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Database: UniProt
Entry: W6AA61_9MOLU
LinkDB: W6AA61_9MOLU
Original site: W6AA61_9MOLU 
ID   W6AA61_9MOLU            Unreviewed;       547 AA.
AC   W6AA61;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=dxs {ECO:0000313|EMBL:AHI53896.1};
GN   ORFNames=SSABA_v1c04890 {ECO:0000313|EMBL:AHI53896.1};
OS   Spiroplasma sabaudiense Ar-1343.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276257 {ECO:0000313|EMBL:AHI53896.1, ECO:0000313|Proteomes:UP000019265};
RN   [1] {ECO:0000313|EMBL:AHI53896.1, ECO:0000313|Proteomes:UP000019265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar-1343 {ECO:0000313|EMBL:AHI53896.1};
RX   PubMed=24534435;
RA   Chang T.H., Lo W.S., Ku C., Chen L.L., Kuo C.H.;
RT   "Molecular evolution of the substrate utilization strategies and putative
RT   virulence factors in mosquito-associated Spiroplasma species.";
RL   Genome Biol. Evol. 6:500-509(2014).
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; CP006934; AHI53896.1; -; Genomic_DNA.
DR   RefSeq; WP_025251037.1; NZ_CP006934.1.
DR   AlphaFoldDB; W6AA61; -.
DR   STRING; 1276257.SSABA_v1c04890; -.
DR   KEGG; ssab:SSABA_v1c04890; -.
DR   PATRIC; fig|1276257.3.peg.499; -.
DR   eggNOG; COG1154; Bacteria.
DR   HOGENOM; CLU_009227_1_4_14; -.
DR   OrthoDB; 9803371at2; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000019265; Chromosome.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR000399; TPP-bd_CS.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR049557; Transketolase_CS.
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; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 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:UP000019265};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          253..416
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   547 AA;  62522 MW;  231DE2C9BADF5ED6 CRC64;
     MKLVDYKDWN DIFDVNIECL NDLITDLRFF LIDYVQENGG HLGSNLGVLE ITVGIINVFG
     LKNSKILFDT GHQSHFYKIL TNRKFAFEKI KSNNKVSNFQ EHLESEFDHI SNGHSSTALS
     IALGHKISNP EDEIIVIIGD AALLNGVALE GLVAIANQDK KIIIVYNDND HGIGENFLKI
     NNPKKFFESL GFEYHFEKSG NDIEKVIDNL KIAKSSLKST VLHLKTLKSN GFLGSDRESL
     NHSINKKPNL NVTNLDQVVK NFYLKKLQNG KSLSIISPGM LISNKLLELK KMYPKNVFDV
     GINEEHALLL GVGLALNNQR VIISIYSTFL QRAYDQLVHD VFRNNLPITF LIEKVGFSWN
     NGISHHGIYD LAICQTFNNA IIGHPRSEFE LNIMLEQSFN NLKAPFFIRL ENNVRENKNF
     QKKFEINEYE LINFNEKNKA TLFTYGENLN IFEEKIFSQK LPINLVNARF LNKLDEKVLA
     KVMKTEIFVY EHVISKSNLA TLFREKQIEI VSYSVETHNV GSGDETSWLK DLKLDYDSVV
     KKILNKK
//
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