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Entry: M1MB24_9PROT
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Original site: M1MB24_9PROT 
ID   M1MB24_9PROT            Unreviewed;       621 AA.
AC   M1MB24;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   13-SEP-2023, entry version 65.
DE   RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            EC=2.2.1.7 {ECO:0000256|HAMAP-Rule:MF_00315};
DE   AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXP synthase {ECO:0000256|HAMAP-Rule:MF_00315};
DE            Short=DXPS {ECO:0000256|HAMAP-Rule:MF_00315};
GN   Name=dxs {ECO:0000256|HAMAP-Rule:MF_00315};
GN   ORFNames=ST1E_0707 {ECO:0000313|EMBL:AGF49080.1};
OS   Candidatus Kinetoplastibacterium galatii TCC219.
OC   Bacteria; Pseudomonadota; Betaproteobacteria;
OC   Candidatus Kinetoplastibacterium.
OX   NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF49080.1, ECO:0000313|Proteomes:UP000011658};
RN   [1] {ECO:0000313|EMBL:AGF49080.1, ECO:0000313|Proteomes:UP000011658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC219 {ECO:0000313|EMBL:AGF49080.1,
RC   ECO:0000313|Proteomes:UP000011658};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA   Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT   and angomonas.";
RL   Genome Biol. Evol. 5:338-350(2013).
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:0000256|HAMAP-Rule:MF_00315}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00315};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00315};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00315};
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, ECO:0000256|HAMAP-Rule:MF_00315}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_00315}.
CC   -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC       {ECO:0000256|ARBA:ARBA00011081, ECO:0000256|HAMAP-Rule:MF_00315}.
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DR   EMBL; CP003806; AGF49080.1; -; Genomic_DNA.
DR   RefSeq; WP_015389565.1; NC_020284.1.
DR   AlphaFoldDB; M1MB24; -.
DR   STRING; 1208921.ST1E_0707; -.
DR   KEGG; kga:ST1E_0707; -.
DR   PATRIC; fig|1208921.3.peg.362; -.
DR   eggNOG; COG1154; Bacteria.
DR   HOGENOM; CLU_009227_1_4_4; -.
DR   OrthoDB; 9803371at2; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000011658; Chromosome.
DR   GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
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   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00204; dxs; 1.
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   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; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229, ECO:0000256|HAMAP-
KW   Rule:MF_00315};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00315};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00315};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00315};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW   Rule:MF_00315};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00315}.
FT   DOMAIN          31..50
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
FT   BINDING         75
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         116..118
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         148..149
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         177
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         177
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         284
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT   BINDING         366
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ   SEQUENCE   621 AA;  68388 MW;  6909A182F241B336 CRC64;
     MATNLLDSIS SPCDLKKFNI IELKKLAKEL RQEILELVSK TGGHLSSNLG VVELTLAIHY
     IFNAPEDRIV WDVGHQSYAH KILTGRRKLM GTLRQFNGIS GFPSKTESCY DAFGTAHSST
     SISAVLGMAV AARELNMDRN NIAIIGDGAI SSGMAFEAIN NADNIKDINL TVILNDNHMS
     ISQPVGSLNN YFSQLMDGRF YAKAKNVGKV VLQHIPSVLK LAKSFESHAK DIIKTTILFE
     EFGFKYFGPI DGHSIDDLIS ELNKVKYYPG LKFLHIVTKK GKGYKLAEKN PILYHGPGKF
     NINTGVKLAE KNIPKTFTNI FSEWICDMAR IDHRLIAITP AMSEGSGLVK FEELFPERYF
     DVGISEQHAI TFAAGISCDG LKPVVAIYST FLQRGYDQFI HDVAIQNLDV TFALDRAGIV
     GADGPTHAGN YDIAFLRCIP GMVIATPSDE NEERILLNTC YKYQGPASVR YPRGNIIGVD
     IDINLNTVVE IGKGVVRRTG KNIAILCFGT LLQKVLDAAD RLNTSVVDMR FVKPIDHEII
     LSISKDHKAI VTIEDSSIMG GAGSAVLETL QKFNLLIPVL QLGIPDNFIA HGDINILMSS
     IGLDVYGIEN SIRSRFYNLI D
//
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