TKTA_CRAPL
ID TKTA_CRAPL Reviewed; 679 AA.
AC Q42675;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transketolase 10;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=TKT10;
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.
CC -!- INDUCTION: By rehydration.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; Z46647; CAA86608.1; -; mRNA.
DR PIR; S54299; S54299.
DR AlphaFoldDB; Q42675; -.
DR SMR; Q42675; -.
DR PRIDE; Q42675; -.
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..679
FT /note="Transketolase 10"
FT /id="PRO_0000191908"
FT ACT_SITE 425
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 129..131
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 277
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 476
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 40
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 277
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 679 AA; 73130 MW; 1109092E136A345B CRC64;
MAKTTPSSPS AAAAAELVVK SVNTIRFLAI DAVENVKSGH PGMPMGCAPM GHVLFDEFMK
FNPKNPYWFN RDRFVLSAGH GAMLLYGLLH LAGYDSVKVE DLKGLRQWGS KTPAHPENFE
TPGVEVTTGP LGQGVGSAVG LALAEKHLGA RYNKPDFEMV DHYTYMILGD GCQMEGISNE
ASSLAAHWGL GKLIALYDDN HITIDGDTDL AFTEDVGKRF EALGWHVLTV ANGNDGYDEI
REAIKVAKSV TDKPTLIKVA TTIGFGSPNK ANTYGVHGNA LGPKEAEATR QNLGWPYETF
HVPDDVKKHW SRHISEGAEL ESAWNAKFAE YEKKYPKEAA ELKSIITGEL PLGWEKALPT
YTPESPGNPT RTLSHQNLNA VAAVLPGLIG GSADLTASNM AFLKSSGDFQ KETPTGRNLK
FGAREHGMGA ICNGVALHSP GLVPFSATYF VFTDYMRAAI RIAALSKARV VYIMTHDSIG
LGEDGPTHQP VEHLASFRAM PNILVLRPAD GNETAGAYKV AVENAGRPSI LSLSRQKLPQ
LPGTSVEGVG RGGYVISDNS KDGEKPEVIL MGTGSELEIA ARAGEELRKE GKKVRVVSLV
SWELFGEQSK EYKEMVLPSE VTARVSVEAG STFGWERFVG LKGRAVGIDR FGASASAERL
YKEFGITVEA VVAAAKELC
