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Database: UniProt
Entry: A0A0U1NH11_9RHOB
LinkDB: A0A0U1NH11_9RHOB
Original site: A0A0U1NH11_9RHOB 
ID   A0A0U1NH11_9RHOB        Unreviewed;       502 AA.
AC   A0A0U1NH11;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
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   ECO:0000313|EMBL:CRK74030.1};
GN   ORFNames=NIG5292_00053 {ECO:0000313|EMBL:CRK74030.1};
OS   Nereida ignava.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Nereida.
OX   NCBI_TaxID=282199 {ECO:0000313|EMBL:CRK74030.1, ECO:0000313|Proteomes:UP000048949};
RN   [1] {ECO:0000313|EMBL:CRK74030.1, ECO:0000313|Proteomes:UP000048949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5292 {ECO:0000313|EMBL:CRK74030.1,
RC   ECO:0000313|Proteomes:UP000048949};
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) 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|RuleBase:RU364045}.
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         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; CVQV01000002; CRK74030.1; -; Genomic_DNA.
DR   RefSeq; WP_048597347.1; NZ_CVQV01000002.1.
DR   AlphaFoldDB; A0A0U1NH11; -.
DR   STRING; 282199.GCA_001049735_00053; -.
DR   OrthoDB; 9803598at2; -.
DR   UniPathway; UPA00035; UER00040.
DR   Proteomes; UP000048949; Unassembled WGS sequence.
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; Anthranilate synthase; 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   NCBIfam; TIGR00564; trpE_most; 1.
DR   PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR   PANTHER; PTHR11236:SF48; 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   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:UP000048949};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU364045}.
FT   DOMAIN          29..173
FT                   /note="Anthranilate synthase component I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04715"
FT   DOMAIN          230..483
FT                   /note="Chorismate-utilising enzyme C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00425"
SQ   SEQUENCE   502 AA;  54792 MW;  CEDD9BDC250E0B5F CRC64;
     MTLTPSYDDF AAQFEAGKNQ LVYTRLAADL DTPVSLMLKL GGAQTNSFML ESVTGGEVRG
     RYSIIGMKPD LIWRCTDQKA AINREARFDD DAFMAEVDDP LTSLRALIAA SKIDLPDDLP
     AACAGLFGYL GYDMIRLVEN LPNINPDPLN VPDAIMLRPS VVAVLDGVKG EVILVSPAWV
     SSGLSARAAY AQAAERVQDA LRDLDRALPA DTRQMRDQPA PANAVSNFAK DDYKAAVETA
     KDYIRAGDIF QCVPSQRWTQ DFKEPPFALY RSLRRTNPSP FMFFFNHGDF QIVGASPEIL
     VRVFDDEVTI RPIAGTRPRG ATPAEDQANE DDLLADQKEL AEHLMLLDLG RNDVGRVSQI
     GTVRPTEEFI VERYSHVMHI VSNVVGKLAP EHDALSAFFA GMPAGTVSGA PKVRAMEIID
     ELEPEKRGIY GGGLGYFSAG GDMDMCIALR TAVIKDQKLY IQAGGGVVYD SDPEFEYQET
     VHKSNAIRKA AADAARFGSG NS
//
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