ID   TRPE3_HALMA             Reviewed;         503 AA.
AC   Q5V631;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Anthranilate synthase component 1 3;
DE            EC=4.1.3.27;
DE   AltName: Full=Anthranilate synthase component I 3;
GN   Name=trpE3; OrderedLocusNames=pNG7327;
OS   Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS   B-1809) (Halobacterium marismortui).
OG   Plasmid pNG700.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Haloarcula.
OX   NCBI_TaxID=272569;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX   PubMed=15520287; DOI=10.1101/gr.2700304;
RA   Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA   Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA   Hood L., Ng W.V.;
RT   "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT   Dead Sea.";
RL   Genome Res. 14:2221-2234(2004).
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   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5.
CC   -!- SUBUNIT: Tetramer of two components I and two components II.
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Component I catalyzes the formation of anthranilate
CC       using ammonia rather than glutamine, whereas component II provides
CC       glutamine amidotransferase activity.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAV45021.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY596296; AAV45021.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_049938601.1; NZ_CP039137.1.
DR   AlphaFoldDB; Q5V631; -.
DR   SMR; Q5V631; -.
DR   EnsemblBacteria; AAV45021; AAV45021; pNG7327.
DR   GeneID; 40151225; -.
DR   KEGG; hma:pNG7327; -.
DR   PATRIC; fig|272569.17.peg.753; -.
DR   HOGENOM; CLU_006493_9_3_2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000001169; Plasmid pNG700.
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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Magnesium; Metal-binding; Plasmid; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           1..503
FT                   /note="Anthranilate synthase component 1 3"
FT                   /id="PRO_0000154124"
FT   BINDING         269..271
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         304..305
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         331
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         419
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
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         453..455
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         455
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         468
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
SQ   SEQUENCE   503 AA;  55112 MW;  93B3EBE2B2A9AE12 CRC64;
     MTEIRFSTDK ESFIETARAA ADGTRVPVEA RVTVADPFEA YRRARDENTD GFYLETTGGQ
     SGWGYFGIEP IERVEVSAGA TPAQDGGSPS LEAIDDLLDR EHLERGDCTV PYPCGAFGWL
     SYDVARELED IPETTVSDGL PRLQFGVFDC IAAWEEPHDG NVEIHVTACP TVDGSPESAF
     ERGRTMAREL AQDAIHGEKH VQSQPTAASQ ATFESECGEA AFADRVRQIK QYVRDGDTFQ
     TNVSHRLTAP AAVHPVDTFD AVRRVNPAPY SALLEFPGVD LVSASPELLL DVDGDQLLTE
     PIAGTRPRGA TPSEDEDLEV DLCSDEKERA EHAMLVDLER NDLGKVSEYG SVDVAEYRRV
     DRYSEVMHLV SLIEGELRDA VSIADAVAAV FPGGTITGAP KPRTMEIIDE VERTRRGPYT
     GSIGMFGFDD RATLNITIRT LVHYDDEYRL RVGSGIVHDS VPEAEYRETL DKARALVTAV
     DEALGEQGSF AVESETEPME GMR