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
//