ID A0A086Y884_9RHOB Unreviewed; 638 AA.
AC A0A086Y884;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ECO:0000313|EMBL:QBJ24954.1};
GN ORFNames=CN97_13090 {ECO:0000313|EMBL:KFI30484.1}, HmaOT1_12285
GN {ECO:0000313|EMBL:QBJ24954.1};
OS Haematobacter massiliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Haematobacter.
OX NCBI_TaxID=195105 {ECO:0000313|EMBL:KFI30484.1, ECO:0000313|Proteomes:UP000028826};
RN [1] {ECO:0000313|EMBL:KFI30484.1, ECO:0000313|Proteomes:UP000028826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 47968 {ECO:0000313|EMBL:KFI30484.1,
RC ECO:0000313|Proteomes:UP000028826};
RA Wang D., Wang G.;
RT "Genome of Haematobacter massiliensis CCUG 47968.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QBJ24954.1, ECO:0000313|Proteomes:UP000291082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT1 {ECO:0000313|EMBL:QBJ24954.1,
RC ECO:0000313|Proteomes:UP000291082};
RA Lee K.;
RT "The first complete genome sequence of Haematobacter massiliensis OT1
RT isolated from human skin.";
RL Submitted (JAN-2019) 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; JGYG01000003; KFI30484.1; -; Genomic_DNA.
DR EMBL; CP035510; QBJ24954.1; -; Genomic_DNA.
DR RefSeq; WP_035709056.1; NZ_NIPY01000013.1.
DR AlphaFoldDB; A0A086Y884; -.
DR STRING; 195105.CN97_13090; -.
DR KEGG; hml:HmaOT1_12285; -.
DR eggNOG; COG1154; Bacteria.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000028826; Unassembled WGS sequence.
DR Proteomes; UP000291082; 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:UP000028826};
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 321..486
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 79
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 120..122
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 153..154
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 181
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 181
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 290
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 372
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ SEQUENCE 638 AA; 67935 MW; 383AE21191B371E0 CRC64;
MSQKPVTPHL DRVRLPADLK GLTDRELSAV ADELRAETIS AVSETGGHLG AGLGVVELTV
ALHAVFDAPR DKIIWDVSHQ SYPHKILTGR RERIRTLRQK NGLSGFTKRS ESPYDPFGAA
HSSTSISAAL GFAVARDLGA EGVGDAVAII GDGSMSAGMA FEAMNNAGHL GKRLFVILND
NDMSIAPPVG ALSSYLARLY AGEPFQELKA AARGAVRFLP PPMQEGARRA KEMLKGMTVG
GTLFEELGFS YIGPIDGHDM EQLLAVLRTA KARARGPVLI HAITRKGKGY APAEAALDKG
HATAKFDVLT GKQAKAPSNA PSYTSVFAKA LLSEAERDDK IVAVTAAMPD GTGLNLFAER
FPKRCFDVGI AEQHAVTFAA GLAAGGMKPF CALYSTFLQR GYDQVVHDVA IQRLPVRFAI
DRAGLVGADG ATHAGSFDIA FLANLPGMVV MAAADEAELI HMVATAAALD DRPSAFRYPR
GEGVGVDLPE RGQPLEIGRG RIVSEGNRVA LLSFGTRLAE VNAAAEALAQ RGLRPTVADA
RFAKPLDREL ILRLAREHEA MITLEEGAVG GFGSHVAQLL AEEGVFDKGF RFRSMVLPDI
FIDQASMEDM YAVAGMNAAE IEAKVLEVLG VARIERRA
//
