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

P0A7E3 (PYRE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Orotate phosphoribosyltransferase

Short name=OPRT
Short name=OPRTase
EC=2.4.2.10
Gene names
Name:pyrE
Ordered Locus Names:b3642, JW3617
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Ref.7

Catalytic activity

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

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01208

Enzyme regulation

Inhibited by sulfate and phosphate ions. Ref.7

Pathway

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

Subunit structure

Homodimer. Ref.1 Ref.7

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed HAMAP-Rule MF_01208
Chain2 – 213212Orotate phosphoribosyltransferase HAMAP-Rule MF_01208
PRO_0000110694

Regions

Region34 – 352Orotate binding By similarity
Region72 – 7325-phosphoribose 1-diphosphate binding HAMAP-Rule MF_01208
Region124 – 13295-phosphoribose 1-diphosphate binding By similarity

Sites

Binding site2615-phosphoribose 1-diphosphate By similarity
Binding site9915-phosphoribose 1-diphosphate; shared with dimeric partner
Binding site10015-phosphoribose 1-diphosphate
Binding site10315-phosphoribose 1-diphosphate; shared with dimeric partner
Binding site10515-phosphoribose 1-diphosphate; shared with dimeric partner By similarity
Binding site1281Orotate By similarity
Binding site1561Orotate By similarity

Experimental info

Sequence conflict1331Missing Ref.1
Sequence conflict1331Missing Ref.2

Secondary structure

....................................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7E3 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F618A6D0A119B9D4

FASTA21323,567
        10         20         30         40         50         60 
MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG RFYAEALVDS 

        70         80         90        100        110        120 
GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK EAKDHGEGGN LVGSALQGRV 

       130        140        150        160        170        180 
MLVDDVITAG TAIRESMEII QANGATLAGV LISLDRQERG RGEISAIQEV ERDYNCKVIS 

       190        200        210 
IITLKDLIAY LEEKPEMAEH LAAVKAYREE FGV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the Escherichia coli pyrE gene and of the DNA in front of the protein-coding region."
Poulsen P., Jensen K.F., Valentin-Hansen P., Carlsson P., Lundberg L.G.
Eur. J. Biochem. 135:223-229(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, SUBUNIT.
Strain: K12.
[2]"Structure of the Escherichia coli pyrE operon and control of pyrE expression by a UTP modulated intercistronic attentuation."
Poulsen P., Bonekamp F., Jensen K.F.
EMBO J. 3:1783-1790(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.
Genomics 16:551-561(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[7]"A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase."
Henriksen A., Aghajari N., Jensen K.F., Gajhede M.
Biochemistry 35:3803-3809(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH DIPHOSPHATE ANALOG, FUNCTION, ENZYME REGULATION, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00781 Genomic DNA. Translation: CAA25358.1.
V01578 Genomic DNA. Translation: CAA24899.1.
L10328 Genomic DNA. Translation: AAA61995.1.
U00096 Genomic DNA. Translation: AAC76666.1.
AP009048 Genomic DNA. Translation: BAE77650.1.
PIRXJEC. D65165.
RefSeqNP_418099.1. NC_000913.3.
YP_491791.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OROX-ray2.40A/B1-213[»]
ProteinModelPortalP0A7E3.
SMRP0A7E3. Positions 1-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP0A7E3. 1 interaction.
STRING511145.b3642.

Proteomic databases

PRIDEP0A7E3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.
GeneID12930578.
948157.
KEGGecj:Y75_p3532.
eco:b3642.
PATRIC32122771. VBIEscCol129921_3762.

Organism-specific databases

EchoBASEEB0801.
EcoGeneEG10808. pyrE.

Phylogenomic databases

eggNOGCOG0461.
HOGENOMHOG000037974.
KOK00762.
OMADRMEKLP.
OrthoDBEOG6091H8.
PhylomeDBP0A7E3.
ProtClustDBPRK00455.

Enzyme and pathway databases

BioCycEcoCyc:OROPRIBTRANS-MONOMER.
ECOL316407:JW3617-MONOMER.
MetaCyc:OROPRIBTRANS-MONOMER.
UniPathwayUPA00070; UER00119.

Gene expression databases

GenevestigatorP0A7E3.

Family and domain databases

HAMAPMF_01208. PyrE.
InterProIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR00336. pyrE. 1 hit.
PROSITEPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0A7E3.
PROP0A7E3.

Entry information

Entry namePYRE_ECOLI
AccessionPrimary (citable) accession number: P0A7E3
Secondary accession number(s): P00495, Q2M7V6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 81 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene