ID   RPE_AQUAE               Reviewed;         222 AA.
AC   O67098;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=aq_968;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000657; AAC07062.1; -; Genomic_DNA.
DR   PIR; G70383; G70383.
DR   RefSeq; NP_213661.1; NC_000918.1.
DR   RefSeq; WP_010880599.1; NC_000918.1.
DR   AlphaFoldDB; O67098; -.
DR   SMR; O67098; -.
DR   STRING; 224324.aq_968; -.
DR   EnsemblBacteria; AAC07062; AAC07062; aq_968.
DR   KEGG; aae:aq_968; -.
DR   PATRIC; fig|224324.8.peg.761; -.
DR   eggNOG; COG0036; Bacteria.
DR   HOGENOM; CLU_054856_2_1_0; -.
DR   InParanoid; O67098; -.
DR   OMA; WLQVDGG; -.
DR   OrthoDB; 1697639at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
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; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Carbohydrate metabolism; Isomerase; Metal-binding; Reference proteome.
FT   CHAIN           1..222
FT                   /note="Ribulose-phosphate 3-epimerase"
FT                   /id="PRO_0000171560"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   ACT_SITE        174
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         32
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
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         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         141..144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         174..176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         174
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
FT   BINDING         196..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02227"
SQ   SEQUENCE   222 AA;  24489 MW;  B4DB8BF805FDDC68 CRC64;
     MKLLAPSILA GDWWCIGEQI QATIRGGADI LHYDVMDGHF VPNITAGYEI LSHIRKRASL
     PIDAHLMIEN PDKYIPKFVE AGANWISVHI ENNYHIHRTL QLIKELGAKA GVVVNPGTSL
     SAIEEALYYA DYVLLMSVNP GFSGQKFIER SIERLRILKE MRDRINPSCL IEIDGGIKEN
     NIAEVVRAGA DVVVVGSGIF GAKDIEAQTR KLKSLMLSAV SV