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Q7V0D8 (PYRF_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:PMM1328
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length239 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 – 239239Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134564

Regions

Region63 – 7210Substrate binding By similarity

Sites

Active site651Proton donor By similarity
Binding site151Substrate By similarity
Binding site361Substrate By similarity
Binding site1271Substrate By similarity
Binding site1891Substrate By similarity
Binding site1981Substrate By similarity
Binding site2181Substrate; via amide nitrogen By similarity
Binding site2191Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7V0D8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: EDE058FD602A8A18

FASTA23926,275
        10         20         30         40         50         60 
MKKFNTEEKI ILAIDGLDIF QAKVLLERCP NIKWVKVGLE LFTREGPSVI KILKNLNKKI 

        70         80         90        100        110        120 
FLDLKFHDIP NTMSAACYEV SKLGVDIISV HASAGSKALT ASKKASLEGA KIATVNAPCV 

       130        140        150        160        170        180 
IGITVLTSLS SEEFQTDLDR KNSIEENVIR LAKLSFDAGL DGCVCSPLEA KILRSMYKNN 

       190        200        210        220        230 
FELITPGIRT NIQKKDDQNR IMTPFEAISN GSSKLVIGRA ITKAKDPNKA FLDICESIC 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE19787.1.
RefSeqNP_893445.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7V0D8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM1328.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE19787; CAE19787; PMM1328.
GeneID1726864.
KEGGpmm:PMM1328.
PATRIC23033724. VBIProMar68066_1516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMADIPNTMR.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-1367-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_PROMP
AccessionPrimary (citable) accession number: Q7V0D8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 72 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