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C3LNL5 (PYRF_VIBCM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Orotidine 5'-phosphate decarboxylase

EC=4.1.1.23
Alternative name(s):
OMP decarboxylase
Short name=OMPDCase
Short name=OMPdecase
Gene names
Name:pyrF
Ordered Locus Names:VCM66_1835
OrganismVibrio cholerae serotype O1 (strain M66-2) [Complete proteome] [HAMAP]
Taxonomic identifier579112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length231 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) By similarity. HAMAP-Rule MF_01200

Catalytic activity

Orotidine 5'-phosphate = UMP + CO2. HAMAP-Rule MF_01200

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 2/2. HAMAP-Rule MF_01200

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01200

Sequence similarities

Belongs to the OMP decarboxylase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionorotidine-5'-phosphate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 231231Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000164586

Regions

Region60 – 6910Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site111Substrate By similarity
Binding site331Substrate By similarity
Binding site1201Substrate By similarity
Binding site1811Substrate By similarity
Binding site1901Substrate By similarity
Binding site2101Substrate; via amide nitrogen By similarity
Binding site2111Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C3LNL5 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: EB2E841A990B582C

FASTA23125,003
        10         20         30         40         50         60 
MNDPKVIVAL DYDNLADALA FVDKIDPSTC RLKVGKEMFT LFGPDFVREL HKRGFSVFLD 

        70         80         90        100        110        120 
LKFHDIPNTC SKAVKAAAEL GVWMVNVHAS GGERMMAASR EILEPYGKER PLLIGVTVLT 

       130        140        150        160        170        180 
SMESADLQGI GILSAPQDHV LRLATLTKNA GLDGVVCSAQ EASLLKQHLG REFKLVTPGI 

       190        200        210        220        230 
RPAGSEQGDQ RRIMTPAQAI ASGSDYLVIG RPITQAAHPE VVLEEINSSL V 

« Hide

References

[1]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M66-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001233 Genomic DNA. Translation: ACP06141.1.
RefSeqYP_002810592.1. NC_012578.1.

3D structure databases

ProteinModelPortalC3LNL5.
SMRC3LNL5. Positions 2-230.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING579112.VCM66_1835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP06141; ACP06141; VCM66_1835.
GeneID7773102.
KEGGvcm:VCM66_1835.
PATRIC20067410. VBIVibCho108967_1752.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMAVIASPHE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycVCHO579112:GJAW-1898-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_B. OMPdecase_type1_B.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
IPR018089. OMPdecase_AS.
IPR001754. OMPdeCOase_dom.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PfamPF00215. OMPdecase. 1 hit.
[Graphical view]
SMARTSM00934. OMPdecase. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR01740. pyrF. 1 hit.
PROSITEPS00156. OMPDECASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRF_VIBCM
AccessionPrimary (citable) accession number: C3LNL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways