ID   RPE_SOLTU               Reviewed;         280 AA.
AC   Q43843;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   20-JAN-2009, entry version 62.
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; Fragment;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Desiree; TISSUE=Leaf;
RX   MEDLINE=96140545; PubMed=8549753; DOI=10.1016/0014-5793(95)01373-3;
RA   Teige M., Kopriva S., Bauwe H., Suess K.-H.;
RT   "Chloroplast pentose-5-phosphate 3-epimerase from potato: cloning,
RT   cDNA sequence, and tissue-specific enzyme accumulation.";
RL   FEBS Lett. 377:349-352(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   MEDLINE=99208761; PubMed=10191144; DOI=10.1006/jmbi.1999.2643;
RA   Kopp J., Kopriva S., Suess K.-H., Schulz G.E.;
RT   "Structure and mechanism of the amphibolic enzyme D-ribulose-5-
RT   phosphate 3-epimerase from potato chloroplasts.";
RL   J. Mol. Biol. 287:761-771(1999).
CC   -!- FUNCTION: Converts xylulose 5-phosphate to ribulose 5-phosphate
CC       via epimerization.
CC   -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane.
CC   -!- TISSUE SPECIFICITY: Highest level of expression in leaves, whereas
CC       it is low in roots, tubers, and stems.
CC   -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
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DR   EMBL; Z50098; CAA90426.1; -; mRNA.
DR   PIR; S68407; S68407.
DR   PDB; 1RPX; X-ray; 2.30 A; A/B/C=47-276.
DR   PDBsum; 1RPX; -.
DR   BRENDA; 5.1.3.1; 296.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; ISS:UniProtKB.
DR   GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; ISS:UniProtKB.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-KW.
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   3D-structure; Calvin cycle; Carbohydrate metabolism; Chloroplast;
KW   Direct protein sequencing; Isomerase; Membrane; Pentose shunt;
KW   Plastid; Thylakoid; Transit peptide.
FT   TRANSIT      <1     45       Chloroplast.
FT   CHAIN        46    280       Ribulose-phosphate 3-epimerase,
FT                                chloroplastic.
FT                                /FTId=PRO_0000025417.
FT   NON_TER       1      1
FT   HELIX        48     51
FT   STRAND       58     62
FT   HELIX        63     65
FT   HELIX        68     70
FT   HELIX        71     80
FT   STRAND       86     97
FT   HELIX       103    109
FT   HELIX       110    112
FT   STRAND      117    125
FT   HELIX       126    135
FT   STRAND      139    144
FT   TURN        147    149
FT   HELIX       153    162
FT   STRAND      165    171
FT   HELIX       177    180
FT   TURN        181    186
FT   STRAND      188    195
FT   HELIX       208    222
FT   STRAND      227    233
FT   TURN        236    238
FT   HELIX       239    245
FT   STRAND      249    253
FT   HELIX       254    257
FT   HELIX       262    270
SQ   SEQUENCE   280 AA;  29881 MW;  3381A798F056491C CRC64;
     SLGSSTLLQS QISGFGGSQK LQKISFSNPN SLTFTRRRIQ TVVNASSRVD KFSKSDIIVS
     PSILSANFSK LGEQVKAIEQ AGCDWIHVDV MDGRFVPNIT IGPLVVDSLR PITDLPLDVH
     LMIVEPDQRV PDFIKAGADI VSVHCEQSST IHLHRTINQI KSLGAKAGVV LNPGTPLTAI
     EYVLDAVDLV LIMSVNPGFG GQSFIESQVK KISDLRKICA ERGLNPWIEV DGGVGPKNAY
     KVIEAGANAL VAGSAVFGAP DYAEAIKGIK TSKRPEAVAV
//