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Protein

Ribulose-phosphate 3-epimerase

Gene

rpe

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

Functioni

Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate.1 Publication

Catalytic activityi

D-ribulose 5-phosphate = D-xylulose 5-phosphate.1 Publication

Cofactori

Co2+1 Publication, Fe2+1 Publication, Mn2+1 Publication, Zn2+1 PublicationNote: Binds 1 divalent metal cation per subunit. Active with Co2+, Fe2+, Mn2+ and Zn2+.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91SubstrateBy similarity
Metal bindingi34 – 341Divalent metal cationBy similarity
Active sitei36 – 361Proton acceptorBy similarity
Metal bindingi36 – 361Divalent metal cationBy similarity
Metal bindingi68 – 681Divalent metal cationBy similarity
Binding sitei68 – 681SubstrateBy similarity
Active sitei177 – 1771Proton donorBy similarity
Metal bindingi177 – 1771Divalent metal cationBy similarity
Binding sitei179 – 1791Substrate; via amide nitrogenBy similarity

GO - Molecular functioni

  • ferrous iron binding Source: EcoCyc
  • ribulose-phosphate 3-epimerase activity Source: EcoCyc

GO - Biological processi

  • cellular carbohydrate metabolic process Source: GO_Central
  • pentose catabolic process Source: EcoCyc
  • pentose-phosphate shunt Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Cobalt, Iron, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:RIBULP3EPIM-MONOMER.
ECOL316407:JW3349-MONOMER.
MetaCyc:RIBULP3EPIM-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribulose-phosphate 3-epimerase (EC:5.1.3.1)
Alternative name(s):
Pentose-5-phosphate 3-epimerase
Short name:
PPE
R5P3E
Gene namesi
Name:rpe
Synonyms:dod, yhfD
Ordered Locus Names:b3386, JW3349
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11960. rpe.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Ribulose-phosphate 3-epimerasePRO_0000171568Add
BLAST

Proteomic databases

EPDiP0AG07.
PaxDbiP0AG07.
PRIDEiP0AG07.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaNP0A9883EBI-546020,EBI-542385
frlDP455434EBI-546020,EBI-562037

Protein-protein interaction databases

BioGridi4259295. 150 interactions.
DIPiDIP-47869N.
IntActiP0AG07. 24 interactions.
MINTiMINT-1228320.
STRINGi511145.b3386.

Structurei

3D structure databases

ProteinModelPortaliP0AG07.
SMRiP0AG07. Positions 6-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 1474Substrate bindingBy similarity
Regioni199 – 2002Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105DJV. Bacteria.
COG0036. LUCA.
HOGENOMiHOG000259347.
InParanoidiP0AG07.
KOiK01783.
OMAiGANYITF.
OrthoDBiEOG67HK17.
PhylomeDBiP0AG07.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AG07-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQYLIAPSI LSADFARLGE DTAKALAAGA DVVHFDVMDN HYVPNLTIGP
60 70 80 90 100
MVLKSLRNYG ITAPIDVHLM VKPVDRIVPD FAAAGASIIT FHPEASEHVD
110 120 130 140 150
RTLQLIKENG CKAGLVFNPA TPLSYLDYVM DKLDVILLMS VNPGFGGQSF
160 170 180 190 200
IPQTLDKLRE VRRRIDESGF DIRLEVDGGV KVNNIGEIAA AGADMFVAGS
210 220
AIFDQPDYKK VIDEMRSELA KVSHE
Length:225
Mass (Da):24,554
Last modified:December 20, 2005 - v1
Checksum:iDD678085698466FA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti203 – 22523FDQPD…KVSHE → LTSQTTKKSTMKCAVNWQR in CAA79663 (PubMed:7603433).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19601 Genomic DNA. Translation: CAA79663.1.
U18997 Genomic DNA. Translation: AAA58183.1.
U00096 Genomic DNA. Translation: AAC76411.1.
AP009048 Genomic DNA. Translation: BAE77905.1.
PIRiE65133.
RefSeqiNP_417845.1. NC_000913.3.
WP_000816280.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76411; AAC76411; b3386.
BAE77905; BAE77905; BAE77905.
GeneIDi947896.
KEGGiecj:JW3349.
eco:b3386.
PATRICi32122204. VBIEscCol129921_3479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z19601 Genomic DNA. Translation: CAA79663.1.
U18997 Genomic DNA. Translation: AAA58183.1.
U00096 Genomic DNA. Translation: AAC76411.1.
AP009048 Genomic DNA. Translation: BAE77905.1.
PIRiE65133.
RefSeqiNP_417845.1. NC_000913.3.
WP_000816280.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AG07.
SMRiP0AG07. Positions 6-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259295. 150 interactions.
DIPiDIP-47869N.
IntActiP0AG07. 24 interactions.
MINTiMINT-1228320.
STRINGi511145.b3386.

Proteomic databases

EPDiP0AG07.
PaxDbiP0AG07.
PRIDEiP0AG07.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76411; AAC76411; b3386.
BAE77905; BAE77905; BAE77905.
GeneIDi947896.
KEGGiecj:JW3349.
eco:b3386.
PATRICi32122204. VBIEscCol129921_3479.

Organism-specific databases

EchoBASEiEB1903.
EcoGeneiEG11960. rpe.

Phylogenomic databases

eggNOGiENOG4105DJV. Bacteria.
COG0036. LUCA.
HOGENOMiHOG000259347.
InParanoidiP0AG07.
KOiK01783.
OMAiGANYITF.
OrthoDBiEOG67HK17.
PhylomeDBiP0AG07.

Enzyme and pathway databases

BioCyciEcoCyc:RIBULP3EPIM-MONOMER.
ECOL316407:JW3349-MONOMER.
MetaCyc:RIBULP3EPIM-MONOMER.

Miscellaneous databases

PROiP0AG07.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR026019. Ribul_P_3_epim.
IPR000056. Ribul_P_3_epim-like.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]
PANTHERiPTHR11749. PTHR11749. 1 hit.
PfamiPF00834. Ribul_P_3_epim. 1 hit.
[Graphical view]
PIRSFiPIRSF001461. RPE. 1 hit.
SUPFAMiSSF51366. SSF51366. 1 hit.
TIGRFAMsiTIGR01163. rpe. 1 hit.
PROSITEiPS01085. RIBUL_P_3_EPIMER_1. 1 hit.
PS01086. RIBUL_P_3_EPIMER_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of three genes in the dam-containing operon of Escherichia coli."
    Lyngstadaas A., Lobner-Olesen A., Boye E.
    Mol. Gen. Genet. 247:546-554(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is rapidly damaged by hydrogen peroxide but can be protected by manganese."
    Sobota J.M., Imlay J.A.
    Proc. Natl. Acad. Sci. U.S.A. 108:5402-5407(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, COFACTOR.

Entry informationi

Entry nameiRPE_ECOLI
AccessioniPrimary (citable) accession number: P0AG07
Secondary accession number(s): P32661, Q2M751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 13, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.