TKT_STRP6
ID TKT_STRP6 Reviewed; 729 AA.
AC Q5XAK5; P82578;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt {ECO:0000250|UniProtKB:Q9KAD7}; OrderedLocusNames=M6_Spy1423;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1] {ECO:0000312|EMBL:AAT87558.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 289-304; 347-364; 376-400; 495-512 AND 696-710.
RC STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
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}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000255}.
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DR EMBL; CP000003; AAT87558.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5XAK5; -.
DR SMR; Q5XAK5; -.
DR EnsemblBacteria; AAT87558; AAT87558; M6_Spy1423.
DR KEGG; spa:M6_Spy1423; -.
DR HOGENOM; CLU_009227_0_0_9; -.
DR OMA; YALQQTD; -.
DR Proteomes; UP000001167; Chromosome.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Magnesium; Metal-binding;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..729
FT /note="Transketolase"
FT /id="PRO_0000287915"
FT ACT_SITE 477
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 332
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 527
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 586
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 97
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 332
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 729 AA; 79311 MW; DCB6E03506D0D002 CRC64;
MATVSTGSLI FIVKKNSPMM SKLVFFWQNR EKEFRDFGGF SEKSVYFCDT IDNRKRLILV
VINREVLLMT FDAIDQLAVN TVRTLSMDAI QAANSGHPGL PMGAAPMAYV LWNHFMNINP
KTSRNWSNRD RFILSAGHGS AMLYSLLHLA GYDLSVEDLK NFRQWGSKTP GHPEVNHTDG
VEATTGPLGQ GIANAVGMAM AEAHLAAKFN KPGFDIVDHY TFALNGDGDL MEGVSQEAAS
MAGHLKLGKL VLLYDSNDIS LDGPTSMAFT EDVKGRFEAY GWQHILVKDG NDLEEIAAAI
EAAKAETEKP TIIEVKTIIG FGAEKQGTSA VHGAPLGAEG IAFAKKAYQW THQDFEVPAE
VTERFAQGLQ ARGEKAEQAW NDLFAAYEAE YPELAAEYQK AFANEAAQVE LEAHELGSSM
ASRVSSQQAI QQISEQVASF WGGSADLSAS NNTMVKAETD FQPGHYEGRN VWFGVREFAM
AAAMNGIALH GGTRVYGGTF FVFSNYLLPA VRMAALQNLP TVYVMTHDSI AVGEDGPTHE
PIEQLASVRS MPNLNVIRPA DGNETNAAWK RAIAETDRPT MLVLTRQNLP VLEGTKELAE
DGLNKGAYIL SEAKGDLEGI LIATGSEVKL AMDTQEALEA EGIHVRVVSM PSQNIFDEQS
AEYKESILPA AVTKRLAIEA GSSFGWAKYV GLAGKTLTID TWGASAPGNR IFEEYGFTVA
NATELYKSL
