ID A0A1B8JAK7_9HELI Unreviewed; 630 AA.
AC A0A1B8JAK7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BA723_03295 {ECO:0000313|EMBL:OBV29986.1}, BKN38_05650
GN {ECO:0000313|EMBL:OHU83193.1};
OS Helicobacter sp. CLO-3.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=211 {ECO:0000313|EMBL:OBV29986.1, ECO:0000313|Proteomes:UP000092701};
RN [1] {ECO:0000313|EMBL:OBV29986.1, ECO:0000313|Proteomes:UP000092701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC1 {ECO:0000313|EMBL:OBV29986.1,
RC ECO:0000313|Proteomes:UP000092701};
RA Greninger A.L., Bateman A., Jerome K., Fang F.;
RT "Genome sequence of Helicobacter sp. CLO-3.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OHU83193.1, ECO:0000313|Proteomes:UP000179541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLO-3 {ECO:0000313|EMBL:OHU83193.1,
RC ECO:0000313|Proteomes:UP000179541};
RA Greninger A.L., Bateman A.C., Fang F., Jerome K.;
RT "Genome sequence of Helicobacter sp. CLO-3 Fennel-37 strain.";
RL Submitted (OCT-2016) 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: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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBV29986.1}.
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DR EMBL; MAMQ01000028; OBV29986.1; -; Genomic_DNA.
DR EMBL; MLQN01000017; OHU83193.1; -; Genomic_DNA.
DR RefSeq; WP_066453669.1; NZ_MLQN01000017.1.
DR AlphaFoldDB; A0A1B8JAK7; -.
DR STRING; 211.BKN38_05650; -.
DR OrthoDB; 9803371at2; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000092701; Unassembled WGS sequence.
DR Proteomes; UP000179541; Unassembled WGS sequence.
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; IPR049557; Transketolase_CS.
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}; Reference proteome {ECO:0000313|Proteomes:UP000092701};
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 306..471
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 67
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 108..110
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 140..141
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 168
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 168
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 275
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
FT BINDING 357
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00315"
SQ SEQUENCE 630 AA; 69171 MW; 0A58DF44AF232BF1 CRC64;
MFPQKPIAEM DIAELESLCA QIRARILEVV SSNGGHLSST LGAVELIVAM HYVFDYHTNP
FIFDVSHQAY AHKLLTGRYD DFASLRKFGG ISGFCKPSES DADYFIAGHS STSISLGVGA
AKAIKLRGEN GMPIVLIGDG SMSAGLVYEA LNELGDRKYP MLIILNDNEM SIAKPIGAIS
KHLSQIISHP MYQSIRNFTK RWLGKMPDSA TYIAKRFEES LKLITPGILF EEMGIDYMGP
VDGHSLEELI FCFKRAREME RPIIVHTQTT KGKGYKIAEG PYEKWHGVSP FDLETGIALK
APSTTPAPTQ IYADTLQNLA ENDPKIVGIT AAMPGGVGLG KLIDLYPDRF WDVGIAEQHC
VTSMAAMAKE GFIPFVSIYS TFLQRAFDQI IHDVAIMRLP VRFSIDRAGI VGEDGETHQG
LFDIAYLQMI PGFVLFAPRD NATLEKAIRF AHKFDSAPCA YRYPRGLFCL DEGVYEASEF
ALGECEVLES GREILLIGYG NGVGRAHLVN AELKRLGFAP TLLDLRFCKP LPNALESALR
AHSISFVFSD SYKEGGVGHA ILGLMSERGI AKPSYSLEIE DAFVPHGDVA SIERAMGLDT
QGLLKRIISL LDRHSISAKS SDLVESKKGQ
//
