ID   B8CLN0_SHEPW            Unreviewed;       523 AA.
AC   B8CLN0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   04-NOV-2026, entry version 86.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|PIRNR:PIRNR001373};
DE            EC=4.1.3.27 {ECO:0000256|PIRNR:PIRNR001373};
GN   OrderedLocusNames=swp_1923 {ECO:0000313|EMBL:ACJ28681.1};
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849 {ECO:0000313|EMBL:ACJ28681.1, ECO:0000313|Proteomes:UP000000753};
RN   [1] {ECO:0000313|EMBL:ACJ28681.1, ECO:0000313|Proteomes:UP000000753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877 {ECO:0000313|Proteomes:UP000000753};
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chorismate + L-glutamine = anthranilate + pyruvate + L-
CC         glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=4.1.3.27;
CC         Evidence={ECO:0000256|ARBA:ARBA00047683,
CC         ECO:0000256|PIRNR:PIRNR001373};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001373-2};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|PIRSR:PIRSR001373-2};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|PIRNR:PIRNR001373}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000256|ARBA:ARBA00009562, ECO:0000256|PIRNR:PIRNR001373}.
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DR   EMBL; CP000472; ACJ28681.1; -; Genomic_DNA.
DR   RefSeq; WP_020912056.1; NC_011566.1.
DR   AlphaFoldDB; B8CLN0; -.
DR   STRING; 225849.swp_1923; -.
DR   KEGG; swp:swp_1923; -.
DR   eggNOG; COG0147; Bacteria.
DR   HOGENOM; CLU_006493_9_4_6; -.
DR   OMA; AADDMGP; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000000753; Chromosome.
DR   GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 1.
DR   InterPro; IPR005801; ADC_synthase.
DR   InterPro; IPR015890; Anth_synth-like_dom.
DR   InterPro; IPR019999; Anth_synth_I-like.
DR   InterPro; IPR005257; Anth_synth_I_TrpE.
DR   NCBIfam; NF010079; PRK13564.1; 1.
DR   NCBIfam; TIGR00565; trpE_proteo; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF49; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PIRSF; PIRSF001373; TrpE; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW   ECO:0000256|PIRSR:PIRSR001373-1};
KW   Aromatic amino acid biosynthesis {ECO:0000256|PIRNR:PIRNR001373};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001373};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR001373-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001373-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000753};
KW   Tryptophan biosynthesis {ECO:0000256|PIRNR:PIRNR001373,
KW   ECO:0000256|PIRSR:PIRSR001373-1}.
FT   DOMAIN          113..514
FT                   /note="Anthranilate synthase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   BINDING         41
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         298..300
FT                   /ligand="L-tryptophan"
FT                   /ligand_id="ChEBI:CHEBI:57912"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         335..336
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
FT   BINDING         456
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         476
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         490..492
FT                   /ligand="chorismate"
FT                   /ligand_id="ChEBI:CHEBI:29748"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-1"
FT   BINDING         505
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001373-2"
SQ   SEQUENCE   523 AA;  57454 MW;  B40DB56545B0ED9F CRC64;
     MAVKDIATVV TNKQSLAYHD DPLRLYQHVT NDAPHTMLLE SAEIESKDHL KSIILTHAAM
     MIRCDGYQLT FTAFTDNGQT LLTPIKAFFT EHYAAVEIDQ ASTTALTVKL CKDSTQLDED
     ARLKATSPLD GLRMLVQHIR CNDTPAFEDL FLGGVLSYDL IDTVEPLPSV PEGDNNCPDY
     LFYLAETLIL VDHQQQSADI ITHQFAAANT VIANTLAARM DELQQSCTSL TAIAELKTID
     ADTQVNISDS EFKQTVNDLK QHIIAGDIFQ VVPSRSFSLP CPNTLGAYRA LRLTNPSPYM
     FYFRGEGFTL FGASPESALK YEASTNQVEI YPIAGTRKRG KTANGEIDFD LDSRNELELR
     LDKKELSEHI MLVDLARNDV ARISQSGTRK VPELLKVDRY SHVMHLVSRV TGQLRTDLDA
     LHAYQACMNM GTLTGAPKVS AEQLIRSAEK TRRGSYGGAV GYLNGLGDMD TCIVIRSAFV
     KDGTAFIQAG AGVVFDSDPQ AEADETRQKA QAVISAIKMG GGL
//