TKT7_CRAPL
ID TKT7_CRAPL Reviewed; 676 AA.
AC Q42677;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Transketolase 7;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT7;
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].
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: Could be involved in the conversion of sugars, which are a
CC major phenomenon in the rehydration process.
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. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Leaves and roots.
CC -!- INDUCTION: By rehydration.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; Z46648; CAA86609.1; -; mRNA.
DR PIR; S54301; S54301.
DR AlphaFoldDB; Q42677; -.
DR SMR; Q42677; -.
DR PRIDE; Q42677; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; Magnesium; Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..676
FT /note="Transketolase 7"
FT /id="PRO_0000191907"
FT ACT_SITE 421
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 125..127
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 421
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 448
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 472
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 480
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 531
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 36
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 273
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 676 AA; 73410 MW; 6119032DCEE31F28 CRC64;
MAPKTTLIAE PELVSKSVNT IRFLAIDAVE KAKSGHPGMP MGCAPMGHVL YDEFMRFNPK
NPYWFNRDRF VLSAGHGCML QYALLHLSGY DSVKEEDLKS LRQWGSRTPA HPENFETPGV
EVTTGPLGQG IASAVGLAVA EKHLAARYNK PGFEIVDHYT YVILGDGCQM EGVSNEACSL
AAHWGLGKLI ALYDDNHITI DGDTDVAFTE DVDKRFDALG WHVIWVKNGN DGCDEIRAAI
EEAKSVKDRP TMIKVTTTIG YGAPSKANTY GVHGNALGPK EAEATRKNLG WPYEPFHVPD
DVKKHWSRHI AEGAALESAW NAKFAEFQKK FPEEAADLKS IITGELPTNW ESIFPTYTPE
NPGLPTRTLS HQILNGLGDV LPGLLGGSAD LTLSNMAFLK NSGDFQKKSP GERNVKFGAR
EHAMGSICNG LALHSPGLLP YCATYFVFTD YMRAAMRISA LSKARVLYIM THDSIGLGED
GPTHQPVEHL ASFRAMPNIL TLRPADGNET AGAYRAAVQN GERPSILVLA RQKLPQLPGT
SIEGVSKGGY VISDNSRGGN SKPDVILIGT GSELEIAARA GDELRKEGKK VRVVSLVCWE
LFAEQSEKYR ETVLPSGVTA RVSVEAGSTF GWERFIGPKG KAVGIDRFGA SAPAERLFKE
FGITVEAVVA AAKEIC
