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Database: UniProt
Entry: J7TF78_MORMO
LinkDB: J7TF78_MORMO
Original site: J7TF78_MORMO 
ID   J7TF78_MORMO            Unreviewed;       350 AA.
AC   J7TF78;
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_1408 {ECO:0000313|EMBL:AGG30454.1};
OS   Morganella morganii subsp. morganii KT.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Morganella.
OX   NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG30454.1, ECO:0000313|Proteomes:UP000011834};
RN   [1] {ECO:0000313|EMBL:AGG30454.1, ECO:0000313|Proteomes:UP000011834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KT {ECO:0000313|EMBL:AGG30454.1};
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; AGG30454.1; -; Genomic_DNA.
DR   RefSeq; WP_004235667.1; NC_020418.1.
DR   STRING; 1124991.MU9_1408; -.
DR   EnsemblBacteria; AGG30454; AGG30454; MU9_1408.
DR   GeneID; 14670619; -.
DR   KEGG; mmk:MU9_1408; -.
DR   KO; K01626; -.
DR   BioCyc; MMOR1124991:G1H94-1487-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       40    338       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   350 AA;  38215 MW;  FA1E8CB447B43BE5 CRC64;
     MNYQNDDVKI KEIRELLPPV ALLESFPATE TAADTVRRTR HAIHEILEGR DDRLLVVIGP
     CSIHDPKAAV EYADRLLTLR KELKGELEIV MRVYFEKPRT TVGWKGLIND PHLDHSFAIN
     DGLRIARKLL LDINDKGLPA AGEFLDMITP QYLADLMSWG AIGARTTESQ VHRELASGLS
     CPVGFKNGTD GTIKVAIDAI NAAGSPHCFL SVTKWGHSAI VNTTGNGDCH IILRGGKKPN
     YSAEDVSAVK EGLAQAGLAP RIMIDFSHAN SSKQYKRQMD VSTDVAQQVA GGEKAIMGVM
     VESHLEEGNQ NLEGDAPLVY GKSVTDACIG WEDTETLLRQ LADAVKARRS
//
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