ID E3ZQ99_LISSE Unreviewed; 630 AA.
AC E3ZQ99;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
DE Flags: Fragment;
GN ORFNames=NT03LS_1643 {ECO:0000313|EMBL:EFS00190.1};
OS Listeria seeligeri FSL N1-067.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFS00190.1};
RN [1] {ECO:0000313|EMBL:EFS00190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFS00190.1};
RX PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT characterized by limited gene acquisition and limited gene loss.";
RL BMC Genomics 11:688-688(2010).
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:EFS00190.1}.
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DR EMBL; ADXJ01000637; EFS00190.1; -; Genomic_DNA.
DR AlphaFoldDB; E3ZQ99; -.
DR PATRIC; fig|702453.3.peg.1338; -.
DR HOGENOM; CLU_433842_0_0_9; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000004302; Chromosome.
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 HAMAP; MF_00315; DXP_synth; 1.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 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 Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 312..477
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFS00190.1"
SQ SEQUENCE 630 AA; 68843 MW; F754B1EC0724D7B0 CRC64;
PRKDPSFIKQ LDIKELEALA ADIRAFLITS TSKSGGHIGP NLGVVELTIA MHYTFTSPKD
KFIWDVGHQS YVHKILTGRA SQFETLRQHG GLDGFPKRRE SLHDVFETGH SSTSLSAAAG
MAIARDIKQE DFCVVPVIGD GALTGGMALE ALNHIGDMGK DMIVILNDND MSIAPNVGAL
HNVLGKLRTS DKFVRTKKDL DKIMRKIPTA GEKVADTAGK IKDSVKHLLV EGTFFEELGF
MYLGPVDGHN LQDLITNLEF AKRTSGPVLL HIVTKKGKGY KPAELDERGT WHGTGPYKVE
TGSFIKPAQT APSWSSIISK ELMRLAAEDD RIVAITPAMP VGSKLEKFAA TFPERFFDVG
IAEQHATTMA AGLASQGMKP FLAIYSTFLQ RAYDQVVHDV CRQKLNVVFG IDRAGLVGAD
GETHQGIFDI SFLSSIPNMI ISMPKDEVEA KRLMDTAFAY DEGPIAIRYP RGNGLGGEQS
ITTELIPIGE WETIIQPIDA VIITFGPTIQ LAIGAAEQLA LEGKRVGVIN ARFIKPLDEA
LLHHIFKLNI PVLTAEESLL KGGFGSSVLE FMEVNNYTDI IFHRIGLPDQ FISHGSVSLI
LESYGISVSG FVVKINEMLA QSEKLRAKRL
//
