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Q74J28 (PYRF_LACJO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. 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:LJ_1282
OrganismLactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]
Taxonomic identifier257314 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length235 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 – 235235Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241869

Regions

Region60 – 6910Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site101Substrate By similarity
Binding site331Substrate By similarity
Binding site1231Substrate By similarity
Binding site1851Substrate By similarity
Binding site1941Substrate By similarity
Binding site2141Substrate; via amide nitrogen By similarity
Binding site2151Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q74J28 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 54F316F69447B10F

FASTA23525,551
        10         20         30         40         50         60 
MSRPVIVALD LDNEKKLNEL LPKLGKPENV FIKIGMELFF NEGPKIVKQL SEQGYQIFLD 

        70         80         90        100        110        120 
LKMNDIPNTV YNGAKALARL GITYTTVHAL GGSQMIKAAK DGLIAGTPID KNVPKLLAVT 

       130        140        150        160        170        180 
ELTSISDEIL HYEQNCNLSM NDQVLSLATT AKKAGADGVI CSPLEVKDLR QKVGEDFLYV 

       190        200        210        220        230 
TPGIRPAGNA KDDQSRVATP LQAKEWGSTA IVVGRPITLA TDPEAAYEAI KKEFN 

« Hide

References

[1]"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533."
Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.
Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017198 Genomic DNA. Translation: AAS09103.1.
RefSeqNP_965137.1. NC_005362.1.

3D structure databases

ProteinModelPortalQ74J28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257314.LJ1282.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS09103; AAS09103; LJ_1282.
GeneID2742202.
KEGGljo:LJ1282.
PATRIC22238945. VBILacJoh1832_1150.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycLJOH257314:GJN3-1146-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_LACJO
AccessionPrimary (citable) accession number: Q74J28
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 71 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