ID A0A0S8GVM8_9BACT Unreviewed; 711 AA.
AC A0A0S8GVM8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Anthranilate synthase {ECO:0000256|PIRNR:PIRNR036934};
DE EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR036934};
GN ORFNames=AMJ79_05705 {ECO:0000313|EMBL:KPK76705.1};
OS Phycisphaerae bacterium SM23_30.
OC Bacteria; Planctomycetota; Phycisphaerae.
OX NCBI_TaxID=1703411 {ECO:0000313|EMBL:KPK76705.1, ECO:0000313|Proteomes:UP000051901};
RN [1] {ECO:0000313|EMBL:KPK76705.1, ECO:0000313|Proteomes:UP000051901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_30 {ECO:0000313|EMBL:KPK76705.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPK76705.1}.
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DR EMBL; LJUC01000060; KPK76705.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8GVM8; -.
DR STRING; 1703411.AMJ79_05705; -.
DR PATRIC; fig|1703411.3.peg.3173; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000051901; Unassembled WGS sequence.
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};
KW Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR036934}.
FT DOMAIN 28..196
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 239..490
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT DOMAIN 522..697
FT /note="Glutamine amidotransferase"
FT /evidence="ECO:0000259|Pfam:PF00117"
FT ACT_SITE 597
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 686
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 688
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
SQ SEQUENCE 711 AA; 79934 MW; 238BF19E92E23549 CRC64;
MREEFITKGK IKVIRDKDEV AITEALAHVY KHIDRAKGCI FASDYEYPGR YSRWDIGFID
PPLELVSRGR KFTIRALNER GKVILALLAP AVTNHQDVAR LEVTAETIEA EVIPMPSDFT
EEQRSKQPSI FSVLRAICDL MACEDEYLTI FGAFGYDLVF QFEPIRFKHD RRKTGVDCHL
FLADRVGAID HQKKQAFTLS YEFSGPAGST EGIPVQGERR ELTRRLTSTD VICDHEPGEY
AAKVEKIRQG CKRGDFFEVV LSQTFSVKCG YWPSEIFGRL RRQNPSPYDF VINLGDEQLI
GASPEMFVRV DDKVVETCPI SGTVRRGENP MEDAEQIRLL LTSKKDESEL TMCTDVDRND
KSRICVPGSV QLIGRRMVES YSRLFHTVDH VRGALRDDCD MFDAFLSHMW ACTLTGSPKP
IAMQTIEDLE NSPRRWYGGS IGFFTFNRQL NTGITIRTVH LRDGLASVRA GATLLYDSIP
DEEEKETRIK ASAFLQAVTT DEYAPPEDAV SMAKAKKETT VLLVDNHDSF VHTLANYVRQ
TGVEVITLRT GFHESKLDEI KPNLVFISPG PKMPQEMGVL KVVDSALKRN LPIFGVCLGH
QGIGQYFGAE LGILKEPVHG KDSMVHHDEK GIFKNIPNPF SAGRYHSIFV KPDTVPDCLE
ITARTEEGVV MGLAHKELPV ASVQFHPESI LTLQDDMGLK IIANVIELLA R
//
