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Q9RVC3 (PYRC_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. 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:DR_1106
OrganismDeinococcus radiodurans
Taxonomic identifier1299 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220_B

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00220_B

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220_B

Subunit structure

Homodimer By similarity. HAMAP MF_00220_B

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processpyrimidine 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 – 416416Dihydroorotase HAMAP MF_00220_B
PRO_0000147233

Regions

Compositional bias200 – 2056Poly-Ala HAMAP MF_00220_B

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

Sequences

Sequence LengthMass (Da)Tools
Q9RVC3 [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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF10679.1.
PIRE75437.
RefSeqNP_294830.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RVC3.
SMRQ9RVC3. Positions 16-416.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1797749.
GenomeReviewsGene locus DR_1106 in contig AE000513_GR.
KEGGdra:DR_1106.
NMPDRfig|243230.1.peg.1289.
PATRIC21629800. VBIDeiRad64572_1302.
TIGRDR_1106.

Phylogenomic databases

HOGENOMHBG724623.
OMASHHQPHE.
PhylomeDBQ9RVC3.
ProtClustDBPRK09357.

Enzyme and pathway databases

BioCycDRAD243230:DR_1106-MONOMER.

Family and domain databases

HAMAPMF_00220_B. PyrC_type2_B.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOase.
IPR002195. Dihydroorotase_CS.
IPR011059. Metal-dep_hydrolase_composite.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
SUPFAMSSF51338. Metalo_hydrolase. 1 hit.
TIGRFAMsTIGR00857. PyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. False negative.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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: January 25, 2012
This is version 87 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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