ID GLNA3_BUTFI Reviewed; 700 AA. AC Q05650; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 08-NOV-2023, entry version 75. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:8103789}; DE Short=GS {ECO:0000303|PubMed:8103789}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15623}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE AltName: Full=Glutamine synthetase III {ECO:0000303|PubMed:8103789}; DE Short=GSIII {ECO:0000303|PubMed:8103789}; GN Name=glnA {ECO:0000303|PubMed:8103789}; OS Butyrivibrio fibrisolvens. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; OC Butyrivibrio. OX NCBI_TaxID=831; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ACTIVITY REGULATION. RC STRAIN=H17C; RX PubMed=8103789; DOI=10.1099/00221287-139-7-1487; RA Goodman H.J., Woods D.R.; RT "Cloning and nucleotide sequence of the Butyrivibrio fibrisolvens gene RT encoding a type III glutamine synthetase."; RL J. Gen. Microbiol. 139:1487-1493(1993). CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from CC glutamate and ammonia. {ECO:0000250|UniProtKB:P15623}. 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:0000250|UniProtKB:P15623}; 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: The activity of this enzyme is not controlled by CC adenylation. {ECO:0000305|PubMed:8103789}. CC -!- SUBUNIT: Homohexamer. {ECO:0000250|UniProtKB:P15623}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P15623}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000250|UniProtKB:P15623}. 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; L08256; AAA71923.1; -; Unassigned_DNA. DR PIR; I40596; I40596. DR AlphaFoldDB; Q05650; -. DR SMR; Q05650; -. 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 3: Inferred from homology; KW ATP-binding; Cytoplasm; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding. FT CHAIN 1..700 FT /note="Glutamine synthetase" FT /id="PRO_0000153278" FT DOMAIN 65..155 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 159..589 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 198 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 267 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 274 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 318..319 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 319 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 323 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" FT BINDING 327 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P77961" FT BINDING 435 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 435 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 472 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P12425" SQ SEQUENCE 700 AA; 78541 MW; 32DDD0FA10B542E7 CRC64; MIEASKLTTE FGSLVFNDKI MKERLPKDIY KAVHKTIEKE PHLEPGCSYS CSSNHEGVGN REQCYHFTPP GSSPMTGLTA EKHDSFISPT EDGRSSWSSQ EKSWLRANLM HQASQWWSSC HNSSMRGYQH GILHHHAFIK DGSLLLPTAF CSYGGEALDR DSLLRSMEAL SNEAVKMMRL LGYEDVNRVN TTIGSEQEYF LIDKDFYKKR KDLLLTGRTL IGAPASKGQE MEDHYFGVIK PKVSAYMHDL DEELWKLGIP AKTKHNEVAP SQHELAPVFE TANIAVDHNQ LTMEVMKKVA DKHNYACLLH EKPFEGVNGS GKHNNWSICT DTGINLLDPG KNPGENIPFL VFLMSVIAAV DEYAPILRLS VASAGNDHRL GGNEAPPAII SIFVGDELAE VLKAVEAGEA YKAAGKSQMT WEQQYFTFTK DNTDRNRTSP FAFTGNKFES DGGHSSVANG KYGPQHMQLQ KEVATLNAKL SAYSGDELKE KVKEVLKETL LAHKRVLFNG NGYTDEWVEE AAKRGLPNLK ALPDCMPYWI SDESIDLFTR HGIFTKEEIY SRYEILLENY SKSIHIESLT MQEMIRKDLT EGLVAYEKDL SKEIVQKKSL LDGDCCALEL GVLKSLDKSS AEMGKALSKL FEDTKKAEGM TEALETASYY ESTVLADMDE LRKYADEAEA LIPEKYLSYP TYGEMLFSLR //