ID A0A105TU42_9BURK Unreviewed; 497 AA.
AC A0A105TU42;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=DF011_35120 {ECO:0000313|EMBL:RQQ01930.1}, WJ35_09140
GN {ECO:0000313|EMBL:AOJ75214.1}, WM16_31400
GN {ECO:0000313|EMBL:KWK83833.1};
OS Burkholderia ubonensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=101571 {ECO:0000313|EMBL:KWK83833.1, ECO:0000313|Proteomes:UP000065504};
RN [1] {ECO:0000313|EMBL:KWK83833.1, ECO:0000313|Proteomes:UP000065504}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB782WGS {ECO:0000313|EMBL:KWK83833.1,
RC ECO:0000313|Proteomes:UP000065504};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AOJ75214.1, ECO:0000313|Proteomes:UP000243680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSMB0783 {ECO:0000313|EMBL:AOJ75214.1,
RC ECO:0000313|Proteomes:UP000243680};
RA Sahl J., Wagner D., Keim P.;
RT "Diversity of Burkholderia near neighbor genomes.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RQQ01930.1, ECO:0000313|Proteomes:UP000274995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp8958 {ECO:0000313|EMBL:RQQ01930.1,
RC ECO:0000313|Proteomes:UP000274995};
RA Hall C., Sahl J., Wagner D.;
RT "Comparative analysis of Burkholderia isolates from Puerto Rico.";
RL Submitted (AUG-2018) 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}.
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DR EMBL; CP013420; AOJ75214.1; -; Genomic_DNA.
DR EMBL; LPLU01000018; KWK83833.1; -; Genomic_DNA.
DR EMBL; QTOC01000051; RQQ01930.1; -; Genomic_DNA.
DR RefSeq; WP_059716634.1; NZ_QTOD01000015.1.
DR UniPathway; UPA00035; UER00040.
DR Proteomes; UP000065504; Unassembled WGS sequence.
DR Proteomes; UP000243680; Chromosome 1.
DR Proteomes; UP000274995; 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 Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU364045}.
FT DOMAIN 26..172
FT /note="Anthranilate synthase component I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF04715"
FT DOMAIN 221..478
FT /note="Chorismate-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00425"
SQ SEQUENCE 497 AA; 55071 MW; 7D243075E45ABCE0 CRC64;
MTELEFQSLA NEGYNRIPLI AEALADLETP LSLYLKLAQP ERGGANSFLL ESVVGGERFG
RYSFIGLPAR TLVRARAGVS EVVRDGEVVE THDGDPFEFI AAFQARFKVA QRPGLPRFCG
GLAGYFGYDA VRYIEKKLAH TAPRDDLGLP DIQLLLTEEV AVIDNLAGKL YLIIYADPGQ
PEAYTKAKQR LRELKQRLRA TVQPPVTSPS VRTETFREFK KEDYLAAVRQ AKEYIAAGEL
MQIQVGQRLT KPYRDNPLSL YRALRSLNPS PYMYYYNFGD FHVVGASPEI LVRQEKRGDD
QIVTIRPLAG TRPRGNTPER DAELATELLN DPKEIAEHVM LIDLARNDVG RIAEIGSVQV
TDKMVIEKYS HVQHIVSSVE GKLKPGMTNY DVLRATFPAG TLSGAPKVRA MELIDELEPV
KRGLYGGAVG YLSFSGEMDL AIAIRTGLIH NGNLYVQAAA GVVADSVPES EWQETENKAR
AVLRAAEQVQ DGLDSDF
//
