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Database: UniProt
Entry: G7Z4T1_AZOL4
LinkDB: G7Z4T1_AZOL4
Original site: G7Z4T1_AZOL4 
ID   G7Z4T1_AZOL4            Unreviewed;       753 AA.
AC   G7Z4T1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE            EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN   Name=trpEG {ECO:0000313|EMBL:CBS86537.1};
GN   OrderedLocusNames=AZOLI_1217 {ECO:0000313|EMBL:CBS86537.1};
OS   Azospirillum lipoferum (strain 4B).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS86537.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
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         Evidence={ECO:0000256|PIRNR:PIRNR036934};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR036934}.
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DR   EMBL; FQ311868; CBS86537.1; -; Genomic_DNA.
DR   RefSeq; WP_014247558.1; NC_016622.1.
DR   AlphaFoldDB; G7Z4T1; -.
DR   STRING; 862719.AZOLI_1217; -.
DR   MEROPS; C26.959; -.
DR   KEGG; ali:AZOLI_1217; -.
DR   HOGENOM; CLU_006493_3_0_5; -.
DR   OMA; AYRSFMN; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000005667; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01743; GATase1_Anthranilate_Synthase; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 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   NCBIfam; TIGR01815; TrpE-clade3; 1.
DR   NCBIfam; TIGR00566; trpG_papA; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF9; ANTHRANILATE SYNTHASE COMPONENT 1; 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   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00099; CPSGATASE.
DR   PRINTS; PR00096; GATASE.
DR   SUPFAM; SSF56322; ADC synthase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR036934};
KW   Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW   Lyase {ECO:0000256|PIRNR:PIRNR036934, ECO:0000313|EMBL:CBS86537.1};
KW   Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT   DOMAIN          128..211
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          258..514
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   DOMAIN          552..729
FT                   /note="Glutamine amidotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF00117"
FT   ACT_SITE        627
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        716
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT   ACT_SITE        718
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ   SEQUENCE   753 AA;  80731 MW;  1358C9BCF424844A CRC64;
     MTPSHLFPSH IFLADPAFLD PFATTTGGGL EVCRTGEPVG IADALETLAT ALDERRGLLL
     SGGVEAPGRY RRQAMGFVDP PLSVTARGRT VRIDALNPRG RLLLPAIASA LDGHEALAGL
     EVTAGRITAL VRRPTGVFAE EERSRQPSVF SVLRASMALF ACADEPFLGL YGAFGYDLAF
     QFEPIRRRLE RPDDQRDLVL YLPDRLLVVD HGAGVARRFA YEFVVDGTST EGVAGGGRTH
     AYRPDTNAAA GCDHVPGEYQ QAVRAAKEAF RRGDLFEVVP GQTFAEPCAD SPSTVFRRLR
     AANPAPYEAL INLGDGEFLV AASPEMYVRV GTGPMAGRVE TCPISGTVAR GADALGDAAQ
     ILTLLNSAKD AAELTMCTDV DRNDKARVCE PGSVRVVGRR MIELYSRLIH TVDHVEGRLR
     DGFDALDAFL SHSWAVTVTG APKRWAMQFL EDTERSPRRW YGGAFGRIGF DGGMDTGLTL
     RTIRMKDGVA FVRAGATLLS DSDPEAEDAE CRLKASAFLD AVRGKGASPK LALVAAAASS
     AARRSGEGRR VLLVDHDDSF VHTLADYFRR TGAMVTTLRH GHARAALRDD PPDLLVLSPG
     PGRPEDFDVG GSVRTALELG VPVFGVCLGL QGMAESFGAT LDRLPEPMHG KASSLIHQGC
     GLFEGLPQGM RVGRYHSLVA KRDSLPPDLR VTAETEDGTV MAIEHRTLPL AAVQFHPESI
     LTLDGGHGLA LIDTVMATLA TRGGRLPERE EAA
//
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