ID A0A1U7Y3Y2_NICSY Unreviewed; 717 AA.
AC A0A1U7Y3Y2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Name=LOC104240771 {ECO:0000313|RefSeq:XP_009793959.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009793959.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009793959.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009793959.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 RefSeq; XP_009793959.1; XM_009795657.1.
DR AlphaFoldDB; A0A1U7Y3Y2; -.
DR SMR; A0A1U7Y3Y2; -.
DR STRING; 4096.A0A1U7Y3Y2; -.
DR GeneID; 104240771; -.
DR KEGG; nsy:104240771; -.
DR eggNOG; KOG0523; Eukaryota.
DR OrthoDB; 3626892at2759; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000189701; Unplaced.
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 Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 396..561
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 717 AA; 77361 MW; 0FBD2DDE4A3FEA54 CRC64;
MALCNYAVPG ILNRTVASDY SKQSPLFSEL FHGTDLQYQF QHKLTQVKKR SRGVQASLSE
RGEYYAQRPP TPLLDTINYP IHMKNLSVKE LKQLAEELRS DTIFNVSKTG GHLGSSLGVV
ELTVALHYVF NTPQDRILWD VGHQSYPHKI LTGRRGKMST LRQTDGLAGF TKRSESEYDC
FGTGHSSTTI SAGLGMAVGR DLKGKNNNVI AVIGDGAMTA GQAYEAMNNA GYLDSDMIVI
LNDNRQVSLP TATLDGPAPP VGALSSALSR LQSNRPLREL REVAKGVTKQ IGGPMHELAA
KVDEYARGMI SGSGSTLFEE LGLYYIGPVD GHNIDDLISI LKEVRSTKTT GPVLIHVITE
KGRGYPYAER AADKYHGVAK FDPATGKQFK VSAKTQSYTT YFAEALIAEA EADKDIVAIH
AAMGGGTGMN LFHRRFPTRC FDVGIAEQHA VTFAAGLACE GLKPFCAIYS SFLQRAYDQV
VHDVDLQKLP VRFAMDRAGL VGADGPTHCG AFDVTFMACL PNMVVMAPSD ETELFHMVAT
AAAIDDRPSC FRYPRGNGIG VELPVGNKGT PLEVGKGRIL VEGERVALLG YGSAVQNCLA
AAAVLETRGL QVTVADARFC KPLDGALIRS LAKSHEVLIT VEEGSIGGFG SHVAQFMALD
GLLDGKLKWR PIVLPDRYID HGSPADQLAE AGLTPSHIAA TVFNILGQTR EALEVMT
//
