ID A0A1H6T7Q9_9EURY Unreviewed; 535 AA.
AC A0A1H6T7Q9; A0A2H4PZX3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05444271_10795 {ECO:0000313|EMBL:SEI76031.1};
OS Halohasta litchfieldiae.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halohasta.
OX NCBI_TaxID=1073996 {ECO:0000313|EMBL:SEI76031.1, ECO:0000313|Proteomes:UP000198888};
RN [1] {ECO:0000313|EMBL:SEI76031.1, ECO:0000313|Proteomes:UP000198888}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22187 {ECO:0000313|EMBL:SEI76031.1,
RC ECO:0000313|Proteomes:UP000198888};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNYR01000007; SEI76031.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6T7Q9; -.
DR STRING; 1073996.SAMN05444271_10795; -.
DR OrthoDB; 25514at2157; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000198888; 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:UP000198888};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 41..205
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 258..515
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 238..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 58064 MW; 169D99CC262518E9 CRC64;
MSSGSELLTF DRDREAFVDL IGKPDAPVVA RVAVTLDVDT SPLATYAALA DQSPYNFLLE
SAEKTASSDP DGAFAPETDA ERHARYSFVG YDPEAIVSVY PDRTEVDRLG PAADLLVEAY
KGDAATDGDI LDRLRRGLPS IERLGFPETT RRQLSGGLVG FLAHETVYDL VLEDVGLDRP
DSELPDAQFA LTTRTVVFDD AEGTVKLVFT PVLDGSDDPG QRYDELRSEA VDIAQTLSEA
SEPEPGGFHR TGETAGPQDE YEEAVRTAKQ HVLDGDIYQG VISRKRELTG EIDPIGLYEA
LRDVNPSPYM YLMAHDDLSI VGASPETLVS VQDREIVSNP IAGTCARGTS PVEDRRLAGE
MLADGKERAE HTMLVDLARN DVRRVSESGS VSVEEFMSVL KYSHVQHIES TVTGRMADEY
DVFDAARVTF PAGTLTGAPK VRAMEIIDDL ERTPRGVYGG GVGYFSWSGD AEFAIVIRTA
TIDHSGGEDR ITVQAGAGLV ADSDPTAEYE ETEQKMDGVL AAIEQIETEP QEAEQ
//
