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B2AH54 (PYRC_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 29. 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:RALTA_A0435
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus

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_1000100039

Sites

Metal binding141Zinc 1 By similarity
Metal binding161Zinc 1 By similarity
Metal binding1001Zinc 1; via carbamate group By similarity
Metal binding1001Zinc 2; via carbamate group By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1751Zinc 2 By similarity
Metal binding2481Zinc 1 By similarity

Amino acid modifications

Modified residue1001N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2AH54 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 44B55466A1D3DDD8

FASTA34437,579
        10         20         30         40         50         60 
MTQKLTITRP DDWHLHLRDG AALAAVLPDT ARQFARAIVM PNLKPPVTTV AQAQAYRARI 

        70         80         90        100        110        120 
LAALPAGMQF EPLMTLYLTD NTGPEEIAAA RASGFVHGVK LYPAGATTNS DAGVTDIRRC 

       130        140        150        160        170        180 
YPALEAMQRA GLPLLVHGEV TDPAIDIFDR EAVFIERVMT PLRRDMPELK VVFEHITTKD 

       190        200        210        220        230        240 
AAQYVRDASG PVGATITAHH LLYNRNAIFT GGIRPHYYCL PVLKRETHRE ALVAAATSGS 

       250        260        270        280        290        300 
ERFFLGTDSA PHARGLKEHA CGCAGCYTAL HAMELYAEAF DAAGALDKLE AFASFNGPAF 

       310        320        330        340 
YGLPRNTGTL TLEREDWELP AELPYGDTTL VPLRGGETLR WKAR

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU633749 Genomic DNA. Translation: CAP63103.1.
RefSeqYP_001795823.1. NC_010528.1.

3D structure databases

ProteinModelPortalB2AH54.
SMRB2AH54. Positions 2-344.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2AH54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6301314.
GenomeReviewsGene locus RALTA_A0435 in contig CU633749_GR.
KEGGcti:RALTA_A0435.
PATRIC21527512. VBICupTai42494_0440.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628648.
OMACLPVAKR.
ProtClustDBPRK05451.

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_CUPTR
AccessionPrimary (citable) accession number: B2AH54
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 29 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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