TKT_AQUAE
ID TKT_AQUAE Reviewed; 689 AA.
AC O67642;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; Synonyms=tktA; OrderedLocusNames=aq_1765;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07607.1; -; Genomic_DNA.
DR PIR; H70451; H70451.
DR RefSeq; NP_214208.1; NC_000918.1.
DR AlphaFoldDB; O67642; -.
DR SMR; O67642; -.
DR STRING; 224324.aq_1765; -.
DR EnsemblBacteria; AAC07607; AAC07607; aq_1765.
DR KEGG; aae:aq_1765; -.
DR PATRIC; fig|224324.8.peg.1361; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_0; -.
DR InParanoid; O67642; -.
DR OMA; HHTEGIE; -.
DR OrthoDB; 188169at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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; 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.
PE 3: Inferred from homology;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..689
FT /note="Transketolase"
FT /id="PRO_0000191850"
FT ACT_SITE 434
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 144..146
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 460
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 543
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 56
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 289
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 689 AA; 77982 MW; 285A8EAADEA20D47 CRC64;
MVVQLDQIHF FIFHEVLKIF KTMPQLFKTS KKIDELVINT IRFLSVDMVE RAKSGHPGMP
LGASHIVYLL YDRIMKYNPK NPNWFNRDRF ILSAGHGSAM LYAAFYMFGF DLTLEDLKAF
RQLNSKTPGH PEYGLTPGVE VTTGNLGQGF GNAVGMAMAE KFLSHYFNRE GYPVIDHYTY
VLVSDGDLME GVSYEAASLA GHFKLNKLIA IWDNNHITID GDTKLTWTED VLKRFEALGW
EVYHLEDGYN LDLLEETILK AKESDKPTFI SVRTHIGYGT PLQDTPEVHG KPMGKEIVEE
TKKKFGWPLE EFYVPEEALN YTRRKVEEGK ALEEEWNKLY AEYREKYPDL AQTLEKALNK
EWSLDWLEKV EEFKEDMPTR KASGKVLNVM ADYIPTMIGG SADLSESVNT VLKKYGDFEA
DTPTGRNVHY GVREHAMGTI LNGMAYHGGI LPYGGTFLIF SEYMRPAIRT AALANLQVIF
VYSHDSIGLG EDGPTHQPVE QLWSLRSIPN LWVVRPADAN EVKYAWEIAL KRKNGPTAII
LTRQKVKTID RSKYASPEGV RKGAYVIADT EGKPDVVIIA TGSEVQVALG AKEILEQKGI
KTRVVNMACC ELFEEQPEEY KREVLPPEVT KRVAVEAGRD TGWYKYVGSD GLVISLNEFG
KSAPGSVLFE YYGFTPENVA NKVIEKWFS
