DXS1_KITGR
ID DXS1_KITGR Reviewed; 649 AA.
AC Q9F1V2;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXP synthase 1 {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXPS 1 {ECO:0000255|HAMAP-Rule:MF_00315};
GN Name=dxs1 {ECO:0000255|HAMAP-Rule:MF_00315};
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Kitasatospora.
OX NCBI_TaxID=2064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MF730-N6;
RX PubMed=12036054; DOI=10.1271/bbb.66.808;
RA Hamano Y., Dairi T., Yamamoto M., Kuzuyama T., Itoh N., Seto H.;
RT "Growth-phase dependent expression of the mevalonate pathway in a terpenoid
RT antibiotic-producing Streptomyces strain.";
RL Biosci. Biotechnol. Biochem. 66:808-819(2002).
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; AB042821; BAB20589.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F1V2; -.
DR SMR; Q9F1V2; -.
DR STRING; 2064.TR51_19475; -.
DR UniPathway; UPA00064; UER00091.
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..649
FT /note="1-deoxy-D-xylulose-5-phosphate synthase 1"
FT /id="PRO_0000189121"
FT REGION 623..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 73
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 113..115
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 145..146
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 174
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 367
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ SEQUENCE 649 AA; 68627 MW; 991B04D46ED515AE CRC64;
MPLLSRITGP ADLRRLHPEQ LPPLAAEIRA FLIDNVTRTG GHLGPNLGVV ELSIALHRVF
DSPHDRILWD TGHQAYVHKL LTGRQDFSRV RAKDGLSGYP SRAESPHDLI ENSHASTALG
HADGIAKADQ LLGVDRCTVA VIGDGALTGG MAWEALNNIA EAEDRPLVIV VNDNERSYAP
TIGGLAHHLA TLRTTKGYER FLAWGKDALQ RTPVVGPPLF DALHGAKKGF KDAFAPQGMF
EDLGLKYLGP IDGHDIAGVE QALRRARNFG GPVIVHCLTV KGRGYRPAEQ DEADRFHAVN
PIDPYTCLPI SPSAGASWTS VFGKEMLALG AERPELVAVT AAMLHPVGLG PFAKAYPGRT
FDVGIAEQHA VASAAGLATG GLHPVVAVYA TFLNRAFDQV LMDVALHRLG VTFVLDRAGV
TGNDGASHNG MWDLSVLQVV PGLRIAAPRD AARVREHVRQ AVAVEDAPTV VRFPKGELGP
EAPAIERIGG VDVLARTGPA PDVLLVAVGP MAAACLDAAA LLAADGITAT VVDPCWVKPV
DPALVELAGA HRMVVTVEDN GRTGGVGAAL AQAMRDADVD TPLRDLGIPQ EFLAHASRGE
ILEEIGLTGT GVAAQTAAHA RRLLPGTGTR PGAQEYRPRM PLTDWSEPA
