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B7HLL7 (PYRF_BACC7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:BCAH187_A3932
OrganismBacillus cereus (strain AH187) [Complete proteome] [HAMAP]
Taxonomic identifier405534 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length238 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 – 238238Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000138514

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site101Substrate By similarity
Binding site321Substrate By similarity
Binding site1221Substrate By similarity
Binding site1841Substrate By similarity
Binding site1931Substrate By similarity
Binding site2131Substrate; via amide nitrogen By similarity
Binding site2141Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B7HLL7 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 1FC1277E5DA9696F

FASTA23826,199
        10         20         30         40         50         60 
MSQSLIVALD FPGKQDVEQF LRHFEGEELF VKVGMELFYK EGPAIITYLK EKGHKIFLDL 

        70         80         90        100        110        120 
KLHDIPNTVK SAMRSLASLD VDMVNVHAAG GSSMMKAAIE GLEEGKQEGK ERPICIAVTQ 

       130        140        150        160        170        180 
LTSTSEAMMK KEIGIEKTLE EAVAHYAKLT KESGLDGVVC STLEVPKLRE VCGDEFVTVT 

       190        200        210        220        230 
PGIRLASDDV NDQVRVATPK RARELGSSYI VVGRSITKAE NPLEAYKTVK QQWEGVTV 

« Hide

References

[1]"Genome sequence of Bacillus cereus AH187."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AH187.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001177 Genomic DNA. Translation: ACJ79121.1.
RefSeqYP_002339872.1. NC_011658.1.

3D structure databases

ProteinModelPortalB7HLL7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405534.BCAH187_A3932.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ79121; ACJ79121; BCAH187_A3932.
GeneID7073608.
KEGGbcr:BCAH187_A3932.
PATRIC18833299. VBIBacCer120511_4120.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycBCER405534:GHXM-3875-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_BACC7
AccessionPrimary (citable) accession number: B7HLL7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 36 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