TKTC_CRAPL
ID TKTC_CRAPL Reviewed; 519 AA.
AC Q42676;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Transketolase, chloroplastic;
DE Short=TK;
DE EC=2.2.1.1;
DE Flags: Fragment;
GN Name=TKT3;
OS Craterostigma plantagineum (Blue gem) (Torenia plantagineum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Linderniaceae; Craterostigma.
OX NCBI_TaxID=4153;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7859749; DOI=10.1002/j.1460-2075.1995.tb07037.x;
RA Bernacchia G., Schwall G., Lottspeich F., Salamini F., Bartels D.;
RT "The transketolase gene family of the resurrection plant Craterostigma
RT plantagineum: differential expression during the rehydration phase.";
RL EMBO J. 14:610-618(1995).
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Constitutively expressed in leaves and roots.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; Z46646; CAA86607.1; -; mRNA.
DR PIR; S54300; S54300.
DR AlphaFoldDB; Q42676; -.
DR SMR; Q42676; -.
DR PRIDE; Q42676; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Chloroplast; Direct protein sequencing; Magnesium; Metal-binding;
KW Plastid; Thiamine pyrophosphate; Transferase.
FT CHAIN <1..519
FT /note="Transketolase, chloroplastic"
FT /id="PRO_0000191906"
FT ACT_SITE 266
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 41
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 118
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 519 AA; 56188 MW; 7AFD034CE2EC5685 CRC64;
VDHYTYCILG DGCQMEGVSN EACSIAAHWG LGKLIALYDD NHISIDGDTD IAFTEDVDKR
FEALGWHVIW VKNGNNGYDK IRAAIKEAQA VKDKPTMIKI TTTIGFGSPN KSNSYSVHGS
ALGAKEVEAT RQNLGWPYEP FHVPDDVKKH WSRHTPQGAS LESEWNAKFA EYEKKYPEEA
AELKSIITGE LPLGWEKALP TYTPENPGDA TRNLSQQNLN ALAKVLPGLL GGSADLASSN
MTLLKSSGDF QKNTPEERNV RFGVREHGMG AICNGIALHS PGLIPYCATF FVFTDYMRAA
MRISALCEAR VIYVMTHDSI GLGEDGPTHQ PIEHLASFRA MPNILMLRPA DGNETAGAYK
VAVQNLKRPS VLALSRQKLP QLPGTSIEGV EKGGYVISDN SSGNKPDVIL IGTGSELEIA
AKAGEVLRKE GKGVRVVSFV SWELFDEQSK EYKESVLPSS VTARVSIEAG STFGWGKIVG
SKGKAIGIDR FGASAPAGKI YEEFGITVEA VVAAAKELI
