ID   TRPE_ARTGO              Reviewed;         531 AA.
AC   P96556;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Anthranilate synthase component 1;
DE            Short=AS;
DE            Short=ASI;
DE            EC=4.1.3.27;
GN   Name=trpE;
OS   Arthrobacter globiformis.
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=1665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 8010 / DSM 20124 / BCRC 10598 / JCM 1332 / KCTC 9101 / NBRC
RC   12137 / NCIMB 8907 / NRRL B-2979 / 168;
RA   Chernova T., Viswanathan V.K., Austria N., Nichols B.P.;
RL   Submitted (MAR-1997) 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 (By similarity).
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P00897};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00897};
CC   -!- ACTIVITY REGULATION: Feedback inhibited by tryptophan. {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a
CC       beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
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DR   EMBL; U89690; AAB49479.1; -; Genomic_DNA.
DR   AlphaFoldDB; P96556; -.
DR   SMR; P96556; -.
DR   UniPathway; UPA00035; UER00040.
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; -; 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   PANTHER; PTHR11236; PTHR11236; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; SSF56322; 1.
DR   TIGRFAMs; TIGR00564; trpE_most; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Magnesium; Metal-binding; Tryptophan biosynthesis.
FT   CHAIN           1..531
FT                   /note="Anthranilate synthase component 1"
FT                   /id="PRO_0000154075"
FT   REGION          506..531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         56
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         284..286
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         324..325
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         351
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         439
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         459
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         473..475
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         475
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
SQ   SEQUENCE   531 AA;  57369 MW;  AFA71DA7A8A6674C CRC64;
     MQDLGIISPG LEEFRELAAH SRVIPVRLKV LADAETPIGL YRKLAQGQPG TFLMESAAVG
     GAWSRYSFIG SRSRATLTTK DGQAHWLGEP PAGVPVDGNP VDAIRDTIEA LRTDRFDGLP
     PFTSGLVGFL GWETVRHWEK LTRPPEDDLQ LPELALNLVT DMAVHDNMDG TVLLIANAIN
     FDNSSERVDE AWHDAVARVK ELLARISTPV LQPVSVLEPA ALDFAASVQE RWNEPEYLAA
     LDRGKEAIVD GEVFQVVISR RFEMECGASP LDVYRVLRNT NPSPYMYIFS LEDAAGRQYS
     IVGSSPEALV TVTGEDVITH PIAGSRPRGK TVDADKALAE ELLADQKERA EHLMLVDLSR
     NDLSKVCVAG SVDVTQFMEV ERFSHIMHLV STVVGRLAPT AKAYDVLKAT FPAGTLSGAP
     KPRALRLLDE LEPHRRGIYG GVVGYLDFAG DMDMAIAIRS ALLREGRAYV QAGGGIVADS
     SNPAEAQETV NKAAAPLRAV HTAGSLHNIT PDSVSAPDSV SSPDSVTEAN S