ID A0A0P4RED1_9ACTN Unreviewed; 683 AA.
AC A0A0P4RED1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:GAO11482.1};
GN ORFNames=TPA0598_08_03930 {ECO:0000313|EMBL:GAO11482.1};
OS Streptomyces lydicamycinicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1546107 {ECO:0000313|EMBL:GAO11482.1, ECO:0000313|Proteomes:UP000048965};
RN [1] {ECO:0000313|Proteomes:UP000048965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110027 {ECO:0000313|Proteomes:UP000048965};
RA Komaki H., Ichikawa N., Katano-Makiyama Y., Hosoyama A., Hashimoto M.,
RA Uohara A., Kitahashi Y., Ohji S., Kimura A., Yamazoe A., Igarashi Y.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Streptomyces sp. NBRC 110027.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GAO11482.1, ECO:0000313|Proteomes:UP000048965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 110027 {ECO:0000313|EMBL:GAO11482.1,
RC ECO:0000313|Proteomes:UP000048965};
RX PubMed=26380643; DOI=10.1186/s40793-015-0046-5;
RA Komaki H., Ichikawa N., Hosoyama A., Fujita N., Igarashi Y.;
RT "Draft genome sequence of marine-derived Streptomyces sp. TP-A0598, a
RT producer of anti-MRSA antibiotic lydicamycins.";
RL Stand. Genomic Sci. 10:58-58(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO11482.1}.
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DR EMBL; BBNO01000008; GAO11482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P4RED1; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000048965; 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; 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:UP000048965};
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 333..497
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 645..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 131..133
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 162
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 163..164
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 192
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 303
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 384
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ SEQUENCE 683 AA; 72273 MW; C1770364FE36EBD3 CRC64;
MQEVPRKACP AGAVAGDGRA LLSRIKGPRD LDRLSSEQLE QLAGEIRTFL VDEVSKTGGH
LGPNLGVVEL TIALHRVFDS PKDKVLFDTG HQSYVHKLLT GRQDFSKLKA KGGLSGYPSR
AESEHDVIEN SHASTVLGWA EGIAKANEVR GCDDRVAAVI GDGALTGGMA WEALNNIAAA
KDRPLVIVVN DNERSYAPTI GGLANHLATL RTTDGYERFL ARGKDLLERT PVVGKPLYET
LHGAKKGLKD FIAPQGMFED LGLKYVGPID GHDIEALESA LTRAKRFGGP VIVHCLTEKG
RGYQPALQDE ADRFHAVGKI HPDTGLPISS GGKDWTSVFG DEMVELGKER KDIVAITAAM
LQPVGLDKFA KAFPDRVFDV GIAEQHGAVS AAGMATGGLH PVFAVYATFL NRAFDQVLMD
VALHKCGVTF VLDRAGITGT DGASHNGMWD MSILQVVPGL RIAAPRDADQ VRAQLREAVE
VDDAPTVVRY SKGAVGPAVE AVGRIGGMDV LREPAEGVTR PDVLLVSVGA LAPMCLEIAD
LLDKQGISTT VVDPRWVKPV DAALPGLAAK HRVVVTVEDN VRSGGVGSAV AQALRDAGVD
VPLRDFGIPE QFLDHASRKE VMAEIGLTAP DIARQVTGLV SKIDGLPQPA LRSTGDTSAE
STADASEGAC AKGAAEPAEA TRD
//
