ID A0A1I0X690_9CLOT Unreviewed; 586 AA.
AC A0A1I0X690;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN04488528_100794 {ECO:0000313|EMBL:SFA96354.1};
OS Clostridium frigidicarnis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84698 {ECO:0000313|EMBL:SFA96354.1, ECO:0000313|Proteomes:UP000198619};
RN [1] {ECO:0000313|EMBL:SFA96354.1, ECO:0000313|Proteomes:UP000198619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12271 {ECO:0000313|EMBL:SFA96354.1,
RC ECO:0000313|Proteomes:UP000198619};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOKI01000007; SFA96354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0X690; -.
DR STRING; 84698.SAMN04488528_100794; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000198619; 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; 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.
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:UP000198619};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 281..445
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 586 AA; 64177 MW; 7F4719440E60335F CRC64;
MLLNILNKIN GPKDLKELTS DELKILSSEI RESIITKVST IGGHFGPNLG MVEATIALHC
VFNSPIDKIV YDVSHQSYTH KILTGRKHAF INPAEYKSVT GYTSPDESEH DFFTIGHTST
SVSLACGLAK ARDVKGGNEN IIAVIGDGSL SGGEAFEGLN NAAASGKNII ILVNDNDMSI
AENYGGLYKN LALLHETYGK SENNFFKSLG FDYYYVKDGN NIESLIETFS KVKDIDHPVV
VHIHSVKGKG YKDSEENKEA FHWVMPFDLK TKEPLVKNNG ETYGGIAGEF LSQKARKDSS
IVAITAATPG PVGLGSFRHE FKDQFIDVGI AEEHAIALAS GIASQGGKPV ASFFSSFIQR
TYDQLSQDLA INNNPALIMV YGGGITGSDV THHGIFDIPL ISNIPNIVYL APTNKEEYIA
MMEWGIEQDK YPVAIRVPNM GVVSATVEVE LSFDNLNTYK KVKDGSEVAI IGLGSFYHLG
EKVQGKLKET TGINATLINP RFISGIDKNL LTELLDNHKL VITLEDGILD GGFGEKISRF
YGDKDMKVLN FGASKEFTDS VSIEELYRRY HLTDELIISD IKKALK
//
