ID   TRPE_NEIG1              Reviewed;         491 AA.
AC   Q5F8B4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Anthranilate synthase component 1;
DE            Short=AS;
DE            Short=ASI;
DE            EC=4.1.3.27;
GN   Name=trpE; OrderedLocusNames=NGO0872;
OS   Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=242231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10417653; DOI=10.1046/j.1365-2958.1999.01514.x;
RA   Zhu P., Morelli G., Achtman M.;
RT   "The opcA and (psi)opcB regions in Neisseria: genes, pseudogenes,
RT   deletions, insertion elements and DNA islands.";
RL   Mol. Microbiol. 33:635-650(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700825 / FA 1090;
RA   Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA   Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA   Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA   Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT   "The complete genome sequence of Neisseria gonorrhoeae.";
RL   Submitted (MAR-2003) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ242839; CAB45014.1; -; Genomic_DNA.
DR   EMBL; AE004969; AAW89573.1; -; Genomic_DNA.
DR   RefSeq; WP_010360232.1; NC_002946.2.
DR   RefSeq; YP_207985.1; NC_002946.2.
DR   AlphaFoldDB; Q5F8B4; -.
DR   SMR; Q5F8B4; -.
DR   STRING; 242231.NGO_0872; -.
DR   PRIDE; Q5F8B4; -.
DR   EnsemblBacteria; AAW89573; AAW89573; NGO_0872.
DR   GeneID; 66753206; -.
DR   KEGG; ngo:NGO_0872; -.
DR   PATRIC; fig|242231.10.peg.1028; -.
DR   HOGENOM; CLU_006493_9_3_4; -.
DR   OMA; GCVGYLD; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000000535; Chromosome.
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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..491
FT                   /note="Anthranilate synthase component 1"
FT                   /id="PRO_0000154101"
FT   BINDING         49
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         271..273
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         306..307
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         333
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         421
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         441
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         455..457
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         457
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
FT   BINDING         470
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00897"
SQ   SEQUENCE   491 AA;  54748 MW;  A810F7B2304FE47F CRC64;
     MISKQEYQAQ AAQGYNRIPL VQELLADLDT PLSLYLKLAN RPYTYLLESV VGGERFGRYS
     FIGLPCSHYL KAGGKHVDVY QNGEIVEQYD GNPLPFIEAF HNRFKTPEIP SLPRFTGGLV
     GYFGYETVYN FEHFAHRLKN TAKANPLGTP DILLMLSQEL AVIDNLSGKI HLIVYADPSQ
     PDSYERARER LEDIRTQLRQ SCAIPLSLGS KQTQAVSEFG EEPFKACVDK IKDYIFAGDC
     MQVVPSQRMS MEFTDNPLAL YRALRTLNPS PYLFYYDFGD FHIVGSSPEI LVRRERDDVI
     VRPIAGTRLR GKTPAEDLAN EQDLLSDAKE IAEHVMLIDL GRNDVGRISK TGEVKVTDKM
     VIEKYSHVMH IVSNVEGCLK EGVTNMDILA ATFPAGTLSG APKVRAMEII EEIEPEKRGI
     YGGAVGVWGF NNDMDLAIAI RTAVIKNNTL FIQSGAGVVA DSDPTSEWQE TQNKARAVVR
     AAQMVQEGLD K