ID A0A240UT13_9GAMM Unreviewed; 496 AA.
AC A0A240UT13;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=B9H00_14925 {ECO:0000313|EMBL:ART64182.1}, C8D96_3012
GN {ECO:0000313|EMBL:RKD76637.1};
OS Kushneria marisflavi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Kushneria.
OX NCBI_TaxID=157779 {ECO:0000313|EMBL:ART64182.1, ECO:0000313|Proteomes:UP000194457};
RN [1] {ECO:0000313|EMBL:ART64182.1, ECO:0000313|Proteomes:UP000194457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SW32 {ECO:0000313|EMBL:ART64182.1};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RKD76637.1, ECO:0000313|Proteomes:UP000285584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15357 {ECO:0000313|EMBL:RKD76637.1,
RC ECO:0000313|Proteomes:UP000285584};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (SEP-2018) 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; CP021358; ART64182.1; -; Genomic_DNA.
DR EMBL; RAPM01000006; RKD76637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240UT13; -.
DR KEGG; kma:B9H00_14925; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000194457; Chromosome.
DR Proteomes; UP000285584; 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; 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:UP000194457};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 28..170
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 224..477
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 496 AA; 55355 MW; 267EE9E6EC116CA7 CRC64;
MMTSERFAEL AAEGYNRIPV THEVLADFET PLSTYLKLAD APWSFLLESV TGGEKWGRYS
IIGLPCRERI EVSGFTVRHY VDGYLQGATE VEDPLEWIEQ FRRRFRAPES SEAMRFDGGL
VGYFGYDTIR LIEPRLRGVE KPDPIDVPDI LLMVADELVV FDNLSGRLTL LVHADPGNDN
ALEQAQERLA ALEYQLRHTP ITTASPGTGR NAVAEEDFFA SFSEQGYKDA VARIREYVAA
GDLMQCVPSQ RMTIAYQAPP LDLYRALRSL NPSPYMFFFN LDDHHVVGAS PEILARLDHD
EITLRPIAGT RHRGANEEED RALEQELLGD PKEIAEHVML IDLGRNDVGR ISEPGSVELT
DRMTIERYSH VMHIVSNVTG RIKPSLGPMD VLRATFPAGT LSGAPKVRAL EVIDELEPVK
RGIYSGAVGY LSWQGNMDMA IAIRTAVIKN GELHVQAGGG IVSDSDPDNE WQETLNKRRA
MFRAVAMAER GLDNLE
//
