ID B0N6R5_9FIRM Unreviewed; 581 AA.
AC B0N6R5;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=CLORAM_02296 {ECO:0000313|EMBL:EDS17503.1};
OS Thomasclavelia ramosa DSM 1402.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Coprobacillaceae; Thomasclavelia.
OX NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS17503.1, ECO:0000313|Proteomes:UP000005798};
RN [1] {ECO:0000313|EMBL:EDS17503.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17503.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS17503.1, ECO:0000313|Proteomes:UP000005798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS17503.1,
RC ECO:0000313|Proteomes:UP000005798};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS17503.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABFX02000008; EDS17503.1; -; Genomic_DNA.
DR RefSeq; WP_003538068.1; NZ_DS499659.1.
DR AlphaFoldDB; B0N6R5; -.
DR eggNOG; COG1154; Bacteria.
DR HOGENOM; CLU_009227_1_4_9; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000005798; 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); 2.
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:UP000005798};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 279..442
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 581 AA; 64357 MW; 682372D4A9811C70 CRC64;
MFLEKIDDTN DLKKLNRKEL KELANEVRAA LINKISKAGG HSGPNLGMVE MTVALHYVFD
SPNDKFVFDV SHQSYPHKIL TGRKEAFLDE EHFHDVTGYT NPLESEHDMF TIGHTSTSVS
LALGLAIGRD LNKKAENIIA IIGDGSLSGG EALEAIDYAG EYNKNLIIIV NDNDQSIAEN
HGGIYQTLKE LRDTNGTSNN NIFTSFGLDY KYLDDGHDIE KLIELFESVK NIDHPIVLHI
HTIKGKGLPY AEVNKEAWHA GGPFNVADGT YKFVDEDDQT LFDSLTNLLN ANKKAIVVNA
GTPMGLGFIE PVRKEYVERG QFIDVGIAEE NAMAMISGIA KNGGIPVFGT FAPFLQRTYD
QLSHDLCLNN NPATILVLSA GVYGMNSNTH IALCDIAMFA HIPNLIYLAP TTKEEYLQMF
KYATTQKDHP IAIRVPVQMI ESGQEDTTDY SIHNKSQIVQ QGNDIAIIGV SNLLPLALKT
AQKYKEDTGK NITVINPKFL TGLDEELLND LTNNHRLIIT LEDGELEGGY GHRISSFYGM
TEMKVKNYGI SKAFHTDFNA DELLAQHGIS VDQLVTYMKN S
//
