ID TRPG_HELPY Reviewed; 194 AA. AC O25868; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 126. 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; OrderedLocusNames=HP_1281; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). 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 (By similarity). CC {ECO:0000250}. 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 -!- 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:0000250}. 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; AE000511; AAD08325.1; -; Genomic_DNA. DR PIR; A64680; A64680. DR RefSeq; NP_208073.1; NC_000915.1. DR RefSeq; WP_000688223.1; NC_018939.1. DR AlphaFoldDB; O25868; -. DR SMR; O25868; -. DR IntAct; O25868; 1. DR STRING; 85962.HP_1281; -. DR MEROPS; C26.960; -. DR PaxDb; 85962-C694_06620; -. DR EnsemblBacteria; AAD08325; AAD08325; HP_1281. DR KEGG; hpy:HP_1281; -. DR PATRIC; fig|85962.47.peg.1374; -. DR eggNOG; COG0512; Bacteria. DR InParanoid; O25868; -. DR OrthoDB; 9786812at2; -. DR PhylomeDB; O25868; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR CDD; cd01743; GATase1_Anthranilate_Synthase; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. 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 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Glutamine amidotransferase; Lyase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1..194 FT /note="Anthranilate synthase component 2" FT /id="PRO_0000056884" FT DOMAIN 2..194 FT /note="Glutamine amidotransferase type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 84 FT /note="Nucleophile; for GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 170 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT ACT_SITE 172 FT /note="For GATase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00605" FT BINDING 57..59 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 88 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" FT BINDING 134..135 FT /ligand="L-glutamine" FT /ligand_id="ChEBI:CHEBI:58359" FT /evidence="ECO:0000250|UniProtKB:P00900" SQ SEQUENCE 194 AA; 21438 MW; A03FD6E279345659 CRC64; MKIFFIDNFD SFSYNLVYEL ECLGYEVAVY QNDIDPSYLM DLMNEESKTP LLFISPGPGN PNSSGNLLKI IAMAKKKFPI LGICLGLQAL AQSYGAKIIR SKEIVHGKAT AIALKKHAVF KGLGESMVVG RYHSLMASGL PKNLEVIAEH DNIPMAIVNE EDKILAYQFH PESIMTLQGR ALLEQSVGFL EGLL //