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Reviewed, UniProtKB/Swiss-Prot Q65JU3 (PYRE_BACLD)

Last modified February 9, 2010. Version 54. 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: BLi01776, BL02280
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length209 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Orotate phosphoribosyltransferase HAMAP MF_01208
PRO_1000066203

Regions

Region120 – 12895-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site9415-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site9815-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site10015-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1241Orotate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65JU3-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: CF51A3B29B7707A0

FASTA20922,109
        10         20         30         40         50         60 
MKTDIANHLL KIKAVFLRPN EPFTWASGIL SPIYCDNRLT LSYPEVRDDI ASGLAGLIQD 

        70         80         90        100        110        120 
KFPGAEMIAG TATAGIPHAA LAADRLSLPM CYVRSKPKAH GKGNQIEGAV VKGQKVVVIE 

       130        140        150        160        170        180 
DLISTGGSVL EAAAALTEAG CEVLGVAAIF TYGLPKAAAA FSEAGVEYHT LTDYDTLTEA 

       190        200 
ALAGGYITEQ DAAKLKEWKA DPESKSWMN 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000002 Genomic DNA. Translation: AAU23311.1.
AE017333 Genomic DNA. Translation: AAU40671.1.
RefSeqYP_078949.1.
YP_091364.1.

3D structure databases

SMRQ65JU3. Positions 1-204.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65JU3.

Genome annotation databases

GeneID3030931.
3098083.
GenomeReviewsGene locus BLi01776 in contig AE017333_GR.
Gene locus BL02280 in contig CP000002_GR.
KEGGbld:BLi01776.
bli:BL02280.
NMPDRfig|279010.5.peg.1718.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0461.
HOGENOMHBG404341.
OMAPMCYVRS.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI01776-MONOMER.
BLIC279010:BL02280-MONOMER.

Family and domain databases

HAMAPMF_01208_B. PyrE_B.
[Tree]
InterProIPR004467. Or_phspho_trans.
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_BACLD
AccessionPrimary (citable) accession number: Q65JU3
Secondary accession number(s): Q62V98
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 25, 2004
Last modified: February 9, 2010
This is version 54 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