ID   Q8DSF2_STRMU            Unreviewed;       344 AA.
AC   Q8DSF2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   Name=aroG {ECO:0000313|EMBL:AAN59459.1};
GN   OrderedLocusNames=SMU_1836 {ECO:0000313|EMBL:AAN59459.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59459.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN59459.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and
CC       D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-
CC       heptulosonate-7-phosphate (DAHP). {ECO:0000256|ARBA:ARBA00003726,
CC       ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + phosphoenolpyruvate + H2O = 7-
CC         phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC         Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC         Evidence={ECO:0000256|ARBA:ARBA00047508,
CC         ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688, ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; AE014133; AAN59459.1; -; Genomic_DNA.
DR   RefSeq; WP_002311767.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSF2; -.
DR   STRING; 210007.SMU_1836; -.
DR   GeneID; 93858748; -.
DR   KEGG; smu:SMU_1836; -.
DR   PATRIC; fig|210007.7.peg.1639; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_0_9; -.
DR   OrthoDB; 9807331at2; -.
DR   PhylomeDB; Q8DSF2; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000002512; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:InterPro.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DAHP_synth_1.
DR   NCBIfam; TIGR00034; aroFGH; 1.
DR   NCBIfam; NF009395; PRK12755.1; 1.
DR   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TYROSINE-INHIBITED; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|PIRNR:PIRNR001361}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT   DOMAIN          38..332
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   344 AA;  39096 MW;  0BFCD7EDDD0E84CC CRC64;
     MGIHQKSKTI DLFTVKQGTQ LKGQDLAKKE ARDRELVSII KGEDNRLLLI IGPCSSDNEE
     AVLEYAKRLA KLQEEVKDRI FMVMRVYTAK PRTNGDGYKG LIHQPNTSKL PDLINGIHAV
     RNLHYRVITE TGLTTADEML YPSNLVLVDD LVSYHAVGAR SVEDQEHRFV ASGIDVPTGM
     KNPTSGNLKV MLNALHAAQN SQNFIYNGAE VETDGNSLAH VILRGGSNEH GDYEPNYYYD
     VLLKLIQQYE NMNLINPFIV VDTNHDNSGK NYLEQVRIVR QTLINRDWND KINKYVRGFM
     IESYLEDGRQ DKPEVFGKSI TDPCLGWENT QQLIYEIYHT LKAK
//