GenomeNet

Database: UniProt
Entry: A0A087G6A2_ARAAL
LinkDB: A0A087G6A2_ARAAL
Original site: A0A087G6A2_ARAAL 
ID   A0A087G6A2_ARAAL        Unreviewed;       699 AA.
AC   A0A087G6A2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
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   OrderedLocusNames=AALP_Aa8g110000 {ECO:0000313|EMBL:KFK25404.1};
OS   Arabis alpina (Alpine rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX   NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK25404.1, ECO:0000313|Proteomes:UP000029120};
RN   [1] {ECO:0000313|Proteomes:UP000029120}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX   PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA   Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA   Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA   Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA   Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA   Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA   Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA   Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA   Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT   "Genome expansion of Arabis alpina linked with retrotransposition and
RT   reduced symmetric DNA methylation.";
RL   Nat. Plants 1:14023-14023(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CM002876; KFK25404.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087G6A2; -.
DR   EnsemblPlants; KFK25404; KFK25404; AALP_AA8G110000.
DR   Gramene; KFK25404; KFK25404; AALP_AA8G110000.
DR   eggNOG; KOG0523; Eukaryota.
DR   OMA; DAGQHTY; -.
DR   OrthoDB; 3626892at2759; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000029120; Chromosome 8.
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   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:UP000029120};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT   DOMAIN          379..544
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   699 AA;  76457 MW;  E7CF0EE60B352777 CRC64;
     MGSSSIGYPF GISSRFDGKF NSRSEITVSA LPCKVDVSSN SFFSASSSTH KECLNRARVC
     SLPNTDEYCD EKVETPILDS IETPLQLKNL SVKELKLLAD EIRTELLSVL WKTQKSMNPS
     LAAIELTLAL HYVFRVPVDK ILWDAVEQTY AHKVLTRRWS AIPSRQENGI SGVTSQLESE
     YDSFGTGHGC NSISAGLGLA VARDMKGKRD RVVAVIDNVT ITAGQAYEAM SNAGYLDSNM
     IVILNDNRHS LHPNMEEGSK ASISALSSIM SKIQSSQIFR KFRGLAKAMT KRIGKGMYEW
     AAKVDEYARG MVGPTGSTLF EELGLYYIGP VDGHNIEDLV CVLREVASLD SMGPVLVHVI
     TEENRDAETA KSIVVKDRRT YSDCFVEALV MEAEKDRDIV VVHAGMEMDP SLVTFQERFP
     DRFFNVGMAE QHAVTFSAGL SSGGLKPFCI IPSAFLQRAY DQVVHDVDRQ RKAVRFVITS
     AGLVGSDGPV QCGAFDIAFM SSLPNMITMA PSDEDELVNM VATAAYVTDR PVCFRFPRGS
     TVKRNYLVPI GLPIEIGRGR VLVEGQDVAF LGYGAMVQNC LNAHSLLSKL GLNVTVADAR
     FCKPLDIKLV RELCQNHKFL ITVEEGCVGG FGSHVAQFIA LDGLLDGNIK WRPIVLPDGY
     IEEASPNEQL ALAGLTGHHI AATALSLLGR TREALLLMS
//
DBGET integrated database retrieval system