ID A0A1U7ZJZ7_NELNU Unreviewed; 643 AA.
AC A0A1U7ZJZ7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=LOC104595318 {ECO:0000313|RefSeq:XP_010254310.1,
GN ECO:0000313|RefSeq:XP_010254311.1, ECO:0000313|RefSeq:XP_010254312.1,
GN ECO:0000313|RefSeq:XP_010254313.1, ECO:0000313|RefSeq:XP_019052950.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010254311.1};
RN [1] {ECO:0000313|RefSeq:XP_010254310.1, ECO:0000313|RefSeq:XP_010254311.1}
RP IDENTIFICATION.
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_010254310.1; XM_010256008.1.
DR RefSeq; XP_010254311.1; XM_010256009.1.
DR RefSeq; XP_010254312.1; XM_010256010.1.
DR RefSeq; XP_010254313.1; XM_010256011.1.
DR RefSeq; XP_019052950.1; XM_019197405.1.
DR GeneID; 104595318; -.
DR OrthoDB; 3626892at2759; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000189703; Unplaced.
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 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; IPR033248; Transketolase_C.
DR NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF3; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE; 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.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000189703};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 323..488
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 643 AA; 70743 MW; AC6B23F6A1EAE11A CRC64;
MVETPIHLKH LSHKELKQLA DEIRSELSFI MSKTRRSFKA SLAAVDLTVA VHHVFHAPMD
KILWDVGEQA YAHKILTGRR SLMHTLRQKN GLSGFTSRSE SEYDPFGAGH GCNSVSAGLG
MAVARDIKGK RDRVVTIISN ETIMAGQIYE AMSNAGYLDS NMVVILNDSR NSLHPKLEEG
PKTAINALSS TLSKLQSSKS FRKFREAAKG VTKKIGRGMH ELAAKVDEYA RGMMGPLGST
LFEELGLYYI GPVDGHNIED LICVLNEVAS LDSSGPVLVH VVTEENQRME DNHKSEMEVK
QQGYCNSDPL QFYPKPVGSS LSWTYSDFFV ESLVMEMERD KEIVVVHAGM EIEPSFELFH
ERFPEKFFDV GMAEQHAVTF SAGLSCGGLK PFCIIPSTFL QRAYDQVVHD VDRQSIPVRF
VITSAGLVGS DGPIKCGAFD ITFMSCLPNM IVMAPSDEDE LVHMVATAAH IDERPICFRY
PRGAIAGINS PVRTGIPLEI GKGRVLAEGK DVALLGYGVM VQNCLKARSL LSNLGIEVTV
ADARFCKPLD IKLVRQLCHD HSFLITVEEG SIGGFGSHVA QFISLDGQLD GRIKWRPIVL
PDNYVEHASP KEQLALAGLS GHHIAATALN LLGRTRDALL LMR
//
