ID V4XBL9_9ARCH Unreviewed; 520 AA.
AC V4XBL9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A07HB70_02336 {ECO:0000313|EMBL:ESS05294.1};
OS uncultured archaeon A07HB70.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412872 {ECO:0000313|EMBL:ESS05294.1, ECO:0000313|Proteomes:UP000030648};
RN [1] {ECO:0000313|Proteomes:UP000030648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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; KI543184; ESS05294.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XBL9; -.
DR STRING; 1412872.A07HB70_02336; -.
DR PATRIC; fig|1412872.3.peg.2457; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000030648; 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|RuleBase:RU364045};
KW Aromatic amino acid biosynthesis {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:UP000030648};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 32..192
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 245..500
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 520 AA; 55129 MW; 67775110C807B805 CRC64;
MTDLDLDREA FRDHAAADGP VVVRVTAPLP AVSPLAAYAA LVGDADHGFL LESAEKTAGS
DPDGAFQPGT DPDRHARYSF VGYDPEAVVT VTGDDRRVTD LGGSAAGLVD PTAEGDVLDA
LRGALPDVAR ANFAAGDRQR LDGGLVGFLA YDAVYDLWLD EVGVERPDPV CPDAEFVLAT
SVVAVDHADD DVELVLTPVV RPDDDPDETY DALAAEAARV ADRLAAAGEP SPGGFVREGE
RAGPRDEYEA AVRRAKEHVL DGDIYQGVIS RSRVLEGEMD PLGLYAALRT VNPSPYMYLL
RHGDRSVVGA SPETLVSVRG DRVTVNPIAG TCPRGTGPVD DRRLAGEMLA DGKERAEHTM
LVDLGRNDVR RVSEAGSVEV DEFMSVIKYS HVQHIESTVT GRLGPTDDAF DATRATFPAG
TLTGAPKVRA MELVDALETS PRGVYGGGVG YFSWDGDADF AIVIRSATVD HATRETTVRA
GAGVVADSDP ASEYEETEAK MGGVLDAVDR VERTAEEATR
//
