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Q89AL6 (PYRF_BUCBP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:
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:bbp_251
OrganismBuchnera aphidicola subsp. Baizongia pistaciae (strain Bp) [Complete proteome] [HAMAP]
Taxonomic identifier224915 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera ›

Protein attributes

Sequence length236 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 – 236236Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134534

Regions

Region66 – 7510Substrate binding By similarity

Sites

Active site681Proton donor By similarity
Binding site171Substrate By similarity
Binding site391Substrate By similarity
Binding site1251Substrate By similarity
Binding site1871Substrate By similarity
Binding site1961Substrate By similarity
Binding site2161Substrate; via amide nitrogen By similarity
Binding site2171Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89AL6 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 3F730373627D2E9D

FASTA23626,565
        10         20         30         40         50         60 
MHLKSNFKNI NIIIALDFFD ENKAMKFIYN LNPTIYALKI GNIMFTLFGV RFIKILQKLG 

        70         80         90        100        110        120 
FKIFLDLKFY DIPNTIFGAI QAVANLNIWM VSIHISGGIQ MLKSARLALK PFKNKPLLMG 

       130        140        150        160        170        180 
VTILTSLDKT DMSKLGIQIS LSKYILSLAK IAHKCNLDGI ICSGTEISNI KKHINVKNFK 

       190        200        210        220        230 
ILTPGIRLNG CSSNDQKNVT TPMLAKQYNV DYIIIGRIVT SSQNPLKTLE LIRSQI

« Hide

References

[1]"Reductive genome evolution in Buchnera aphidicola."
van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F., Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J., Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.
Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bp.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016826 Genomic DNA. Translation: AAO26978.1.
RefSeqNP_777873.1. NC_004545.1.

3D structure databases

ProteinModelPortalQ89AL6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224915.bbp251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAO26978; AAO26978; bbp_251.
GeneID1058214.
KEGGbab:bbp251.
PATRIC21245283. VBIBucAph80364_0244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycBAPH224915:GJ9D-251-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_BUCBP
AccessionPrimary (citable) accession number: Q89AL6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: May 14, 2014
This is version 75 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

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