ID A1XP41_HEVBR Unreviewed; 711 AA.
AC A1XP41;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=DXS2 {ECO:0000313|EMBL:ABF18929.1};
OS Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Micrandreae;
OC Hevea.
OX NCBI_TaxID=3981 {ECO:0000313|EMBL:ABF18929.1};
RN [1] {ECO:0000313|EMBL:ABF18929.1}
RP NUCLEOTIDE SEQUENCE.
RA Seetang-nun Y., Suvachittanont W., Sharkey T.D.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABF18929.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17852343; DOI=10.1080/10425170701576768;
RA Seetang-Nun Y., Sharkey T.D., Suvachittanont W.;
RT "Isolation and characterization of two distinct classes of DXS genes in
RT Hevea brasiliensis.";
RL DNA Seq. 19:291-300(2008).
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; DQ473433; ABF18929.1; -; mRNA.
DR AlphaFoldDB; A1XP41; -.
DR OrthoDB; 3626892at2759; -.
DR UniPathway; UPA00064; UER00091.
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: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; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 391..556
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 711 AA; 76345 MW; 7149389EAB8F3837 CRC64;
MAVSSSSFVS NQSFSPFLKA PRSNLCGRKQ FCLRASAGHP DEEGKMMIRK EKDGWKIDFS
GEKPPTPLLD TINYPVHTKN LSTQDLEQLA AELRADIVYS VSKTGGHLSS SLGVVELAVA
LHHVFSTPDD KIIWDVGHQA YPHKILTGRR SRMHTIRKTS GLAGFPKRDE SVYDAFGAGH
SSTSISAGLG MAVARDLLGK NNNVISVIGD GAMTAGQAYE AMNNAGFLDA NLIVILNDNK
QVSLPTATLD GPATPVGALS SALAKIQAST QFRKLREAAK SITKQIGGKT HQVAAKVDEY
ARGMISASGS TLFEELGLYY IGPVDGHNIE DLVTIFQKVK AMPAPGPVLI HIVTEKGKGY
PPAEAAADKM HGVVKFDVQT GKQFKPKSPT LSYTQYFAEA LIKEAETDNK IVAIHAAMGG
GTGLNYFQKR FPDRCFDVGI AEQHAVTFAA GLATEGLKPF CAIYSSFLQR GYDQVVHDVD
LQKLPVRFAM DRAGLVGADG PTHCGAFDIA YMACLPNMVV MAPSDEAELM HMVATAAAID
DRPSCFRFPR GNGIGAALPP NNKGTPLEIG KGRILMEGNR VAILGYGSIV QQCVEAASML
RTQGISVTVA DARFCKPLDT DLIRQLAKEH EFLITVEEGS IGGFSSHVSH FLSLSGILDG
PLKLRAMVLP DRYIDHGSPQ DQIQEAGISS NHITATVLSL LGKPKEALQF K
//
