ID A0A0T9QTX3_9GAMM Unreviewed; 348 AA.
AC A0A0T9QTX3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=aroH {ECO:0000313|EMBL:CNI28504.1};
GN ORFNames=ERS008529_03597 {ECO:0000313|EMBL:CNI28504.1};
OS Yersinia pekkanenii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=1288385 {ECO:0000313|EMBL:CNI28504.1, ECO:0000313|Proteomes:UP000045840};
RN [1] {ECO:0000313|Proteomes:UP000045840}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A125KOH2 {ECO:0000313|Proteomes:UP000045840};
RG Pathogen Informatics;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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; CQAZ01000038; CNI28504.1; -; Genomic_DNA.
DR RefSeq; WP_049614505.1; NZ_CWJL01000016.1.
DR AlphaFoldDB; A0A0T9QTX3; -.
DR STRING; 1288385.ERS137968_03036; -.
DR OrthoDB; 9807331at2; -.
DR UniPathway; UPA00053; UER00084.
DR Proteomes; UP000045840; Unassembled WGS sequence.
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:SF6; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, TRP-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|PIRNR:PIRNR001361};
KW Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW Transferase {ECO:0000256|PIRNR:PIRNR001361, ECO:0000313|EMBL:CNI28504.1}.
FT DOMAIN 41..337
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 348 AA; 38116 MW; CA73C47DB09BDC0A CRC64;
MHKTDELRTT RIDSLITPQQ LAEKLPISGT IASNVTASRK RIEKILTGED PRLLVIVGPC
SIHDPDAAID YATRLNVLRE RYQDSLEIVM RTYFEKPRTV VGWKGLISDP ALDGSCQVNL
GIEMARRLLL AVNQLGLPTA TEFLDMVTGQ YIADLISWGA IGARTTESQI HREMASALSC
PVGFKNGTDG NTRIAIDAIR AAQASHMFLS PDKTGQMTIY QTKGNPYGHI IMRGGKQPNY
GASDIAAACD SLREFDLPEH LVVDFSHGNC QKMYHRQLEV AADIAQQIRA GSMAIVGVMA
ESFLIEGTQK IVAGQPLTYG QSITDPCLNW ADTEQLLNLL ADAVSSRF
//