ID GLNA_SQUAC Reviewed; 403 AA. AC P41320; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 08-NOV-2023, entry version 99. DE RecName: Full=Glutamine synthetase, mitochondrial {ECO:0000305}; DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104}; DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305}; DE Flags: Precursor; OS Squalus acanthias (Spiny dogfish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Squalomorphii; Squaliformes; Squalidae; Squalus. OX NCBI_TaxID=7797; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MITOCHONDRIAL AND CYTOPLASMIC), AND RP SUBCELLULAR LOCATION. RC TISSUE=Liver; RX PubMed=7914934; DOI=10.1007/bf00178254; RA Laud P.R., Campbell J.W.; RT "Genetic basis for tissue isozymes of glutamine synthetase in RT elasmobranchs."; RL J. Mol. Evol. 39:93-100(1994). 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: [Isoform Mitochondrial]: Mitochondrion CC {ECO:0000269|PubMed:7914934}. CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm CC {ECO:0000269|PubMed:7914934}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Mitochondrial; CC IsoId=P41320-1; Sequence=Displayed; CC Name=Cytoplasmic; CC IsoId=P41320-2; Sequence=VSP_018735; CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7914934}. 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; U04617; AAA61871.1; -; mRNA. DR PIR; I51326; I51326. DR AlphaFoldDB; P41320; -. DR SMR; P41320; -. DR BRENDA; 6.3.1.2; 5813. 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; 2. 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:SF45; 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 Alternative initiation; ATP-binding; Cytoplasm; Ligase; Magnesium; KW Manganese; Metal-binding; Mitochondrion; Nucleotide-binding; KW Transit peptide. FT TRANSIT 1..14 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 15..403 FT /note="Glutamine synthetase, mitochondrial" FT /id="PRO_0000011171" FT DOMAIN 55..135 FT /note="GS beta-grasp" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330" FT DOMAIN 142..403 FT /note="GS catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331" FT BINDING 163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 163 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 165 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 225 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 232..237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 232 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 275..276 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 282 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 284..286 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 348 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 348 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT BINDING 353 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 365..367 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 367 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P15104" FT BINDING 369 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:P9WN39" FT VAR_SEQ 1..29 FT /note="Missing (in isoform Cytoplasmic)" FT /evidence="ECO:0000305" FT /id="VSP_018735" SQ SEQUENCE 403 AA; 45409 MW; E003D3F2A33E240B CRC64; MRICRSFLFL VKKCGNITPT IWRNQHTYKM ATSASANLSK IVKKNYMELP QDGKVQAMYI WIDGTGEAVR CKTRTLDNEP KSIAELPEWN FDGSSTYQSE GSNSDMYLVP SAMFRDPFRR DPNKLVLCEV LKYNRKPAES NLRHSCQKIM SMIANEYPWF GMEQEYTLLG TDGHPFGWPS NCFPGPQGPY YCGVGADKAY GRDIVEAHYR ACLYAGIELS GTNAEVMAAQ WEYQVGPCEG IQMGDHLWIS RFILHRVCED FGIIASFDPK PIPGNWNGAG CHTNFSTKAM RDDGGLKYIE DSIEKLGKRH QYHIRAYDPK GGLDNARALT GHHETSNINE FSAGVANRGA SIRIPRSVGQ DKKGYFEDRR PSANCDPYAV TEALVRTCLL DESGDKPIEY NKN //