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B3DS55 (PYRE_BIFLD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:BLD_0528
OrganismBifidobacterium longum (strain DJO10A) [Complete proteome] [HAMAP]
Taxonomic identifier205913 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium

Protein attributes

Sequence length231 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 – 231231Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_1000138764

Regions

Region79 – 8025-phosphoribose 1-diphosphate binding By similarity
Region133 – 14195-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site2715-phosphoribose 1-diphosphate By similarity
Binding site10615-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10715-phosphoribose 1-diphosphate By similarity
Binding site11015-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site11215-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1371Orotate By similarity
Binding site1661Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
B3DS55 [UniParc].

Last modified July 22, 2008. Version 1.
Checksum: 84DF5B359E827AE3

FASTA23124,884
        10         20         30         40         50         60 
MAETLAHRFT EFLLESNALK FGDFTLKSGR KSPYFINAGA FDDGKKIAAL GAFYAEKISQ 

        70         80         90        100        110        120 
AIVHNTIPRN IDTVFGPAYK GIPLAVSTAI ALTAGHNMTV GYTFDRKEKK DHGDGGWMVG 

       130        140        150        160        170        180 
TPLTDGMKVL LVDDVMTAGT AVREVIPKLK AEANVEVVGL VLSVDRMEKT KDSDLSAVKA 

       190        200        210        220        230 
VEAEFGFPVL AIANVREIFD AAAKMKNADS APLLSHDIQQ RAAAYLEEYG A

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References

[1]"Comparative genomic analysis of the gut bacterium Bifidobacterium longum reveals loci susceptible to deletion during pure culture growth."
Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R., Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V., Slesarev A.I., Weimer B., O'Sullivan D.J.
BMC Genomics 9:247-247(2008) [PubMed: 18505588] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DJO10A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000605 Genomic DNA. Translation: ACD97974.1.
RefSeqYP_001954472.1. NC_010816.1.

3D structure databases

ProteinModelPortalB3DS55.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3DS55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6363882.
GenomeReviewsGene locus BLD_0528 in contig CP000605_GR.
KEGGblj:BLD_0528.
PATRIC21113982. VBIBifLon134794_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG404341.
OMAFAFNRKE.
ProtClustDBPRK00455.

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_BIFLD
AccessionPrimary (citable) accession number: B3DS55
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 22, 2008
Last modified: January 25, 2012
This is version 25 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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