ID W7KAR5_PLAFO Unreviewed; 1205 AA.
AC W7KAR5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ORFNames=CK202_2817 {ECO:0000313|EMBL:PKC47184.1}, CYL21_5345
GN {ECO:0000313|EMBL:KAF4326384.1}, PFNF54_04474
GN {ECO:0000313|EMBL:EWC86732.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000313|EMBL:EWC86732.1, ECO:0000313|Proteomes:UP000030673};
RN [1] {ECO:0000313|EMBL:EWC86732.1, ECO:0000313|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:EWC86732.1,
RC ECO:0000313|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PKC47184.1, ECO:0000313|Proteomes:UP000232684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:PKC47184.1};
RA Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT "Plasmodium falciparum NF54 genome assembly.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAF4326384.1, ECO:0000313|Proteomes:UP000754359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000313|EMBL:KAF4326384.1};
RA Baumgarten S., Treeck M., Scherf A.;
RT "Genome assembly of Plasmodium falciparum NF54 DiCre.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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; KE123864; EWC86732.1; -; Genomic_DNA.
DR EMBL; QFXU01000024; KAF4326384.1; -; Genomic_DNA.
DR EMBL; NYMT01000007; PKC47184.1; -; Genomic_DNA.
DR AlphaFoldDB; W7KAR5; -.
DR SMR; W7KAR5; -.
DR EnsemblProtists; EWC86732; EWC86732; PFNF54_04474.
DR VEuPathDB; PlasmoDB:PfNF54_130042000; -.
DR OMA; IFISPAM; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR Proteomes; UP000754359; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR PANTHER; PTHR43322:SF5; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE, CHLOROPLASTIC; 1.
DR Pfam; PF13292; DXP_synthase_N; 2.
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 Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030673};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 828..994
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 256..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1205 AA; 140230 MW; 3B1547C010AAFB6D CRC64;
MIFNYVFFKN FVPVVLYILL IIYINLNGMN NKNQIKTEKI YIKKLNRLSR KNSLCSSKNK
IACLFDIGND DNRNTTYGYN VNVKNDDINS LLKNNYSNKL YMDKRKNINN VISTNKISGS
ISNICSRNQK ENEQKRNKQR CLTQCHTYNM SHEQDKLAND NNRNNKKNFN LLFINYFNLK
RMKNSLLNKD NFFYCKEKKL SFLHKAYKKK NCTFQNYSLK RKSNRDSHKL FSGEFDDYTN
NNALYESEKK EYITLNNNNK NNNNKNNDNK NNDNNDYNNN NSCNNLGERS NHYDNYGGDN
NNPCNNNNDK YDIGKYFKQI NTFINIDEYK TIYGDEIYKE IYELYVERNI PEYYERKYFS
EDIKKSVLFD IDKYNDVEFE KAIKEEFINN GVYINNIDNT YYKKENILIM KKILHYFPLL
KLINNPSDLK KLKKQYLPLL AHELKIFLFF IVNITGGHFS SVLSSLEIQL LLLYIFNQPY
DNVIYDIGHQ AYVHKILTGR KLLFLSLRNK KGISGFLNIF ESIYDKFGAG HSSTSLSAIQ
GYYEAEWQVK NKEKYGNGDI EISDNANVTN NERIFQKGIH NDNNINNNIN NNNYINPSDV
VGRENTNVPN VRNDNHNVDK VHIAIIGDGG LTGGMALEAL NYISFLNSKI LIIYNDNGQV
SLPTNAVSIS GNRPIGSISD HLHYFVSNIE ANAGDNKLSK NAKENNIFEN LNYDYIGVVN
GNNTEELFKV LNNIKENKLK RATVLHVRTK KSNDFINSKS PISILHSIKK NEIFPFDTTI
LNGNIHKENK IEEEKNVSSS TKYDVNNKNN KNNDNSEIIK YEDMFSKETF TDIYTNEMLK
YLKKDRNIIF LSPAMLGGSG LVKISERYPN NVYDVGIAEQ HSVTFAAAMA MNKKLKIQLC
IYSTFLQRAY DQIIHDLNLQ NIPLKVIIGR SGLVGEDGAT HQGIYDLSYL GTLNNAYIIS
PSNQVDLKRA LRFAYLDKDH SVYIRIPRMN ILSDKYMKGY LNIHMKNESK NIDVNVDIND
DVDKYSEEYM DDDNFIKSFI GKSRIIKMDN ENNNTNEHYS SRGDTQTKKK KVCIFNMGSM
LFNVINAIKE IEKEQYISHN YSFSIVDMIF LNPLDKNMID HVIKQNKHQY LITYEDNTIG
GFSTHFNNYL IENNYITKHN LYVHNIYLSN EPIEHASFKD QQEVVKMDKC SLVNRIKNYL
KNNPT
//
