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TKT1_XANFL
ID   TKT1_XANFL              Reviewed;         668 AA.
AC   P51010;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Transketolase 1 {ECO:0000250|UniProtKB:P27302};
DE            Short=TK 1 {ECO:0000250|UniProtKB:P27302};
DE            EC=2.2.1.1 {ECO:0000250|UniProtKB:P27302};
GN   Name=tkt {ECO:0000312|EMBL:AAA96746.2};
OS   Xanthobacter flavus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H4-14;
RA   Van Keulen G., Komduur J., Dijkhuizen L., Meijer W.G.;
RT   "Expression of triosephosphate isomerase and the tkt encoded transketolase
RT   is independent of the autotrophic regulator CbbR.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-668.
RC   STRAIN=H4-14;
RX   PubMed=7928974; DOI=10.1128/jb.176.19.6120-6126.1994;
RA   Meijer W.G.;
RT   "The Calvin cycle enzyme phosphoglycerate kinase of Xanthobacter flavus
RT   required for autotrophic CO2 fixation is not encoded by the cbb operon.";
RL   J. Bacteriol. 176:6120-6126(1994).
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|UniProtKB:P27302}.
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:0000250|UniProtKB:P27302};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P27302};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P27302};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000250|UniProtKB:P27302};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC       {ECO:0000250|UniProtKB:P27302}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27302}.
CC   -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR   EMBL; U33064; AAA96746.2; -; Genomic_DNA.
DR   AlphaFoldDB; P51010; -.
DR   SMR; P51010; -.
DR   PRIDE; P51010; -.
DR   UniPathway; UPA00116; -.
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; Thiamine pyrophosphate;
KW   Transferase.
FT   CHAIN           1..668
FT                   /note="Transketolase 1"
FT                   /id="PRO_0000191890"
FT   ACT_SITE        414
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         74
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         123..125
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         162
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         191
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         265
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         265
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         360
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         387
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         440
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         464
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         472
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   BINDING         523
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   SITE            34
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
FT   SITE            265
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27302"
SQ   SEQUENCE   668 AA;  70203 MW;  E266940879A4EEDD CRC64;
     MSSRTSDSVT SHDRLANAIR FLAIDAVEAA NSGHPGLPMG AADIATVLFT KVLKYDPSRP
     FWPDRDRFVL SAGHGSMLLY SVLHLAGYEK VTIDEIKRFR QLGSLTPGHP ENFVTEGIET
     TTGPLGQGIA TAVGMAMAER LLAARFGSDV VDHYTYALAS DGDLMEGISQ EAADLAGHLK
     LSKLIVMWDD NKISIDGPTS ISGSTNQLAR FAASGWATAA VDGHDPEAIL AALEAAKASD
     RPTLIACRTT IGFGSPKKAG SEKVHGSPLG AEEIVATRAA LGWEAPAFVV PEDALNGWRA
     AGAAGRAARE AWEARFAARP AEERAEFERR VAGTLPAALE GAIVAVKEKA VKDGGAVATR
     KSSEMVLDFI TPAVPEMVGG SADLTGSNNT KAKGAKSVTP DDFSGSFIHY GVREHGMAAA
     MNGMALHKGL IPFSGGFMVF SDYCRPAIRL AALMGERVIH VLTHDSIGLG EDGPTHQPVE
     HLAALRAIPN LLVMRPCDTV ETAECWQIAL QSTDRPSALI LSRQNLPLLR TDATAVNRSA
     EGAYEILAAS GPAQASLFAT GSEVSLAVEA AKLLEAQGVP TRVVSISSFE LFLERPAAER
     AKVIGDAPAK VAVEAAIRMG WDAIVGSNAA FVGMTSFGAS APAKELYAHF GITAQQVAAR
     ALDQLRQA
 
 
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