ID TKTP_CUPNH Reviewed; 670 AA.
AC P21726;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Transketolase, plasmid;
DE Short=TK;
DE EC=2.2.1.1;
GN Name=cbbTP; OrderedLocusNames=PHG420;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OG Plasmid megaplasmid pHG1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8226680; DOI=10.1128/jb.175.22.7329-7340.1993;
RA Schaeferjohann J., Yoo J.-G., Kusian B., Bowien B.;
RT "The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus
RT encode phosphoglycolate phosphatase.";
RL J. Bacteriol. 175:7329-7340(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL J. Mol. Biol. 332:369-383(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX PubMed=2559876; DOI=10.1016/0378-1119(89)90490-3;
RA Kossmann J., Klintworth R., Bowien B.;
RT "Sequence analysis of the chromosomal and plasmid genes encoding
RT phosphoribulokinase from Alcaligenes eutrophus.";
RL Gene 85:247-252(1989).
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR EMBL; M68905; AAA20194.1; -; Unassigned_DNA.
DR EMBL; AY305378; AAP86169.1; -; Genomic_DNA.
DR EMBL; M33562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C49934; C49934.
DR RefSeq; WP_011154332.1; NZ_CP039289.1.
DR AlphaFoldDB; P21726; -.
DR SMR; P21726; -.
DR GeneID; 39976481; -.
DR KEGG; reh:PHG420; -.
DR PATRIC; fig|381666.6.peg.348; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_4; -.
DR OrthoDB; 8732661at2; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000008210; Plasmid megaplasmid pHG1.
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; Plasmid;
KW Reference proteome; Thiamine pyrophosphate; Transferase.
FT CHAIN 1..670
FT /note="Transketolase, plasmid"
FT /id="PRO_0000191892"
FT ACT_SITE 417
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 120..122
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 162
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 443
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 475
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 32
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 267
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 670 AA; 71474 MW; A71583509327627A CRC64;
MNAPERIDPA ARCANALRFL AADAVELARS GHPGAPMGMA EMAEVVWRRH LRHNPANPAW
PDRDRFVLSN GHASMLQYAL LHLTGYDLPM SQLRQFRQLH AVTPGHPEVD VTPGVETTTG
PLGQGLANAV GMALAEKLLA ATFNRPGFDI VDHHTYVFLG DGCLMEGLSH EACSLAGTLG
LGKLICLYDD NGISIDGEVA GWFADDTPKR FAAYGWHVIA DVDGHDAHAL DAALHEAKAE
RDRPTLICCR TVIGKGAPAK AGGHDVHGAP LGAPEIAAMR TALGWEAEPF TVPADVADAW
DARAQGAARE AEWEARFVSY CAAHPELAEE FVRRANGRLP EGFDAELMAL LDAPSPLQGK
IATRKASQLC LEALTPALPE LLGGSADLTG SNLTNVKASV WVNHAGHGNY VSYGVREFGM
AAVMNGIALH GGLIPYGGTF MTFSDYSRNA IRMAALMRLR VVHVLTHDSI GLGEDGPTHQ
PVEHAASLRL IPNNQVWRPC DGAETAYAWL AALQRENGPT CLVLSRQALM PFERDAAQRA
DIARGGYVLR DVPAPRVVLI ATGSEVEIAA RAALDLADAG IAARVVSMPC VELFYAQDAA
YRDSVLPPGL PRISVEAGAT WYWRGVVGEQ GLALGIDSFG ESAPAEALYQ HFGLTPAHVA
AAARVLLEDA
//
