ID   AROG_CORGL              Reviewed;         366 AA.
AC   P35170;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase;
DE            EC=2.5.1.54;
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase;
DE   AltName: Full=DAHP synthase;
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase;
GN   Name=aroG; Synonyms=aroF; OrderedLocusNames=Cgl0990, cg1129;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CCRC 18310;
RX   PubMed=8097175; DOI=10.1111/j.1574-6968.1993.tb06034.x;
RA   Chen C.-C., Liao C.-C., Hsu W.-H.;
RT   "The cloning and nucleotide sequence of a Corynebacterium glutamicum 3-
RT   deoxy-D-arabinoheptulosonate-7-phosphate synthase gene.";
RL   FEMS Microbiol. Lett. 107:223-230(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 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   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family. {ECO:0000305}.
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DR   EMBL; L07603; AAA23292.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB98383.1; -; Genomic_DNA.
DR   EMBL; BX927151; CAF19696.1; -; Genomic_DNA.
DR   PIR; I40837; I40837.
DR   RefSeq; NP_600217.1; NC_003450.3.
DR   RefSeq; WP_011014031.1; NC_006958.1.
DR   AlphaFoldDB; P35170; -.
DR   SMR; P35170; -.
DR   STRING; 196627.cg1129; -.
DR   KEGG; cgb:cg1129; -.
DR   KEGG; cgl:Cgl0990; -.
DR   PATRIC; fig|196627.13.peg.974; -.
DR   eggNOG; COG0722; Bacteria.
DR   HOGENOM; CLU_030903_0_1_11; -.
DR   OMA; DINTGLR; -.
DR   BRENDA; 2.5.1.54; 960.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000000582; Chromosome.
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:UniProtKB-KW.
DR   GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..366
FT                   /note="Phospho-2-dehydro-3-deoxyheptonate aldolase"
FT                   /id="PRO_0000140829"
FT   CONFLICT        109
FT                   /note="I -> T (in Ref. 1; AAA23292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="R -> RR (in Ref. 1; AAA23292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="A -> T (in Ref. 1; AAA23292)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   366 AA;  39131 MW;  1EDA38DD26E29D58 CRC64;
     MSSPVSLENA ASTSNKRVVA FHELPSPTDL IAANPLTPKQ ASKVEQDRQD IADIFAGDDD
     RLVVVVGPCS VHDPEAAIDY ANRLAPLAKR LDQDLKIVMR VYFEKPRTIV GWKGLINDPH
     LNETYDIPEG LRIARKVLID VVNLDLPVGC EFLEPNSPQY YADTVAWGAI GARTTESQVH
     RQLASGMSMP IGFKNGTDGN IQVAVDAVQA AQNPHFFFGT SDDGALSVVE TAGNSNSHII
     LRGGTSGPNH DAASVEAVVE KLGENARLMI DASHANSGKD HIRQVEVVRE IAEQISGGSE
     AVAGIMIESF LVGGAQNLDP AKLRINGGEG LVYGQSVTDK CIDIDTTIDL LAELAAAVRE
     RRAAAK