ID A0A061FXB1_THECC Unreviewed; 200 AA.
AC A0A061FXB1;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ribulose-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00013188};
DE EC=5.1.3.1 {ECO:0000256|ARBA:ARBA00013188};
DE AltName: Full=Pentose-5-phosphate 3-epimerase {ECO:0000256|ARBA:ARBA00030599};
GN ORFNames=TCM_014095 {ECO:0000313|EMBL:EOY21921.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY21921.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY21921.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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:0000256|ARBA:ARBA00001782};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR001461-2};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000256|PIRSR:PIRSR001461-2};
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000256|ARBA:ARBA00009541}.
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DR EMBL; CM001881; EOY21921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FXB1; -.
DR EnsemblPlants; EOY21921; EOY21921; TCM_014095.
DR Gramene; EOY21921; EOY21921; TCM_014095.
DR HOGENOM; CLU_054856_1_1_1; -.
DR Proteomes; UP000026915; Chromosome 3.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:InterPro.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR01163; rpe; 1.
DR PANTHER; PTHR11749; RIBULOSE-5-PHOSPHATE-3-EPIMERASE; 1.
DR PANTHER; PTHR11749:SF3; RIBULOSE-PHOSPHATE 3-EPIMERASE; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR PIRSF; PIRSF001461; RPE; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR001461-2};
KW Manganese {ECO:0000256|PIRSR:PIRSR001461-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001461-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW Zinc {ECO:0000256|PIRSR:PIRSR001461-2}.
FT ACT_SITE 141
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-1"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 108..111
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 141
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-2"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
FT BINDING 163..164
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001461-3"
SQ SEQUENCE 200 AA; 21453 MW; 5280BA7665634598 CRC64;
MDGRFVPNIT IGPIVVDALR PVTDLPLDVH LMIVEPEQRV PDFIKAGADI VSVHCEQSST
IHLHRTLNQI KGLGAKAGVV LNPATPLSTI EYVLDVVDLV LIMSVNPGFG GQSFIESQVK
KISDLRRMCA EKGVNPWIEV DGGVGPKNAY KVIEAGANAL VAGSAVFGAK DYAEGMDREL
FLNFPIRGIK TSKKPEAVAV
//
