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Database: UniProt
Entry: A4N3N9_HAEIF
LinkDB: A4N3N9_HAEIF
Original site: A4N3N9_HAEIF 
ID   A4N3N9_HAEIF            Unreviewed;       320 AA.
AC   A4N3N9;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 72.
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=CGSHi22421_10122 {ECO:0000313|EMBL:EDJ91089.1};
OS   Haemophilus influenzae R3021.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=375432 {ECO:0000313|EMBL:EDJ91089.1, ECO:0000313|Proteomes:UP000003798};
RN   [1] {ECO:0000313|EMBL:EDJ91089.1, ECO:0000313|Proteomes:UP000003798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R3021 {ECO:0000313|EMBL:EDJ91089.1,
RC   ECO:0000313|Proteomes:UP000003798};
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
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; AAZE01000005; EDJ91089.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4N3N9; -.
DR   UniPathway; UPA00064; UER00091.
DR   Proteomes; UP000003798; Unassembled WGS sequence.
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; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 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   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; 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); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 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, ECO:0000313|EMBL:EDJ91089.1}.
FT   DOMAIN          15..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   320 AA;  34892 MW;  A104B93FA5EF0C2E CRC64;
     MIQSVANCPK NNSKPTYSKI FGDWLCEMAE KDAKIIGITP AMREGSGMVE FSQRFPKQYF
     DVAIAEQHAV TFATGLAIGG YKPVVAIYST FLQRAYDQLI HDVAIQNLPV LFAIDRAGIV
     GADGATHQGA FDISFMRCIP NMIIMTPSDE NECRQMLYTG YQCGKPAAVR YPRGNAVGVK
     LTPLEMLPIG KSRLIRKGQK IAILNFGTLL PSALELSEKL NATVVDMRFV KPIDIEMINM
     LAQTHDYLVT LEENAIQGGA GSAVAEVLNS SGKSTALLQL GLPDYFIPQA TQQEALADLG
     LDTKGIEEKI LNFIAKQGNL
//
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