DXS_STRC1
ID DXS_STRC1 Reviewed; 631 AA.
AC Q9RBN6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
OS Streptomyces sp. (strain CL190).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=93372;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=10648511; DOI=10.1128/jb.182.4.891-897.2000;
RA Kuzuyama T., Takagi M., Takahashi S., Seto H.;
RT "Cloning and characterization of 1-deoxy-D-xylulose 5-phosphate synthase
RT from Streptomyces sp. strain CL190, which uses both the mevalonate and
RT nonmevalonate pathways for isopentenyl diphosphate biosynthesis.";
RL J. Bacteriol. 182:891-897(2000).
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).
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0.;
CC Temperature dependence:
CC Optimum temperature is 42-44 degrees Celsius.;
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.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR EMBL; AB026631; BAA85847.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RBN6; -.
DR SMR; Q9RBN6; -.
DR KEGG; ag:BAA85847; -.
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 1: Evidence at protein level;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..631
FT /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT /id="PRO_0000189156"
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 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 631 AA; 67962 MW; 306042CDFA287694 CRC64;
MTILENIRQP RDLKALPEEQ LHELSEEIRQ FLVHAVTRTG GHLGPNLGVV ELTIALHRVF
ESPVDRILWD TGHQSYVHKL LTGRQDFSKL RGKGGLSGYP SREESEHDVI ENSHASTALG
WADGLAKARR VQGEKGHVVA VIGGRALTGG MAWEALNNIA AAKDQPLIIV VNDNERSYAP
TIGGLANHLA TLRTTDGYEK VLAWGKDVLL RTPIVGHPLY EALHGAKKGF KDAFAPQGMF
EDLGLKYVGP IDGHDIGAVE SALRRAKRFH GPVLVHCLTV KGRGYEPALA HEEDHFHTVG
VMDPLTCEPL SPTDGPSWTS VFGDEIVRIG AEREDIVAIT AAMLHPVGLA RFADRFPDRV
WDVGIAEQHA AVSAAGLATG GLHPVVAVYA TFLNRAFDQL LMDVALHRCG VTFVLDRAGV
TGVDGASHNG MWDMSVLQVV PGLRIAAPRD ADHVRAQLRE AVAVDDAPTL IRFPKESVGP
RIPALDRVGG LDVLHRDERP EVLLVAVGVM AQVCLQTAEL LRARGIGCTV VDPRWVKPVD
PVLPPLAAEH RLVAVVEDNS RAAGVGSAVA LALGDADVDV PVRRFGIPEQ FLAHARRGEV
LADIGLTPVE IAGRIGASLP VREEPAEEQP A
