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P46535 (PYRF_BACCL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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
OrganismBacillus caldolyticus
Taxonomic identifier1394 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP) Probable. Ref.1

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 244244Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134525

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
P46535 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 41A248D489BAC272

FASTA24426,579
        10         20         30         40         50         60 
MHTPFIVALD FPSKQEVERF LRPFAGTPLF VKVGMELYYQ EGPAIVAFLK EQGHAVFLDL 

        70         80         90        100        110        120 
KLHDIPNTVK QAMKGLARVG ADLVNVHAAG GRRMMEAAIE GLDAGTPSGR MRPRCIAVTQ 

       130        140        150        160        170        180 
LTSTDERMLH EELWISRPLA ETVAHYAALA KESGLDGVVC SANEAAFIKE RCGASFLAVT 

       190        200        210        220        230        240 
PGIRFADDAA HDQVRVVTPR KARALGSDYI VVGRSLTRAA DPLGAYARLQ HEWNGGERES 


TTPT 

« Hide

References

[1]"Molecular characterization of pyrimidine biosynthesis genes from the thermophile Bacillus caldolyticus."
Ghim S.Y., Nielsen P., Neuhard J.
Microbiology 140:479-491(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: DSM 405 / NBRC 15313 / YP-T.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X73308 Genomic DNA. Translation: CAA51742.1.
PIRI40172.

3D structure databases

ProteinModelPortalP46535.
SMRP46535. Positions 2-234.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_BACCL
AccessionPrimary (citable) accession number: P46535
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 68 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