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 27-MAR-2024, entry version 99.
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; Pseudomonadota; 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 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; 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:SF2; TRANSKETOLASE 1-RELATED; 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; 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
//
