TKT1_VIBCH
ID TKT1_VIBCH Reviewed; 665 AA.
AC Q9KUP2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1;
GN Name=tkt1; OrderedLocusNames=VC_0473;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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=AAF93646.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE003852; AAF93646.1; ALT_INIT; Genomic_DNA.
DR PIR; F82319; F82319.
DR RefSeq; NP_230127.1; NC_002505.1.
DR RefSeq; WP_000098688.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KUP2; -.
DR SMR; Q9KUP2; -.
DR STRING; 243277.VC_0473; -.
DR DNASU; 2615135; -.
DR EnsemblBacteria; AAF93646; AAF93646; VC_0473.
DR GeneID; 57739219; -.
DR KEGG; vch:VC_0473; -.
DR PATRIC; fig|243277.26.peg.447; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR OMA; HHTEGIE; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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..665
FT /note="Transketolase 1"
FT /id="PRO_0000191880"
FT ACT_SITE 412
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 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 521
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 665 AA; 71612 MW; 024B8A8D0A186043 CRC64;
MSSRKQLANA IRALSMDGVQ KANSGHPGAP MGMADIAEVL WRSHLNHNPQ NPNWADRDRF
VLSNGHGSML IYSLLHLSGY ELSIDDLKNF RQLHSKTPGH PEYGYAPGIE TTTGPLGQGI
TNAVGMAIAE KALAAQFNKP GHDIVDHFTY VFMGDGCLME GISHEACSLA GTLGLGKLIA
FWDDNGISID GHVEGWFSDD TPKRFEAYGW HVIPAVDGHD ADAINAAIEA AKAETSRPTL
ICTKTIIGFG SPNKAGSHDC HGAPLGNDEI KAAREFLGWE HAPFEIPADI YAAWDAKQAG
ASKEAAWNEK FAAYAKAYPA EAAEYKRRVA GELPANWEAA TSEIIANLQA NPANIASRKA
SQNALEAFGK LLPEFMGGSA DLAPSNLTMW SGSKSLTAED ASGNYIHYGV REFGMTAIIN
GIALHGGFVP YGATFLMFME YARNAMRMAA LMKVQNIQVY THDSIGLGED GPTHQPVEQI
ASLRMTPNMS TWRPCDQVES AVAWKLAIER KDAPSALIFS RQNLAQQPRS AEQVANIAKG
GYILKDCAGQ PELILIATGS EVELAVAAYE QLSAEGKAVR VVSMPSTDAF DKQDAAYREA
VLPAAVTKRI AIEAGIADFW YKYVGFGGRI IGMTSFGESA PAGELFKLFG FTTENVVKQA
KELLA
