Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

C4LEZ7 (PYRF_TOLAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:Tola_1553
OrganismTolumonas auensis (strain DSM 9187 / TA4) [Complete proteome] [HAMAP]
Taxonomic identifier595494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeTolumonas

Protein attributes

Sequence length232 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 – 232232Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_1000213828

Regions

Region60 – 6910Substrate binding By similarity

Sites

Active site621Proton donor By similarity
Binding site111Substrate By similarity
Binding site331Substrate By similarity
Binding site1201Substrate By similarity
Binding site1811Substrate By similarity
Binding site1911Substrate By similarity
Binding site2111Substrate; via amide nitrogen By similarity
Binding site2121Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C4LEZ7 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: 494361F11DE1650F

FASTA23225,215
        10         20         30         40         50         60 
MTEPKVIVAL DFAKKEEALS FVDQVTPSDC RLKIGKEMFT YYGPQFVEQL VKKGFDVFLD 

        70         80         90        100        110        120 
LKFHDIPTTV AKAVKASAEM GVWMVNVHAS GGRKMMEAAR SALLPYGDKA PLLIAVTVLT 

       130        140        150        160        170        180 
SMEQSDLADI GLDIPPFEQV LRLATLTQQA GLDGVVCSAQ EASVLKSRLG NEFKLITPGI 

       190        200        210        220        230 
RLDVSTKVDD QSRVMTPVDA IKAGADYLVI GRPVTQAAHP LDVLRKINLS LA 

« Hide

References

[1]"Complete sequence of Tolumonas auensis DSM 9187."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Spring S., Beller H.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 9187 / TA4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001616 Genomic DNA. Translation: ACQ93164.1.
RefSeqYP_002892750.1. NC_012691.1.

3D structure databases

ProteinModelPortalC4LEZ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING595494.Tola_1553.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ93164; ACQ93164; Tola_1553.
GeneID7885157.
KEGGtau:Tola_1553.
PATRIC23979741. VBITolAue42623_1544.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycTAUE595494:GHEF-1607-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_TOLAT
AccessionPrimary (citable) accession number: C4LEZ7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: May 14, 2014
This is version 33 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