGAV MFTDDGLTNE NARVLRLGME YAKSLGMVIS VHAEDDALRA 

       190        200        210        220        230        240 
GGVMNEGPVS ESLGLPGNPA AAAAARVARD MEIVALTGAR LHVQHLSTAR ELDIVRDAKR 

       250        260        270        280        290        300 
RGLPVTCEVC PHHLDLTDES LRTFDAMYKV APPLRTRADA DYLLEGLLDG SVDCIATDHA 

       310        320        330        340        350        360 
PHTRAEKERD LLDAPSGIAY IEIAFPIMWT RFGERLGLEK LIDLMTAGPA RVMGWPEPSL 

       370        380        390        400        410 
EAGAPADMVV LDLETEREVN PAEFKSKAKF TPWQGQKLRG FPLLTVVDGK VAYRRE

« Hide

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Cross-references

Sequence databases

AE000513 Genomic DNA. Translation: AAF10679.1.
PIRE75437.
RefSeqNP_294830.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1797749.
GenomeReviewsGene locus DR_1106 in contig AE000513_GR.
KEGGdra:DR_1106.
NMPDRfig|243230.1.peg.1289.
TIGRDR_1106.

Phylogenomic databases

HOGENOMQ9RVC3.
OMAQ9RVC3. SHHQPHE.

Enzyme and pathway databases

BioCycDRAD243230:DR_1106-MON.
BRENDA3.5.2.3. 96172.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
ProDomPD000518. DHOase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePYRC_DEIRA
AccessionPrimary (citable) accession number: Q9RVC3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: June 16, 2009
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents