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Reviewed, UniProtKB/Swiss-Prot A9I0G7 (PYRE_BORPD)

Last modified November 3, 2009. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Bpet0423
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Cofactor

Magnesium By similarity.

Pathway

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

Subunit structure

Homodimer By similarity.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_1000138765

Regions

Region37 – 382Orotate binding By similarity
Region75 – 7625-phosphoribose 1-diphosphate binding By similarity
Region130 – 13895-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site2915-phosphoribose 1-diphosphate By similarity
Binding site10515-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10615-phosphoribose 1-diphosphate By similarity
Binding site10915-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site11115-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1341Orotate By similarity
Binding site1621Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9I0G7-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 8C7424C10635B827

FASTA22523,392
        10         20         30         40         50         60 
MAAASATSTD FVRFALDEGV LRFGSFKVKS GRTSPYFFNA GLFNSGASVG RLAQFYAQAL 

        70         80         90        100        110        120 
VDSGIAFDML FGPAYKGIPL ATATAVALAG HPAMQGRDVP FAFNRKEAKD HGEGGTLVGA 

       130        140        150        160        170        180 
PLQGRVVIID DVITAGTSVR ESVEIIRAAG AEPAAVLIAL DRQERAGPDD ALSPHSAVQD 

       190        200        210        220 
VAKTYGMPVV SIASLADILA LLQGDAQFAG NREAVLAYRG KYGVV 

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM902716 Genomic DNA. Translation: CAP40755.1.
RefSeqYP_001629026.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5818649.
GenomeReviewsGene locus Bpet0423 in contig AM902716_GR.
KEGGbpt:Bpet0423.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYKGITLA.

Family and domain databases

HAMAPMF_01208.
[Tree]
InterProIPR004467. Or_phspho_trans.
IPR002375. Pr/py_Pribosyl_transf_CS.
IPR000836. PRibTrfase.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. pyrE. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRE_BORPD
AccessionPrimary (citable) accession number: A9I0G7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents