DXS_DEHMB
ID DXS_DEHMB Reviewed; 633 AA.
AC A5FRB9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=1-deoxy-D-xylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE EC=2.2.1.7 {ECO:0000255|HAMAP-Rule:MF_00315};
DE AltName: Full=1-deoxyxylulose-5-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXP synthase {ECO:0000255|HAMAP-Rule:MF_00315};
DE Short=DXPS {ECO:0000255|HAMAP-Rule:MF_00315};
GN Name=dxs {ECO:0000255|HAMAP-Rule:MF_00315};
GN OrderedLocusNames=DehaBAV1_0675;
OS Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS BAV1).
OC Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=216389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Ritalahti K.M., Loeffler F., Richardson P.;
RT "Complete sequence of Dehalococcoides sp. BAV1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|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:0000255|HAMAP-
CC Rule:MF_00315};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00315};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00315};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00315}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00315}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00315}.
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DR EMBL; CP000688; ABQ17259.1; -; Genomic_DNA.
DR RefSeq; WP_011929013.1; NC_009455.1.
DR AlphaFoldDB; A5FRB9; -.
DR SMR; A5FRB9; -.
DR KEGG; deb:DehaBAV1_0675; -.
DR PATRIC; fig|216389.18.peg.724; -.
DR HOGENOM; CLU_009227_1_4_0; -.
DR OMA; QVGYHAQ; -.
DR UniPathway; UPA00064; UER00091.
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 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; 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.
PE 3: Inferred from homology;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Thiamine biosynthesis;
KW Thiamine pyrophosphate; Transferase.
FT CHAIN 1..633
FT /note="1-deoxy-D-xylulose-5-phosphate synthase"
FT /id="PRO_1000119543"
FT BINDING 74
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 115..117
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 147..148
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 175
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 286
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
FT BINDING 363
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00315"
SQ SEQUENCE 633 AA; 68581 MW; BCDCA8DDB704BFEE CRC64;
MSKLLDTINS PSDLKKLSLD ELRELAVQIR EELVNRVTLN GGHLASSLGV VELTIALHRV
FESPKDKIIW DVGHQSYAHK LLTGRREQFA TLRQHGGLSG FTCRDESPHD PFGAGHASTS
ISAGLGMAVA RDLAKEDYSV ISVIGDGAIS GGMSFEAINN AGHLHTKFIV ILNDNGMAIS
PSTGALSKFL NNVRFDPRFE FAKRNAKQTI TNMPFGKAVW AFTKSIKRKF EKSMLPGSLW
EELGFIYLGP VDGHNIRELE AALKRAKDFE SKPVLIHMIT KKGKGYDDAE ADAVKYHGIS
PKSGGLKSSH GLSYSQVFGQ TLHKIMSQNP QVVAITAAMT DGCGLGEIAA AFPDRVFDVG
ICEQHAVTFA AGMATQGYIP VVVIYSTFLQ RGFDQIIHDV CLQKLPVVFA IDRGGIVGDD
GKTHQGIFDL SFMSLIPDMV VSAPSDENDL QHLLYTAVNS GKPFALRYPR GFGEGVEIES
SLHNIPIGQN EILVNGSDVA ILATGKSVAF AREALEILTE SGIKPTLVNN RYISPLDSEL
VLKIAQSHKY LVTVEENVIS GGLGSRINTL LAEAGLVNKI KIANIGIPDK FVEHGNQSLL
RAKYGLDGKG IAQRVLSLVG NPNEMKHPQI ICP
