ID   RPE_PONAB               Reviewed;         228 AA.
AC   Q5R5Y2;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Ribulose-phosphate 3-epimerase;
DE            EC=5.1.3.1 {ECO:0000250|UniProtKB:Q96AT9};
DE   AltName: Full=Ribulose-5-phosphate-3-epimerase;
GN   Name=RPE;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC       phosphate to D-xylulose 5-phosphate. {ECO:0000250|UniProtKB:Q96AT9}.
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:0000250|UniProtKB:Q96AT9};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000250|UniProtKB:Q96AT9};
CC       Note=Binds 1 divalent metal cation per subunit. Active with Fe(2+), and
CC       probably also with Mn(2+), Zn(2+) and Co(2+).
CC       {ECO:0000250|UniProtKB:Q96AT9};
CC   -!- PATHWAY: Carbohydrate degradation. {ECO:0000250|UniProtKB:Q96AT9}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96AT9}.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC       {ECO:0000305}.
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DR   EMBL; CR860719; CAH92834.1; -; mRNA.
DR   RefSeq; NP_001126655.1; NM_001133183.1.
DR   AlphaFoldDB; Q5R5Y2; -.
DR   SMR; Q5R5Y2; -.
DR   STRING; 9601.ENSPPYP00000014676; -.
DR   PRIDE; Q5R5Y2; -.
DR   GeneID; 100173655; -.
DR   KEGG; pon:100173655; -.
DR   CTD; 6120; -.
DR   eggNOG; KOG3111; Eukaryota.
DR   InParanoid; Q5R5Y2; -.
DR   OrthoDB; 1554029at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006098; P:pentose-phosphate shunt; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Carbohydrate metabolism; Cobalt; Iron; Isomerase; Manganese;
KW   Metal-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AT9"
FT   CHAIN           2..228
FT                   /note="Ribulose-phosphate 3-epimerase"
FT                   /id="PRO_0000171589"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         35
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         37
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         70
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         146..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         175..177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         175
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   BINDING         197..198
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P32719"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AT9"
SQ   SEQUENCE   228 AA;  24898 MW;  4F7190008AC53330 CRC64;
     MASGCKIGPS ILNSDLANLG AECLRMLDSG ADYLHLDVMD GHFVPNITFG HPVVESLRKQ
     LGQDPFFDMH MMVSKPEQWV KPMAVAGANQ YAFHLEATEN PGALIKDIRE NGMKVGLAIK
     PGTSVEYLAP WANQIDMALV MTVEPGFGGQ KFMEDMMPKV HWLRTQFPSL DIEVDGGVGP
     DTVHKCAEAG ANMIVSGSAI MRSEDPRSVI NLLRNVCSEA AQKRSLDR