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Database: UniProt
Entry: J7TG10_MORMO
LinkDB: J7TG10_MORMO
Original site: J7TG10_MORMO 
ID   J7TG10_MORMO            Unreviewed;       349 AA.
AC   J7TG10;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   08-MAY-2019, entry version 38.
DE   RecName: Full=Phospho-2-dehydro-3-deoxyheptonate aldolase {ECO:0000256|PIRNR:PIRNR001361};
DE            EC=2.5.1.54 {ECO:0000256|PIRNR:PIRNR001361};
GN   ORFNames=MU9_2420 {ECO:0000313|EMBL:AGG31465.1};
OS   Morganella morganii subsp. morganii KT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG31465.1, ECO:0000313|Proteomes:UP000011834};
RN   [1] {ECO:0000313|EMBL:AGG31465.1, ECO:0000313|Proteomes:UP000011834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT {ECO:0000313|EMBL:AGG31465.1};
RX   PubMed=23282187;
RA   Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M.,
RA   Chen C.H., Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT   "Whole-genome sequencing and identification of Morganella morganii KT
RT   pathogenicity-related genes.";
RL   BMC Genomics 13:S4-S4(2012).
CC   -!- FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP)
CC       and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-
CC       arabino-heptulosonate-7-phosphate (DAHP).
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;
CC         EC=2.5.1.54; Evidence={ECO:0000256|PIRNR:PIRNR001361};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate
CC       biosynthesis; chorismate from D-erythrose 4-phosphate and
CC       phosphoenolpyruvate: step 1/7. {ECO:0000256|PIRNR:PIRNR001361}.
CC   -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001361}.
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DR   EMBL; CP004345; AGG31465.1; -; Genomic_DNA.
DR   RefSeq; WP_004235412.1; NC_020418.1.
DR   STRING; 1124991.MU9_2420; -.
DR   EnsemblBacteria; AGG31465; AGG31465; MU9_2420.
DR   GeneID; 14671630; -.
DR   KEGG; mmk:MU9_2420; -.
DR   KO; K01626; -.
DR   BioCyc; MMOR1124991:G1H94-2511-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000011834; 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:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006219; DHAP_synth_1.
DR   PANTHER; PTHR21225; PTHR21225; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   PIRSF; PIRSF001361; DAHP_synthase; 1.
DR   TIGRFAMs; TIGR00034; aroFGH; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011834};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011834};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       43    336       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   349 AA;  38341 MW;  C789AD99A87C782A CRC64;
     MEKTDELRTR AIDKLITPSA LAGEFPATEA INKNVTTSRT RIERILTGDD PRLLVIVGPC
     SVHDPIAALD YAQRLSELLP KYSSRLEIVM RTYFEKPRTV VGWKGLISDP RLDNSCQVNE
     GIRLARKLLI DVNALNVPTA TEFLDMVTGQ YIADLISWGA IGARTTESQI HREMASALSC
     PVGFKNGTDG NIKIAIDAIR AAQAGHMFLS PDKDGQMTIY QTKGNPFGHI IMRGGKTPNY
     AAGDIAHACD QLRQFDLPEH LVIDFSHGNC QKIHRRQLDV AKDVAQQIKD GSRAISGVMA
     ESFIQEGTQK LVNHKAPVYG QSITDPCLSW ADTVTMLDIL ADAADARFS
//
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