TKT_POPEU
ID TKT_POPEU Reviewed; 15 AA.
AC P84540;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 11-DEC-2019, entry version 30.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
DE Flags: Fragment;
OS Populus euphratica (Euphrates poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=75702;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Leaf;
RX PubMed=16740589; DOI=10.1093/aob/mcl106;
RA Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA Roepstorff P., Pais M.S.;
RT "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL Ann. Bot. 98:361-377(2006).
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 Evidence={ECO:0000250|UniProtKB:P23254};
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|UniProtKB:P23254};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P23254};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P23254}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000255}.
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DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Thiamine pyrophosphate; Transferase.
FT CHAIN <1..>15
FT /note="Transketolase"
FT /id="PRO_0000191909"
FT NON_TER 1
FT NON_TER 15
SQ SEQUENCE 15 AA; 1590 MW; 7041E7E7EC8959BE CRC64;
ALPTYTPESP ADATR