ID   RPE_ECOL6               Reviewed;         225 AA.
AC   P0AG08; P32661;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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};
GN   Name=rpe {ECO:0000255|HAMAP-Rule:MF_02227}; OrderedLocusNames=c4156;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC       phosphate to D-xylulose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_02227}.
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   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02227};
CC       Note=Binds 1 divalent metal cation per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_02227};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000255|HAMAP-Rule:MF_02227}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02227}.
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DR   EMBL; AE014075; AAN82594.1; -; Genomic_DNA.
DR   RefSeq; WP_000816280.1; NC_004431.1.
DR   AlphaFoldDB; P0AG08; -.
DR   SMR; P0AG08; -.
DR   STRING; 199310.c4156; -.
DR   EnsemblBacteria; AAN82594; AAN82594; c4156.
DR   GeneID; 67417012; -.
DR   KEGG; ecc:c4156; -.
DR   eggNOG; COG0036; Bacteria.
DR   HOGENOM; CLU_054856_2_1_6; -.
DR   OMA; WLQVDGG; -.
DR   BioCyc; ECOL199310:C4156-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019323; P:pentose catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Metal-binding.
FT   CHAIN           1..225
FT                   /note="Ribulose-phosphate 3-epimerase"
FT                   /id="PRO_0000171570"
FT   ACT_SITE        36
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   ACT_SITE        177
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         34
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         36
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         68
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         144..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         177..179
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         177
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         199..200
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
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