TKT_MYCPN
ID TKT_MYCPN Reviewed; 648 AA.
AC P75611;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Transketolase;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=tkt; Synonyms=tktA; OrderedLocusNames=MPN_082; ORFNames=MP073;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
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 -!- INTERACTION:
CC P75611; P04004: VTN; Xeno; NbExp=3; IntAct=EBI-12654979, EBI-1036653;
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; U00089; AAB95721.1; -; Genomic_DNA.
DR PIR; S73399; S73399.
DR RefSeq; NP_109770.1; NC_000912.1.
DR RefSeq; WP_010874439.1; NC_000912.1.
DR AlphaFoldDB; P75611; -.
DR SMR; P75611; -.
DR IntAct; P75611; 2.
DR STRING; 272634.MPN_082; -.
DR EnsemblBacteria; AAB95721; AAB95721; MPN_082.
DR KEGG; mpn:MPN_082; -.
DR PATRIC; fig|272634.6.peg.84; -.
DR HOGENOM; CLU_009227_0_0_14; -.
DR OMA; YALQQTD; -.
DR BioCyc; MetaCyc:MON-583; -.
DR BioCyc; MPNE272634:G1GJ3-129-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
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; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; PTHR43522; 1.
DR Pfam; PF02779; Transket_pyr; 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; PS00802; TRANSKETOLASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Magnesium; Metal-binding; Reference proteome;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..648
FT /note="Transketolase"
FT /id="PRO_0000191862"
FT ACT_SITE 397
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 109..111
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 447
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 22
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 252
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 648 AA; 72378 MW; EFE8247D7F0837C9 CRC64;
MKNLFACQHL ALSAIQHAKG GHVGMALGAS PILYTLWTKH IQFNPNCPKW INRDRLVMSA
GHGSMALYPI LHFAGLITKQ EMLHHKYGQV NTSSHPEYAP NNFIDASTGP LGQGLGMAVG
MALTQRVLAA EFKALSPKLF DHFTYVVVGD GDLQEGVSYE VAHLAGVYQL NKLIVLHDSN
RVQMDSVVRD VSLENLQTRF TNMGWNYLET SDAVADIDAA IKQAKKSDKP TFIEVHTTIA
KNTTLEDQPA GHWFIPTDKD FARFNSNTKT NFTPFEYPQT VYDFFHKQVI ARQAKPVQAY
KELLEKLKDK PLYTKFINWT ENDYQALYLN QLDERKVAQA NAATRNYLKD FLGQINNSNS
NLYCLNADVA RSCNIKLGDD NLHTNPHSRN IQVGIREFGM STIMNGMALH GGVKVMGGTF
LAFADYSKPA IRLGALMNLP TFYVYTHDSY QVGGDGPTHQ PYDQLPMLRA IENVQVWRPC
DEKETAAGVN YGLLSQDQTN VLILTRQALP SLEQSDSVQT LKGGYIISNR KQPDVIVAAS
GSEVQLALQL EQALNEQQLK TRVVSVPNIN MLLSQPQSYL QQLFDPNSVL LTLEASASME
WYALAKYVKK HTHLGAFSFG ESNDGQVVYE HKGFNVTNLL KLIKTLKS
