ID D7DTM9_METV3 Unreviewed; 446 AA. AC D7DTM9; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 02-SEP-2026, entry version 76. DE RecName: Full=Glutamine synthetase {ECO:0000256|RuleBase:RU004356}; DE EC=6.3.1.2 {ECO:0000256|RuleBase:RU004356}; GN OrderedLocusNames=Mvol_0830 {ECO:0000313|EMBL:ADI36489.1}; OS Methanococcus voltae (strain ATCC BAA-1334 / A3). OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group; OC Methanococci; Methanococcales; Methanococcaceae; Methanococcus. OX NCBI_TaxID=456320 {ECO:0000313|EMBL:ADI36489.1, ECO:0000313|Proteomes:UP000007722}; RN [1] {ECO:0000313|EMBL:ADI36489.1, ECO:0000313|Proteomes:UP000007722} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1334 / A3 {ECO:0000313|Proteomes:UP000007722}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Lowry S., Clum A., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Whitman W.B., Woyke T.; RT "Complete sequence of Methanococcus voltae A3."; RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + NH4(+) + ATP = L-glutamine + ADP + phosphate + CC H(+); Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; CC Evidence={ECO:0000256|RuleBase:RU004356}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604809-3}; CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR604809- CC 3}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|RuleBase:RU000385}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330, CC ECO:0000256|RuleBase:RU000384}. 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; CP002057; ADI36489.1; -; Genomic_DNA. DR AlphaFoldDB; D7DTM9; -. DR FunCoup; D7DTM9; 98. DR STRING; 456320.Mvol_0830; -. DR KEGG; mvo:Mvol_0830; -. DR eggNOG; arCOG01909; Archaea. DR HOGENOM; CLU_017290_1_3_2; -. DR InParanoid; D7DTM9; -. DR OrthoDB; 36124at2157; -. DR Proteomes; UP000007722; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:TreeGrafter. DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC. DR FunFam; 3.30.590.10:FF:000003; Glutamine synthetase 2; 1. DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1. DR InterPro; IPR008147; Gln_synt_N. DR InterPro; IPR036651; Gln_synt_N_sf. 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; IPR004809; Gln_synth_I. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR NCBIfam; TIGR00653; GlnA; 1. DR PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR43407:SF1; LENGSIN; 1. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1. DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. DR PROSITE; PS51986; GS_BETA_GRASP; 1. DR PROSITE; PS51987; GS_CATALYTIC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR604809- KW 2}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU000385}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR604809-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR604809-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR604809-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000007722}. FT DOMAIN 14..107 FT /note="GS beta-grasp" FT /evidence="ECO:0000259|PROSITE:PS51986" FT DOMAIN 114..446 FT /note="GS catalytic" FT /evidence="ECO:0000259|PROSITE:PS51987" FT BINDING 138 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 140 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 192 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 199 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 202..204 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 243..244 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 301 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 307 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 319 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" FT BINDING 331 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-2" FT BINDING 336 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-3" FT BINDING 338 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000256|PIRSR:PIRSR604809-1" SQ SEQUENCE 446 AA; 50109 MW; 84722EC264795B78 CRC64; MTSLEMALEY IKINNVKFLR FQFVDIHGEP KNIAYPVKLG TADGEEELLG VLENGLFFDG SSIEGFVEIE DSDMVLKPDL STLSVLPWRP SEKSVARIIC DVYRKNGKPF EGDPRGCLKR VLGEFKEEFK GEYFVGPEPE FFILKNENGK WVPGDNAGYF DLEPVDEGND LRRNIVFALE NLGFHVEASH HEVADGQHEV DFKYDNAVRT ADSVVTFKTT IKTLAKQSGS VATFMPKPFF GINGSGMHCN QSIWLDGKPS FYDENNPYQL SDICLSYIGG ILEHTKSLVS ITNPTVNSYK RLVPGYEAPV NIAWANSNRS SIIRVPAARG KGTRVEFRAP DPTCNPYLAF TVMLAAGLDG VRKKLIAPEP VEENIFAMSE AQKRDANIAS VPSNLCEAIE ELKQDKVLKK ALGDHIFNKF IEIKTQEWDS YRTAVTDWEF NKYVKF //