ID A0A238UR32_HALVU Unreviewed; 551 AA.
AC A0A238UR32;
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|RuleBase:RU364045};
DE EC=4.1.3.27 {ECO:0000256|RuleBase:RU364045};
GN Name=trpE {ECO:0000256|RuleBase:RU364045};
GN ORFNames=SAMN06264855_101256 {ECO:0000313|EMBL:SNR24374.1};
OS Halorubrum vacuolatum (Natronobacterium vacuolatum).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=63740 {ECO:0000313|EMBL:SNR24374.1, ECO:0000313|Proteomes:UP000198397};
RN [1] {ECO:0000313|EMBL:SNR24374.1, ECO:0000313|Proteomes:UP000198397}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8800 {ECO:0000313|EMBL:SNR24374.1,
RC ECO:0000313|Proteomes:UP000198397};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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|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; FZNQ01000001; SNR24374.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238UR32; -.
DR OrthoDB; 25514at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000198397; 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; IPR010116; Anthranilate_synth_I_arc_typ.
DR InterPro; IPR015890; Chorismate_C.
DR NCBIfam; TIGR01820; TrpE-arch; 1.
DR PANTHER; PTHR11236; AMINOBENZOATE/ANTHRANILATE SYNTHASE; 1.
DR PANTHER; PTHR11236:SF9; 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|RuleBase:RU364045};
KW Metal-binding {ECO:0000256|RuleBase:RU364045};
KW Reference proteome {ECO:0000313|Proteomes:UP000198397};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 31..195
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 248..508
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 518..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 59255 MW; D9C1D39415A1363D CRC64;
MLDRSREAFI ELVSDADRPV VARVAASLDA DVTPLSTYAT LVGDGPYGFL LESGEKVASS
DPDGAFSAGG KADRHARYSF VGYDPEAIVS IHPDRTDVER LGPAADRIEA AGLGPEAGDV
IDRIRAAFPE VTRRGFPETD RQILSGGFVG FLAYEAVYDL WLEEVGVERP ETTFPDAEFA
LTTRTVVFDD VEGSVELVFT PIIDIDDDAG AVYDSLLAEA ERVAEALAGA TAPETGGVRE
TDSTAGAQET YEEAVRRAKR HVLDGDIYQG VISRSREVRG EVDPLGLYAA LREVNPSPYM
YVLRHADRTI VGASPETLVS VTGDRIVSNP IAGTCPRGES PVEDRRLAGE MLADGKERAE
HTMLVDLARN DVRRVSKPGS VRVEEFMNVL KYSHVQHIES TVTGTVATEY DAFDATRAAF
PAGTLTGAPK VRAMEIINDL EETPREAYGG GVGYYSWTGD ADFAIVIRTA TIRGSESDPD
ESVVTVRAGA GLVADSDPTA EYEETEQKMN GVLAAIDAIR EGDDHDREGD DHDRGSDMVD
DGVTAGTEAP R
//
