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Database: UniProt
Entry: A0A287GK35_HORVV
LinkDB: A0A287GK35_HORVV
Original site: A0A287GK35_HORVV 
ID   A0A287GK35_HORVV        Unreviewed;       710 AA.
AC   A0A287GK35;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|ARBA:ARBA00013150};
DE            EC=2.2.1.7 {ECO:0000256|ARBA:ARBA00013150};
OS   Hordeum vulgare subsp. vulgare (Domesticated barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=112509 {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.1HG0085440.1, ECO:0000313|Proteomes:UP000011116};
RN   [1] {ECO:0000313|Proteomes:UP000011116}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Morex {ECO:0000313|Proteomes:UP000011116};
RX   PubMed=23075845; DOI=10.1038/nature11543;
RG   The International Barley Genome Sequencing Consortium;
RA   Mayer K.F., Waugh R., Brown J.W., Schulman A., Langridge P., Platzer M.,
RA   Fincher G.B., Muehlbauer G.J., Sato K., Close T.J., Wise R.P., Stein N.;
RT   "A physical, genetic and functional sequence assembly of the barley
RT   genome.";
RL   Nature 491:711-716(2012).
RN   [2] {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.1HG0085440.1}
RP   IDENTIFICATION.
RC   STRAIN=subsp. vulgare
RC   {ECO:0000313|EnsemblPlants:HORVU.MOREX.r3.1HG0085440.1};
RG   EnsemblPlants;
RL   Submitted (JAN-2022) 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   AlphaFoldDB; A0A287GK35; -.
DR   EnsemblPlants; HORVU.MOREX.r3.1HG0085440.1; HORVU.MOREX.r3.1HG0085440.1; HORVU.MOREX.r3.1HG0085440.
DR   Gramene; HORVU.MOREX.r2.1HG0070270.1; HORVU.MOREX.r2.1HG0070270.1; HORVU.MOREX.r2.1HG0070270.
DR   Gramene; HORVU.MOREX.r2.1HG0070270.1.mrna1; HORVU.MOREX.r2.1HG0070270.1.mrna1; HORVU.MOREX.r2.1HG0070270.1.
DR   Gramene; HORVU.MOREX.r3.1HG0085440.1; HORVU.MOREX.r3.1HG0085440.1; HORVU.MOREX.r3.1HG0085440.
DR   OrthoDB; 3626892at2759; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000011116; Chromosome 1H.
DR   ExpressionAtlas; A0A287GK35; baseline and differential.
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:UP000011116};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          390..555
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   710 AA;  75969 MW;  27E56788E292C2E2 CRC64;
     MALQASVPSA FHTAPAIAHA SCRRQFQLRA SAASSPGAGD GKVAMRKEPA TGAWKIDYSS
     EKPATPLLDT INHPVHMKNL STTDLEQLAA ELRVEIVHTV SKTGGHLSSS LGVVELSVAL
     HHVFDTPEDK IIWDVGHQSY PHKILTGRRS RMHTIRKTSG LAGFPKRDES AHDAFGAGHS
     STSISAALGM AVARDLQGKK NHVISVIGDG AMTAGQAYEA MNNSGYLDSN MIVVLNDNKQ
     VSLPTATLDG PSKPVGALSK ALTTLQSSTK FRRLREAAKN VTKQIGGSTH EVAAKVDEYA
     RGMMSAPGST LFEELGLYYI GPVDGHSLED LVTIFEKVKS MPATGPVLIH IVTEKGKGYP
     PAEAAADKMH GVVKFDPTTG KQFKTKSPTL SYTQYFAESL IREAEVDDKV VAIHAAMGGG
     TGLNYFQKRF PERCFDVGIA EQHAVTFAAG LAAEGMKPFC AIYSSFLQRG YDQVVHDVDL
     QRLPVRFALD RAGLVGADGP THCGAFDVTY MACLPNMVVM APADEAELMH MVATASAIDD
     RPSCFRFPRG NGVGAVLPLN NRGTPMQVGK GRVLVGGNRV ALLGYGTMVQ ACLKAAEALK
     EHGVFITVAD ARFCKPLDTE LIRDLAAEHE ILVTVEEGSI GGFGSHVAHY LSLSGLLDGP
     LKLRSMFLPD RYIDHGAAED QMEEAGLTPR HIAATVLSLL GRPLEALHIK
//
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