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Database: UniProt
Entry: Q5NG89_FRATT
LinkDB: Q5NG89_FRATT
Original site: Q5NG89_FRATT 
ID   Q5NG89_FRATT            Unreviewed;       370 AA.
AC   Q5NG89; A0A0G2RNT2;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   05-JUN-2019, entry version 98.
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:CAG45596.1};
GN   OrderedLocusNames=FTT_0963c {ECO:0000313|EMBL:CAG45596.1};
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416 {ECO:0000313|EMBL:CAG45596.1, ECO:0000313|Proteomes:UP000001174};
RN   [1] {ECO:0000313|EMBL:CAG45596.1, ECO:0000313|Proteomes:UP000001174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4 {ECO:0000313|Proteomes:UP000001174};
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M., Duffield M.,
RA   Fuxelius H.H., Garcia E., Halltorp G., Johansson D., Isherwood K.,
RA   Karp P., Larsson E., Lui Y., Michell S., Prior J., Prior R.,
RA   Sjostedt A., Svensson K., Thompson N., Vergez L., Wagg J., Wren B.,
RA   Lindler L.E., Andersson S.G., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
RN   [2] {ECO:0000213|PDB:3TQK}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 12-354 IN COMPLEX WITH
RP   MANGANESE.
RX   PubMed=23704901; DOI=10.1371/journal.pone.0063369;
RA   Chaudhury S., Abdulhameed M.D., Singh N., Tawa G.J., D'haeseleer P.M.,
RA   Zemla A.T., Navid A., Zhou C.E., Franklin M.C., Cheung J.,
RA   Rudolph M.J., Love J., Graf J.F., Rozak D.A., Dankmeyer J.L.,
RA   Amemiya K., Daefler S., Wallqvist A.;
RT   "Rapid countermeasure discovery against Francisella tularensis based
RT   on a metabolic network reconstruction.";
RL   PLoS ONE 8:e63369-e63369(2013).
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; AJ749949; CAG45596.1; -; Genomic_DNA.
DR   RefSeq; WP_003019186.1; NZ_CP010290.1.
DR   RefSeq; YP_169953.1; NC_006570.2.
DR   PDB; 3TQK; X-ray; 2.30 A; A=12-354.
DR   PDBsum; 3TQK; -.
DR   SMR; Q5NG89; -.
DR   IntAct; Q5NG89; 1.
DR   DNASU; 3190950; -.
DR   EnsemblBacteria; AJI68989; AJI68989; BZ14_1891.
DR   EnsemblBacteria; CAG45596; CAG45596; FTT_0963c.
DR   GeneID; 3190950; -.
DR   KEGG; ftu:FTT_0963c; -.
DR   PATRIC; fig|177416.36.peg.1895; -.
DR   eggNOG; ENOG4105E99; Bacteria.
DR   eggNOG; COG0722; LUCA.
DR   HOGENOM; HOG000220501; -.
DR   KO; K01626; -.
DR   OMA; YDINTGL; -.
DR   BioCyc; FTUL177416:G1G1C-1084-MONOMER; -.
DR   UniPathway; UPA00053; UER00084.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; 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; -; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0000213|PDB:3TQK};
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001361};
KW   Calcium {ECO:0000213|PDB:3TQK};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001174};
KW   Manganese {ECO:0000213|PDB:3TQK};
KW   Metal-binding {ECO:0000213|PDB:3TQK};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001174};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001361,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:CAG45596.1}.
FT   METAL       263    263       Calcium. {ECO:0000213|PDB:3TQK}.
FT   METAL       274    274       Manganese; via tele nitrogen.
FT                                {ECO:0000213|PDB:3TQK}.
FT   METAL       307    307       Manganese. {ECO:0000213|PDB:3TQK}.
FT   METAL       330    330       Manganese. {ECO:0000213|PDB:3TQK}.
SQ   SEQUENCE   370 AA;  40851 MW;  E407A9D3FB2782AC CRC64;
     MIGDKNFDKV SNINIKKEKV LIPAEVLIQD IPLLKTSFET VRKSRKEIAN IIHGNDDRVA
     VVVGPCSIHD PAAAIEYATK LKEQVKKFHK DILIIMRVYF EKPRTTIGWK GFINDPDLDN
     SYNINKGLRL ARNLLSDLTN MGLPCATEFL DVITPQYFAE LITWGAIGAR TVESQVHREL
     ASGLSASIGF KNATNGDVQV AVDAVKSATY PHHFLSTTKS GSTAIFATKG NQNGHVILRG
     GASGPNFSKE HVDDCIAKLK KADINTKVMI DCSHGNSQKD HSKQISVLAD ICEQIKHSND
     IFGVMIESNL VAGNQDINKK PLTYGQSVTD KCVDFEETVK MLEMLAEAVQ VRRGSQTKQQ
     VKEESQFSLL
//
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