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DXS_ALTMD
ID   DXS_ALTMD               Reviewed;         625 AA.
AC   B4RVY8; F2G6Y5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=MADE_1012415;
OS   Alteromonas mediterranea (strain DSM 17117 / CIP 110805 / LMG 28347 / Deep
OS   ecotype).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX   NCBI_TaxID=1774373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17117 / CIP 110805 / LMG 28347 / Deep ecotype;
RX   PubMed=18670397; DOI=10.1038/ismej.2008.74;
RA   Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S.,
RA   Johnson J., Friedman R., Rodriguez-Valera F.;
RT   "Comparative genomics of two ecotypes of the marine planktonic copiotroph
RT   Alteromonas macleodii suggests alternative lifestyles associated with
RT   different kinds of particulate organic matter.";
RL   ISME J. 2:1194-1212(2008).
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; CP001103; AEA98619.1; -; Genomic_DNA.
DR   RefSeq; WP_012518937.1; NC_011138.3.
DR   AlphaFoldDB; B4RVY8; -.
DR   SMR; B4RVY8; -.
DR   EnsemblBacteria; AEA98619; AEA98619; MADE_1012415.
DR   KEGG; amc:MADE_1012415; -.
DR   HOGENOM; CLU_009227_1_4_6; -.
DR   OMA; QVGYHAQ; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000001870; 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; Thiamine biosynthesis;
KW   Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..625
FT                   /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT                   /id="PRO_1000115718"
FT   BINDING         80
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         121..123
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         153..154
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         181
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         288
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT   BINDING         370
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   625 AA;  67725 MW;  A1D039E0381AD915 CRC64;
     MSLDLQHYPT LALAQTPDKL RQLPQDKLRE LADELREYLL NSVSQTSGHF ASGLGTVELT
     VALHYVYNTP FDRLLWDVGH QAYPHKILTG RAERMSTIRQ KNGLHPFPWP PESEYDTFAV
     GHSSTSISAA LGMAVAAEKE GKDRKVVSVI GDGAMTAGMA FEALNHAGDI KKDMVVVLND
     NEMSISENVG ALNSHLARLL TGNFFNSIRD GGKKLLSNVP PIKEFASRAE EHLKGMVVPG
     TIFEELGFNY IGPIDGHDVN AVVDTLRNMR NFDGPQLLHV VTKKGKGYAV AEEDPIKFHA
     VPKFNPADNA LPKSKPSAPT YSAIFGQWLC DMAAQDPKLM AVTPAMREGS GMVEFSQRFP
     EQYFDVAIAE QHAVTFGAGL AKDGMNAVVA IYSSFLQRAY DQLIHDVAIQ DLPVLFAIDR
     AGIVGADGPT HQGAFDIAFL RCIPNMVVMA PSDENECRQM LYTGHKLQKP AAVRYPRGAG
     MGVTPDEAMT ALEIGKSRTC RETAKDKSES VAILNFGCLL PYALEAAVAI DATVIDMRFI
     KPLDGDAVLK AANEHSALIT LEDGCIMGGA GSAVLEHLQQ NGVLKAVKML GLPDSFILQG
     TQQEMYKEHG LDAEGIIAAA KSLIG
 
 
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