(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZLM7_PSEAB

ID   A0A0H2ZLM7_PSEAB        Unreviewed;       492 AA.
AC   A0A0H2ZLM7;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 9.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|RuleBase:RU364045};
DE            EC=4.1.3.27 {ECO:0000256|RuleBase:RU364045};
GN   Name=trpE {ECO:0000256|RuleBase:RU364045,
GN   ECO:0000313|EMBL:ABJ15573.1};
GN   OrderedLocusNames=PA14_07940 {ECO:0000313|EMBL:ABJ15573.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15573.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15573.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15573.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the
CC       two-step biosynthesis of anthranilate, an intermediate in the
CC       biosynthesis of L-tryptophan. In the first step, the glutamine-
CC       binding beta subunit (TrpG) of anthranilate synthase (AS) provides
CC       the glutamine amidotransferase activity which generates ammonia as
CC       a substrate that, along with chorismate, is used in the second
CC       step, catalyzed by the large alpha subunit of AS (TrpE) to produce
CC       anthranilate. In the absence of TrpG, TrpE can synthesize
CC       anthranilate directly from chorismate and high concentrations of
CC       ammonia. {ECO:0000256|RuleBase:RU364045}.
CC   -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate +
CC       pyruvate + L-glutamate. {ECO:0000256|RuleBase:RU364045}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364045};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC       {ECO:0000256|RuleBase:RU364045}.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits:
CC       a beta subunit (TrpG) and a large alpha subunit (TrpE).
CC       {ECO:0000256|RuleBase:RU364045}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I
CC       family. {ECO:0000256|RuleBase:RU364045}.
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DR   EMBL; CP000438; ABJ15573.1; -; Genomic_DNA.
DR   RefSeq; WP_003085126.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZLM7; -.
DR   EnsemblBacteria; ABJ15573; ABJ15573; PA14_07940.
DR   KEGG; pau:PA14_07940; -.
DR   KO; K01657; -.
DR   OMA; IAGTFKR; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.120.10; -; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR006805; Anth_synth_I_N.
DR   InterPro; IPR005256; Anth_synth_I_PabB.
DR   InterPro; IPR015890; Chorismate_C.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00564; trpE_most; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZLM7.
DR   SWISS-2DPAGE; A0A0H2ZLM7.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Aromatic amino acid biosynthesis {ECO:0000256|RuleBase:RU364045};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Lyase {ECO:0000256|RuleBase:RU364045};
KW   Magnesium {ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|RuleBase:RU364045};
KW   Tryptophan biosynthesis {ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN       28    168       Anth_synt_I_N. {ECO:0000259|Pfam:
FT                                PF04715}.
FT   DOMAIN      223    476       Chorismate_bind. {ECO:0000259|Pfam:
FT                                PF00425}.
SQ   SEQUENCE   492 AA;  54587 MW;  9D5BA5EC152E4107 CRC64;
     MNREEFLRLA ADGYNRIPLS FETLADFDTP LSIYLKLADA PNSYLLESVQ GGEKWGRYSI
     IGLPCRTVLR VYDHQVRISI DGMETERFDC ADPLAFVEEF KARYQVPTVP GLPRFDGGLV
     GYFGYDCVRY VEKRLATCPN PDPLGNPDIL LMVSDAVVVF DNLAGKIHAI VLADPSEENA
     YERGQARLEE LLERLRQPIT PRRGLDLEAA QGREPAFRAS FTREDYENAV GRIKDYILAG
     DCMQVVPSQR MSIEFKAAPI DLYRALRCFN PTPYMYFFNF GDFHVVGSSP EVLVRVEDGL
     VTVRPIAGTR PRGINEEADL ALEQDLLSDA KEIAEHLMLI DLGRNDVGRV SDIGAVKVTE
     KMVIERYSNV MHIVSNVTGQ LREGLSAMDA LRAILPAGTL SGAPKIRAME IIDELEPVKR
     GVYGGAVGYL AWNGNMDTAI AIRTAVIKNG ELHVQAGGGI VADSVPALEW EETINKRRAM
     FRAVALAEQS VE
//

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