ID D4MTV3_ANAHA Unreviewed; 582 AA.
AC D4MTV3;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 70.
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=CL2_19290 {ECO:0000313|EMBL:CBL38819.1};
OS Anaerostipes hadrus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerostipes.
OX NCBI_TaxID=649756 {ECO:0000313|EMBL:CBL38819.1, ECO:0000313|Proteomes:UP000008960};
RN [1] {ECO:0000313|EMBL:CBL38819.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38819.1,
RC ECO:0000313|Proteomes:UP000008960};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Clostridiales sp. SSC/2.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL38819.1, ECO:0000313|Proteomes:UP000008960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSC/2 {ECO:0000313|EMBL:CBL38819.1,
RC ECO:0000313|Proteomes:UP000008960};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929061; CBL38819.1; -; Genomic_DNA.
DR RefSeq; WP_008392282.1; NC_021016.1.
DR AlphaFoldDB; D4MTV3; -.
DR STRING; 649756.ERS852387_00393; -.
DR GeneID; 15231910; -.
DR KEGG; bprl:CL2_19290; -.
DR PATRIC; fig|245018.3.peg.2213; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000008960; Chromosome.
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; 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); 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 Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transferase {ECO:0000313|EMBL:CBL38819.1}.
FT DOMAIN 278..444
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 582 AA; 64445 MW; 302A8F81EFD8CEA0 CRC64;
MYIENINGPE DVKKLSEDQL NVLAEEIRDA LLKKLSKHGG HFGPNFGMVE ATIAMHYVFE
SPKDKIVYDV SHQSYPHKML TGRKDAFLYE EHYDDVSGYS NPGESEHDHF TIGHTSTSIS
LALGLAKARD LKEENGNVIA VIGDGSLSGG EALEGLDYAA ELGGNLIIVV NDNDMSIAEN
HGGLYDNLKE LRDTNGEAEC NLFKALGLDY IYVKEGNKVA DLIEAFKRVK DTKKAVVVHI
NTQKGKGYKL AEEHKEDWHY CAPFDVETGK PLDFFDGEDF SSVTAQYLLK KMKEDKKVVA
ITSATPTVMG FTEDKRKEAG KQFIDVGIAE ETAMAMAAGI AAGGGKPVYG VYSTFVQRTY
DQITQDLCID SNAATIVTFW GSVYGMNDVT HLGLQDIPMM SNIPNLIYLA PTTKEEYIAM
LDWSIDQDQY PVAIKLPGGE MISDGKKITK DFSQLNKYEV TEKGSKVAVI GLGTFYNMGC
EVAKAVEEKT GTKATVINPY YITGIDEVLL EDLKKDHDVV ITLEDGFLEG GFGEKIARFY
GNSDMKVFNY GVKKELLDRY DVTELLEKNH LTVQQIVGDL KF
//
