ID   B8GCG2_CHLAD            Unreviewed;       503 AA.
AC   B8GCG2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   02-SEP-2026, entry version 72.
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   OrderedLocusNames=Cagg_2120 {ECO:0000313|EMBL:ACL25006.1};
OS   Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Chloroflexineae; Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=326427 {ECO:0000313|EMBL:ACL25006.1, ECO:0000313|Proteomes:UP000002508};
RN   [1] {ECO:0000313|EMBL:ACL25006.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 9485 {ECO:0000313|EMBL:ACL25006.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D., Richardson P.;
RT   "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL   Submitted (DEC-2008) 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 + 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|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}.
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DR   EMBL; CP001337; ACL25006.1; -; Genomic_DNA.
DR   RefSeq; WP_015940864.1; NC_011831.1.
DR   AlphaFoldDB; B8GCG2; -.
DR   STRING; 326427.Cagg_2120; -.
DR   KEGG; cag:Cagg_2120; -.
DR   eggNOG; COG0147; Bacteria.
DR   HOGENOM; CLU_006493_9_3_0; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000002508; 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; IPR005256; Anth_synth_I_PabB.
DR   NCBIfam; TIGR00564; trpE_most; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF48; ISOCHORISMATE SYNTHASE MENF; 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|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364045};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002508};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          91..490
FT                   /note="Anthranilate synthase-like"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   503 AA;  55867 MW;  1FD5B333436470B9 CRC64;
     MYYPTLDQMY ELRRQGNLCP IYREIMADLE TPVSAYLKIA QNGLGFLLES VTGGQNIGRY
     SFIGSDPYMV LRMHDGVAQA THGGYKQTLS YSDPLIVLES YLNAYRPIRL PNLPIFVGGA
     VGYLSYEAAR YFERLPVPSV RPYDMPDSWW MFVDTLLAFD HVRHKMIVIS HVHLDVEDLA
     AEYQRAVTRI ETLIARLQKP LPPTIGFSLR NYEPHSTPAR TVPNPVVSNR TEAEFKAAVL
     RAKEYIMAGD IFQVQISQRF SKATSADSFT IYRALRTINP SPYMFYIRTG EGDLVGASPE
     MLVQVRDGNV TTRPIAGTRW RGRDAAEDER LAAELLADEK ERAEHLMLVD LGRNDIGRIS
     EPGTVHVPVF MTIEKYSHVQ HIVSEVVGKL RADLKSIDAL RACFPAGTVT GAPKIRSMEI
     IAELEGEQRG IYAGAVGHLG FNGDLDTCIA LRTLIVKDGV AYAQAAAGVV ADSTPEYEFN
     ESCNKAAASL RAIDLAEELQ AGL
//