ID TRPG_PSEPU Reviewed; 198 AA. AC P00901; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 02-SEP-2026, entry version 114. DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE Short=ASII; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, GATase component; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; GN Name=trpG; OS Pseudomonas putida (Arthrobacter siderocapsulatus). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=303; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 23287 / C1S; RX PubMed=2404959; DOI=10.1128/jb.172.2.867-883.1990; RA Essar D.W., Eberly L., Crawford I.P.; RT "Evolutionary differences in chromosomal locations of four early genes of RT the tryptophan pathway in fluorescent pseudomonads: DNA sequences and RT characterization of Pseudomonas putida trpE and trpGDC."; RL J. Bacteriol. 172:867-883(1990). RN [2] RP PROTEIN SEQUENCE, AND ACTIVE SITE. RX PubMed=659439; DOI=10.1016/s0021-9258(17)30440-4; RA Kawamura M., Keim P.S., Goto Y., Zalkin H., Heinrikson R.L.; RT "Anthranilate synthetase component II from Pseudomonas putida. Covalent RT structure and identification of the cysteine residue involved in RT catalysis."; RL J. Biol. Chem. 253:4659-4668(1978). 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:0000269|PubMed:2404959}. 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 -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: a CC beta subunit (TrpG) and a large alpha subunit (TrpE). {ECO:0000305}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene fail to grow on low- CC ammonia medium but grew on the high-ammonium medium. CC {ECO:0000269|PubMed:2404959}. 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; M33799; AAA80553.1; -; Genomic_DNA. DR PIR; A01122; NNPS2P. DR AlphaFoldDB; P00901; -. DR SMR; P00901; -. DR MEROPS; C26.955; -. DR eggNOG; COG0512; Bacteria. DR UniPathway; UPA00035; UER00040. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0046820; F:aminodeoxychorismate synthase activity; IEA:TreeGrafter. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0000162; P:L-tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:TreeGrafter. DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1. DR FunFam; 3.40.50.880:FF:000003; Anthranilate synthase component II; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR050472; Anth_synth/Amidotransfase. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. DR NCBIfam; NF006462; PRK08857.1; 1. DR NCBIfam; TIGR00566; trpG_papA; 1. DR PANTHER; PTHR43418:SF4; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN; 1. DR PANTHER; PTHR43418; MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED; 1. DR Pfam; PF00117; GATase; 1. DR PRINTS; PR00097; ANTSNTHASEII. DR PRINTS; PR00099; CPSGATASE. DR PRINTS; PR00096; GATASE. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Direct protein sequencing; Glutamine amidotransferase; Lyase; KW Tryptophan biosynthesis. FT CHAIN 1..198 FT /note="Anthranilate synthase component 2" FT /id="PRO_0000056896" FT DOMAIN 2..198 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 80 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 174 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 176 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT BINDING 53..55 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 84 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 130..131 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT CONFLICT 5 FT /note="Missing (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 198 AA; 21824 MW; 6AA7BDC12ED02FB3 CRC64; MLLMMIDNYD SFTYNVVQYL GELGAEVKVI RNDEMTIAQI EALNPERIVV SPGPCTPSEA GVSIEAILHF AGKLPILGVC LGHQSIGQAF GGDVVRARQV MHGKTSPVHH RDLGVFTGLN NPLTVTRYHS LVVKRETLPD CLEVTAWTAH EDGSVDEIMG LRHKTLNIEG VQFHPESILT EQGHELFANF LKQTGGRR //