ID   GLNA_CHICK              Reviewed;         373 AA.
AC   P16580; B0FZC2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   04-NOV-2026, entry version 140.
DE   RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:19895308};
DE            Short=GS {ECO:0000303|PubMed:19895308};
DE            EC=6.3.1.2 {ECO:0000269|PubMed:19895308};
DE   AltName: Full=Glutamate decarboxylase {ECO:0000303|PubMed:19895308};
DE            EC=4.1.1.15 {ECO:0000269|PubMed:19895308};
DE   AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE   AltName: Full=p42;
GN   Name=GLUL {ECO:0000250|UniProtKB:P15104}; Synonyms=GLNS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=2572512; DOI=10.1016/0378-1119(89)90348-x;
RA   Pu H., Young A.P.;
RT   "The structure of the chicken glutamine synthetase-encoding gene.";
RL   Gene 81:169-175(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=1356223; DOI=10.1093/oxfordjournals.molbev.a040759;
RA   Campbell J.W., Smith D.D. Jr.;
RT   "Metabolic compartmentation of vertebrate glutamine synthetase: putative
RT   mitochondrial targeting signal in avian liver glutamine synthetase.";
RL   Mol. Biol. Evol. 9:787-805(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RA   Matthews G.D., Gur N., Pines O., Vardimon L.;
RT   "Evolution of mitochondrial targeting mechanisms: tissue-specific
RT   subcellular localization of glutamine synthetase.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=4401992; DOI=10.1016/s0021-9258(19)45277-0;
RA   Vorhaben J.E., Campbell J.W.;
RT   "Glutamine synthetase. A mitochondrial enzyme in uricotelic species.";
RL   J. Biol. Chem. 247:2763-2767(1972).
RN   [5]
RP   COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=12965260; DOI=10.1016/s0165-5728(03)00173-5;
RA   Sattayasai N., Sattayasai J., Daduang S., Chahomchuen T., Ketkaew S.,
RA   Puchongkavarin H.;
RT   "A non-mitochondrial carboxylase, related to glutamate action is
RT   synthesized in the retina of the chick embryo.";
RL   J. Neuroimmunol. 141:104-111(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP   COFACTOR, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=19895308; DOI=10.3109/02713680903094723;
RA   Arunchaipong K., Sattayasai N., Sattayasai J., Svasti J., Rimlumduan T.;
RT   "A biotin-coupled bifunctional enzyme exhibiting both glutamine synthetase
RT   activity and glutamate decarboxylase activity.";
RL   Curr. Eye Res. 34:809-818(2009).
CC   -!- FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent
CC       conversion of glutamate and ammonia to glutamine (PubMed:19895308).
CC       When expressed in liver, it may be involved in detoxifying
CC       intramitochondrially generated ammonia (PubMed:4401992). Also acts as
CC       glutamate decarboxylase by catalyzing the production of 4-
CC       aminobutanoate (gamma-aminobutyric acid, GABA) in a pyridoxal
CC       phosphate-independent manner (PubMed:19895308).
CC       {ECO:0000269|PubMed:19895308, ECO:0000269|PubMed:4401992}.
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:0000269|PubMed:19895308};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate + H(+) = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000269|PubMed:19895308};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000269|PubMed:19895308};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19895308};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19895308};
CC   -!- ACTIVITY REGULATION: Glutamate to glutamine ratio influences catalytic
CC       activity (PubMed:19895308). At glutamate to glutamine ratios greater
CC       than 4, decarboxylase activity ceases (PubMed:19895308). In the
CC       presence of manganese, synthetase activity is limited to concentrations
CC       between 10 mM and 20 mM, whereas decarboxylase activity is not affected
CC       (PubMed:19895308). Both catalytic activities are inhibited by avidin
CC       (PubMed:19895308). {ECO:0000269|PubMed:19895308}.
CC   -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000269|PubMed:19895308}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12965260}.
CC       Mitochondrion {ECO:0000269|PubMed:4401992}. Note=In the liver found in
CC       mitochondria, in brain and retina in the cytoplasm (PubMed:12965260,
CC       PubMed:4401992). In retinal cells found in the outer part of the inner
CC       nuclear layer and in the bacillary layer of the photoreceptor, and is
CC       probably associated with the cell membrane (PubMed:12965260,
CC       PubMed:4401992). {ECO:0000269|PubMed:12965260,
CC       ECO:0000269|PubMed:4401992}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina, brain and liver
CC       (PubMed:1356223). Little or no detectable expression in breast muscle,
CC       pancreas and spleen (PubMed:1356223). {ECO:0000269|PubMed:1356223}.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed in retina on embryonic day 18,
CC       with levels increasing until day 6 after hatching and then remaining
CC       high until day 21 (at protein level). {ECO:0000269|PubMed:12965260}.
CC   -!- INDUCTION: In the retina, down-regulated upon application of glutamate
CC       concentrations of 15 umol/eye or higher. {ECO:0000269|PubMed:12965260}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; M29076; AAA48783.1; -; mRNA.
DR   EMBL; S45408; AAC69361.1; -; mRNA.
DR   EMBL; EU369427; ABY71840.1; -; Genomic_DNA.
DR   PIR; JQ0025; AJCHQ.
DR   RefSeq; NP_990824.2; NM_205493.2.
DR   AlphaFoldDB; P16580; -.
DR   SMR; P16580; -.
DR   BioGRID; 676736; 1.
DR   FunCoup; P16580; 2520.
DR   IntAct; P16580; 1.
DR   STRING; 9031.ENSGALP00000067937; -.
DR   PaxDb; 9031-ENSGALP00000067937; -.
DR   GeneID; 396489; -.
DR   KEGG; gga:396489; -.
DR   CTD; 2752; -.
DR   VEuPathDB; HostDB:geneid_396489; -.
DR   eggNOG; KOG0683; Eukaryota.
DR   InParanoid; P16580; -.
DR   PhylomeDB; P16580; -.
DR   PRO; PR:P16580; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; EXP:UniProtKB.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; EXP:UniProtKB.
DR   GO; GO:0004356; F:glutamine synthetase activity; EXP:UniProtKB.
DR   GO; GO:1901704; P:L-glutamine biosynthetic process; IBA:GO_Central.
DR   FunFam; 3.10.20.70:FF:000004; Glutamine synthetase; 1.
DR   FunFam; 3.30.590.10:FF:000011; Glutamine synthetase; 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; IPR027302; Gln_synth_N_conserv_site.
DR   InterPro; IPR050292; Glutamine_Synthetase.
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   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Ligase; Lyase; Magnesium; Manganese; Metal-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..373
FT                   /note="Glutamine synthetase"
FT                   /id="PRO_0000153144"
FT   DOMAIN          24..106
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          113..373
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   373 AA;  42146 MW;  505254A25E8733DB CRC64;
     MATSASSHLS KAIKHMYMKL PQGEKVQAMY IWIDGTGEHL RCKTRTLDHE PKSLEDLPEW
     NFDGSSTFQA EGSNSDMYLR PAAMFRDPFR KDPNKLVLCE VFKYNRQSAD TNLRHTCRRI
     MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP SNCFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGVKI GGTNAEVMPA QWEFQVGPCE GIEMGDHLWI ARFILHRVCE DFGVIVSFDP
     KPIPGNWNGA GCHTNFSTKN MREDGGLKHI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL
     TGFHETSSIH EFSAGVANRG ASIRIPRNVG HEKKGYFEDR GPSANCDPYA VTEALVRTCL
     LNETGDEPFE YKN
//