ID A0A0S3R7W1_PHAAN Unreviewed; 732 AA.
AC A0A0S3R7W1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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.01G474600 {ECO:0000313|EMBL:BAT76699.1};
GN ORFNames=VIGAN_01474600 {ECO:0000313|EMBL:BAT76699.1};
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:BAT76699.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT76699.1, 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; BAT76699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3R7W1; -.
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: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 NCBIfam; TIGR00204; dxs; 1.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF6; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
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 408..573
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT COILED 94..121
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 732 AA; 78692 MW; 1E182794840388DE CRC64;
MPSFVLGTSF LPFLHSHDKH CGSPTISNIT TKISVTIPQR INQVIAAGGD NVCEEVDNTV
VKKTYQPNQP LRRSLNFSGE KPSTPVLDTV NYPIHMKNLS IQELEELADE LREEIVYTVS
KTGGHLSSSL GVAELTVALH HVFDTPQDKI IWDVGHQTYA HKILTGRRSK MHTIRQTGGL
AGFPKRDESV HDAFGAGHSS TSISAGLGMA VARDLNGSDN HVISVIGDGA MTGGQAYEAM
NNAGFLDTNL IIILNENEQV SLPTATVDGA APPVGALSKA LARLHTSPKF HQLREVAKST
KQIESQARQF ASQLDSYVRG MIGGAGACLF EELGLFYIGP VDGHDMEDLV HILKSVKGMP
TLGAVLIHVI TEKGKGYHPA EVAADKMHGV VKFDPKSGKQ LKSKTSTLSY TQYFAESLIA
EAEVDEKIVA IHAAMGGGTG LNLFQKRFPE RCFDVGIAEQ HAVTFAAGLA AEGCKPFCAI
YSSFLQRGYD QVAHDVDLQK LPVRFALDRA GLVGADGPTH CGAFDTTFMA CLPNMVVMAP
SDETELMHMI ATAAAIDDRP SCFRYPRGNG VGSVLPPNNK GTPLEVGKGR VLKEGSRVAL
VGYGTMVQSC MEAAKVLEAH GISTTVVDAR FCKPLDGDLM RQLAREHEIL ITVEEGSVGG
FGSHVSHFLG LNGLLDGNLK WRAMTLPDMY INHGSQKDQI AMAGLSSNHI AATALSLTNV
NWDSRLLLSL QI
//
