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Database: UniProt
Entry: A0A1H0KGH0_9ACTN
LinkDB: A0A1H0KGH0_9ACTN
Original site: A0A1H0KGH0_9ACTN 
ID   A0A1H0KGH0_9ACTN        Unreviewed;       639 AA.
AC   A0A1H0KGH0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05216259_110239 {ECO:0000313|EMBL:SDO54913.1};
OS   Actinacidiphila guanduensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=310781 {ECO:0000313|EMBL:SDO54913.1, ECO:0000313|Proteomes:UP000199341};
RN   [1] {ECO:0000313|EMBL:SDO54913.1, ECO:0000313|Proteomes:UP000199341}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDO54913.1,
RC   ECO:0000313|Proteomes:UP000199341};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNIE01000010; SDO54913.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0KGH0; -.
DR   STRING; 310781.SAMN05216259_110239; -.
DR   OrthoDB; 9803371at2; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000199341; Unassembled WGS sequence.
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; IPR005474; Transketolase_N.
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:UP000199341};
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          29..48
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
FT   BINDING         73
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         113..115
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         144
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         145..146
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         174
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         174
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         285
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         366
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   639 AA;  67894 MW;  1BF0CB69BB732E26 CRC64;
     MAALTRINGP RDLDRLGPQQ LVELAAEIRA FLVDAVSKTG GHLGPNLGVV ELTIALHRVF
     HSPADRILWD TGHQSYVHKL LTGRQDFAKL KSTGGLSGYP SRAESEHDVI ENSHASTVLG
     WADGLAKANQ LRGRGDHVVA VIGDGALTGG MAWEALNNIA AAKDRPLVIV VNDNEWSYSP
     TIGGLANHLA TLRTTDGYEQ FLARTREVLE RTPLIGRPLY ETLHGAKKGL KDFITPQGMF
     EDLGLKYVGP IDGHDIEAVE SALQRAKRFN GPVIVHCITE KGRGYSPAEQ DEIDRFHGIA
     PIHPDTGLPL SAGGPDWTSV FGDEMLQLGR EREDIVAITA AMLHPVGLTK FAKAFPERVY
     DVGIAEQHAA VSAAGLATGG LHPVVAVYAT FLNRAFDQVL MDVALHKCGV TFVLDRAGVT
     GSDGASHNGM WDMSILQVVP GIRIAAPRDA DQVRAQLREA VAVDDAPTVV RYSKGAVGPA
     VPAVGRIGGM DVLRAPEGAP ERPDVLLVSV GALAPMCLEI AALLDAQGIT STVVDPRWVT
     PVDPELPPLA ARHRVVVTVE DNGRVGGVGA TVAQALRDAE VDVPLRDFGI PQQFLAHGSR
     KDVMAAIGLT APDIARQVTG VVAVLGGRFA DEAEGVSQE
//
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