ID A0A0S3R3F9_PHAAN Unreviewed; 714 AA.
AC A0A0S3R3F9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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=Vigan.01G290300 {ECO:0000313|EMBL:BAT75097.1};
GN ORFNames=VIGAN_01290300 {ECO:0000313|EMBL:BAT75097.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT75097.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT75097.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
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; AP015034; BAT75097.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R3F9; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000291084; Chromosome 1.
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:SF4; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE 2, CHLOROPLASTIC-RELATED; 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:UP000291084};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 394..559
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 714 AA; 77069 MW; DC4EFC992C0CDAFD CRC64;
MAFCGGTFVK PNHSFSQTHK PKAPTPYYDT RKKFCVRVSA SDSGEVEKTV IRKEKDGWKI
NYSGEKPQTP LLDTVNHPIH MKNLSTQDLE QLAAELRADI VHSVSNTGGH LSSSLGVVEL
AVALHHVFDT PEDKIIWDVG HQAYPHKILT GRRSRMHTIR KTSGLAGFPK RDESTHDAFG
VGHSSTSISA GLGMAVARDL LGKKNSIISV IGDGALTAGQ AYEALNNAGF LDSNMIVVLN
DNKQVSLPTA TLDGPASPVG ALSSALSKIQ ASTEFRKLRE AAKSITKQIG GQTHQVAAKV
DEYARGMISG SGSTLFEELG LYYIGPVDGH NIEDLVTIFE KVKSMPAPGP VLIHIVTEKG
KGYPPAEKAA DRMHGVVKFD PKTGKQFKAK SSTLSYTQYF AESLIQEAEI DDKVVAIHAA
MGGGTGLNYF HKRFPDRCFD VGIAEQHAVT FAAGLAAEGL KPFCAIYSSF LQRGYDQVVH
DVDLQKLPVR FAMDRAGLVG ADGPTHCGAF DIAYMACLPN MVVMAPSDEA ELMHMVATAA
TIDDRPSCFR FPRGNGIGAT LPLNNKGTPL EIGKGRILME GSRVAILGYG SVVQQCRHAS
ELLKEVGVNV TIADARFCKP LDTDLIRLLA KEHEILITVE EGSIGGFGSH VSQFLSLSGI
LDGPVKWRAM VLPDRYIDHG SPQDQVEEAG LSSKHIAATV LSLLQRPKEV LLFK
//
