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Database: UniProt
Entry: R7R198_9FIRM
LinkDB: R7R198_9FIRM
Original site: R7R198_9FIRM 
ID   R7R198_9FIRM            Unreviewed;       585 AA.
AC   R7R198;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=BN520_00427 {ECO:0000313|EMBL:CDF43713.1};
OS   Roseburia sp. CAG:182.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1262942 {ECO:0000313|EMBL:CDF43713.1, ECO:0000313|Proteomes:UP000018104};
RN   [1] {ECO:0000313|EMBL:CDF43713.1, ECO:0000313|Proteomes:UP000018104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:182 {ECO:0000313|Proteomes:UP000018104};
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:CDF43713.1}.
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DR   EMBL; CBKT010000376; CDF43713.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7R198; -.
DR   STRING; 1262942.BN520_00427; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000018104; 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:UP000018104};
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   585 AA;  63871 MW;  DCF4B186F12AF54C CRC64;
     MYIETINGPA DVKKLSLEQL PVLAEEMRHA LLIRASRHGG HFGPNFGMVE ATIALHYVFD
     SPKDKIVYDV SHQSYPHKML TGRKDAYLHE EHYDDVSGYS NPHESEHDFF TVGHTSTSVS
     LACGLAKARD LNGEDGNVIA VIGDGSLSGG EALEGLDYAA ELGGNLIIIA NDNDMSIAEN
     HGGLYTNLKL LRETKGQAEC NLFRAMGLDY LYVDKGNDTA ALIEAFRKVK DSKKPVVVHI
     NTLKGKGYAP AEQHKEEWHY NGPFDIETGK PLDTFAGEDY SSVTRDYLLK KMKADKSVVA
     ITSGTPTVMG FTEDKRKEAG SQFVDVGIAE ETAVALASGI AANGGKPVYG VYSTFVQRTF
     DQISQDLCIN NSPATIVTFC GSVYGMNDVT HLGLQDIPML ANIPNLVYLA PTTKEEYLAM
     LDWSIEQKEH PVAVKLPGGA MISDGKKVTK NFGKLNTYEV TEKGSRVAVI GLGTFYGLGQ
     EAAAKIKEKT GAAPTVINPY YITGLDEALL EDLKKDHSVV VTIEDGMLDG GFGEKIARFY
     GDSDMKVLNF GLKKEFLDRY DVNEVLKENH LTAEQIAEDV ARMLA
//
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