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DXS_CLOAB
ID   DXS_CLOAB               Reviewed;         619 AA.
AC   Q97HD5;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315}; OrderedLocusNames=CA_C2077;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC       and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC       xylulose-5-phosphate (DXP). {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC         xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC         ChEBI:CHEBI:59776; EC=2.2.1.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00315};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC       phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC       glyceraldehyde 3-phosphate and pyruvate: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR   EMBL; AE001437; AAK80036.1; -; Genomic_DNA.
DR   PIR; A97156; A97156.
DR   RefSeq; NP_348696.1; NC_003030.1.
DR   RefSeq; WP_010965377.1; NC_003030.1.
DR   AlphaFoldDB; Q97HD5; -.
DR   SMR; Q97HD5; -.
DR   STRING; 272562.CA_C2077; -.
DR   EnsemblBacteria; AAK80036; AAK80036; CA_C2077.
DR   GeneID; 44998559; -.
DR   KEGG; cac:CA_C2077; -.
DR   PATRIC; fig|272562.8.peg.2281; -.
DR   eggNOG; COG1154; Bacteria.
DR   HOGENOM; CLU_009227_1_4_9; -.
DR   OMA; QVGYHAQ; -.
DR   OrthoDB; 566385at2; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000000814; Chromosome.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0052865; P:1-deoxy-D-xylulose 5-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd02007; TPP_DXS; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   HAMAP; MF_00315; DXP_synth; 1.
DR   InterPro; IPR005477; Dxylulose-5-P_synthase.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR033248; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43322; PTHR43322; 1.
DR   Pfam; PF13292; DXP_synthase_N; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00204; dxs; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW   Thiamine biosynthesis; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..619
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_0000189105"
FT   BINDING         74
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         115..117
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         146
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         147..148
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         175
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         285
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         365
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   619 AA;  68976 MW;  4625513C8D245431 CRC64;
     MYNILDNYED VDDIKNMSSD ELKEFASEIR KFLIDKISKT GGHLASNLGV VELTLSLHKV
     FNLKKDKIIW DVGHQAYVHK ILTGRKDKFD SLKQFNGLSG FPKRNESIYD AFETGHSSTS
     ISAASGIARA RDLSKDNYDV IAVIGDGALT GGMALEALND IGYKKTNVII ILNDNQMSIA
     KNVGSISKYL NKIRLDPKYN KLKKDVKTKL QRTNIGSEVA NSIERIKGGI KQMVVSGMFF
     EDIGIKYLGP IDGHNIEELT SVISKAKEIK GPVILHVKTQ KGKGYSYAEE NPNKFHSIGK
     FNSKTGEALS KPKDTYSKAF GKAMVQMAEN NDKIVAITAA MTDGTGLCEF SKKFPQRFFD
     VGISEQHAVT MAAGLAATGY KPVFAVYSTF LQRAYDQVLH DVCIQKLPVV FAIDRAGIVG
     EDGETHQGVF DISYLSSIPN MTIMAPKCVE ELNYIMNWAV KQNYPIAVRY PKGGNDISDV
     LAPLKEFRHG KWEILKDGKD VAIVAVGKMV QRAMVVRDEL LKYGIDCAII NATFIKPIDK
     DTLNRFARDN YKFVVIEDNV LHGGIGSLIL EHLNDMKFKN DVLNLGFKDE FITHGNIEIL
     YKLYDLDIEG ICKRIISFK
 
 
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