DXS_CAPAN
ID DXS_CAPAN Reviewed; 719 AA.
AC O78328;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic;
DE Short=1-deoxyxylulose-5-phosphate synthase;
DE Short=DXP synthase;
DE Short=DXPS;
DE EC=2.2.1.7;
DE AltName: Full=CapTKT2;
DE Flags: Precursor;
GN Name=TKT2;
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9701598; DOI=10.1104/pp.117.4.1423;
RA Bouvier F., D'Harlingue A., Suire C., Backhaus R.A., Camara B.;
RT "Dedicated roles of plastid transketolases during the early onset of
RT isoprenoid biogenesis in pepper fruits.";
RL Plant Physiol. 117:1423-1431(1998).
CC -!- FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2
CC and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-
CC xylulose-5-phosphate (DXP). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + H(+) + pyruvate = 1-deoxy-D-
CC xylulose 5-phosphate + CO2; Xref=Rhea:RHEA:12605, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57792,
CC ChEBI:CHEBI:59776; EC=2.2.1.7;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000305}.
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DR EMBL; Y15782; CAA75778.1; -; mRNA.
DR PIR; T09543; T09543.
DR AlphaFoldDB; O78328; -.
DR SMR; O78328; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000189700; Genome assembly.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.50.920; -; 1.
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; IPR005474; Transketolase_N.
DR PANTHER; PTHR43322; PTHR43322; 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; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00204; dxs; 1.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Isoprene biosynthesis; Magnesium; Metal-binding; Plastid;
KW Thiamine biosynthesis; Thiamine pyrophosphate; Transferase;
KW Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..719
FT /note="Probable 1-deoxy-D-xylulose-5-phosphate synthase,
FT chloroplastic"
FT /id="PRO_0000007394"
FT BINDING 145
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 186..188
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 218..219
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250"
SQ SEQUENCE 719 AA; 77527 MW; 51E887A11A607674 CRC64;
MALCAYAFPG ILNRTVAVAS DASKPTPLFS EWIHGTDLQF QFHQKLTQVK KRSRTVQASL
SESGEYYTQR PPTPIVDTIN YPIHMKNLSL KELKQLADEL RSDTIFNVSK TGGHLGSSLG
VVELTVALHY VFNAPQDRIL WDVGHQSYPH KILTGRREKM STLRQTNGLA GFTKRSESEY
DCFGTGHSST TISAGLGMAV GRDLKGRNNN VIAVIGDGAM TAGQAYEAMN NAGYLDSDMI
VILNDNRQVS LPTATLDGPV PPVGALSSAL SRLQSNRPLR ELREVAKGVT KQIGGPMHEL
AAKVDEYARG MISGSGSTLF EELGLYYIGP VDGHNIDDLI SILKEVRSTK TTGPVLIHVV
TEKGRGYPYA ERAADKYHGV AKFDPATGKQ FKGSAKTQSY TTYFAEALIA EAEADKDIVA
IHAAMGGGTG MNLFLRRFPT RCFDVGIAEQ HAVTFAAGLA CEGLKPFCAI YSSFMQRAYD
QVVHDVDLQK LPVRFAMDRA GLVGADGPTH CGAFDVTFMA CLPNMVVMAP SDEAELFHIV
ATAAAIDDRP SCFRYPRGNG IGVELPAGNK GIPLEVGKGR ILVEGERVAL LGYGSAVQNC
LAAASVLESR GLQVTVADAR FCKPLDRALI RSLAKSHEVL VTVEKGSIGG FGSHVVQFMA
LDGLLDGKLK WRPIVLPDRY IDHGSPADQL AEAGLTPSHI AATVFNILGQ TREALEVMT
