ID A0A0B4RAW8_9BACL Unreviewed; 636 AA.
AC A0A0B4RAW8;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315};
GN ORFNames=Plano_1354 {ECO:0000313|EMBL:AIY05319.1};
OS Planococcus sp. PAMC 21323.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Planococcus.
OX NCBI_TaxID=1526927 {ECO:0000313|EMBL:AIY05319.1, ECO:0000313|Proteomes:UP000031496};
RN [1] {ECO:0000313|EMBL:AIY05319.1, ECO:0000313|Proteomes:UP000031496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 21323 {ECO:0000313|EMBL:AIY05319.1,
RC ECO:0000313|Proteomes:UP000031496};
RA Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-i.;
RT "Complete genome sequence of Planococcus sp. PAMC21323 isolated from the
RT Antarctica.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00315};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00315};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|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.
CC {ECO:0000256|ARBA:ARBA00004980, ECO:0000256|HAMAP-Rule:MF_00315}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00315}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081, ECO:0000256|HAMAP-Rule:MF_00315}.
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DR EMBL; CP009129; AIY05319.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B4RAW8; -.
DR STRING; 1526927.Plano_1354; -.
DR KEGG; pln:Plano_1354; -.
DR eggNOG; COG1154; Bacteria.
DR HOGENOM; CLU_009227_1_4_9; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000031496; 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 CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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; IPR049557; Transketolase_CS.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 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; 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 Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00315};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00315}; Reference proteome {ECO:0000313|Proteomes:UP000031496};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_00315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00315}.
FT DOMAIN 318..483
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 74
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 115..117
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 147..148
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 175
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 286
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 369
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ SEQUENCE 636 AA; 70064 MW; 49953A5B14B2A771 CRC64;
MAMDLHSITG PSFLKELNTK QLEVLSEDIR RFLIENLSRT GGHIGPNLGV VELTLALHKV
FDSPADKFIW DVGHQSYVHK ILTGRASQFD TLRQFKGLCG FPKRNESDHD VWETGHSSTS
LSAAMGMAAA RDIKKDSNYV IPIIGDGALT GGMAFEALNH IGHTKTDMII ILNDNEMSIA
PNVGAMHSML GRMRTAGKYN KVKDDLEYLL KKVPAVGDRL ASTAERVKDS LKYLVVSGMF
FEELGFTYLG PIDGHDLEEL EDNLRYAKKT KGPVLLHVIT KKGKGFLPAE QDTIGTWHGT
GPYKMETGDL VKSSSKAPSW SGLVAETVRK LARTDERIVA ITPAMPVGSK LEGFASEFPE
RMYDVGIAEQ HATTMAAGLA TQNMKPFLAI YSTFLQRAYD QVVHDICRQN LNVFIGIDRS
GLVGADGETH QGVFDIAFLR HLPNMVIMMP KDENEGQHMV KTAIDYNGGP IALRYPRGNG
LGVPMDEELE ALPIGSWEVL VKGTDAVILT FGTTIPMAIK AAEQLFEHGI SVEVVNARFI
KPMDVEMLHT IFKREIPVLT IEEAVLQGGF GSAVLEFAQE QQYRGAVIDR LGIPDHFIEH
GDVAELMDEI HLNSDEVVRV IKERAQSKKQ AGTTSL
//
