ID A0A1H4F8T9_9FIRM Unreviewed; 586 AA.
AC A0A1H4F8T9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN02910384_02766 {ECO:0000313|EMBL:SEA93198.1};
OS Pseudobutyrivibrio sp. ACV-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1520801 {ECO:0000313|EMBL:SEA93198.1, ECO:0000313|Proteomes:UP000199179};
RN [1] {ECO:0000313|Proteomes:UP000199179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACV-2 {ECO:0000313|Proteomes:UP000199179};
RA Varghese N., Submissions S.;
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; FNQZ01000016; SEA93198.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4F8T9; -.
DR STRING; 1520801.SAMN02910384_02766; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000199179; 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 Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 281..446
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 586 AA; 64552 MW; A5A06829CE11203D CRC64;
MYEILKNIDS PADVKKLSAD ELENLAGEMR EALFNRLTKI GGHFGPNFGM VEATIALHYV
FDSPKDKFVF DVSHQSYPHK LLTGRRNGYI DDARFTEDSG YTNPEESEHD FFNIGHTSTS
IALAAGLAKA RDLKKDKENI IAIIGDGSLS GGEAMEALNV AGEMNTNFIV IVNDNEMAIA
ETHGGMYKNL ADLRESNGKA ENNIFKAYGL DYIYEENGND IQSMIALFEK VKDINHPIVL
HIHTKKGLGY ALAEENKEAW HWTLPFDRET GKPTISFGDG ESYTDITIKY IIDKAKADKD
FLVITPSMPG AIGLTPEVRA ELGEQYLDVG IAEEAAVAIA SGVAKNGAKP LVVTNMTFMQ
RAYDQISQDV CINNNPVTML LNYSSFDGLT DVTHLGIFGL AAFTNIPNLV VLAPSSAEEY
SNMLAWSVDQ NEHPVMILVP GNQVTHRAAD ASYSTIDKYK VELSGEKVAI LALGDFYQRG
EALADTIKSE MGFTPTLINP RFASGVDKEL LEKLKSNHQV IVTLEDGIVE GGFGQKIASF
YGSSDMKVLN YGLDKEFYDR YNPEDLIKSV GMSTEQIVED IKNIIK
//
