TKT2_ECOLI
ID TKT2_ECOLI Reviewed; 667 AA.
AC P33570;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Transketolase 2;
DE Short=TK 2;
DE EC=2.2.1.1 {ECO:0000269|PubMed:8396116};
GN Name=tktB {ECO:0000303|PubMed:8396116}; OrderedLocusNames=b2465, JW2449;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=8396116; DOI=10.1128/jb.175.17.5375-5383.1993;
RA Iida A., Teshiba S., Mizobuchi K.;
RT "Identification and characterization of the tktB gene encoding a second
RT transketolase in Escherichia coli K-12.";
RL J. Bacteriol. 175:5375-5383(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-342, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group
CC from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing
CC xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of
CC a two-carbon ketol group from a ketose donor to an aldose acceptor, via
CC a covalent intermediate with the cofactor thiamine pyrophosphate.
CC {ECO:0000269|PubMed:8396116}.
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:0000269|PubMed:8396116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10509;
CC Evidence={ECO:0000269|PubMed:8396116};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10510;
CC Evidence={ECO:0000269|PubMed:8396116};
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; D12473; BAA02039.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75518.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16340.1; -; Genomic_DNA.
DR PIR; A48660; A48660.
DR RefSeq; NP_416960.1; NC_000913.3.
DR RefSeq; WP_000087280.1; NZ_LN832404.1.
DR AlphaFoldDB; P33570; -.
DR SMR; P33570; -.
DR BioGRID; 4262216; 19.
DR DIP; DIP-10999N; -.
DR IntAct; P33570; 6.
DR STRING; 511145.b2465; -.
DR iPTMnet; P33570; -.
DR jPOST; P33570; -.
DR PaxDb; P33570; -.
DR PRIDE; P33570; -.
DR EnsemblBacteria; AAC75518; AAC75518; b2465.
DR EnsemblBacteria; BAA16340; BAA16340; BAA16340.
DR GeneID; 945865; -.
DR KEGG; ecj:JW2449; -.
DR KEGG; eco:b2465; -.
DR PATRIC; fig|511145.12.peg.2559; -.
DR EchoBASE; EB2024; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_6; -.
DR InParanoid; P33570; -.
DR OMA; YALQQTD; -.
DR PhylomeDB; P33570; -.
DR BioCyc; EcoCyc:TRANSKETOII-MON; -.
DR BioCyc; MetaCyc:TRANSKETOII-MON; -.
DR BRENDA; 2.2.1.1; 2026.
DR PRO; PR:P33570; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IMP:EcoliWiki.
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 1: Evidence at protein level;
KW Acetylation; Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..667
FT /note="Transketolase 2"
FT /id="PRO_0000191857"
FT ACT_SITE 410
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 113..115
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186
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 436
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 519
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 260
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 342
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
SQ SEQUENCE 667 AA; 73043 MW; 451D748B13ED51E5 CRC64;
MSRKDLANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPTD PTWYDRDRFI
LSNGHASMLL YSLLHLTGYD LPLEELKNFR QLHSKTPGHP EIGYTPGVET TTGPLGQGLA
NAVGLAIAER TLAAQFNQPD HEIVDHFTYV FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF
YDHNGISIDG ETEGWFTDDT AKRFEAYHWH VIHEIDGHDP QAVKEAILEA QSVKDKPSLI
ICRTVIGFGS PNKAGKEEAH GAPLGEEEVA LARQKLGWHH PPFEIPKEIY HAWDAREKGE
KAQQSWNEKF AAYKKAHPQL AEEFTRRMSG GLPKDWEKTT QKYINELQAN PAKIATRKAS
QNTLNAYGPM LPELLGGSAD LAPSNLTIWK GSVSLKEDPA GNYIHYGVRE FGMTAIANGI
AHHGGFVPYT ATFLMFVEYA RNAARMAALM KARQIMVYTH DSIGLGEDGP THQAVEQLAS
LRLTPNFSTW RPCDQVEAAV GWKLAVERHN GPTALILSRQ NLAQVERTPD QVKEIARGGY
VLKDSGGKPD IILIATGSEM EITLQAAEKL AGEGRNVRVV SLPSTDIFDA QDEEYRESVL
PSNVAARVAV EAGIADYWYK YVGLKGAIVG MTGYGESAPA DKLFPFFGFT AENIVAKAHK
VLGVKGA
