RPE_SOLTU
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 03-AUG-2022, entry version 113.
DE RecName: Full=Ribulose-phosphate 3-epimerase, chloroplastic;
DE EC=5.1.3.1 {ECO:0000250|UniProtKB:Q43157};
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RX 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, cDNA
RT sequence, and tissue-specific enzyme accumulation.";
RL FEBS Lett. 377:349-352(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), AND SUBUNIT.
RX 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-phosphate 3-
RT epimerase from potato chloroplasts.";
RL J. Mol. Biol. 287:761-771(1999).
CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-
CC phosphate to D-xylulose 5-phosphate. {ECO:0000250|UniProtKB:Q43157}.
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:Q43157};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q96AT9};
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 Note=Binds 1 divalent metal cation per subunit. Active with Co(2+),
CC Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250|UniProtKB:Q96AT9};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000250|UniProtKB:Q43157}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:10191144}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q43157}.
CC -!- TISSUE SPECIFICITY: Highest level of expression in leaves, whereas it
CC is low in roots, tubers, and stems. {ECO:0000269|PubMed:8549753}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
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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 AlphaFoldDB; Q43843; -.
DR SMR; Q43843; -.
DR STRING; 4113.PGSC0003DMT400050256; -.
DR PRIDE; Q43843; -.
DR eggNOG; KOG3111; Eukaryota.
DR SABIO-RK; Q43843; -.
DR UniPathway; UPA00116; -.
DR EvolutionaryTrace; Q43843; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43843; baseline.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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 3D-structure; Calvin cycle; Carbohydrate metabolism; Chloroplast; Cobalt;
KW Direct protein sequencing; Iron; Isomerase; Manganese; Membrane;
KW Metal-binding; Pentose shunt; Plastid; Reference proteome; Thylakoid;
KW Transit peptide; Zinc.
FT TRANSIT <1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:8549753"
FT CHAIN 46..280
FT /note="Ribulose-phosphate 3-epimerase, chloroplastic"
FT /id="PRO_0000025417"
FT ACT_SITE 89
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT ACT_SITE 231
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 89
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 120
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 198..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 231..233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 231
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 253..254
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT NON_TER 1
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 117..125
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1RPX"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1RPX"
FT TURN 181..186
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 188..195
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:1RPX"
FT TURN 236..238
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:1RPX"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:1RPX"
FT HELIX 262..270
FT /evidence="ECO:0007829|PDB:1RPX"
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
