ID E4ZB78_NEIL0 Unreviewed; 351 AA.
AC E4ZB78;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
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=aroG {ECO:0000313|EMBL:CBN86605.1};
GN OrderedLocusNames=NLA_3650 {ECO:0000313|EMBL:CBN86605.1};
OS Neisseria lactamica (strain 020-06).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=489653 {ECO:0000313|EMBL:CBN86605.1, ECO:0000313|Proteomes:UP000008723};
RN [1] {ECO:0000313|EMBL:CBN86605.1, ECO:0000313|Proteomes:UP000008723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=020-06 {ECO:0000313|EMBL:CBN86605.1,
RC ECO:0000313|Proteomes:UP000008723};
RX PubMed=21092259; DOI=10.1186/1471-2164-11-652;
RA Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I.,
RA White B., Parkhill J., Maiden M.C.;
RT "Independent evolution of the core and accessory gene sets in the genus
RT Neisseria: insights gained from the genome of Neisseria lactamica isolate
RT 020-06.";
RL BMC Genomics 11:652-652(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; FN995097; CBN86605.1; -; Genomic_DNA.
DR RefSeq; WP_013448416.1; NC_014752.1.
DR AlphaFoldDB; E4ZB78; -.
DR KEGG; nla:NLA_3650; -.
DR eggNOG; COG0722; Bacteria.
DR HOGENOM; CLU_030903_0_1_4; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000008723; 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 43..335
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 351 AA; 38626 MW; 2D329C231591EE4D CRC64;
MTHHYPTDDI KIKEVKELLP PIAHLYELPI SKEASGLVHR TRQEISDLVH GRDKRLLVII
GPCSIHDPKA ALEYAERLLK LRKQYENELL IVMRVYFEKP RTTVGWKGLI NDPHLDGTFD
INFGLRQARS LLLSLNNMGM PASTEFLDMI TPQYYADLIS WGAIGARTTE SQVHRELASG
LSCPVGFKNG TDGNLKIAID AIGAASHSHH FLSVTKAGHS AIVHTGGNPD CHVILRGGKE
PNYDAEHVSE AAEQLRAAGV TDKLMIDCSH ANSRKDYTRQ MEVAQDIAAQ LEQDGGNIMG
VMVESHLVEG RQDKPEVYGK SITDACIGWG ATEELLALLA GANKKRMARA G
//
