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Q3SK77 (PYRF_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:Tbd_0960
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length245 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 – 245245Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241925

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site101Substrate By similarity
Binding site321Substrate By similarity
Binding site1271Substrate By similarity
Binding site1881Substrate By similarity
Binding site1971Substrate By similarity
Binding site2171Substrate; via amide nitrogen By similarity
Binding site2181Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3SK77 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: D098850A4380FBD1

FASTA24525,177
        10         20         30         40         50         60 
MTHKIIVALD FPAGAPALAL ADRLDPARCR LKVGKELFTA AGPDLVRALV ARGFEVFLDL 

        70         80         90        100        110        120 
KFHDIPNTVA AACRAAAGLG VWMLNVHAAG GRRMMDAARE ALESLPPGDG AADTPQRPLL 

       130        140        150        160        170        180 
IAVTVLTSMS AGDLAETGVA DTPAEQVMRL ARLAHACALD GVVCSAQEAA GLRAALGADF 

       190        200        210        220        230        240 
RLVTPGIRPA GAAAADQRRV MTPVEALRAG ATDLVIGRPI TGAGDPLAAL AAIQADIEEN 


LGRAF 

« Hide

References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ96913.1.
RefSeqYP_314718.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SK77.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_0960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ96913; AAZ96913; Tbd_0960.
GeneID3672752.
KEGGtbd:Tbd_0960.
PATRIC23968063. VBIThiDen82923_0945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226070.
KOK01591.
OMAVIASPHE.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-983-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_THIDA
AccessionPrimary (citable) accession number: Q3SK77
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 11, 2005
Last modified: May 14, 2014
This is version 62 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