ID A0A098G3W1_9GAMM Unreviewed; 712 AA.
AC A0A098G3W1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN Name=trpE(G {ECO:0000313|EMBL:CEG57167.1};
GN ORFNames=LFA_1768 {ECO:0000313|EMBL:CEG57167.1};
OS Legionella fallonii LLAP-10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG57167.1, ECO:0000313|Proteomes:UP000032430};
RN [1] {ECO:0000313|Proteomes:UP000032430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA Gomez-Valero L.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; LN614827; CEG57167.1; -; Genomic_DNA.
DR RefSeq; WP_045095717.1; NZ_LN614827.1.
DR AlphaFoldDB; A0A098G3W1; -.
DR STRING; 1212491.LFA_1768; -.
DR KEGG; lfa:LFA_1768; -.
DR HOGENOM; CLU_006493_3_0_6; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000032430; 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; 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:CEG57167.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032430};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 120..199
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 239..491
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 523..695
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 598
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 690
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 712 AA; 80437 MW; 7A16C61B40B2AFFE CRC64;
MLQQYKTQGG VHVESSQESL DYHQGIKFLI ESIDSQRGAI FASSFEYPGR YTCWDLGFYN
PPLAIICKQD LISLEALNQR GEVLLAFIYP LLASQNNLEL LLHTNVLCQV KMKPSQQVFS
EEERSQQPSV FSIIRLLLAF FKSEEDSHLG LYGAFGFDLI YQFEQLEQCK ERDPKQRDMV
LYLPDEIFIV NHRKEEAYVR RYDFQYQGKS TQSLAREGVY LPYQAINQPD KSGDHELGEY
ANVVNKAKER FACGDLFEVV PSQTFYSHYT EQPSALFSKM RRINPSPYGF FINLGNEEYL
IGASPEMYVR VQGKRVETCP ISGTIKRGDD AIEDALNIQA LLDSPKEESE LTMCTDVDRN
DKSRICEAGS VKVIGRRQIE MYSRLIHTVD HVEGILRDGF DSVDAFLTHM WVVTVTGAPK
LWAMNFIEQH EKSPRKWYAG AVGWFGFDGN LNTGLVLRTV RIEKGVAELR VGATLLYDSI
PEAEEQETRL KASAFLDMLQ NVEIKNKKET ESLPLTGKGK RVLLIDHQDS FVHTLANYIR
QTGAEVSTIR FDKALSYLKE SHYDLVVLSP GPGKPSDFKL SEAIDEIINR GIPLFGVCLG
LQGIVEYFGG VLDVLNYPMH GKASIMKISD SDGLFSGLGE TFRAGRYHSL YARLKTVPKE
LTVTAMSEDG IVMAVSHQNL PIHAVQFHPE TILSLPNQAG MKIITNLMGM IK
//
