TKT_RHOCA
ID TKT_RHOCA Reviewed; 672 AA.
AC P0CZ16; O68024; Q52723;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tktA;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33303 / B10;
RX PubMed=8635754; DOI=10.1016/0378-1119(95)00796-2;
RA Sury D'Aspremont R., Toussaint B., Vignais P.M.;
RT "Isolation of Rhodobacter capsulatus transketolase: cloning and sequencing
RT of its structural tktA gene.";
RL Gene 169:81-84(1996).
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 -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; L48803; AAB06805.1; -; Genomic_DNA.
DR PIR; JC4637; JC4637.
DR AlphaFoldDB; P0CZ16; -.
DR SMR; P0CZ16; -.
DR UniPathway; UPA00115; -.
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:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
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; Magnesium; Metal-binding; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..672
FT /note="Transketolase"
FT /id="PRO_0000191868"
FT ACT_SITE 415
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 124..126
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 192
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 266
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266
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 35
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 266
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 672 AA; 72771 MW; 92DA88145D9634EC CRC64;
MDLAALRAKT PDHWKLATAI RVLAIDAVQA ANSGHPGMPM GMADVATVLF RNHLKFDAKA
PNWADRDRFV LSAGHGSMLL YALLHLTGYE QATLDEVKNF RQWGARMAGH PEYGHLEGVE
TTTGPLGQGI STAVGMAIAE KSMAARFGKK LVDHKIWVIA GDGCLMEGIS QEAIGLAGKQ
ELDNLIVLWD NNNITIDGRV TVSDVTDQKA RFAASGWDVL SCDGHDAEDI DRALTAAKKA
KRPVLVDCKT LIGFGSPNKA DSYAVHGAPL GDAEIKLTRE AYGWEHGPFV IPAEIKAEWE
AIGAKGAAER AEWEARLAAL PAGKRAEFER QMARGVAPKL AGAIRAFKKA QSEAAPKVAT
RKASEMVLAA VNPVVLRNHR RLADLTGSNL TKTSDIEDFM PGNHKGRYMR YGIREHAMAA
AMNGMWLHGG VRPYGGTFFC FTDYARGAMR LSSLMGVPTV YVMTHDSIGL GEDGPTHQPV
EHLTICRATP NTWTFRPADV IETAEAWELA LSSERTPSVL ALSRQNLPTL RTKHEAKNLT
AKGAYVIAEA EGKRQAILMA TGSEVEIALK ARALLQAEAI GTRVVSMPCM ELFAAQDEAY
RKRILPAGGV RVAVEAAIRQ PWDRWLLGER GMERKAGFVG MEGFGASAPA ERLYAEFGIT
PEAIAAKVKS LL
