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A5GF42 (PYRC_GEOUR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 36. 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:Gura_1857
OrganismGeobacter uraniireducens (strain Rf4) (Geobacter uraniumreducens) [Complete proteome] [HAMAP]
Taxonomic identifier351605 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter

Protein attributes

Sequence length425 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
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 – 425425Dihydroorotase HAMAP MF_00220_B
PRO_1000078107

Sites

Metal binding611Zinc 1 By similarity
Metal binding631Zinc 1 By similarity
Metal binding1431Zinc 1; via carbamate group By similarity
Metal binding1431Zinc 2; via carbamate group By similarity
Metal binding1801Zinc 2 By similarity
Metal binding2331Zinc 2 By similarity
Metal binding3061Zinc 1 By similarity

Amino acid modifications

Modified residue1431N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5GF42 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: AC06964FA760C291

FASTA42544,938
        10         20         30         40         50         60 
MNLLIKGGRV VDPSQNIDDT MDLLVEDGRI KEIGKGLKAP AGAEIIDAAG LLVTPGLIDM 

        70         80         90        100        110        120 
HVHLRDPGLE YKEDIVTGTR AAAAGGFTSV ACMPNTKPVN DNKAITSYIV NKAAKEALVN 

       130        140        150        160        170        180 
VFPVGSITQG SKGESLAEMG ELKESGCVAV SDDGRPVVNG ELMRRALEYA KGMGIMVISH 

       190        200        210        220        230        240 
SEELALVGEG VMNEGFTATE LGLKGIPWAA EDVAVARDVY LAEFTDSPLH IAHISTSGSV 

       250        260        270        280        290        300 
RIIRNAKARG VKVTCETAPH YFSLTDDAVR GYNTNAKMNP PLREAADVAA IKAGLADGTI 

       310        320        330        340        350        360 
DAIATDHAPH HLDEKDLEFN LALNGIVGLE TSLPLSLQLV EEGVVDLKVL LEKMTCNPAK 

       370        380        390        400        410        420 
ILGIDRGTLK VGAAADITVI DPDREWLVAA EKLASKSKNS PFIGRKMKGA AVYTVVGGKV 


VYKID

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References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M., Lovley D., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Rf4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000698 Genomic DNA. Translation: ABQ26047.1.
RefSeqYP_001230620.1. NC_009483.1.

3D structure databases

ProteinModelPortalA5GF42.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5GF42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5166201.
GenomeReviewsGene locus Gura_1857 in contig CP000698_GR.
KEGGgur:Gura_1857.
NMPDRfig|351605.3.peg.377.
PATRIC22033812. VBIGeoUra13052_1987.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
OMACDVHPVG.
ProtClustDBCLSK828273.

Enzyme and pathway databases

BioCycGURA351605:GURA_1857-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. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_GEOUR
AccessionPrimary (citable) accession number: A5GF42
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: January 25, 2012
This is version 36 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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