ID GLNA_PANAR Reviewed; 361 AA. AC Q04831; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 08-NOV-2023, entry version 83. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:8100791}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; OS Panulirus argus (Caribbean spiny lobster) (Palinurus argus). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea; OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata; OC Palinuroidea; Palinuridae; Panulirus. OX NCBI_TaxID=6737; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Olfactory organ; RX PubMed=8100791; DOI=10.1016/0378-1119(93)90279-c; RA Trapido-Rosenthal H.G., Linser P.J., Greenberg R.M., Gleeson R.A., RA Carr W.E.; RT "cDNA clones from the olfactory organ of the spiny lobster encode a protein RT related to eukaryotic glutamine synthetase."; RL Gene 129:275-278(1993). 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; M96798; AAA02583.1; -; mRNA. DR PIR; JN0716; JN0716. DR AlphaFoldDB; Q04831; -. DR SMR; Q04831; -. 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:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 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. FT CHAIN 1..361 FT /note="Glutamine synthetase" FT /id="PRO_0000153145" FT DOMAIN 23..103 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 110..361 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 131 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 131 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 133 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 200..205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 200 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 243..244 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 250 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 252..254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 316 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 316 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 321 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 333..335 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 335 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 337 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" SQ SEQUENCE 361 AA; 40768 MW; 3D8C3C507676099C CRC64; MNQGANKTVL DRYLRLDIPD QKCQAMYIWV DGTGENLRSK TRTLNFTPKS PSELPIWNFD GSSTGQAERS NSDVYLYPVA VYRDPFRLGN NKLVLCETYK YNKKPADTNQ RWKCMEVMTR AADQHPWFGM EQEYTLLDID KHPLGWPKNG YPGPQGPYYC GVGANRVYGR DVVEAHYRAC LCAGINISGE NAKVMPAQWE FQVGPCEGIT MGDDLWMARY LLHRVAEDFD VVVTLDPKPI PGDWNGAGMH TNFSTEAMRG PNGILEIESA IDKLSKVHEK HIKAYDPHAG KDNERRLTGH YETSSIHDFS AGVANRGASI RIPRGVAEEK TGYLEDRRPS SNADPYVVSE RLVRTICLNE Q //