ID A0A419SYT6_9FIRM Unreviewed; 586 AA.
AC A0A419SYT6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
GN ORFNames=BET01_07535 {ECO:0000313|EMBL:RKD30427.1};
OS Lacrimispora algidixylanolytica.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lacrimispora.
OX NCBI_TaxID=94868 {ECO:0000313|EMBL:RKD30427.1, ECO:0000313|Proteomes:UP000284277};
RN [1] {ECO:0000313|EMBL:RKD30427.1, ECO:0000313|Proteomes:UP000284277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SPL73 {ECO:0000313|EMBL:RKD30427.1,
RC ECO:0000313|Proteomes:UP000284277};
RA Poppleton D.I., Gribaldo S.;
RT "A new outlook on sporulation: Clostridium algidixylanolyticum.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081}.
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:RKD30427.1}.
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DR EMBL; MCIA01000031; RKD30427.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419SYT6; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000284277; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
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:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
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 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; IPR033248; Transketolase_C.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF1; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE; 1.
DR Pfam; PF13292; DXP_synthase_N; 2.
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); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000284277};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 278..443
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 586 AA; 64952 MW; 66DF12249C8F4F56 CRC64;
MYLEQINQPS DVRKLNKEQR TELAAEMRQA LLEKLSKHGG HFGPNFGMVE ATIALHYVFD
SPTDKMVYDI SHQSYCHKML TGRKDAFLYE ENYDDVTGFS NQNESEHDFF ILGHTSTSVS
LACGLAKARD LKSEKENIIA IIGDGSLSGG EALEGLDFAP ELESNLIIVV NDNDMSIAEN
HGGLYRNLKQ LRDSNGTTEC NLFKAMGLDY LFVKDGNDTE QLIEAFEKAK DINHPIVVHI
NTQKGKGYLP AEKDRENWHY SGPFEIETGK SVYSSNRENY SDMTAEFLME KMKEDKTLVA
ISSGTPTVLG FTADKRKEVG SQFVDVGIAE EHAVALASGI AAGGGNPVYG VYSTFLQRTY
DQLSQDLCIN NNPATIVNFA ASVYGMTDVT HLGFFDIPMI SNIPNLVYLA PTTKEEYIAM
LDWSITQKEH PVAIRVPGGG VISGGESITR DYGNLNQYEV AQKGKKAAIV ALGTFYSLGK
EVASEIAEKT GVQPTLINPL YITGIDEKLL EELKAEHEVV ITIEDGILDG GFGEKITRFY
GASDVKVINY GFKKEFLDRY DVKEVLHKNR MTKEQIVEDI LDIIGN
//
