ID U1PNW6_9EURY Unreviewed; 597 AA.
AC U1PNW6;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=J07HQW2_01863 {ECO:0000313|EMBL:ERG95407.1};
OS Haloquadratum walsbyi J07HQW2.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=1238425 {ECO:0000313|EMBL:ERG95407.1, ECO:0000313|Proteomes:UP000030710};
RN [1] {ECO:0000313|EMBL:ERG95407.1, ECO:0000313|Proteomes:UP000030710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J07HQW2 {ECO:0000313|Proteomes:UP000030710};
RX PubMed=23637883;
RA Podell S., Ugalde J.A., Narasingarao P., Banfield J.F., Heidelberg K.B.,
RA Allen E.E.;
RT "Assembly-driven community genomics of a hypersaline microbial ecosystem.";
RL PLoS ONE 8:E61692-E61692(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; KE356561; ERG95407.1; -; Genomic_DNA.
DR AlphaFoldDB; U1PNW6; -.
DR STRING; 1238425.J07HQW2_01863; -.
DR eggNOG; arCOG02014; Archaea.
DR HOGENOM; CLU_006493_9_0_2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000030710; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 39..212
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 265..537
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 554..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 64553 MW; B37F848A5FA67EE0 CRC64;
MSDSTPLSKS RSAFIAEITN KLESTSEPLI AHVAASLPTV TPLTAYAALV ARSDYGFLLE
SAEKTPSSDP DGAFAPDHVT ADRHARFSFV GYDPDAVITI SPDEFECTTL GGRAAKYVTT
SDTNLDNSDN NTSGDDVLDN LRTAMPTFPR VGFPDDDRHR LRGGLVGFLA YEAVYDIWLN
EVGVDRPDTQ TPDAEFVLTT KTLSIDHADR SVSLVLTPII APDDDLDVIY DELVAEAIDI
QETLESAAPP DPDGFLQTNS AAGSQTDYET AVHTAKQRVL DGDIYQGVIS RVREQYGDID
PLGLYASLRE VNPSPYMYLL RHDDRYIVGA SPETLVSVQD DRIVSNPIAG TCSRGNSPVE
DRRLAGEMLA DGKERAEHTM LVDLARNDVR RVSDPGSVRV EEFMNVLKYS HVQHIESTVT
GTLASDADAF DATRATFPAG TLTGAPKIRA MEIVDKLETT PRGVYGGGVG YYSWSGDADF
AIVIRTATIE DNETAISNAH QTEIIAETAP ATVRVQAGAG IVADSDPASE YRETEQKMDG
VLSALEMITT EAAEMAQTQT QTQTTQANGN LSGDRDTDNK MGDDMKSESS HTEEASR
//
