ID A0A0Q7KWE7_9BURK Unreviewed; 500 AA.
AC A0A0Q7KWE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=ASD34_21905 {ECO:0000313|EMBL:KQX84633.1};
OS Variovorax sp. Root473.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1736541 {ECO:0000313|EMBL:KQX84633.1, ECO:0000313|Proteomes:UP000051275};
RN [1] {ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|Proteomes:UP000051275};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQX84633.1, ECO:0000313|Proteomes:UP000051275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root473 {ECO:0000313|EMBL:KQX84633.1,
RC ECO:0000313|Proteomes:UP000051275};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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|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:KQX84633.1}.
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DR EMBL; LMEV01000020; KQX84633.1; -; Genomic_DNA.
DR RefSeq; WP_056584602.1; NZ_LMEV01000020.1.
DR AlphaFoldDB; A0A0Q7KWE7; -.
DR OrthoDB; 9803598at2; -.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000051275; 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:SF48; ISOCHORISMATE SYNTHASE MENF; 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|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364045};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364045};
KW Reference proteome {ECO:0000313|Proteomes:UP000051275};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 27..177
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 226..484
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 500 AA; 54787 MW; D3E63EE63A6AB239 CRC64;
MITELEFKSL SAQGYNRIPL MAEAFADLET PLSLYLKLAH SQGGGKHSFL LESVVGGERF
GRYSFIGLPA RTLLRASGFG DEAVTEVVTD GQVVETAKGN PLDFVADYQK RFKVALRPGL
PRFCGGLAGY FGYDTVRHIE RKLEKSCPPD ALGCPDILLL QCEELAVIDN LSGKLYLIVY
ADPKQPEAYA VGKRRLRELK DKLKYSVSAP VVKPTQAHPP ERSFAKADYL AAVERAKEMI
AAGDFMQVQV GQRISKRYTE SPLSLYRALR SLNPSPYMYY YNLGDFHVVG ASPEILVRQE
NTGDGEQKIT IRPLAGTRPR GASIELDKAA EVELINDPKE RAEHVMLIDL ARNDIGRIAK
TGTVKVTEAF AVERYSHVMH IVSNVEGTLK DGMTAIDVLK ATFPAGTLTG APKVHAMELI
DQLEPTKRGL YGGACGYISY AGDMDVAIAI RTGIVKDQML HVQAAAGVVA DSVPELEWKE
TEAKARALLR AAELVEEGLE
//
