TKT1_ALIF1
ID TKT1_ALIF1 Reviewed; 664 AA.
AC Q5E7R1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1;
GN Name=tkt1; OrderedLocusNames=VF_0440;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW84935.1; -; Genomic_DNA.
DR RefSeq; WP_011261222.1; NC_006840.2.
DR RefSeq; YP_203823.1; NC_006840.2.
DR AlphaFoldDB; Q5E7R1; -.
DR SMR; Q5E7R1; -.
DR STRING; 312309.VF_0440; -.
DR PRIDE; Q5E7R1; -.
DR EnsemblBacteria; AAW84935; AAW84935; VF_0440.
DR KEGG; vfi:VF_0440; -.
DR PATRIC; fig|312309.11.peg.430; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR OMA; EYRWTSG; -.
DR OrthoDB; 188169at2; -.
DR Proteomes; UP000000537; 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_0000191882"
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; 71806 MW; 1E85C234ABFC55B0 CRC64;
MSSRKHLANA IRALSMDGVQ QANSGHPGAP MGMADIAEVL WRSHLNHNPQ NPEWADRDRF
ILSNGHGSML IYSLLHLSGY DLSIEDLKNF RQLHSKTPGH PEYGYAPGVE TTTGPLGQGI
TNGVGMAMAE KALAAQFNRE GHDIVDHNTY VFMGDGCLME GISHEACSLA GTLGLGKLIA
FWDDNGISID GEVEGWFSDD TPKRFEAYGW HVIPAVDGHD SDAINAAIEA AKADPRPSLI
CTKTVIGFGS PNKQGTHDCH GAPLGAEEIA ATKAQLGWEY GAFDIPADVY AGWDAKEVGA
EKEAAWNAKF DAYAAAHPEL AAEYKRRVNG DLPAEWEEKA NTIIADLQAN PANIASRKAS
QNALEAFGAM LPEFMGGSAD LAPSNLTMWS GSKSLEANDF SGNYIHYGVR EFGMTAIMNG
IALHGGFVPY GATFLMFMEY ARNAMRMAAL MKVQNIQVYT HDSIGLGEDG PTHQPVEQIA
SLRLTPNMST WRPCDQVESA VAWKLAIERK DGPSSLIFSR QNLAQQERTQ EQVADIAKGA
YILKDCEGQP ELILIATGSE VELAVEAAAQ LTAEGKAVRV VSMPSTDAFD KQDEGYREAV
FPSAVTKRIA IEAGIADFWY KYVGFGGKII GMTTFGESAP ADELFKMFGF TTENVVNTAK
ELLA
