TKT1_PASMU
ID TKT1_PASMU Reviewed; 668 AA.
AC P57927;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Transketolase 1;
DE Short=TK 1;
DE EC=2.2.1.1;
GN Name=tktA; OrderedLocusNames=PM1242;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004439; AAK03326.1; -; Genomic_DNA.
DR RefSeq; WP_010907090.1; NC_002663.1.
DR AlphaFoldDB; P57927; -.
DR SMR; P57927; -.
DR STRING; 747.DR93_724; -.
DR EnsemblBacteria; AAK03326; AAK03326; PM1242.
DR KEGG; pmu:PM1242; -.
DR PATRIC; fig|272843.6.peg.1252; -.
DR HOGENOM; CLU_009227_0_0_6; -.
DR OMA; NSGHSGM; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..668
FT /note="Transketolase 1"
FT /id="PRO_0000191864"
FT ACT_SITE 413
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 26
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 114..116
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 156
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 185
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 439
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 261
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 668 AA; 73369 MW; 1C91876D523C6ACA CRC64;
MATRRELANA IRFLSMDAVQ KAKSGHPGAP MGMADIAEVL WRDFLKHNPS NPHWADRDRF
ILSNGHGSML IYSLLHLSGY DLSIEDLKQF RQLHSKTPGH PEYGYAPGVE TTTGPLGQGI
TNAVGFAIAE KTLAHQFNRP GHEIVDHHTY VFLGDGCLME GISHEACSLA GTLGLGKLIA
FYDDNNISID GHVDGWFTDD TQKRFEAYGW HVIPAVDGHN PEQILEAVKQ AQAETTKPTL
IICKTIIGYG SPNKANSHDC HGAPLGDDEI AAAREFLKWE HAPFEIPAEI YAQWDAKEKG
QVAEKAWEEK LAAYAKAYPE LAAEFTRRVN AELPANWAAE SQAFIEHLQA NPANIASRKA
SQNAIEAYAK LLPEFLGGSA DLASSNLTLW SGSKPIRAVE NADGNYINYG VREFGMSAIM
NGIALHGGFI PYGATFLMFM EYAHNAVRMA ALMKQRSLFV YTHDSIGLGE DGPTHQPVEQ
TSALRLIPNL ETWRPCDQVE SAVAWKAAVE RKEGPSALIF TRQNLAQMDR TAEQLANVAR
GGYVLRHCCE NQNCPDLILI ATGSEVELAM KAADVLDAEG VKVRVVSMPS TNVFDKQDAA
YRESVLPSHI TKRVAIEAGI ADFWYKYVGF EGRVVGMNSF GESAPADQLF KLFGFTVENI
VEKAKAIL
