Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8K9Q1 (PYRF_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BUsg_260
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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_0000134533

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 site1861Substrate By similarity
Binding site1951Substrate By similarity
Binding site2151Substrate; via amide nitrogen By similarity
Binding site2161Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K9Q1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 5609A1CF78746BA7

FASTA23626,562
        10         20         30         40         50         60 
MLYTNNYNIP KIIIALDFYN KKEAMTLVDL LDPSVFYLKI GKEMFTILGF KFVKELHKLG 

        70         80         90        100        110        120 
FNVFLDLKFH DIPNTVFNAT KAAADLGIWM LSVHASGGKN MLLSAKKALK SFKKPPLLIA 

       130        140        150        160        170        180 
VTMLTSLKEK DLKEIGIKIS LKDYILILSK LSNDCGLDGI VCPGNQAKKI KSLYGDKYKI 

       190        200        210        220        230 
ITPGIRLSSD SSFDQKHIIT PKEAKEFQID YIVIGRSITT SKNPIKKLNL IIESMR 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67818.1.
RefSeqNP_660607.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8K9Q1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING198804.BUsg260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM67818; AAM67818; BUsg_260.
GeneID1005462.
KEGGbas:BUsg260.
PATRIC21247325. VBIBucAph100086_0272.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycBAPH198804:GHMG-274-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_BUCAP
AccessionPrimary (citable) accession number: Q8K9Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 77 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

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names