ID C2GUN1_BIFLN Unreviewed; 609 AA.
AC C2GUN1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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 ORFNames=HMPREF0175_0729 {ECO:0000313|EMBL:EEI81158.1};
OS Bifidobacterium longum subsp. longum ATCC 55813.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=548480 {ECO:0000313|EMBL:EEI81158.1, ECO:0000313|Proteomes:UP000004443};
RN [1] {ECO:0000313|EMBL:EEI81158.1, ECO:0000313|Proteomes:UP000004443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55813 {ECO:0000313|EMBL:EEI81158.1,
RC ECO:0000313|Proteomes:UP000004443};
RA Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L.,
RA Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G.,
RA Francisco L., Fu Q., Gubbala S., Hale W., Han Y., Hemphill L.,
RA Highlander S.K., Hirani K., Hogues M., Jackson L., Jakkamsetti A.,
RA Javaid M., Jiang H., Korchina V., Kovar C., Lara F., Lee S., Mata R.,
RA Mathew T., Moen C., Morales K., Munidasa M., Nazareth L., Ngo R.,
RA Nguyen L., Okwuonu G., Ongeri F., Patil S., Petrosino J., Pham C., Pham P.,
RA Pu L.-L., Puazo M., Raj R., Reid J., Rouhana J., Saada N., Shang Y.,
RA Simmons D., Thornton R., Warren J., Weissenberger G., Zhang J., Zhang L.,
RA Zhou C., Zhu D., Muzny D., Worley K., Gibbs R.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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:EEI81158.1}.
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DR EMBL; ACHI01000018; EEI81158.1; -; Genomic_DNA.
DR AlphaFoldDB; C2GUN1; -.
DR HOGENOM; CLU_009227_1_4_11; -.
DR UniPathway; UPA00064; UER00091.
DR Proteomes; UP000004443; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
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; 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.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977}.
FT DOMAIN 247..418
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 174..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 64214 MW; 079A69496368C395 CRC64;
MLTGRAAAYL DPDRFSEVTG FTNPDESKHD QFVLGHTGTS ISLACGLAKT RDMEGPNSGI
GNVIAVIGDG SLSSGVAFEG LNNAAEQGGN LIIVFNDNEM SIAGDFGGMY GPLARLRASG
GTAQPNLFNA FGLDYRYVEA GNDVSALVAA FEEVRDIDHP VVVHIHTLKG AGYDGEETHA
DRQTASASPV SFDSPTGVHP TDNVNHSEPW HSDHCNLSDH EPHEGQCEAS HWQNPDAAIG
KPDDPRKHYG KMAMAALEPR FAAEPGLVVI SPATPGSNGI THEFRERAGA HYVDTGITES
HAVAYAAGIA RAGGTPVVAT TASFFQRAYD QFFQEMSLNR SRVTVLDFLG GLSGSDNTHS
GAYDVTMFSN IPGATMLVPT SARDYLADLA WATAPAGSAD APAGPVVIRV PGEAILTAER
DATLLPVTGG QIADRPQSTS LPASASSASG GISAATVRGT VSVTAQRAGV RHMLDWRVNQ
TGSHVAIIGL GNAYPLAEQT AAALSADYGI TATVIDPRQC TSLDSDVLES LRDGHQQVIT
LEDGQLEGGW GEKVTAYYAN HHVSDGSRNP RVLNFGAAKE FTDRVSLDEL NERYGLTVEQ
VTEAITRCF
//
