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

B8D7G7 (PYRF_BUCAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:BUAPTUC7_267
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7) [Complete proteome] [HAMAP]
Taxonomic identifier561501 [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_1000164563

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
B8D7G7 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: AD776041A49EE520

FASTA23626,480
        10         20         30         40         50         60 
MLNPNIFHMP KIIIALDFCN KKSAMKLVNL LNPSIFYLKI GKEMFTILGC KFVKELHQLG 

        70         80         90        100        110        120 
FNIFLDLKFH DIPNTVFNAT KAAADLGIWM LSVHASGGKE MLISAKKALK SFKKAPLLIA 

       130        140        150        160        170        180 
VTALTSFKEE ALKEIGINIS LTEYILKLSK LSNDCGLDGI VCPGKEAKKI KFLFGNKYKI 

       190        200        210        220        230 
ITPGIRIAKD LLYDQNNIIT PKEAKEYKID YIVIGRSITM SKNPIKKLDL IIKSMQ 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuc7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001158 Genomic DNA. Translation: ACL30082.1.
RefSeqYP_002468577.1. NC_011834.1.

3D structure databases

ProteinModelPortalB8D7G7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561501.BUAPTUC7_267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30082; ACL30082; BUAPTUC7_267.
GeneID7263119.
KEGGbau:BUAPTUC7_267.
PATRIC21248619. VBIBucAph26317_0264.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycBAPH561501:GHRN-266-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_BUCAT
AccessionPrimary (citable) accession number: B8D7G7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 38 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