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Protein

Orotate phosphoribosyltransferase

Gene

pyrE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by sulfate and phosphate ions.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei26 – 2615-phosphoribose 1-diphosphateBy similarity
Binding sitei99 – 9915-phosphoribose 1-diphosphate; shared with dimeric partner
Binding sitei100 – 10015-phosphoribose 1-diphosphate
Binding sitei103 – 10315-phosphoribose 1-diphosphate; shared with dimeric partner
Binding sitei105 – 10515-phosphoribose 1-diphosphate; shared with dimeric partnerBy similarity
Binding sitei128 – 1281OrotateBy similarity
Binding sitei156 – 1561OrotateBy similarity

GO - Molecular functioni

  1. magnesium ion binding Source: EcoCyc
  2. orotate phosphoribosyltransferase activity Source: EcoCyc

GO - Biological processi

  1. 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoCyc
  2. 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  3. pyrimidine nucleotide biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciEcoCyc:OROPRIBTRANS-MONOMER.
ECOL316407:JW3617-MONOMER.
MetaCyc:OROPRIBTRANS-MONOMER.
UniPathwayiUPA00070; UER00119.

Names & Taxonomyi

Protein namesi
Recommended name:
Orotate phosphoribosyltransferase (EC:2.4.2.10)
Short name:
OPRT
Short name:
OPRTase
Gene namesi
Name:pyrE
Ordered Locus Names:b3642, JW3617
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10808. pyrE.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 213212Orotate phosphoribosyltransferasePRO_0000110694Add
BLAST

Proteomic databases

PRIDEiP0A7E3.

Expressioni

Gene expression databases

GenevestigatoriP0A7E3.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiP0A7E3. 1 interaction.
STRINGi511145.b3642.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1412Combined sources
Beta strandi17 – 248Combined sources
Beta strandi30 – 356Combined sources
Helixi37 – 393Combined sources
Helixi43 – 6018Combined sources
Beta strandi65 – 695Combined sources
Turni71 – 733Combined sources
Helixi74 – 8916Combined sources
Beta strandi94 – 985Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi111 – 1144Combined sources
Beta strandi118 – 1236Combined sources
Helixi130 – 1334Combined sources
Helixi134 – 1429Combined sources
Beta strandi146 – 15510Combined sources
Beta strandi161 – 1644Combined sources
Helixi166 – 1749Combined sources
Beta strandi177 – 1837Combined sources
Helixi184 – 1918Combined sources
Helixi195 – 1973Combined sources
Helixi198 – 21114Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OROX-ray2.40A/B1-213[»]
ProteinModelPortaliP0A7E3.
SMRiP0A7E3. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7E3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 352Orotate bindingBy similarity
Regioni72 – 7325-phosphoribose 1-diphosphate binding
Regioni124 – 13295-phosphoribose 1-diphosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0461.
HOGENOMiHOG000037974.
InParanoidiP0A7E3.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG6091H8.
PhylomeDBiP0A7E3.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPYQRQFIE FALSKQVLKF GEFTLKSGRK SPYFFNAGLF NTGRDLALLG
60 70 80 90 100
RFYAEALVDS GIEFDLLFGP AYKGIPIATT TAVALAEHHD LDLPYCFNRK
110 120 130 140 150
EAKDHGEGGN LVGSALQGRV MLVDDVITAG TAIRESMEII QANGATLAGV
160 170 180 190 200
LISLDRQERG RGEISAIQEV ERDYNCKVIS IITLKDLIAY LEEKPEMAEH
210
LAAVKAYREE FGV
Length:213
Mass (Da):23,567
Last modified:January 23, 2007 - v2
Checksum:iF618A6D0A119B9D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331Missing (PubMed:6349999).Curated
Sequence conflicti133 – 1331Missing (PubMed:6207018).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD65165. XJEC.
RefSeqiNP_418099.1. NC_000913.3.
YP_491791.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.
GeneIDi12930578.
948157.
KEGGiecj:Y75_p3532.
eco:b3642.
PATRICi32122771. VBIEscCol129921_3762.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD65165. XJEC.
RefSeqiNP_418099.1. NC_000913.3.
YP_491791.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OROX-ray2.40A/B1-213[»]
ProteinModelPortaliP0A7E3.
SMRiP0A7E3. Positions 1-213.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0A7E3. 1 interaction.
STRINGi511145.b3642.

Proteomic databases

PRIDEiP0A7E3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.
GeneIDi12930578.
948157.
KEGGiecj:Y75_p3532.
eco:b3642.
PATRICi32122771. VBIEscCol129921_3762.

Organism-specific databases

EchoBASEiEB0801.
EcoGeneiEG10808. pyrE.

Phylogenomic databases

eggNOGiCOG0461.
HOGENOMiHOG000037974.
InParanoidiP0A7E3.
KOiK00762.
OMAiMKAYQRQ.
OrthoDBiEOG6091H8.
PhylomeDBiP0A7E3.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00119.
BioCyciEcoCyc:OROPRIBTRANS-MONOMER.
ECOL316407:JW3617-MONOMER.
MetaCyc:OROPRIBTRANS-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A7E3.
PROiP0A7E3.

Gene expression databases

GenevestigatoriP0A7E3.

Family and domain databases

Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE.
InterProiIPR023031. OPRT.
IPR004467. Or_phspho_trans_dom.
IPR000836. PRibTrfase_dom.
IPR029057. PRTase-like.
[Graphical view]
PfamiPF00156. Pribosyltran. 1 hit.
[Graphical view]
SUPFAMiSSF53271. SSF53271. 1 hit.
TIGRFAMsiTIGR00336. pyrE. 1 hit.
PROSITEiPS00103. PUR_PYR_PR_TRANSFER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiPYRE_ECOLI
AccessioniPrimary (citable) accession number: P0A7E3
Secondary accession number(s): P00495, Q2M7V6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.