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Database: UniProt
Entry: B8DVX4_BIFA0
LinkDB: B8DVX4_BIFA0
Original site: B8DVX4_BIFA0 
ID   B8DVX4_BIFA0            Unreviewed;       415 AA.
AC   B8DVX4;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE            EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
DE   AltName: Full=3-deoxy-D-arabino-heptulosonate 7-phosphate synthase {ECO:0000256|ARBA:ARBA00032193};
DE   AltName: Full=DAHP synthase {ECO:0000256|ARBA:ARBA00031349};
DE   AltName: Full=Phospho-2-keto-3-deoxyheptonate aldolase {ECO:0000256|ARBA:ARBA00031111};
GN   OrderedLocusNames=BLA_0323 {ECO:0000313|EMBL:ACL28625.1};
OS   Bifidobacterium animalis subsp. lactis (strain AD011).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=442563 {ECO:0000313|EMBL:ACL28625.1, ECO:0000313|Proteomes:UP000002456};
RN   [1] {ECO:0000313|EMBL:ACL28625.1, ECO:0000313|Proteomes:UP000002456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AD011 {ECO:0000313|EMBL:ACL28625.1,
RC   ECO:0000313|Proteomes:UP000002456};
RX   PubMed=19011029; DOI=10.1128/JB.01515-08;
RA   Kim J.F., Jeong H., Yu D.S., Choi S.-H., Hur C.-G., Park M.-S., Yoon S.H.,
RA   Kim D.-W., Ji G.E., Park H.-S., Oh T.K.;
RT   "Genome sequence of the probiotic bacterium Bifidobacterium animalis subsp.
RT   lactis AD011.";
RL   J. Bacteriol. 191:678-679(2009).
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   -!- 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|ARBA:ARBA00001370};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       1/7. {ECO:0000256|ARBA:ARBA00004688}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|ARBA:ARBA00007985}.
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DR   EMBL; CP001213; ACL28625.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8DVX4; -.
DR   STRING; 442563.BLA_0323; -.
DR   KEGG; bla:BLA_0323; -.
DR   HOGENOM; CLU_030903_0_1_11; -.
DR   OMA; DINTGLR; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000002456; 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: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   PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR   PANTHER; PTHR21225:SF12; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHE-SENSITIVE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002456};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACL28625.1}.
FT   DOMAIN          102..400
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   415 AA;  45231 MW;  D4614E20F560E314 CRC64;
     MSENPYEPMS KEQKDAIVQG NGLTYTHEQM RQVQHAIAAG KNPLVVLENV PRWEDMAGVD
     RIINRRVLEL DPLPTPAQVL AELPLTRQMQ DIVAYSRDEV RACLYGQDDR LLVIVGPCSV
     HDPKAALDYA HRLRTLKDEL GEDLLIVMRV YFEKPRTTVG WKGLINDPDI DGSHNIQKGL
     LLARRTLLDV LGAGVATATE FLEPTSPQYI ADAVSWGAIG ARNTESQVHR QLASGMSMPI
     GFKNATDGSV KAAVNSCIAA EDQHTFFGID HRGRACAVET LGNPDCHVVL RGSSSGPNYD
     AESVAQALAS IRDKMGDEAA ASHGLVIDCS HGNSGKDDVR QAQVVREIAE RIAGGERGIS
     GVMMESFIVG GNQAPAPLAE LTYGQSITDK CLSWPVTDEL LHTLADAVRT RRWNR
//
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