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Database: UniProt
Entry: D6KAP0_9ACTN
LinkDB: D6KAP0_9ACTN
Original site: D6KAP0_9ACTN 
ID   D6KAP0_9ACTN            Unreviewed;       350 AA.
AC   D6KAP0;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Anthranilate synthase component 1 {ECO:0000256|ARBA:ARBA00020653};
DE            EC=4.1.3.27 {ECO:0000256|ARBA:ARBA00012266};
DE   Flags: Fragment;
GN   ORFNames=SSTG_00808 {ECO:0000313|EMBL:EFF90490.2};
OS   Streptomyces sp. e14.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=645465 {ECO:0000313|EMBL:EFF90490.2, ECO:0000313|Proteomes:UP000004704};
RN   [1] {ECO:0000313|EMBL:EFF90490.2, ECO:0000313|Proteomes:UP000004704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=e14 {ECO:0000313|Proteomes:UP000004704};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces sp. strain e14.";
RL   Submitted (OCT-2009) 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}.
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         Evidence={ECO:0000256|ARBA:ARBA00000329};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 1/5. {ECO:0000256|ARBA:ARBA00004873}.
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}.
CC   -!- SIMILARITY: Belongs to the anthranilate synthase component I family.
CC       {ECO:0000256|ARBA:ARBA00009562}.
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DR   EMBL; GG753626; EFF90490.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6KAP0; -.
DR   STRING; 645465.SSTG_00808; -.
DR   eggNOG; COG0147; Bacteria.
DR   Proteomes; UP000004704; Unassembled WGS sequence.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.60.120.10; Anthranilate synthase; 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; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF46; ANTHRANILATE SYNTHASE COMPONENT 1; 1.
DR   Pfam; PF04715; Anth_synt_I_N; 1.
DR   Pfam; PF00425; Chorismate_bind; 1.
DR   PRINTS; PR00095; ANTSNTHASEI.
DR   SUPFAM; SSF56322; ADC synthase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004704}.
FT   DOMAIN          17..160
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          220..350
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
FT   NON_TER         350
FT                   /evidence="ECO:0000313|EMBL:EFF90490.2"
SQ   SEQUENCE   350 AA;  38040 MW;  2D819710751A63E5 CRC64;
     MATDRRVIPV TRKLLADGDT PVALYRKLAA ERPGTFLLES AENGRTWSRY SFVGVRSAAT
     LTEKDGRAHW QGAPPVGVPV EGDPLAALRA TVEALHTPRD LAHDLGLPPF TGGMVGYLGY
     DIVRRLEKIG PGDRDDLKLP ELTMLLTSDL AVLDHWDGTV LLIANAINHN DLDTGVDEAY
     ADAVARLDAM EADLSRAVPQ PPAALPPSEL PEYTARWGGA DFKAAVEDIK ERIRAGEAFQ
     VVPSQRFETP CTASALDVYR VLRATNPSPY MYLLRFDGFD VVGSSPEALV KVEDGRAMVH
     PIAGTRPRGA TPQRDQALAE ELLADPKERA EHLMLVDLGR NDLGRVCEPG
//
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