TKTC_SOLTU
ID TKTC_SOLTU Reviewed; 741 AA.
AC Q43848;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transketolase, chloroplastic;
DE Short=TK;
DE EC=2.2.1.1;
DE Flags: Precursor;
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].
RC STRAIN=cv. Desiree; TISSUE=Leaf;
RA Teige M., Kopriva S., Bauwe H., Suess K.-H.;
RT "Primary structure of chloroplast transketolase from potato.";
RL (er) Plant Gene Register PGR96-121(1996).
CC -!- FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group
CC from fructose-6-phosphate or sedoheptulose-7-phosphate to
CC glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-
CC 4-phosphate or ribose-5-phosphate, respectively. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; Z50099; CAA90427.1; -; mRNA.
DR PIR; S58083; S58083.
DR RefSeq; NP_001275202.1; NM_001288273.1.
DR AlphaFoldDB; Q43848; -.
DR SMR; Q43848; -.
DR STRING; 4113.PGSC0003DMT400056799; -.
DR PRIDE; Q43848; -.
DR GeneID; 102591899; -.
DR KEGG; sot:102591899; -.
DR eggNOG; KOG0523; Eukaryota.
DR OrthoDB; 354970at2759; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q43848; baseline and differential.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; ISS:UniProtKB.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Chloroplast; Magnesium; Membrane; Metal-binding; Plastid;
KW Reference proteome; Thiamine pyrophosphate; Thylakoid; Transferase;
KW Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000250"
FT CHAIN 68..741
FT /note="Transketolase, chloroplastic"
FT /id="PRO_0000035751"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 192..194
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 515
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 598
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 103
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 340
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 741 AA; 79992 MW; 2B4C83DB54BF554A CRC64;
MASSSSLTLS QVIFSPSLPR HGSSSSSSPS LSFSTFSGLK STPFTSSHRR ILPSTTVTKQ
QFSVRASAAV ETLEKTDAAI VEKSVNTIRF LAIDAVEKAN SGHPGLPMGC APMGHILYDE
VMKYNPKNPY WFNRDRFVLS AGHGCMLQYA LLHLAGYDSV QEDDLKSFRQ WGSRIPGHPE
NFETPGVEVT TGPLGQGIAN AVGLAVAEKH LAARFNKPDA EIVDHYTYVI LGDGCQMEGI
SNEVCSLAGH WGLGKLIAFY DDNHISIDGD TEIAFTEDVS ARFESLGWHV IWVKNGNTGY
DEIRAAIKEA KAVKDKPTMI KVTTTIGFGS PNKANSYSVH GSGLGAKEVE ATRNNLGWPY
EPFHVPEDVK SHWSRHTPEG AALETEWNAK FAEYEKKYAE EAADLKSIIT GELPAGWEKA
LPTYTPESPA DATRNLSQQN LNALAKVLPG FLGGSADLAS SNMTLLKMFG DFQKNTPEER
NLRFGVREHG MGAICNGIAL HSLGLIPYCA TFFVFTDYMR GAMRISALSE AGVIYVMTHD
SIGLGEDGPT HQPIEHLASF RAMPNILMFR PADGNETAGA YKVAVLKRKT PSILALSRQK
LPQLAGTSIE GAAKGGYIVS DNSSGNKPDV ILIGTGSELE IAVKAAEELK KEGKTVRVVS
FVCWELYDEQ SAEYKESVLP SSVTARVSIE AGSTFGWQKF VGDKGKAIGI DGFGASAPAD
KIYKEFGITA EAVVAAAKQV S
