ID A7LA00_PICAB Unreviewed; 717 AA.
AC A7LA00;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=DXS1 {ECO:0000313|EMBL:ABS50518.1};
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329 {ECO:0000313|EMBL:ABS50518.1};
RN [1] {ECO:0000313|EMBL:ABS50518.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17687625; DOI=10.1007/s11103-007-9212-5;
RA Phillips M.A., Walter M.H., Ralph S.G., Dabrowska P., Luck K., Uros E.M.,
RA Boland W., Strack D., Rodriguez-Concepcion M., Bohlmann J., Gershenzon J.;
RT "Functional identification and differential expression of 1-deoxy-D-
RT xylulose 5-phosphate synthase in induced terpenoid resin formation of
RT Norway spruce (Picea abies).";
RL Plant Mol. Biol. 65:243-257(2007).
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; EF688331; ABS50518.1; -; mRNA.
DR BRENDA; 1.1.1.267; 4815.
DR BRENDA; 2.2.1.7; 4815.
DR UniPathway; UPA00064; UER00091.
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 2: Evidence at transcript level;
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 396..561
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 717 AA; 77304 MW; 877DFAAD72B07E89 CRC64;
MATTMAMASP AVIQSNANQL TSMPSALSSR SLRYQIKHTK LEFEKLGRRF GKVHAAALSD
QGEYYSEKPP TPLLDTINYP IHMKNLSIRE LKQLSNELRS DTIFEVARTG GHLGSSLGVV
ELTVALHYVF DAPEDKILWD VGHXAYPHKI LTGRRDKMPT LRQTNGLSGF TKRSESEYDC
FGAGHSSTSI SAGLGMAVGR DLKGRNNHVI SVIGDGAMTA GQAFEAMNNA GYLDSNMIVI
LNDNKQVSLP TANLDGPMPP VGALSSALSK LQSSKPLREL REVAKGVTKQ LGAPMHELAA
KVDEYARGMI SGSRSTLFEE LGLYYIGPVD GHNIDDLLTI LQDVKATHTT GPVLIHVVTE
KGRGYPYAXR AADKYHGVAK FDPATGKQFK GKAPTQTYTA YFAEALISEA DIDNXVVAIH
AAMGGGTGLN MFSKRFPSRC FDVGIAEQHA VTFAAGLACE GLKPFCAIYS SFLQRAYDQV
IHDVDLQKLP VRFAMDRAGL VGADGPTHCG AFDVTYLACL PNMVVMAPSD EAELFHMVAT
AAAIDDRPSC FRFPRGNGVG ARLPPGNKGV PLEVGKGRIL LEGDRVALLG YGTVVQNCLA
ASALLEEQGL SLTVADARFC KPLDRDLIRS LAREHEVIIT VEEGTIGGFG SHVAHFLALD
GFLDGKLKWR PMVLPDHYIE HGAPNDQMVE AGLTASHIAA SVLNILGRTR EALQVMS
//
