ID A0A0K1XDM4_9GAMM Unreviewed; 492 AA.
AC A0A0K1XDM4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=AKN88_04500 {ECO:0000313|EMBL:AKX59278.1};
OS Thiopseudomonas alkaliphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Thiopseudomonas.
OX NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX59278.1, ECO:0000313|Proteomes:UP000063953};
RN [1] {ECO:0000313|EMBL:AKX59278.1, ECO:0000313|Proteomes:UP000063953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E5571 {ECO:0000313|EMBL:AKX59278.1,
RC ECO:0000313|Proteomes:UP000063953};
RX PubMed=26679585;
RA Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA Juieng P., Loparev V., McQuiston J.R.;
RT "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT a Novel Bacterium of the Pseudomonadaceae Family.";
RL Genome Announc. 3:e01474-15(2015).
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; CP012365; AKX59278.1; -; Genomic_DNA.
DR RefSeq; WP_053100443.1; NZ_CP012365.1.
DR AlphaFoldDB; A0A0K1XDM4; -.
DR STRING; 1697053.AKN87_06495; -.
DR PATRIC; fig|1698449.3.peg.902; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000063953; 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; 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; ISOCHORISMATE SYNTHASE MENF; 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:UP000063953};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 27..169
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 223..476
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 492 AA; 54251 MW; 9C113C1A1D39691A CRC64;
MNFEEFQCLA EQGYNRIPVS RETLADFDTP LSIYLKLADV PNSYLLESVQ GGEKWGRYSI
IGLAAKTVLS ARGELVEIHH QGELIESCET TDPLAFVEDF QARYQVPHIA GLPRFNGGLV
GYFGYDCVRY VQPKLGPAPS QDTLQNPDIL LLVSEAVVVF DNLAGKLHLI VLADPEQDDA
YQQAQLQLDQ LMEQLRQPIT PRPGLNPQLA NQPEPAFTSS FTQADYLNSV NKIKDYIAAG
DCMQVVISQR MSIPFTAAPI DLYRALRSSN PTPYMYFFNF GDFHVVGSSP EVLVRVEDGL
VTVRPIAGTR PRGATNEEDL ALEQDLLSDK KELSEHLMLI DLGRNDVGQV AQTGSVKVTE
KMIIERYSNV MHIVSNVTGQ IQPQLNAMDA LRSILPAGTL SGAPKVRAME IIDELEPVKR
GVYGGAVGYL AWNGNMDTAI AIRTAVIQDG QLHVQAGAGI VSDSQPQLEW EETLNKRRAM
FKAVALASQP HK
//
