TKT1_VIBVY
ID TKT1_VIBVY Reviewed; 664 AA.
AC Q7MHK7;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1;
GN Name=tkt1; OrderedLocusNames=VV2862;
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016;
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA Lee C.-T., Hor L.-I., Tsai S.-F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC95626.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000037; BAC95626.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043877323.1; NC_005139.1.
DR AlphaFoldDB; Q7MHK7; -.
DR SMR; Q7MHK7; -.
DR STRING; 672.VV93_v1c25680; -.
DR EnsemblBacteria; BAC95626; BAC95626; BAC95626.
DR KEGG; vvy:VV2862; -.
DR PATRIC; fig|196600.6.peg.2849; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_1_6; -.
DR OMA; NSGHSGM; -.
DR OrthoDB; 188169at2; -.
DR Proteomes; UP000002675; Chromosome I.
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 3: Inferred from homology;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..664
FT /note="Transketolase 1"
FT /id="PRO_0000191888"
FT ACT_SITE 411
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 260
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 26
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 664 AA; 71755 MW; DC73FF383BE78149 CRC64;
MPSRKHLANA IRALSMDGVQ KANSGHPGAP MGMADIAEVL WRGHLNHNPS NPEWADRDRF
VLSNGHGSML IYSLLHLSGY ELSIDDLKNF RQLHSKTPGH PEYGYAPGIE TTTGPLGQGI
TNAVGMAMAE KALAAQFNKE GHDIVDHFTY VFMGDGCLME GISHEACSLA GTLGLGKLIA
FWDDNGISID GHVEGWFSDD TPKRFEAYGW HVIPAVDGHN AEAINAAIEA AKADPRPTLI
CTKTIIGFGS PNKSGSHDCH GAPLGAEEIA AAREFLGWEH PAFEIPADVY AEWDAKAAGA
AKEAAWNAKF DAYAAAYPAE AAEFKRRVNG ELPAQWEEKA NQIIADLQAN PANIASRKAS
QNALEAFGKM LPEFMGGSAD LAPSNLTMWS GSKSLEASDF SGNYIHYGVR EFGMTAIMNG
IALHGGFVPY GATFLMFMEY ARNAMRMAAL MKVQNIQVYT HDSIGLGEDG PTHQPVEQIA
SLRLTPNMST WRPCDQVESA VAWKLAIERK DGPSALIFSR QNLAQQPRSA EQVADIAKGG
YILKDSDGKP ELILIATGSE VELAVKAAEQ LTAEGKKVRV VSMPATDAFD KQDAAYRESV
LPSDVTARIA IEAGIADFWY KYVGFDGRII GMTTFGESAP ADQLFEMFGF TVENVVNTAK
ELLA
