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Database: UniProt
Entry: R6AGE1_9BACT
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ID   R6AGE1_9BACT            Unreviewed;       587 AA.
AC   R6AGE1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=BN693_00237 {ECO:0000313|EMBL:CDA45596.1};
OS   Prevotella sp. CAG:5226.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1262930 {ECO:0000313|EMBL:CDA45596.1, ECO:0000313|Proteomes:UP000018184};
RN   [1] {ECO:0000313|EMBL:CDA45596.1, ECO:0000313|Proteomes:UP000018184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:5226 {ECO:0000313|Proteomes:UP000018184};
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:CDA45596.1}.
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DR   EMBL; CBBW010000217; CDA45596.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6AGE1; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000018184; Unassembled WGS sequence.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR049557; Transketolase_CS.
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); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018184};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          280..445
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   587 AA;  64005 MW;  83BEE5F07E6364EB CRC64;
     MYIEKIKSPA DLKGLDIKAL QIVADETRDA VLNRVSQHGG HVGPNLGFVE ATVALHYVFD
     APKDKLVFDV SHQCYPHKVL TGRAAGFLGS INDMNAISGY SSPAECPEYD NFEVGHTSTS
     ISLATGLQKA RDIKGTDENI IAIIGDGSLS GGEAFEGLDE ASELGTGIII VVNDNEMSIA
     ENHGGIYKNL RALRESNGTC AHNWFKAWGF EYKYLEEGND IEKLIKVFES VKGTDKPTVV
     HIHTEKGHGF APAVANKEAW HWGLPFNRLD GSRPPKPAVE TYEELFSNWM LNEMKHDPTL
     IAVTAGTPAA AGFTPEKRKL AGKQHIDMGI AEEQAAAMIS GMAKGGLHPV WTVYSTFIQR
     TYDQIAQDIC INANPAVINV VGGGVNSMND ITHICLFDIP MLCSIPGLIY LAPTNCEEYF
     AMLRWAIAQD KMPIALRVPT NGVHHATAPV DTEYGYEPSY KVMHRGSRVA IIAAGSFYQK
     GEHVARLLAD KGIDATLINP RYLHAVDADT LNSLKADHQF VVTLEDGCKD GGFGERIASF
     YGTSSMRVLV GGIKKGLYDR FDVNELLADS RLLDEQIVED VIEGLEG
//
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