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 24-JAN-2024, entry version 132.
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=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:0000269|PubMed:19895308};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + L-glutamate = 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:4401992,
CC PubMed:12965260). 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:4401992,
CC PubMed:12965260). {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_990824.1; NM_205493.1.
DR AlphaFoldDB; P16580; -.
DR SMR; P16580; -.
DR BioGRID; 676736; 1.
DR IntAct; P16580; 1.
DR STRING; 9031.ENSGALP00000067937; -.
DR PaxDb; 9031-ENSGALP00000005819; -.
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; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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: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
//
