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

A5UBN7 (PYRF_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:CGSHiEE_03855
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [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_1000065911

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
A5UBN7 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 735AC301F27FB7B9

FASTA23025,222
        10         20         30         40         50         60 
MTSKIIVALD YEKEAEALAL VDQIDPSLCR LKVGKEMFTT LGINFVKQLH QRNFDVFLDL 

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

       130        140        150        160        170        180 
MEDLDLLQIG INASPMEQVL RLAHLTQRAG LDGVVCSPQE VEILRNACGE DFKLVTPGIR 

       190        200        210        220        230 
PIGTDFGDQR RVMTPTAAIR AGSDYLVIGR PITQADNPAE VLRSINVSIG 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ98188.1.
RefSeqYP_001290571.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UBN7.
SMRA5UBN7. Positions 3-229.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_03855.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ98188; ABQ98188; CGSHiEE_03855.
GeneID5225041.
KEGGhip:CGSHiEE_03855.
PATRIC20277667. VBIHaeInf81350_0781.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0284.
HOGENOMHOG000226071.
KOK01591.
OMARPITQSA.
OrthoDBEOG6N6815.

Enzyme and pathway databases

BioCycHINF374930:GJDD-748-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_HAEIE
AccessionPrimary (citable) accession number: A5UBN7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 45 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