RPE_SPIOL
ID RPE_SPIOL Reviewed; 285 AA.
AC Q43157;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ribulose-phosphate 3-epimerase, chloroplastic;
DE EC=5.1.3.1 {ECO:0000269|PubMed:8616224, ECO:0000269|PubMed:9733539, ECO:0000269|PubMed:9890975};
DE AltName: Full=Pentose-5-phosphate 3-epimerase;
DE Short=PPE;
DE AltName: Full=R5P3E;
DE Short=RPE;
DE Flags: Precursor;
GN Name=RPE;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP PATHWAY.
RC STRAIN=cv. Melody;
RX PubMed=9733539; DOI=10.1104/pp.118.1.199;
RA Chen Y.-R., Hartman F.C., Lu T.-Y.S., Larimer F.W.;
RT "D-ribulose-5-phosphate 3-epimerase: cloning and heterologous expression of
RT the spinach gene, and purification and characterization of the recombinant
RT enzyme.";
RL Plant Physiol. 118:199-207(1998).
RN [3]
RP PROTEIN SEQUENCE OF 51-66, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=cv. Matador;
RX PubMed=9523694; DOI=10.1046/j.1432-1327.1998.2520237.x;
RA Teige M., Melzer M., Suess K.-H.;
RT "Purification, properties and in situ localization of the amphibolic
RT enzymes D-ribulose 5-phosphate 3-epimerase and transketolase from spinach
RT chloroplasts.";
RL Eur. J. Biochem. 252:237-244(1998).
RN [4]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE,
RP MUTAGENESIS OF ASP-236, AND PATHWAY.
RX PubMed=9890975; DOI=10.1074/jbc.274.4.2132;
RA Chen Y.-R., Larimer F.W., Serpersu E.H., Hartman F.C.;
RT "Identification of a catalytic aspartyl residue of D-ribulose 5-phosphate
RT 3-epimerase by site-directed mutagenesis.";
RL J. Biol. Chem. 274:2132-2136(1999).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:8616224,
CC ECO:0000269|PubMed:9523694, ECO:0000269|PubMed:9733539}.
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:0000269|PubMed:8616224,
CC ECO:0000269|PubMed:9733539, ECO:0000269|PubMed:9890975};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal cation per subunit. Active with Co(2+),
CC Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=250 uM for ribulose 5-phosphate {ECO:0000269|PubMed:9523694,
CC ECO:0000269|PubMed:9890975};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:9523694,
CC ECO:0000269|PubMed:9890975};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000269|PubMed:8616224, ECO:0000269|PubMed:9523694,
CC ECO:0000269|PubMed:9733539, ECO:0000269|PubMed:9890975}.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:9733539,
CC ECO:0000269|PubMed:9890975}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:9523694}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
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DR EMBL; L42328; AAC41677.1; -; mRNA.
DR EMBL; AF070941; AAC24708.1; -; mRNA.
DR PIR; S62724; S62724.
DR AlphaFoldDB; Q43157; -.
DR SMR; Q43157; -.
DR PRIDE; Q43157; -.
DR OrthoDB; 1554029at2759; -.
DR BRENDA; 5.1.3.1; 5812.
DR SABIO-RK; Q43157; -.
DR UniPathway; UPA00116; -.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; NAS:UniProtKB.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS: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 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 1: Evidence at protein level;
KW Calvin cycle; Carbohydrate metabolism; Chloroplast; Cobalt;
KW Direct protein sequencing; Iron; Isomerase; Manganese; Membrane;
KW Metal-binding; Pentose shunt; Plastid; Thylakoid; Transit peptide; Zinc.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:9523694"
FT CHAIN 51..285
FT /note="Ribulose-phosphate 3-epimerase, chloroplastic"
FT /id="PRO_0000025416"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT ACT_SITE 236
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:9890975"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 92
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 203..206
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 236..238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 236
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 258..259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT MUTAGEN 236
FT /note="D->A,E,N: Almost abolished enzyme activity."
FT /evidence="ECO:0000269|PubMed:9890975"
SQ SEQUENCE 285 AA; 30366 MW; ED0236FB7B629512 CRC64;
MSAASLCQST LQSQINGFCG GLNIRKLQPS TSSPNSLTFT RRKVQTLVKA TSRVDKFSKS
DIIVSPSILS ANFAKLGEQV KAVELAGCDW IHVDVMDGRF VPNITIGPLV VDALRPVTDL
PLDVHLMIVE PEQRVPDFIK AGADIVSVHC ELASTIHLHR TVNQIKSLGA KAGVVLNPGT
PLSTIEYVLD VVDLVLIMSV NPGFGGQSFI ESQVKKISDL RKMCVEKGVN PWIEVDGGVT
PANAYKVIEA GANALVAGSA VFGAKDYAEA IKGIKASKRP EPVAV
