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A9BBV1 (PYRF_PROM4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:P9211_13821
OrganismProchlorococcus marinus (strain MIT 9211) [Complete proteome] [HAMAP]
Taxonomic identifier93059 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length241 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 – 241241Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000138546

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
A9BBV1 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: E7B12C49CCA3FE5F

FASTA24126,229
        10         20         30         40         50         60 
MTLVNPSEKL ILALDGMDVL EALSFIDKVP DLIWVKVGLE LFATSGLEIF TELRARGKKV 

        70         80         90        100        110        120 
FLDLKFHDIP NTMAGACYRA ARNGAELITV HACAGSKALL VANEAAKKGA ASVGLPSPTL 

       130        140        150        160        170        180 
LGVTVLTSWT SYEFGDELDI HHSLEKRVEH LAQLAFKAGL GGCICSPCEV KRLREIFPES 

       190        200        210        220        230        240 
FELITPGIRF LDSGLDDQAR VMQPRDAFTS GASRLVLGRI ITRSTNPAEA FTRVCRDIQT 


D 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9211.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000878 Genomic DNA. Translation: ABX09313.1.
RefSeqYP_001551267.1. NC_009976.1.

3D structure databases

ProteinModelPortalA9BBV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93059.P9211_13821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX09313; ABX09313; P9211_13821.
GeneID5730782.
KEGGpmj:P9211_13821.
PATRIC22988384. VBIProMar136502_1460.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMADIPNTMR.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPMAR93059:GHJV-1417-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_PROM4
AccessionPrimary (citable) accession number: A9BBV1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 46 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