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A8G6D9 (PYRF_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:P9215_15571
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length242 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 – 242242Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000065928

Regions

Region64 – 7310Substrate binding By similarity

Sites

Active site661Proton donor By similarity
Binding site161Substrate By similarity
Binding site371Substrate By similarity
Binding site1281Substrate By similarity
Binding site1901Substrate By similarity
Binding site1991Substrate By similarity
Binding site2191Substrate; via amide nitrogen By similarity
Binding site2201Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G6D9 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 0D6EA458FFDC484F

FASTA24226,679
        10         20         30         40         50         60 
MNKRFNSEDK IILAIDGLDV SQAKLLLEEC PNIKWVKVGL ELFVREGPRV IEILKGLNKK 

        70         80         90        100        110        120 
IFLDLKFHDI PNTMRAACSQ VSKLGVDIIS IHASAGLKAL KDSKKASLEG ATSVSVKPPL 

       130        140        150        160        170        180 
VVGITVLTSF SLKDFQTDLD RNNSIEENVL RLAKLSFDAG LDGCVCSPWE AKMLRSIYKD 

       190        200        210        220        230        240 
NFELITPGIR LNIDNKDDQN RIMTPSEAID NGASKLVIGR SISKAIDPNK ALIEIFKSID 


SD 

« 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 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV51170.1.
RefSeqYP_001484756.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G6D9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_15571.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV51170; ABV51170; P9215_15571.
GeneID5616344.
KEGGpmh:P9215_15571.
PATRIC22992696. VBIProMar119824_1609.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMADIPNTMR.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycPMAR93060:GI08-1608-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_PROM2
AccessionPrimary (citable) accession number: A8G6D9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: May 14, 2014
This is version 44 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