ID Q8G7E6_BIFLO Unreviewed; 377 AA.
AC Q8G7E6;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=aroG2 {ECO:0000313|EMBL:AAN24160.1};
GN OrderedLocusNames=BL0320 {ECO:0000313|EMBL:AAN24160.1};
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN24160.1, ECO:0000313|Proteomes:UP000000439};
RN [1] {ECO:0000313|EMBL:AAN24160.1, ECO:0000313|Proteomes:UP000000439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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 + 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 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|ARBA:ARBA00007985, ECO:0000256|PIRNR:PIRNR001361}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014295; AAN24160.1; -; Genomic_DNA.
DR RefSeq; NP_695524.1; NC_004307.2.
DR RefSeq; WP_007051442.1; NC_004307.2.
DR AlphaFoldDB; Q8G7E6; -.
DR SMR; Q8G7E6; -.
DR STRING; 206672.BL0320; -.
DR EnsemblBacteria; AAN24160; AAN24160; BL0320.
DR GeneID; 69577536; -.
DR KEGG; blo:BL0320; -.
DR PATRIC; fig|206672.9.peg.1059; -.
DR HOGENOM; CLU_030903_0_1_11; -.
DR OrthoDB; 9807331at2; -.
DR PhylomeDB; Q8G7E6; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000000439; Chromosome.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
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; 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 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|PIRNR:PIRNR001361};
KW Reference proteome {ECO:0000313|Proteomes:UP000000439};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR001361}.
FT DOMAIN 62..362
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 377 AA; 41413 MW; 30269EDF21B4A611 CRC64;
MAALRGPDSS EDERRLGEQA VFPETVDVNI RQLDPIPAPR AFLREQPLTD EMSELVLHSR
QEIRDVLNGR DDRLLVIVGP CSIHDPKAAH EYAEKLAAVK RELEDRLVIV MRVYFEKPRT
TIGWKGLIND PDLDGRFNIR KGMWLARKVL TDVLSLGLPA ATEWLDPITP QYICDAISWG
AIGARNTESQ VHRELASGLS MPVGFKNSTD GSIKAAADSC FAAGFEHHFL SINLDGRVIS
AETKGNPDCH LVLRGSSHGP NYDAESVRQA LEDLKVSKAS GPSQHGLVID AAHGNCGKDE
NREAEVIEEI AERLAHGEQG ITGVMMESFL VGGHQKPAPL DQLVYGQSVT DSCVPWERTN
ELLHTLADAV TARRSAK
//
