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Q6FD29 (PYRC_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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:ACIAD1150
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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_1000024007

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
Q6FD29 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: DE11304473479E6E

FASTA34438,867
        10         20         30         40         50         60 
MDTITLLQPD DWHAHLRDGL ALKRTVPDLA QQFARAICMP NLVPPVKTVD EAEAYRERIM 

        70         80         90        100        110        120 
AHVPEGVHFD PRMVLYFTDH TSPSEVKKIK DSAHVNAIKL YPAGATTNSD NGVSDIRKVY 

       130        140        150        160        170        180 
AVIEQLEEHQ VPLLLHGEVT HHHVDIFDRE KRFLDEVLSP LLKQFPKLKL VLEHITTSEA 

       190        200        210        220        230        240 
AHFVLEQDRN VAATITPQHL LFNRNDMLVG GIKPHFYCLP ILKRQTHQQT LIEVATSGNP 

       250        260        270        280        290        300 
KFFLGTDSAP HSKNAKENAC GCAGCYSAPT AIELYAQAFD QVNKIERLEG FASHFGADFY 

       310        320        330        340 
GLPRNTNTIT LVKEDQIIPE QLDYLDDEKI IPLYAGKTIQ WRKV

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR543861 Genomic DNA. Translation: CAG68030.1.
RefSeqYP_045852.1. NC_005966.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
ProteinModelPortalQ6FD29.
SMRQ6FD29. Positions 2-342.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FD29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2879564.
GenomeReviewsGene locus ACIAD1150 in contig CR543861_GR.
KEGGaci:ACIAD1150.
NMPDRfig|62977.3.peg.65.
PATRIC20740141. VBIAciSp98416_1030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHBG628648.
OMACLPVAKR.
PhylomeDBQ6FD29.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycASP62977:ACIAD1150-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_ACIAD
AccessionPrimary (citable) accession number: Q6FD29
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
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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