ID GLNA3_BACFR Reviewed; 729 AA. AC P15623; Q64XI6; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 2. DT 27-MAR-2024, entry version 118. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2576872}; DE Short=GS {ECO:0000303|PubMed:2576872}; DE EC=6.3.1.2 {ECO:0000305|Ref.3}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:2576872}; DE Short=GSIII {ECO:0000305}; GN Name=glnA {ECO:0000303|PubMed:2576872}; OrderedLocusNames=BF1040; OS Bacteroides fragilis (strain YCH46). OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; OC Bacteroides. OX NCBI_TaxID=295405; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BF1; RX PubMed=2576872; DOI=10.1099/00221287-136-4-787; RA Hill R.T., Parker J.R., Goodman H.J.K., Jones D.T., Woods D.R.; RT "Molecular analysis of a novel glutamine synthetase of the anaerobe RT Bacteroides fragilis."; RL J. Gen. Microbiol. 135:3271-3279(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YCH46; RX PubMed=15466707; DOI=10.1073/pnas.0404172101; RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N., RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.; RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions RT regulating cell surface adaptation."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004). RN [3] RP FUNCTION, ACTIVITY REGULATION, AND SUBUNIT. RC STRAIN=BF1; RA Southern J.A., Parker J.R., Woods D.R.; RT "Novel structure, properties and inactivation of glutamine synthetase RT cloned from Bacteroides fragilis."; RL J. Gen. Microbiol. 133:2437-2446(1987). CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from CC glutamate and ammonia. {ECO:0000305|Ref.3}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; CC Evidence={ECO:0000305|Ref.3}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P12425}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P12425}; CC -!- ACTIVITY REGULATION: Inhibited by L-histidine (46%), L-arginine (38%) CC and L-methionine-DL-sulphoximine. The activity of this enzyme is not CC controlled by adenylation. {ECO:0000269|Ref.3}. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|Ref.3}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}. 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; M28252; AAA62314.1; -; Genomic_DNA. DR EMBL; AP006841; BAD47790.1; -; Genomic_DNA. DR PIR; A37191; A37191. DR RefSeq; WP_005785391.1; NC_006347.1. DR RefSeq; YP_098324.1; NC_006347.1. DR AlphaFoldDB; P15623; -. DR SMR; P15623; -. DR DIP; DIP-59116N; -. DR STRING; 295405.BF1040; -. DR KEGG; bfr:BF1040; -. DR PATRIC; fig|295405.11.peg.1032; -. DR HOGENOM; CLU_024307_0_0_10; -. DR OrthoDB; 9807095at2; -. DR BRENDA; 6.3.1.2; 755. DR Proteomes; UP000002197; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.20.120.1560; -; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1. DR InterPro; IPR040577; Gln-synt_C. DR InterPro; IPR008147; Gln_synt_N. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR InterPro; IPR008146; Gln_synth_cat_dom. DR InterPro; IPR027303; Gln_synth_gly_rich_site. DR InterPro; IPR022147; GSIII_N. DR PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF18318; Gln-synt_C-ter; 1. DR Pfam; PF12437; GSIII_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR PROSITE; PS00181; GLNA_ATP; 1. DR PROSITE; PS51986; GS_BETA_GRASP; 1. DR PROSITE; PS51987; GS_CATALYTIC; 1. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding. FT CHAIN 1..729 FT /note="Glutamine synthetase" FT /id="PRO_0000153277" FT DOMAIN 85..174 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 179..615 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 215 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 217 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 286 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 337..338 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 338 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 342 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 346 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 458 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 458 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT CONFLICT 152 FT /note="V -> G (in Ref. 1; AAA62314)" FT /evidence="ECO:0000305" FT CONFLICT 531 FT /note="P -> L (in Ref. 1; AAA62314)" FT /evidence="ECO:0000305" FT CONFLICT 566 FT /note="T -> M (in Ref. 1; AAA62314)" FT /evidence="ECO:0000305" SQ SEQUENCE 729 AA; 82825 MW; 1916071619EB9562 CRC64; MSKMRFFALQ ELSNRKPLEI TTPSNKLSDY YASHVFDRKK MQEYLPKEAY KAVVDATEKG TPISREMADL IANGMKSWAK SLNVTHYTHW FQPLTDGTAE KHDGFIEFGE DGEVIERFSG KLLIQQEPDA SSFPNGGIRN TFEARGYTAW DVSSPAFVVD TTLCIPTIFI SYTGEALDYK TPLLKALAAV DKAATEVCQL FDKNITRVFT NLGWEQEYFL VDTSLYNARP DLRLTGRTLM GHSSAKDQQL EDHYFGSIPP RVTAFMKELE IECHKLGIPV KTRHNEVAPN QFELAPIFEN CNLANDHNQL VMDLMKRIAR KHHFAVLFHE KPYNGVNGSG KHNNWSLCTD TGINLFAPGK NPKGNMLFLT FLVNVLMMVH KNQDLLRASI MSAGNSHRLG ANEAPPAILS IFLGSQLSAT LDEIVRQVTN SKMTPEEKTT LKLGIGRIPE ILLDTTDRNR TSPFAFTGNR FEFRAAGSSA NCAAAMIAIN AAMANQLNEF KASVDKLMEE GIGKDEAIFR ILKENIIASE PIRFEGDGYS EEWKQEAARR GLTNICHVPE ALMHYTDNQS RAVLIGERIF NETELACRLE VELEKYTMKV QIESRVLGDL AINHIVPIAV SYQNRLLENL CRMKEIFSEE EYEVMSADRK ELIKEISHRV SAIKVLVRDM TEARKVANHK ENFKEKAFAY EETVRPYLES IRDHIDHLEM EIDDEIWPLP KYRELLFTK //