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   05-MAY-2009, entry version 55.
DE   RecName: Full=Ribulose-phosphate 3-epimerase, chloroplastic;
DE            EC=5.1.3.1;
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   Caryophyllales; Amaranthaceae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   MEDLINE=96191291; 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-
RT   phosphate 3-epimerase (EC 5.1.3.1) from spinach chloroplasts:
RT   functional and evolutionary aspects.";
RL   Plant Mol. Biol. 29:1279-1291(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=cv. Melody;
RX   MEDLINE=98404247; 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
RT   expression of the spinach gene, and purification and characterization
RT   of the recombinant enzyme.";
RL   Plant Physiol. 118:199-207(1998).
RN   [3]
RP   PROTEIN SEQUENCE OF 51-66, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Matador;
RX   MEDLINE=98181867; PubMed=9523694;
RX   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
RT   spinach chloroplasts.";
RL   Eur. J. Biochem. 252:237-244(1998).
RN   [4]
RP   ACTIVE SITE, AND MUTAGENESIS OF ASP-236.
RX   MEDLINE=99107865; 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-
RT   phosphate 3-epimerase by site-directed mutagenesis.";
RL   J. Biol. Chem. 274:2132-2136(1999).
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=250 uM for ribulose 5-phosphate;
CC       pH dependence:
CC         Optimum pH is 8.5;
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homooctamer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
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DR   EMBL; L42328; AAC41677.1; -; mRNA.
DR   EMBL; AF070941; AAC24708.1; -; mRNA.
DR   PIR; S62724; S62724.
DR   HSSP; Q43843; 1RPX.
DR   SMR; Q43157; 52-281.
DR   BRENDA; 5.1.3.1; 286.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:UniProtKB.
DR   GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IDA:UniProtKB.
DR   GO; GO:0006098; P:pentose-phosphate shunt; NAS:UniProtKB.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS:UniProtKB.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000056; Ribul_P_3_epim.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11749; Ribul_P_3_epim; 1.
DR   Pfam; PF00834; Ribul_P_3_epim; 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;
KW   Direct protein sequencing; Isomerase; Membrane; Pentose shunt;
KW   Plastid; Thylakoid; Transit peptide.
FT   TRANSIT       1     50       Chloroplast.
FT   CHAIN        51    285       Ribulose-phosphate 3-epimerase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000025416.
FT   ACT_SITE    236    236       Electrophile (Probable).
FT   MUTAGEN     236    236       D->A,E,N: Change in activity.
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
//