ID   TRPE_AZOBR              Reviewed;         732 AA.
AC   P50872;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Anthranilate synthase;
DE            EC=4.1.3.27;
DE   Includes:
DE     RecName: Full=Glutamine amidotransferase;
GN   Name=trpE(G);
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX   PubMed=8939798; DOI=10.1007/s002849900139;
RA   de Troch P., Dosselaere F., Keijers V., de Wilde P., Vanderleyden J.;
RT   "Isolation and characterization of the Azospirillum brasilense trpE(G)
RT   gene, encoding anthranilate synthase.";
RL   Curr. Microbiol. 34:27-32(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + H(+) + L-glutamate +
CC         pyruvate; Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:58359; EC=4.1.3.27;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
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DR   EMBL; U44127; AAC45141.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50872; -.
DR   SMR; P50872; -.
DR   MEROPS; C26.A25; -.
DR   UniPathway; UPA00035; UER00040.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
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; IPR015890; Chorismate_C.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR017926; GATASE.
DR   InterPro; IPR010112; TrpE-G_bact.
DR   InterPro; IPR006221; TrpG/PapA_dom.
DR   PANTHER; PTHR11236; PTHR11236; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   Pfam; PF00117; GATase; 1.
DR   PIRSF; PIRSF036934; TrpE-G; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR01815; TrpE-clade3; 1.
DR   TIGRFAMs; TIGR00566; trpG_papA; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Glutamine amidotransferase; Lyase; Tryptophan biosynthesis.
FT   CHAIN           1..732
FT                   /note="Anthranilate synthase"
FT                   /id="PRO_0000056867"
FT   DOMAIN          533..728
FT                   /note="Glutamine amidotransferase type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        610
FT                   /note="Nucleophile; for GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        699
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        701
FT                   /note="For GATase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00605"
FT   BINDING         583..585
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         614
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
FT   BINDING         660..661
FT                   /ligand="L-glutamine"
FT                   /ligand_id="ChEBI:CHEBI:58359"
FT                   /evidence="ECO:0000250|UniProtKB:P00900"
SQ   SEQUENCE   732 AA;  78042 MW;  4195A53D381B4B7A CRC64;
     MYPADLLASP DLLEPLRFQT RGGVTVTRRA TALDPRTALD PVIDALDRRR GLLLSSGVEA
     PGRYRRHALG FTDPAVALTA RGRTLRIDAL NGRGQVLLPA VAEALRGLEA LAGLEEAPSR
     VTASSASPAP LPGEERSRQP SVFSVLRAVL DLFAAPDDPL LGLYGAFAYD LAFQFEPIRQ
     RLERPDDQRD LLLYLPDRLV ALDPIAGLAR LVAYEFITAA GSTEGLECGG RDHPYRPDTN
     AEAGCDHAPG DYQRVVESAK AAFRRGDLFE VVPGQTFAEP CADAPSSVFR RLRAANPAPY
     EAFVNLGRGE FLVAASPEMY VRVAGGRVET CPISGTVARG ADALGDAAQV LRLLTSAKDA
     AELTMCTDVD RNDKARVCEP GSVRVIGRRM IELYSRLIHT VDHVEGRLRS GMDALDAFLT
     HSWAVTVTGA PKRWAMQFLE DTEQSPRRWY GGAFGRLGFD GGMDTGLTLR TIRMAEGVAY
     VRAGATLLSD SDPDAEDAEC RLKAAAFRDA IRGTAAGAAP TLPAAPRGGE GRRVLLVDHD
     DSFVHTLADY LRQTGASVTT LRHSHARAAL AERRPDLVVL SPGPGRPADF DVAGTIDAAL
     ALGLPVFGVC LGLQGMVERF GGALDVLPEP VHGKATEVRV LGGALFAGLP ERLTVGRYHS
     LVARRDRLPA DLTVTAETAD GLVMAVEHRR LPLAAVQFHP ESILSLDGGA GLALLGNVMD
     RLAAGALTDA AA