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

Q6F9Z3 (PYRF_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:ACIAD2341
OrganismAcinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length227 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 – 227227Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000241840

Regions

Region57 – 6610Substrate binding By similarity

Sites

Active site591Proton donor By similarity
Binding site81Substrate By similarity
Binding site301Substrate By similarity
Binding site1161Substrate By similarity
Binding site1771Substrate By similarity
Binding site1861Substrate By similarity
Binding site2061Substrate; via amide nitrogen By similarity
Binding site2071Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F9Z3 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 5F4FBEC3086D846C

FASTA22724,887
        10         20         30         40         50         60 
MSIIVALDAK SQYDALSIAD QLDPSLCRVK VGKELFTHDG PQTVRILQDR GFELFLDLKF 

        70         80         90        100        110        120 
HDIPNTTAQA VCAAADLGVW MVNVHASGGR KMMETCVERL KAGNYRTQLI AVTVLTSMGR 

       130        140        150        160        170        180 
EDLRDIGLDV EPFEQVKRLA QLTQESGLDG VVCSAQEAKM LRDLLGTEFA LVTPGIRPEG 

       190        200        210        220 
ANADDQKRIV TPKQAMLDGS THLVIGRPIT KSERPNEMLK QILSSLA 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33305 / BD413 / ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG69120.1.
RefSeqYP_046942.1. NC_005966.1.

3D structure databases

ProteinModelPortalQ6F9Z3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING62977.ACIAD2341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG69120; CAG69120; ACIAD2341.
GeneID2879567.
KEGGaci:ACIAD2341.
PATRIC20742320. VBIAciSp98416_2102.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycASP62977:GJVV-2194-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_ACIAD
AccessionPrimary (citable) accession number: Q6F9Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: July 19, 2004
Last modified: May 14, 2014
This is version 70 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