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Database: UniProt
Entry: A0A176QBS0_9MICO
LinkDB: A0A176QBS0_9MICO
Original site: A0A176QBS0_9MICO 
ID   A0A176QBS0_9MICO        Unreviewed;       525 AA.
AC   A0A176QBS0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653, ECO:0000256|RuleBase:RU364045};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266, ECO:0000256|RuleBase:RU364045};
GN   Name=trpE {ECO:0000256|RuleBase:RU364045};
GN   ORFNames=AWH69_12590 {ECO:0000313|EMBL:OAB87182.1};
OS   Janibacter melonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=262209 {ECO:0000313|EMBL:OAB87182.1, ECO:0000313|Proteomes:UP000076976};
RN   [1] {ECO:0000313|EMBL:OAB87182.1, ECO:0000313|Proteomes:UP000076976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD11-4 {ECO:0000313|EMBL:OAB87182.1,
RC   ECO:0000313|Proteomes:UP000076976};
RA   Nair G.R., Kaur G., Chander A.M., Mayilraj S.;
RT   "Janibacter melonis strain CD11_4 genome sequencing and assembly.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the two-
CC       step biosynthesis of anthranilate, an intermediate in the biosynthesis
CC       of L-tryptophan. In the first step, the glutamine-binding beta subunit
CC       (TrpG) of anthranilate synthase (AS) provides the glutamine
CC       amidotransferase activity which generates ammonia as a substrate that,
CC       along with chorismate, is used in the second step, catalyzed by the
CC       large alpha subunit of AS (TrpE) to produce anthranilate. In the
CC       absence of TrpG, TrpE can synthesize anthranilate directly from
CC       chorismate and high concentrations of ammonia.
CC       {ECO:0000256|ARBA:ARBA00025634, ECO:0000256|RuleBase:RU364045}.
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|ARBA:ARBA00000329,
CC         ECO:0000256|RuleBase:RU364045};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU364045};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873,
CC       ECO:0000256|RuleBase:RU364045}.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC       beta subunit (TrpG) and a large alpha subunit (TrpE).
CC       {ECO:0000256|ARBA:ARBA00011575, ECO:0000256|RuleBase:RU364045}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|RuleBase:RU364045}.
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:OAB87182.1}.
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DR   EMBL; LQZG01000003; OAB87182.1; -; Genomic_DNA.
DR   RefSeq; WP_068276135.1; NZ_LQZG01000003.1.
DR   AlphaFoldDB; A0A176QBS0; -.
DR   STRING; 262209.AWH69_12590; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000076976; Unassembled WGS sequence.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR005256; Anth_synth_I_PabB.
DR   InterPro; IPR015890; Chorismate_C.
DR   NCBIfam; TIGR00564; trpE_most; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU364045};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU364045};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU364045};
KW   Magnesium {ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|RuleBase:RU364045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076976};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          38..177
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          240..497
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   525 AA;  56426 MW;  66F6EF52EB4FD0E0 CRC64;
     MTALPELGYG RTWPDADTFG VLARDRRVIP VVRRLMADAE TPLSVYRKLA KGEPGTFLLE
     SAEQGVWSRW SIIGARSRAT LTERDGEALW IGEPPAGVPT TGSPVEVLRA TLEALRTEPV
     EGLPPLTSGM VGAISYDAVR RWERVPATLP DVLGVPEVGM VLATDVAVLD HSDGSLLLIA
     NAINYDDTDE RVDQAYDDAV TRLDEMVLAL AEPAPSTVAT VDPDVVADAM ASVTSDVTPE
     RYQEIVEEAK EDIRAGEVFQ VVLSQRFSMD CPADPTEVYR ALRAANPSPY MYFFRLPRAD
     GSTYDVVGGS PEALVTVTGR EALTHPIAGT RPRGKTLEED IALAEELLAD PKERSEHVML
     VDLGRNDLQR VCEAGTVDCL ELMDVRRYSH VTHLESTVVG RMRPEVSAYD VLVSTFPAGT
     LSGAPKPRAL ALIEHYERSR RGVYGGVVGY LDFHGDMDMA IAIRTALVVD GRAHVQAGAG
     IVADSVPHLE HAECVAKAGA ALRAVATAGA MRTVGPARPS DGGTA
//
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