ID D6ZY22_BIFLJ Unreviewed; 377 AA.
AC D6ZY22;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN OrderedLocusNames=BLJ_0336 {ECO:0000313|EMBL:ADG99818.1};
OS Bifidobacterium longum subsp. longum (strain JDM301).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=759350 {ECO:0000313|EMBL:ADG99818.1, ECO:0000313|Proteomes:UP000006740};
RN [1] {ECO:0000313|EMBL:ADG99818.1, ECO:0000313|Proteomes:UP000006740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM301 {ECO:0000313|EMBL:ADG99818.1,
RC ECO:0000313|Proteomes:UP000006740};
RX PubMed=20525832; DOI=10.1128/JB.00538-10;
RA Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA Wang S., Guo X.K.;
RT "Complete genome sequence of Bifidobacterium longum JDM301.";
RL J. Bacteriol. 192:4076-4077(2010).
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}.
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DR EMBL; CP002010; ADG99818.1; -; Genomic_DNA.
DR RefSeq; WP_013140215.1; NC_014169.1.
DR AlphaFoldDB; D6ZY22; -.
DR KEGG; bll:BLJ_0336; -.
DR HOGENOM; CLU_030903_0_1_11; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000006740; 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 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; 41344 MW; 30269EDE91B4A611 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 TARSSAK
//
