TKT_SINMW
ID TKT_SINMW Reviewed; 695 AA.
AC P56900; A6UGF2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=cbbT; OrderedLocusNames=Smed_3922;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OG Plasmid pSMED01.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fenner B.J., Tiwari R.P., Dilworth M.J.;
RT "Genetic regulation of C1 metabolism in Sinorhizobium meliloti.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01.";
RL Submitted (JUN-2007) 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: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 -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AF211846; AAF25377.1; -; Genomic_DNA.
DR EMBL; CP000739; ABR62732.1; -; Genomic_DNA.
DR RefSeq; WP_011969554.1; NC_009620.1.
DR RefSeq; YP_001312665.1; NC_009620.1.
DR AlphaFoldDB; P56900; -.
DR SMR; P56900; -.
DR EnsemblBacteria; ABR62732; ABR62732; Smed_3922.
DR GeneID; 61612433; -.
DR KEGG; smd:Smed_3922; -.
DR PATRIC; fig|366394.8.peg.368; -.
DR HOGENOM; CLU_009227_0_0_5; -.
DR OMA; YALQQTD; -.
DR OrthoDB; 188169at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000001108; Plasmid pSMED01.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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; Calvin cycle; Magnesium; Metal-binding; Plasmid;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..695
FT /note="Transketolase"
FT /id="PRO_0000191867"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 126..128
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 441
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 473
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 524
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 37
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 268
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT CONFLICT 14
FT /note="S -> W (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="I -> M (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="A -> V (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..176
FT /note="AI -> VM (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="V -> F (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="S -> W (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> F (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="S -> W (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="L -> R (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="E -> Q (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
FT CONFLICT 463..465
FT /note="LTH -> KKK (in Ref. 1; AAF25377)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 695 AA; 75147 MW; 3BB42CE8081246C4 CRC64;
MNVSQQIEPR AAASERNMAD AIRFLSMDAV EKANSGHPGM PMGMADAVTV LFNRFIRIDP
SLPDWPDRDR FVLSAGHGSM LLYSLHHLIG FADMPMAELS SFRQLGSKTA GHPEYGHALG
IETTTGPLGQ GISTAVGMAM AEQMMASRFG SALCNHFTYV VAGDGCLQEG ISHEAIDLAG
HLKLRKLVVL WDDNRISIDG STDLSTSMNQ LARFRAASWD AQAVDGHDPE AVAKALERAR
RTRKPSLIAC RTRIGKGAAS MEGSHKTHGA ALGDKEIAAT REKLGWPHPP FFVPPEIRAA
WAKVAARGRT AREAWDIRLD ASRSKKRYEQ TIRRQFDGEL GDLLAKFRSA HRTRATKVAT
RQASQMALEV INGATALTIG GSADLTGSNL TMTSQTQPIS PGNFKGRYLH YGIREHGMAA
AMNGIALHGG FIPYGGTFLV FSDYARGAMR LSALMGLPVI YVLTHDSIGL GEDGPTHQPV
EHLAMLRATP NLNVFRPADI IETAECWEIA LGEKNTPSVL ALSRQALPML RRTEGNENQS
ALGAYVLREA RGNRDITILA TGSEVEIAVA AAERLQAEEG IAAAVVSMPC WEKFEVQDLA
YRRKVLGDAP RIAIEAAGRL GWDRWMGPDG AFVGMTGFGA SAPAGDLYRH FGITADHVVA
EALELLRRAY SETLPIGARI GPHPSAHTVR SSQEA
