ID C3T0J2_ECOLX Unreviewed; 667 AA.
AC C3T0J2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN Name=tkt {ECO:0000313|EMBL:EAA2871713.1};
GN ORFNames=BF481_001116 {ECO:0000313|EMBL:EFI1480771.1}, C9E67_07815
GN {ECO:0000313|EMBL:QCL47107.1}, CQ986_001244
GN {ECO:0000313|EMBL:EFC5410679.1}, DN627_18070
GN {ECO:0000313|EMBL:EAA2871713.1}, ECs3327
GN {ECO:0000313|EMBL:ACI80226.1}, FIJ20_17160
GN {ECO:0000313|EMBL:EFB2193925.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACI80226.1};
RN [1] {ECO:0000313|EMBL:ACI80226.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=493/89 {ECO:0000313|EMBL:ACI80226.1}, 86-24
RC {ECO:0000313|EMBL:ACI80227.1}, 87-14 {ECO:0000313|EMBL:ACI80228.1},
RC and TB182A {ECO:0000313|EMBL:ACI80229.1};
RX PubMed=19439656; DOI=10.1073/pnas.0812949106;
RA Leopold S.R., Magrini V., Holt N.J., Shaikh N., Mardis E.R., Cagno J.,
RA Ogura Y., Iguchi A., Hayashi T., Mellmann A., Karch H., Besser T.E.,
RA Sawyer S.A., Whittam T.S., Tarr P.I.;
RT "A precise reconstruction of the emergence and constrained radiations of
RT Escherichia coli O157 portrayed by backbone concatenomic analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8713-8718(2009).
RN [2] {ECO:0000313|EMBL:QCL47107.1, ECO:0000313|Proteomes:UP000298553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=143 {ECO:0000313|EMBL:QCL47107.1,
RC ECO:0000313|Proteomes:UP000298553};
RA Bono J.L., Arthur T.M.;
RT "WGA of Escherichia coli O157:H7: comparison of multiple isolates.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:EAA2871713.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=454895 {ECO:0000313|EMBL:EAA2871713.1};
RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Proteomes:UP000539823, ECO:0000313|Proteomes:UP000585348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOD1-EC3652 {ECO:0000313|EMBL:EFI1480771.1,
RC ECO:0000313|Proteomes:UP000585348}, and MOD1-EC4555
RC {ECO:0000313|EMBL:EFC5410679.1, ECO:0000313|Proteomes:UP000539823};
RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback;
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:EFB2193925.1, ECO:0000313|Proteomes:UP000519859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSIS11921886 {ECO:0000313|EMBL:EFB2193925.1,
RC ECO:0000313|Proteomes:UP000519859};
RG NARMS: The National Antimicrobial Resistance Monitoring System;
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU004996}.
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:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
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+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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DR EMBL; EU897675; ACI80226.1; -; Genomic_DNA.
DR EMBL; EU897676; ACI80227.1; -; Genomic_DNA.
DR EMBL; EU897677; ACI80228.1; -; Genomic_DNA.
DR EMBL; EU897678; ACI80229.1; -; Genomic_DNA.
DR EMBL; AAABAB010000031; EAA2871713.1; -; Genomic_DNA.
DR EMBL; AASDFP010000037; EFB2193925.1; -; Genomic_DNA.
DR EMBL; AASHWA010000004; EFC5410679.1; -; Genomic_DNA.
DR EMBL; AASYAS010000003; EFI1480771.1; -; Genomic_DNA.
DR EMBL; CP028607; QCL47107.1; -; Genomic_DNA.
DR RefSeq; WP_000087269.1; NZ_WTPO01000006.1.
DR PATRIC; fig|562.7073.peg.1573; -.
DR Proteomes; UP000298553; Chromosome.
DR Proteomes; UP000519859; Unassembled WGS sequence.
DR Proteomes; UP000539823; Unassembled WGS sequence.
DR Proteomes; UP000585348; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF13; TRANSKETOLASE 2; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 354..524
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 73029 MW; 2E6DEAFB3D9DE1E5 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 PPFEIPKDIY 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
//
