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Q7VLR5 (PYRF_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:HD_1356
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length230 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 – 230230Orotidine 5'-phosphate decarboxylase HAMAP-Rule MF_01200
PRO_0000134545

Regions

Region59 – 6810Substrate binding By similarity

Sites

Active site611Proton donor By similarity
Binding site101Substrate By similarity
Binding site321Substrate By similarity
Binding site1191Substrate By similarity
Binding site1801Substrate By similarity
Binding site1891Substrate By similarity
Binding site2091Substrate; via amide nitrogen By similarity
Binding site2101Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VLR5 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F7AC64029B72E973

FASTA23025,276
        10         20         30         40         50         60 
MDNKIIVALD YETENEALNF IDQVDPSLCR LKVGKEMFTT LGAHFVKQLH DRKFDVFLDL 

        70         80         90        100        110        120 
KYHDIPNTVA RAVRSAADLG VWMVDLHASG GLTMMEEAKK ILEPYGKDAP LLIAVTVLTS 

       130        140        150        160        170        180 
MEDLDLLQIG INASPMEQVI RLSHLAKRAG LDGVVCSPQE VEVLRTHCGD DFKLVTPGIR 

       190        200        210        220        230 
PAGSDFGDQR RVMTPKQAIQ TGADFLVIGR PITQAQEPLS ILKAINASIA 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP96170.1.
RefSeqNP_873781.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VLR5.
SMRQ7VLR5. Positions 2-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD1356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP96170; AAP96170; HD_1356.
GeneID1491249.
KEGGhdu:HD1356.
PATRIC20178994. VBIHaeDuc133973_1131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-1227-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_HAEDU
AccessionPrimary (citable) accession number: Q7VLR5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 21, 2003
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 69 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