ID A0A0P7HF66_9MICC Unreviewed; 528 AA.
AC A0A0P7HF66;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-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=AO716_13525 {ECO:0000313|EMBL:KPN18784.1};
OS Arthrobacter sp. Edens01.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1732020 {ECO:0000313|EMBL:KPN18784.1, ECO:0000313|Proteomes:UP000054460};
RN [1] {ECO:0000313|EMBL:KPN18784.1, ECO:0000313|Proteomes:UP000054460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Edens01 {ECO:0000313|EMBL:KPN18784.1,
RC ECO:0000313|Proteomes:UP000054460};
RA Couger M.B.;
RT "Draft Genome of Arthrobacter sp. strain Edens01.";
RL Submitted (SEP-2015) 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|ARBA:ARBA00025634, 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPN18784.1}.
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DR EMBL; LKIU01000005; KPN18784.1; -; Genomic_DNA.
DR RefSeq; WP_055241441.1; NZ_LKIU01000005.1.
DR AlphaFoldDB; A0A0P7HF66; -.
DR STRING; 1732020.AO716_13525; -.
DR OrthoDB; 3518032at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000054460; 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:SF46; 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:UP000054460};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 33..172
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 237..495
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 528 AA; 57128 MW; CB4026C974E5D3AF CRC64;
MQDLGVISPS LEEFRELAAD RRVVPVRLKV LADAHTPIGI YRKLTGGEPG TFLMESAASG
GVWSRYSFIG ARSRATLTTR DGEAFWLGEP PAGVPVDGNP VEAMAATLAL LATDRFEGLP
PFTSGLVGFV GWESVRHWEK LTSPPVDDLD LPEIAMNLVS DMAIHDNSDG TVLLVANAIN
FDGSDERVDD AWLDAVGRLH SMLDRLAAQS PQAVTVLEGG TVDVSALTAG VKESWPKPEY
LRAVERGKEA IVDGEVFQVV ISRRFEMDCR AEALDVYRVL RTTNPSPYMY LFNFEDARGN
PFAVVGSSPE ALVTVTGREV ITHPIAGSRP RGKTQELDRA LAEELLADEK ERAEHLMLVD
LARNDLSKVC RPGSVDVTQF MEVERFSHIM HLVSTVVGEL SPQHSSYDVL SATFPAGTLS
GAPKPRALRL LDELEPHRRG IYGGVVGYLD FAGDMDMAIA IRSALLRDGK AYVQAGGGIV
ADSDLEAEAL ETVNKAAAPL RAALIAGGLE PVTESVARQI FNSQEENK
//