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

Q12X87 (PYRF_METBU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:Mbur_1000
OrganismMethanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M) [Complete proteome] [HAMAP]
Taxonomic identifier259564 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanococcoides

Protein attributes

Sequence length215 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 – 215215Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065919

Regions

Region60 – 6910Substrate binding By similarity
Region170 – 18011Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site121Substrate By similarity
Binding site341Substrate By similarity
Binding site1171Substrate By similarity
Binding site1931Substrate; via amide nitrogen By similarity
Binding site1941Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12X87 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 41C32FD2B9344847

FASTA21522,814
        10         20         30         40         50         60 
MEKKNRLILA LDVTDRENAL RIANEVSDYV DSIKVGYPLV LGEGLSIVKE LVEIAPVIAD 

        70         80         90        100        110        120 
FKVADIPNTD RLICEHVFNA GAAGIITHGF TGRDSLDSCV KVANEFGTDV YVVTEMSHPG 

       130        140        150        160        170        180 
GVEFFRPVAE DIASMAVEAG ASGVVAPATR PERVKDIRKI IGEELSIISP GVGAQGGSAA 

       190        200        210 
DVIRAGADWV IVGRSIYNSD SPAEAAKKIC DEMNC 

« Hide

References

[1]"Complete sequence of Methanococcoides burtonii DSM 6242."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Kadner K., Aerts A., Dehal P., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Anderson I., Franzmann P., Thomas T., Saunders N., Cavicchioli R., Sowers K., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 6242 / NBRC 107633 / OCM 468 / ACE-M.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000300 Genomic DNA. Translation: ABE51939.1.
RefSeqYP_565689.1. NC_007955.1.

3D structure databases

ProteinModelPortalQ12X87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259564.Mbur_1000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE51939; ABE51939; Mbur_1000.
GeneID3998105.
KEGGmbu:Mbur_1000.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226069.
KOK01591.
OMATEMSHPG.

Enzyme and pathway databases

BioCycMBUR259564:GHBZ-1023-MONOMER.
UniPathwayUPA00070; UER00120.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01200_A. OMPdecase_type1_A.
InterProIPR013785. Aldolase_TIM.
IPR014732. OMPdecase.
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.
ProtoNetSearch...

Entry information

Entry namePYRF_METBU
AccessionPrimary (citable) accession number: Q12X87
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 56 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