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Reviewed, UniProtKB/Swiss-Prot A5GF42 (PYRC_GEOUR)

Last modified September 2, 2008. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

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Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 3/6.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

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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: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Dihydroorotase
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

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Sequences

Sequence LengthMass (Da)Tools
A5GF42-1 [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

« Hide

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References

[1]"Complete sequence of Geobacter uraniireducens Rf4."
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].

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Cross-references

Sequence databases

CP000698 Genomic DNA. Translation: ABQ26047.1.
RefSeqYP_001230620.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

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

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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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: September 2, 2008
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents