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Q2NCC9 (PYRC_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 46. 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:ELI_02850
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Sphingomonadales › Erythrobacteraceae › Erythrobacter ›

Protein attributes

Sequence length344 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.

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.

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: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Dihydroorotase HAMAP-Rule MF_00219
PRO_1000024014

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
Q2NCC9 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: A0E7989C2B46FD83

FASTA34437,576
        10         20         30         40         50         60 
MTETLTIRRP DDWHLHFRDG AMMRGVVPYT ARQFARAIVM PNLTPPVTTT ALGAAYRERI 

        70         80         90        100        110        120 
LAAVPEGVDF RPLMTAYLTD ETDADDLIDG YTHGVFTAAK LYPANATTNS ASGVTDVEAL 

       130        140        150        160        170        180 
YPVFERMAAA GMVLCIHGEV TDADVDVFDR EKEFIERTMA PLHAAIPALK IAFEHITTSD 

       190        200        210        220        230        240 
AVDFVVGAND NIGATITPQH LHINRNAMLV GGIQPHNYCL PVAKRETHRL ALRQAATSGP 

       250        260        270        280        290        300 
PKFFLGTDSA PHEKHTKESA CGCAGIFGAP YALESYLAVF EEEDALDKFE AFASLNGPAF 

       310        320        330        340 
YGLPVNDETI TLERVPHNVP DSLETEGGKV VPFHAGQELN WRLK

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000157 Genomic DNA. Translation: ABC62662.1.
RefSeqYP_457459.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2NCC9.
SMRQ2NCC9. Positions 2-344.
ModBaseSearch...

Protein-protein interaction databases

STRING314225.ELI_02850.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC62662; ABC62662; ELI_02850.
GeneID3869096.
KEGGeli:ELI_02850.
PATRIC21858252. VBIEryLit102657_0569.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHOG000256259.
KOK01465.
OMAFEHITTE.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycELIT314225:GHLE-613-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.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_ERYLH
AccessionPrimary (citable) accession number: Q2NCC9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 46 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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