ID GLNA_XENLA Reviewed; 392 AA. AC P51121; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:7556612}; DE Short=GS {ECO:0000303|PubMed:7556612}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; GN Name=glul {ECO:0000250|UniProtKB:P15104}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=7556612; DOI=10.1016/0014-5793(95)00913-t; RA Hatada S., Kinoshita M., Noda M., Asashima M.; RT "Identification of a Xenopus glutamine synthetase gene abundantly expressed RT in the embryonic nervous system but not in adult brain."; RL FEBS Lett. 371:287-292(1995). CC -!- FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent CC conversion of glutamate and ammonia to glutamine. CC {ECO:0000250|UniProtKB:P15104}. 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:P15104}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P09606}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:P15104}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P15104}. Microsome CC {ECO:0000250|UniProtKB:P09606}. Mitochondrion CC {ECO:0000250|UniProtKB:P09606}. 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; D50062; BAA08779.1; -; mRNA. DR PIR; I51422; I51422. DR RefSeq; NP_001082548.1; NM_001089079.1. DR AlphaFoldDB; P51121; -. DR SMR; P51121; -. DR GeneID; 398556; -. DR KEGG; xla:398556; -. DR AGR; Xenbase:XB-GENE-6256042; -. DR Xenbase; XB-GENE-6256042; glul.L. DR OMA; TKDYADH; -. DR OrthoDB; 1115057at2759; -. DR Proteomes; UP000186698; Chromosome 8L. DR Bgee; 398556; Expressed in egg cell and 19 other cell types or tissues. DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; 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; 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; IPR027302; Gln_synth_N_conserv_site. DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1. DR PANTHER; PTHR20852:SF43; GLUTAMINE SYNTHETASE; 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 2: Evidence at transcript level; KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Ligase; Magnesium; KW Manganese; Metal-binding; Microsome; Mitochondrion; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..392 FT /note="Glutamine synthetase" FT /id="PRO_0000153146" FT DOMAIN 26..106 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 113..392 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 134 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 134 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 136 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 196 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 203..208 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 203 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 246..247 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 253 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 255..257 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 319 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 324 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 336..338 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 338 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 340 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" SQ SEQUENCE 392 AA; 43985 MW; D69C175E95FA8D2F CRC64; MSVSHSSRLN KGVREQYMKL PQGEKVQVTY VWIDGTGEGV RCKTRTLDQE PKTIDEIPEW NFDGSSTHQA EGSNSDMYLI PVQMFRDPFC LDPNKLVMCE VLKYNRKSAE TNLRHTCKKI MEMVNDHRPW FGMEQEYTLL GINGHPYGWP ENGFPGPQGP YYCGVGADKV YGRDVVESHY KACLYAGIKI CGTNAEVMPS QWEFQVGPCE GIDMGDHLWM ARFILHRVCE DFGVVATLDP KPMTGNWNGA GCHTNYSTES MRVEGGLKHI EDAIEKLGKR HDYHICVYDP RGGKDNSRRL TGQHETSSIH EFSAGVANRG ASIRIPRQVG QEGYGYFEDR RPAANCDPYA VTEALVRTTI LNETGSETKD YKNGAGFSRA IGMASPRDAA VF //