RPE_ECOLI
ID RPE_ECOLI Reviewed; 225 AA.
AC P0AG07; P32661; Q2M751;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Ribulose-phosphate 3-epimerase {ECO:0000255|HAMAP-Rule:MF_02227};
DE EC=5.1.3.1 {ECO:0000255|HAMAP-Rule:MF_02227, ECO:0000269|PubMed:21402925};
DE AltName: Full=Pentose-5-phosphate 3-epimerase;
DE Short=PPE;
DE AltName: Full=R5P3E;
GN Name=rpe {ECO:0000255|HAMAP-Rule:MF_02227}; Synonyms=dod, yhfD;
GN OrderedLocusNames=b3386, JW3349;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=7603433; DOI=10.1007/bf00290345;
RA Lyngstadaas A., Lobner-Olesen A., Boye E.;
RT "Characterization of three genes in the dam-containing operon of
RT Escherichia coli.";
RL Mol. Gen. Genet. 247:546-554(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX PubMed=21402925; DOI=10.1073/pnas.1100410108;
RA Sobota J.M., Imlay J.A.;
RT "Iron enzyme ribulose-5-phosphate 3-epimerase in Escherichia coli is
RT rapidly damaged by hydrogen peroxide but can be protected by manganese.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5402-5407(2011).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02227,
CC ECO:0000269|PubMed:21402925}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:13677, ChEBI:CHEBI:57737, ChEBI:CHEBI:58121;
CC EC=5.1.3.1; Evidence={ECO:0000255|HAMAP-Rule:MF_02227,
CC ECO:0000269|PubMed:21402925};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:21402925};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:21402925};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21402925};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21402925};
CC Note=Binds 1 divalent metal cation per subunit. Active with Co(2+),
CC Fe(2+), Mn(2+) and Zn(2+). {ECO:0000269|PubMed:21402925};
CC -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227,
CC ECO:0000269|PubMed:21402925}.
CC -!- INTERACTION:
CC P0AG07; P0A988: dnaN; NbExp=4; IntAct=EBI-546020, EBI-542385;
CC P0AG07; P0A6P9: eno; NbExp=3; IntAct=EBI-546020, EBI-368855;
CC P0AG07; P45543: frlD; NbExp=5; IntAct=EBI-546020, EBI-562037;
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000255|HAMAP-Rule:MF_02227, ECO:0000305}.
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DR EMBL; Z19601; CAA79663.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58183.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76411.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77905.1; -; Genomic_DNA.
DR PIR; E65133; E65133.
DR RefSeq; NP_417845.1; NC_000913.3.
DR RefSeq; WP_000816280.1; NZ_STEB01000004.1.
DR AlphaFoldDB; P0AG07; -.
DR SMR; P0AG07; -.
DR BioGRID; 4259295; 200.
DR BioGRID; 852205; 2.
DR DIP; DIP-47869N; -.
DR IntAct; P0AG07; 24.
DR STRING; 511145.b3386; -.
DR jPOST; P0AG07; -.
DR PaxDb; P0AG07; -.
DR PRIDE; P0AG07; -.
DR EnsemblBacteria; AAC76411; AAC76411; b3386.
DR EnsemblBacteria; BAE77905; BAE77905; BAE77905.
DR GeneID; 67417012; -.
DR GeneID; 947896; -.
DR KEGG; ecj:JW3349; -.
DR KEGG; eco:b3386; -.
DR PATRIC; fig|1411691.4.peg.3344; -.
DR EchoBASE; EB1903; -.
DR eggNOG; COG0036; Bacteria.
DR HOGENOM; CLU_054856_2_1_6; -.
DR InParanoid; P0AG07; -.
DR OMA; WLQVDGG; -.
DR PhylomeDB; P0AG07; -.
DR BioCyc; EcoCyc:RIBULP3EPIM-MON; -.
DR BioCyc; MetaCyc:RIBULP3EPIM-MON; -.
DR PRO; PR:P0AG07; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IDA:EcoCyc.
DR GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0019323; P:pentose catabolic process; IMP:EcoCyc.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_02227; RPE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR026019; Ribul_P_3_epim.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR01163; rpe; 1.
DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cobalt; Iron; Isomerase; Manganese; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..225
FT /note="Ribulose-phosphate 3-epimerase"
FT /id="PRO_0000171568"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT ACT_SITE 177
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 36
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 68
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 177..179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT BINDING 199..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719, ECO:0000255|HAMAP-
FT Rule:MF_02227"
FT CONFLICT 203..225
FT /note="FDQPDYKKVIDEMRSELAKVSHE -> LTSQTTKKSTMKCAVNWQR (in
FT Ref. 1; CAA79663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 225 AA; 24554 MW; DD678085698466FA CRC64;
MKQYLIAPSI LSADFARLGE DTAKALAAGA DVVHFDVMDN HYVPNLTIGP MVLKSLRNYG
ITAPIDVHLM VKPVDRIVPD FAAAGASIIT FHPEASEHVD RTLQLIKENG CKAGLVFNPA
TPLSYLDYVM DKLDVILLMS VNPGFGGQSF IPQTLDKLRE VRRRIDESGF DIRLEVDGGV
KVNNIGEIAA AGADMFVAGS AIFDQPDYKK VIDEMRSELA KVSHE
