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Database: UniProt
Entry: A3MYQ7_ACTP2
LinkDB: A3MYQ7_ACTP2
Original site: A3MYQ7_ACTP2 
ID   A3MYQ7_ACTP2            Unreviewed;       353 AA.
AC   A3MYQ7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   11-DEC-2019, entry version 81.
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=aroF {ECO:0000313|EMBL:ABN73293.1};
GN   OrderedLocusNames=APL_0185 {ECO:0000313|EMBL:ABN73293.1};
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN73293.1, ECO:0000313|Proteomes:UP000001432};
RN   [1] {ECO:0000313|EMBL:ABN73293.1, ECO:0000313|Proteomes:UP000001432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20 {ECO:0000313|EMBL:ABN73293.1,
RC   ECO:0000313|Proteomes:UP000001432};
RX   PubMed=18065534; DOI=10.1128/JB.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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|PIRNR:PIRNR001361}.
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         Evidence={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|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP000569; ABN73293.1; -; Genomic_DNA.
DR   RefSeq; WP_005600235.1; NC_009053.1.
DR   STRING; 416269.APL_0185; -.
DR   EnsemblBacteria; ABN73293; ABN73293; APL_0185.
DR   GeneID; 4848729; -.
DR   KEGG; apl:APL_0185; -.
DR   PATRIC; fig|416269.6.peg.189; -.
DR   eggNOG; ENOG4105E99; Bacteria.
DR   eggNOG; COG0722; LUCA.
DR   HOGENOM; HOG000220501; -.
DR   KO; K01626; -.
DR   OMA; VMENVAN; -.
DR   BioCyc; APLE416269:G1G87-191-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000001432; 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: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 {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:ABN73293.1}.
FT   DOMAIN          49..344
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   353 AA;  38828 MW;  42573C5CF96CEE7D CRC64;
     MNTVVNQDSL HNVNIVDEKV LLTPAELKAE LPLPEYLRKQ IETSRREISD IIHKRDQRKL
     IVIGPCSIHD PIAAIEYGKK LKALADTVSD KLYIVMRVYF EKPRTTVGWK GLINDPKIDG
     TFDVETGLRV GRKLCLDLAE LGLPLATEAL DPMTPQYLAD LFSWSAIGAR TTESQTHREL
     ASGLSMAVGF KNGTDGSLSV AINAMQSAAQ SHSFIGINQK GQVNLLHTKG NPDSHVILRG
     GKTPNFEKQY VEECEAALRK AGLAEAIMID CSHGNSNKDY RRQPLVAEDA LSQLLAGNTS
     IIGLMIESHL NAGNQSSDQA FNQMQYGVSI TDACIDWQTT ENLLTDFAEK LRA
//
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