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Database: UniProt
Entry: R5WCL7_9FIRM
LinkDB: R5WCL7_9FIRM
Original site: R5WCL7_9FIRM 
ID   R5WCL7_9FIRM            Unreviewed;       583 AA.
AC   R5WCL7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=BN751_00315 {ECO:0000313|EMBL:CCZ93501.1};
OS   Coprococcus eutactus CAG:665.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Coprococcus.
OX   NCBI_TaxID=1263071 {ECO:0000313|EMBL:CCZ93501.1, ECO:0000313|Proteomes:UP000017949};
RN   [1] {ECO:0000313|EMBL:CCZ93501.1, ECO:0000313|Proteomes:UP000017949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:665 {ECO:0000313|Proteomes:UP000017949};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CCZ93501.1}.
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DR   EMBL; CBAW010000114; CCZ93501.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5WCL7; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000017949; 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   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          278..444
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   583 AA;  63960 MW;  E832D32F36DDE10D CRC64;
     MYIENINGPQ DVKKLTVDEM RTLADEMRHA LLIRASKHGG HFGPNFGMVE ATIALHYVFE
     SPKDKIVYDV SHQSYPHKML TGRKDAYLYE EHYDDVTGYS NPHESEHDFF TVGHTSTSIS
     LAAGLAKARD LQGAEGNVIA VIGDGSLSGG EALEGLDYAK ELDGNLIIVV NDNDMSIAEN
     HGGLYTNLRL LRDTNGTAEC NLFRAMGLDY YYVHEGNDVA ALIDTFQKVK DSKKPVVVHI
     RTLKGKGYAP AEEHKEQWHY SGPFDIETGR SLFEGDEEDY SSVSCDYLLD KMKKDPKVVA
     ITAGTPTVIG FTEDKRREAG KQFVDVGIAE ETAVALASGI AAGGGKPVFG VYSSFVQRTF
     DQISQDLCIN NNAATIVTFA GSVYGMNDVT HLGFQDIPML SNIPNLVYLA PTTKEEYIAM
     LDWSIEQNEH PVAIKLPGGA MVSGSPVTKN FGDLNKYEVT QKGSKVAILG LGTFYSLANA
     AADEMKSELG IDATVINPYY ITGLDEELLE SLKADHSVVI TIEDGILDGG FGEKIARFYG
     DSDMKVLNYG LKKEFLDRYD VEEVLKDNRL DAEMIAEDVK GLL
//
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