ID A0AAN0R6R8_9PSED Unreviewed; 493 AA. AC A0AAN0R6R8; DT 02-OCT-2024, integrated into UniProtKB/TrEMBL. DT 02-OCT-2024, sequence version 1. DT 27-NOV-2024, entry version 2. 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=PVLB_23120 {ECO:0000313|EMBL:AGZ37403.1}; OS Pseudomonas sp. VLB120. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=69328 {ECO:0000313|EMBL:AGZ37403.1, ECO:0000313|Proteomes:UP000017756}; RN [1] {ECO:0000313|EMBL:AGZ37403.1, ECO:0000313|Proteomes:UP000017756} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VLB120 {ECO:0000313|EMBL:AGZ37403.1, RC ECO:0000313|Proteomes:UP000017756}; RX PubMed=25128338; DOI=10.1128/AEM.01940-14; RA Volmer J., Neumann C., Buhler B., Schmid A.; RT "Engineering of Pseudomonas taiwanensis VLB120 for Constitutive Solvent RT Tolerance and Increased Specific Styrene Epoxidation Activity."; RL Appl. Environ. Microbiol. 80:6539-6548(2014). 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 + pyruvate + L- CC glutamate + H(+); Xref=Rhea:RHEA:21732, ChEBI:CHEBI:15361, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16567, ChEBI:CHEBI:29748, CC ChEBI:CHEBI:29985, 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 --------------------------------------------------------------------------- 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; CP003961; AGZ37403.1; -; Genomic_DNA. DR RefSeq; WP_023382659.1; NC_022738.1. DR Proteomes; UP000017756; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. 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 27..167 FT /note="Anthranilate synthase component I N-terminal" FT /evidence="ECO:0000259|Pfam:PF04715" FT DOMAIN 223..476 FT /note="Chorismate-utilising enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF00425" SQ SEQUENCE 493 AA; 54486 MW; 16B011E1993DF166 CRC64; MTREEFLRLA AAGYNRIPLA CETLADFDTP LSIYLKLADQ PNSYLLESVQ GGEKWGRYSM IGLPSRTVMR VHGYHVSILQ DGVEVENHDV EDPLAFVETF KDRYKVADIP GLPRFNGGLV GYFGYDCVRY VEKRLGACPN PDPLGVPDIL LMVSDAVVVF DNLAGKMHAI VLVDPTEEQA FEQGQARLQG LLETLRQPIT PRRGLDLSGP LAAEPEFRSS YTRDDYENAV GRIKEYILAG DCMQVVPSQR MSIDFKAAPI DLYRALRCFN PTPYMYFFNF GDFHVVGSSP EVLVRVEDNL VTVRPIAGTR PRGATEEADR ALEDDLLSDE KEIAEHLMLI DLGRNDVGRV SSTGSVRLTE KMVIERYSNV MHIVSNVTGQ LRQGLTAMDA LRAILPAGTL SGAPKIRAME IIDELEPVKR GVYGGAVGYF AWNGNMDTAI AIRTAVIKDG ELHVQAGGGI VADSVPALEW EETINKRRAM FRAVALAEQT SAK //