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Database: UniProt
Entry: F0NV74_LACHH
LinkDB: F0NV74_LACHH
Original site: F0NV74_LACHH 
ID   F0NV74_LACHH            Unreviewed;       589 AA.
AC   F0NV74;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:ADX69568.1};
GN   OrderedLocusNames=LBHH_0337 {ECO:0000313|EMBL:ADX69568.1};
OS   Lactobacillus helveticus (strain H10).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=767462 {ECO:0000313|EMBL:ADX69568.1, ECO:0000313|Proteomes:UP000008640};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=H10;
RA   Zhang H., Zhao W., Chen Y., Sun Z., Sun T., Meng H.;
RT   "Complete genome sequence of Lactobacillus helveticus strain H10.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADX69568.1, ECO:0000313|Proteomes:UP000008640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H10 {ECO:0000313|EMBL:ADX69568.1,
RC   ECO:0000313|Proteomes:UP000008640};
RX   PubMed=21398542; DOI=10.1128/JB.00166-11;
RA   Zhao W., Chen Y., Sun Z., Wang J., Zhou Z., Sun T., Wang L., Chen W.,
RA   Zhang H.;
RT   "Complete genome sequence of Lactobacillus helveticus H10.";
RL   J. Bacteriol. 193:2666-2667(2011).
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; CP002429; ADX69568.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0NV74; -.
DR   KEGG; lhl:LBHH_0337; -.
DR   PATRIC; fig|767462.3.peg.374; -.
DR   HOGENOM; CLU_009227_1_4_9; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000008640; Chromosome.
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; 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   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; IPR049557; Transketolase_CS.
DR   PANTHER; PTHR43322; 1-D-DEOXYXYLULOSE 5-PHOSPHATE SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR43322:SF1; 1-DEOXY-D-XYLULOSE-5-PHOSPHATE SYNTHASE; 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; 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   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          294..457
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   589 AA;  64420 MW;  86D902A302DCF28D CRC64;
     MSLRKELLFM NKHPEYLLNK ISGPQDLKKL SIPEMEQLAQ EIRTLILEKD AAEGGHLGPD
     LGIVEATIAY HYVFDAPKDK IVWDVSHQTY PHKMLTGRAL AWLDPDHYED VTPYSNPDES
     PYDYYAVGHT STSIALATGM AKARDLMGGH ENIMALIGDG SMTGGLAYEG LNNAAIKKHN
     LVVVVNDNQM SIDENVGGLV TALKKLRDSN GETKENPFTA MGFDYRYVAD GNDIKSMIEA
     FKAVKDVDHP ILLHINTLKG KGYKPAIDQE EAHHWVMPFD LNTDKPLAPA SSAPTANSVA
     LDVVSEEIEK GTKLMAINAA IPGVFGLDKI KNKYPDHYTD VGIAEQESVA FAAGAAKEGA
     VPVLFENSTF LQRAFDQLSH DVAANDLPVV MMVAGGGISG TSKTHLGIFD QVMISNLPNW
     IYLAPTNLAE EKAMMKWAIK QRKHPAAIKM PTKAVPENGD AQADYSKIKY QIKPGKDVAV
     LALGDMYAML GEKVAHELGA TLVNPVSANI LDKDALDKLA KENKVIITIE DNVLDGGFGE
     KVASYLGDQD VKVLNYGQKR VYTDQTPLKD ILKDNRLTVE QIVEDVKNA
//
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