ID A0AAJ1DZ51_9ENTR Unreviewed; 662 AA. AC A0AAJ1DZ51; DT 24-JUL-2024, integrated into UniProtKB/TrEMBL. DT 24-JUL-2024, sequence version 1. DT 27-NOV-2024, entry version 3. DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|NCBIfam:TIGR00232}; DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|NCBIfam:TIGR00232}; 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-sedoheptulose 7-phosphate + D-glyceraldehyde 3-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JAFKCP010000019; MBU3769100.1; -; Genomic_DNA. DR RefSeq; WP_021241799.1; NZ_LPQP01000073.1. DR Proteomes; UP000813349; Unassembled WGS sequence. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004802; F:transketolase activity; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:TreeGrafter. DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1. DR CDD; cd02012; TPP_TK; 1. DR FunFam; 3.40.50.920:FF:000003; Transketolase; 1. DR FunFam; 3.40.50.970:FF:000003; Transketolase; 1. DR FunFam; 3.40.50.970:FF:000004; Transketolase; 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; IPR055152; Transketolase-like_C_2. 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" FT BINDING 25 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 260 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 357 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 384 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 460 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 468 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 472 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT BINDING 519 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-1" FT SITE 25 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-5" FT SITE 260 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR605478-5" 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 //