TKT_PHYPO
ID TKT_PHYPO Reviewed; 661 AA.
AC A6YB01;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=17562012; DOI=10.1186/1471-2148-7-89;
RA Rogers M.B., Watkins R.F., Harper J.T., Durnford D.G., Gray M.W.,
RA Keeling P.J.;
RT "A complex and punctate distribution of three eukaryotic genes derived by
RT lateral gene transfer.";
RL BMC Evol. Biol. 7:89-89(2007).
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 -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; EF216684; ABQ23348.1; -; mRNA.
DR AlphaFoldDB; A6YB01; -.
DR SMR; A6YB01; -.
DR PRIDE; A6YB01; -.
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..661
FT /note="Transketolase"
FT /id="PRO_0000331221"
FT REGION 99..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 118..120
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 266
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 357
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 437
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 461
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 520
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 30
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 266
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 661 AA; 70941 MW; E4B9FB0D5225D3DF CRC64;
MSLNLAALAQ AANEARGLGM DAVEKAASGH LGLPLGCAEL GATLFGHAFR YNPDKPEWLN
RDIFVLSAGH GSMFLYAWLH LSGYKVSLDD IKQFRQLSST TPGHPEFRDT PGVEATTGPL
GQGVGNGLGY AVACKMAQAH FNTKDHKIFD QKVVVLAGDG CLQEGVAQEA SALAGHLHLD
NLIIFYDSND VTLDAMAIES QSEDTAKRYE AYGFEVVTVK EGHNIERILE AYEHAKNSTS
GKPQLIILKT TIAKGITEVA GTNKGHGEAG VKFVAAARKG LGLPEEKFFV SKGTRDYFQA
HKEKLQKEYA SWEKLYSEWR SANPELAALL DSAKVTPDAS KLFSVIPKFA DAPIATRKAG
SDVLQPLAKA LPLFISGSAD LHGSTLNYIA GAGDYTPKNT GGRNIKFGIR EHAMGAMLNG
FAYHGIFRPS GATFLVFSDY LRPSIRLAAL SHLPVIYIFT HDSVAVGEDG PTHQPVETVS
SLRLIPNLDV IRPGDHEETA GAFVAALSRT TGPTLLALCR QNLPNLSQFD VNARREGVLK
GGYILQKETG ALKVIVISTG SELNVAVEAA KRLGDGVRVV SMPSTYRFDQ QPAEYKEEVL
PSSCKKRVVI EAGVTPLWHK YVGLEGKIIG IDRFGTSAPG ATVLKTLGIT ADAVVAAANS
F
