ID A0A235GAM2_9NOCA Unreviewed; 528 AA.
AC A0A235GAM2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=BDB13_4255 {ECO:0000313|EMBL:OYD70626.1};
OS Rhodococcus sp. OK302.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1882769 {ECO:0000313|EMBL:OYD70626.1, ECO:0000313|Proteomes:UP000215121};
RN [1] {ECO:0000313|EMBL:OYD70626.1, ECO:0000313|Proteomes:UP000215121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK302 {ECO:0000313|EMBL:OYD70626.1,
RC ECO:0000313|Proteomes:UP000215121};
RA Pelletier D.;
RT "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL Submitted (AUG-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|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:OYD70626.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NPJZ01000001; OYD70626.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235GAM2; -.
DR OrthoDB; 3518032at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000215121; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 50..191
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 248..506
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 56068 MW; BF3AE8F1AA06DCDF CRC64;
MHGEPTSKSA PSSDTAIVGA ASDSTTTREQ FRALAAEHRV VPVTRKVLAD SETPLSAYEK
LAGNRPGTFM LESAENGRSW SRWSFIGVGS PAALTVIDGE AAWYGNVPAG APSGGDPIDA
LGATLELLRS ERLPDLPPLT GGMVGFLGYD AVRRLEKLGN SAVDDLQIPE MVMLLAADIA
AVDHHEGAIT LIANAVNWDG TDERVDSAYD DAVARLDAMT LALAAPAKST VSTFAKATPE
YRRQRTTESF GVDVKKLIGD IEAGEAFQVV LSQRFEIDCT AAPIDVYRML RASNPSPYMY
LLNVPNGDGE TAFSIVGSSP EALVTVAEGV ATTHPIAGTR WRGATEEDDI LLEKDLLADE
KENSEHLMLV DLGRNDLGRV CRPGTVKVHD YRHIERYSHV MHLVSTVTGH LAEGKNALDA
VTACFPAGTL SGAPKVRAMQ LIEELEPTRR GVYGGIVGYL DFAGDADTAI AIRTALIKDG
IGYVQAGAGI VADSDPVYED TEARNKAMAV LSAIASAHTL RTIGGEGK
//
