ID   A0AAJ1DZ51_9ENTR        Unreviewed;       662 AA.
AC   A0AAJ1DZ51;
DT   24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2024, sequence version 1.
DT   02-OCT-2024, entry version 2.
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:MBU3769100.1};
GN   ORFNames=J0A64_21130 {ECO:0000313|EMBL:MBU3769100.1};
OS   Enterobacter roggenkampii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=1812935 {ECO:0000313|EMBL:MBU3769100.1, ECO:0000313|Proteomes:UP000813349};
RN   [1] {ECO:0000313|EMBL:MBU3769100.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BK34275 {ECO:0000313|EMBL:MBU3769100.1};
RX   PubMed=34079986; DOI=10.1093/cid/ciab511;
RA   Klein S., Boutin S., Kocer K., Fiedler M.O., Storzinger D., Weigand M.A.,
RA   Tan B., Richter D., Rupp C., Mieth M., Mehrabi A., Hackert T.,
RA   Zimmermann S., Heeg K., Nurjadi D.;
RT   "Rapid Development of Cefiderocol Resistance in Carbapenem-resistant
RT   Enterobacter cloacae During Therapy Is Associated With Heterogeneous
RT   Mutations in the Catecholate Siderophore Receptor cirA.";
RL   Clin. Infect. Dis. 74:905-908(2022).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBU3769100.1}.
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DR   EMBL; JAFKCP010000019; MBU3769100.1; -; Genomic_DNA.
DR   Proteomes; UP000813349; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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; PF22613; Transketolase_C_1; 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..525
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   662 AA;  72445 MW;  976701894FE469C6 CRC64;
     MSRKELANAI RALSMDAVQK ANSGHPGAPM GMADIAEVLW NDFLKHNPND PTWYDRDRFI
     LSNGHASMLL YSLLHLSGYD LPLEELKNFR QLHSKTPGHP EIGYTPGVET TTGPLGQGLA
     NAVGLAIAER TLAAQFNQPD HEIVDHYTYV FMGDGCLMEG ISHEVCSLAG TLGLGKLIGF
     YDHNGISIDG ETEGWFTDDT AKRFEAYHWH VVHEIDGHDP EAVKKAIQEA QSVKDKPSLI
     ICRTVIGFGS PNKAGKEEAH GAALGDEEVA LTRQKLGWKY PPFEIPKEIY RAWDAREDGE
     KAQQAWNEKF AAYKKAYPEL AAEFSRRMSG GLPEDWDDKT QALIENLQSN PAKIATRKAS
     QNTLNAIGPL LPELLGGSAD LAPSNLTIWS GSKSLKEDIA GNYIHYGVRE FGMTAIANGI
     AHHGGFVPYT ATFLMFVEYA RNAARMAALM KARQIMVYTH DSIGLGEDGP THQAVEQLAS
     LRLTPNFSTW RPCDQVEAAV GWKLAVERHN GPTALILSRQ NLTQIERTPE QVKNIARGGY
     ILKDSGGKPD VILIATGSEV EITVKAAEKL TAEGHAVRVV SLPSTDTFDA QDEAYRESVL
     PSNVAARVAV EAGIADYWYK YVGLKGAIVG MRGYGESAPA DKLFPYFGFT VENVVEKALS
     VI
//