ID   RPE_RHORU               Reviewed;         225 AA.
AC   P51013;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   03-AUG-2022, entry version 77.
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}; Synonyms=cbbE;
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=STR-2;
RX   PubMed=8349547; DOI=10.1128/jb.175.16.5066-5077.1993;
RA   Falcone D.L., Tabita F.R.;
RT   "Complementation analysis and regulation of CO2 fixation gene expression in
RT   a ribulose 1,5-bisphosphate carboxylase-oxygenase deletion strain of
RT   Rhodospirillum rubrum.";
RL   J. Bacteriol. 175:5066-5077(1993).
RN   [2]
RP   CONCEPTUAL TRANSLATION.
RX   PubMed=8616224; DOI=10.1007/bf00020468;
RA   Nowitzki U., Wyrich R., Westhoff P., Henze K., Schnarrenberger C.,
RA   Martin W.F.;
RT   "Cloning of the amphibolic Calvin cycle/OPPP enzyme D-ribulose-5-phosphate
RT   3-epimerase (EC 5.1.3.1) from spinach chloroplasts: functional and
RT   evolutionary aspects.";
RL   Plant Mol. Biol. 29:1279-1291(1995).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB27778.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; S64484; AAB27778.1; ALT_FRAME; Genomic_DNA.
DR   PIR; A53305; A53305.
DR   AlphaFoldDB; P51013; -.
DR   SMR; P51013; -.
DR   PRIDE; P51013; -.
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   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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   Calvin cycle; Carbohydrate metabolism; Isomerase; Metal-binding.
FT   CHAIN           1..225
FT                   /note="Ribulose-phosphate 3-epimerase"
FT                   /id="PRO_0000171559"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         37
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         175..177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         175
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ   SEQUENCE   225 AA;  23765 MW;  143D9631241F0E3C CRC64;
     MTRAIRIAPS LLSADFAISR PRCPSDGRTG ADILHFDVMD NHYVPNLTVG PLVCAALRPH
     TSLPIDVHLM TRPVDPLIDS FAEAGADMIT FHPEASDHVH RSVQMIRKRG LKAGVALNPA
     SPLSLLDHIL EDLDLVLIMS VNPGFGGQSF IPSALPKIAA LANGRRRACR GDRVDGGVNP
     ADARALARPG ADILVRLAIF GASDRAKAIA SIRGAAESGL GQEAA