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Q39US3 (PYRC_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:Gmet_1770
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter

Protein attributes

Sequence length424 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.

Sequence caution

The sequence ABB32001.1 differs from that shown. Reason: Erroneous initiation.

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 – 424424Dihydroorotase HAMAP MF_00220_B
PRO_0000325594

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
Q39US3 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 0DC8AA0CE041462B

FASTA42444,713
        10         20         30         40         50         60 
MNLLIQGGRV IDPSQGIDEV LDILVENGAV KELGKGVKAP SGTETIDASG LIVTPGLIDM 

        70         80         90        100        110        120 
HVHLRDPGHE YKEDIVSGTK AAAAGGFTSV ACMPNTKPVN DNKAVTSYII AKAKAEGSVN 

       130        140        150        160        170        180 
VFPVGSITQG SKGELLSEMG ELKESGCVAV SDDGHPVTNS ELMRRALEYA KGMGIMVISH 

       190        200        210        220        230        240 
AEDLSLVGAG VMNEGFVSTE LGLKGIPWAA EDAATARDVY LAEFTDSPLH IAHVSTKGSL 

       250        260        270        280        290        300 
RIIRNAKARG VKVTCETAPH YFSLTDDAVR GYDTNAKMNP PLRTADDVTA VKEALKDGTI 

       310        320        330        340        350        360 
DAIATDHAPH HIDEKDLEFN EALNGIVGLE TSLTLSLRLV EEGVLTLPVL VDKMACNPAK 

       370        380        390        400        410        420 
ILGIDRGTLK PGSVADITVI DPKATWTVDA DKLASKSKNS PFLGWEVKGA AAFTIVGGKV 


VYKR

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000148 Genomic DNA. Translation: ABB32001.1. Different initiation.
RefSeqYP_384726.2. NC_007517.1.

3D structure databases

ProteinModelPortalQ39US3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ39US3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3741446.
GenomeReviewsGene locus Gmet_1770 in contig CP000148_GR.
KEGGgme:Gmet_1770.
NMPDRfig|269799.3.peg.2087.
PATRIC22002774. VBIGeoMet55070_1812.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0044.
HOGENOMHBG724623.
ProtClustDBCLSK828273.

Enzyme and pathway databases

BioCycGMET269799:GMET_1770-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_GEOMG
AccessionPrimary (citable) accession number: Q39US3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: January 25, 2012
This is version 42 of the entry and version 2 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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