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Q2KU70 (PYRE_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Orotate phosphoribosyltransferase
Short name=OPRT
Short name=OPRTase
EC=2.4.2.10
Gene names
Name:pyrE
Ordered Locus Names:BAV3180
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP) By similarity. HAMAP MF_01208

Catalytic activity

Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01208

Cofactor

Magnesium By similarity. HAMAP MF_01208

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. HAMAP MF_01208

Subunit structure

Homodimer By similarity. HAMAP MF_01208

Sequence similarities

Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMagnesium
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processnucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

pyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionorotate phosphoribosyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_1000066210

Regions

Region34 – 352Orotate binding By similarity
Region72 – 7325-phosphoribose 1-diphosphate binding By similarity
Region126 – 13495-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site2615-phosphoribose 1-diphosphate By similarity
Binding site10115-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10215-phosphoribose 1-diphosphate By similarity
Binding site10515-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10715-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1301Orotate By similarity
Binding site1581Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2KU70 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: 0352833CACE4ADDF

FASTA22023,280
        10         20         30         40         50         60 
MSNTATDFVR FALDEGVLRF GSFKVKSGRM SPYFFNAGLF NSGRSVGKLA AFYAQALLDS 

        70         80         90        100        110        120 
GLNFDMLFGP AYKGIPLATA TAVALAGHPQ ASGDIPFAYN RKEAKDHGEG GTLVGAPLAG 

       130        140        150        160        170        180 
RVVIIDDVIT AGTSVRESVE IIRAAGAQPA AVLIAMDRME RAGPDEALSP HSAVQDVAKT 

       190        200        210        220 
YGIPVISIAS LADILQLLQD DEQFAAHRDS VLAYREQYGV

« Hide

References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed: 16885469] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM167904 Genomic DNA. Translation: CAJ50790.1.
RefSeqYP_787675.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2KU70.
SMRQ2KU70. Positions 1-220.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2KU70.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6267055.
GenomeReviewsGene locus BAV3180 in contig AM167904_GR.
KEGGbav:BAV3180.
NMPDRfig|521.1.peg.2057.
PATRIC21132675. VBIBorAvi43433_3215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG404341.
OMAFAFNRKE.
ProtClustDBPRK00455.

Enzyme and pathway databases

BioCycABAU360910:BAV3180-MONOMER.

Family and domain databases

HAMAPMF_01208. PyrE.
[Tree]
InterProIPR004467. Or_phspho_trans_clade-1.
IPR023031. Orotate_PribosylTferase.
IPR000836. PRibTrfase.
[Graphical view]
KOK00762.
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. PyrE. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRE_BORA1
AccessionPrimary (citable) accession number: Q2KU70
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: March 7, 2006
Last modified: January 25, 2012
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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