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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).UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Inhibited by sulfate and phosphate ions.1 Publication

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes UMP from orotate.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Orotate phosphoribosyltransferase (pyrE)
  2. Orotidine 5'-phosphate decarboxylase (pyrF)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UMP from orotate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei265-phosphoribose 1-diphosphateUniRule annotation1
Binding sitei995-phosphoribose 1-diphosphate; shared with dimeric partnerUniRule annotation1 Publication1
Binding sitei1005-phosphoribose 1-diphosphateUniRule annotation1 Publication1
Binding sitei1035-phosphoribose 1-diphosphate; shared with dimeric partnerUniRule annotation1 Publication1
Binding sitei1055-phosphoribose 1-diphosphate; shared with dimeric partnerUniRule annotation1
Binding sitei128OrotateUniRule annotation1
Binding sitei156OrotateUniRule annotation1

GO - Molecular functioni

  • magnesium ion binding Source: EcoCyc
  • orotate phosphoribosyltransferase activity Source: EcoCyc

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: EcoCyc
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • 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 phosphoribosyltransferaseUniRule annotation (EC:2.4.2.10UniRule annotation)
Short name:
OPRTUniRule annotation
Short name:
OPRTaseUniRule annotation
Gene namesi
Name:pyrE1 Publication
Ordered Locus Names:b3642, JW3617
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10808. pyrE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001106942 – 213Orotate phosphoribosyltransferaseAdd BLAST212

Proteomic databases

EPDiP0A7E3.
PaxDbiP0A7E3.
PRIDEiP0A7E3.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi4259572. 15 interactors.
IntActiP0A7E3. 1 interactor.
STRINGi511145.b3642.

Structurei

Secondary structure

1213
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Beta strandi17 – 24Combined sources8
Beta strandi30 – 35Combined sources6
Helixi37 – 39Combined sources3
Helixi43 – 60Combined sources18
Beta strandi65 – 69Combined sources5
Turni71 – 73Combined sources3
Helixi74 – 89Combined sources16
Beta strandi94 – 98Combined sources5
Beta strandi104 – 107Combined sources4
Beta strandi111 – 114Combined sources4
Beta strandi118 – 123Combined sources6
Helixi130 – 133Combined sources4
Helixi134 – 142Combined sources9
Beta strandi146 – 155Combined sources10
Beta strandi161 – 164Combined sources4
Helixi166 – 174Combined sources9
Beta strandi177 – 183Combined sources7
Helixi184 – 191Combined sources8
Helixi195 – 197Combined sources3
Helixi198 – 211Combined sources14

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7E3.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni34 – 35Orotate bindingUniRule annotation2
Regioni72 – 735-phosphoribose 1-diphosphate bindingUniRule annotation1 Publication2
Regioni124 – 1325-phosphoribose 1-diphosphate bindingUniRule annotation9

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QP2. Bacteria.
COG0461. LUCA.
HOGENOMiHOG000037974.
InParanoidiP0A7E3.
KOiK00762.
OMAiMKAYQRQ.
PhylomeDBiP0A7E3.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti133Missing (PubMed:6349999).Curated1
Sequence conflicti133Missing (PubMed:6207018).Curated1

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.
WP_000806177.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.
GeneIDi948157.
KEGGiecj:JW3617.
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.
WP_000806177.1. NZ_LN832404.1.

3D structure databases

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

Protein-protein interaction databases

BioGridi4259572. 15 interactors.
IntActiP0A7E3. 1 interactor.
STRINGi511145.b3642.

Proteomic databases

EPDiP0A7E3.
PaxDbiP0A7E3.
PRIDEiP0A7E3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76666; AAC76666; b3642.
BAE77650; BAE77650; BAE77650.
GeneIDi948157.
KEGGiecj:JW3617.
eco:b3642.
PATRICi32122771. VBIEscCol129921_3762.

Organism-specific databases

EchoBASEiEB0801.
EcoGeneiEG10808. pyrE.

Phylogenomic databases

eggNOGiENOG4107QP2. Bacteria.
COG0461. LUCA.
HOGENOMiHOG000037974.
InParanoidiP0A7E3.
KOiK00762.
OMAiMKAYQRQ.
PhylomeDBiP0A7E3.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0A7E3.
PROiP0A7E3.

Family and domain databases

CDDicd06223. PRTases_typeI. 1 hit.
Gene3Di3.40.50.2020. 1 hit.
HAMAPiMF_01208. PyrE. 1 hit.
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...

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: November 2, 2016
This is version 99 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

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 one 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.