ID A0A1Y4BJ22_9ACTN Unreviewed; 598 AA.
AC A0A1Y4BJ22;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=B5F84_08745 {ECO:0000313|EMBL:OUO33249.1};
OS Olsenella sp. An290.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1965625 {ECO:0000313|EMBL:OUO33249.1, ECO:0000313|Proteomes:UP000196134};
RN [1] {ECO:0000313|Proteomes:UP000196134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An290 {ECO:0000313|Proteomes:UP000196134};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-2017) 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:OUO33249.1}.
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DR EMBL; NFIU01000021; OUO33249.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4BJ22; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000196134; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:UP000196134};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 291..456
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 598 AA; 63167 MW; 3BC55215BFAD3180 CRC64;
MCYETTGRNE GGATVYLERI ASPEDLRALP EDALPALCDE IRSAVVESSA AIGGHVGSNL
SVVELTVALH RVFESPRDRL VFDVSHQTYP HKMLTGRAAA FLDPARYEDV SGFSNPGESE
HDLFAMGHTS TSVSLACGLA TARDLAGEKY DVVAVIGDGS LSGGLAFEGL DNAAELGSGL
IIVVNDNEWS IAPNHGGIYR NLAELRATRG ASPTNVFRAL GLDYRYLEDG HDLPALERAL
SELRGCDHPV VLHVHTEKGH GFAPALADPE SWHHAAPFDV ATGIAASAPG PDYAELTGAF
LAERMASDPR VVAVSAATPY IMGFTPRRRA AAGARFVDVG IAEEHAVTYV TGLARAGARP
VLGIYGTFLQ RAYDEVWHDL CLNAAPAVIL VFGASAFGTT DATHLGFFDI PLLGAMPGLP
YLAPTCQEEY LDMLSWALSH EDGPVAIRVP GAGVVSRADF ARPSAGYARG WEVVRRGAEV
AVLALGDLLP LGERVADALA ERGVSATLVN PRLATTADEE LLGRLAAGHG VIATLEDGVL
EGGFGERVAR ALGCDDVRVR CYGLPRAFPD RYDPAALLES CGMTAEGVAA DLVRELRG
//
