ID G0A6E9_METMM Unreviewed; 494 AA. AC G0A6E9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 53. 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 OrderedLocusNames=Metme_4596 {ECO:0000313|EMBL:AEG02934.1}; OS Methylomonas methanica (strain MC09). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales; OC Methylococcaceae; Methylomonas. OX NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG02934.1, ECO:0000313|Proteomes:UP000008888}; RN [1] {ECO:0000313|EMBL:AEG02934.1, ECO:0000313|Proteomes:UP000008888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09 {ECO:0000313|EMBL:AEG02934.1, RC ECO:0000313|Proteomes:UP000008888}; RX PubMed=22123758; DOI=10.1128/JB.06267-11; RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G., RA Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H., RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L., RA Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T., RA Stein L., Murrell J.C.; RT "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas RT methanica MC09."; RL J. Bacteriol. 193:7001-7002(2011). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=MC09; RA Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M., RA Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H., RA Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L., RA Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T., RA Stein L.Y., Murrell C.; RT "Complete genome sequence of the aerobic marine methanotroph Methylomonas RT methanica MC09."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000008888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888}; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.; RT "Complete sequence of Methylomonas methanica MC09."; RL Submitted (MAY-2011) 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 --------------------------------------------------------------------------- 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; CP002738; AEG02934.1; -; Genomic_DNA. DR RefSeq; WP_013821147.1; NC_015572.1. DR AlphaFoldDB; G0A6E9; -. DR STRING; 857087.Metme_4596; -. DR KEGG; mmt:Metme_4596; -. DR eggNOG; COG0147; Bacteria. DR HOGENOM; CLU_006493_9_3_6; -. DR OrthoDB; 9803598at2; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000008888; Chromosome. 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:UP000008888}; KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822, KW ECO:0000256|RuleBase:RU364045}. FT DOMAIN 26..167 FT /note="Anthranilate synthase component I N-terminal" FT /evidence="ECO:0000259|Pfam:PF04715" FT DOMAIN 222..475 FT /note="Chorismate-utilising enzyme C-terminal" FT /evidence="ECO:0000259|Pfam:PF00425" SQ SEQUENCE 494 AA; 54501 MW; 1F00CDAC48A83D8D CRC64; MTPAQFTDYA QQGYNRIPVC REVLADLDTP LSAYLKLADG AYSYLFESVH GGEQWGRYSI IGLPCKTRVK ISGNTISLEQ DGADTQTFEH AQPLEWIEEF RQQYQVPDIE GLPRFNGGLV GYFGYETIGY IEPRLKSAGK PDPIGTPDIL LMVSQDLLVF DNLSGKMLLL THADPAQEGA YELAQARLAE LVDKLHQLKA HPQPHPAVKQ VHENDFVSGF TQQGFEDAVR KAKQYITDGD VMQVVLSQRM SIPFSASPLD LYRSLRCLNP SPYMYYLNLD GFHIVGSSPE ILVRLEDDEV TVRPIAGTRP RGATHEQDQA LEQELLADPK EIAEHLMLID LGRNDAGRVA KIGSVKLTDK MIIERYSHVM HIVSNVTGQL QDGKNAFDVL AATFPAGTVS GAPKIRAMEI IDELEPVKRG IYSGAVGYIS WSGNLDTAIA IRTAVIKDQT LHIQAGAGIV YDSVPRNEWD ETMNKGRAVF RAVSMAEAGL GGKA //