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Database: UniProt
Entry: P16580
LinkDB: P16580
Original site: P16580 
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   29-OCT-2014, entry version 94.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate decarboxylase;
DE            EC=4.1.1.15;
DE   AltName: Full=Glutamate--ammonia ligase;
DE   AltName: Full=p42;
GN   Name=GLUL; Synonyms=GLNS;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Testudines + Archosauria group; Archosauria; Dinosauria; Saurischia;
OC   Theropoda; Coelurosauria; Aves; Neognathae; 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;
RA   Campbell J.W., Smith D.D. Jr.;
RT   "Metabolic compartmentation of vertebrate glutamine synthetase:
RT   putative mitochondrial targeting signal in avian liver glutamine
RT   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;
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, ENZYME REGULATION, AND SUBUNIT.
RX   PubMed=19895308; DOI=10.3109/02713680903094723;
RA   Arunchaipong K., Sattayasai N., Sattayasai J., Svasti J.,
RA   Rimlumduan T.;
RT   "A biotin-coupled bifunctional enzyme exhibiting both glutamine
RT   synthetase activity and glutamate decarboxylase activity.";
RL   Curr. Eye Res. 34:809-818(2009).
CC   -!- FUNCTION: This enzyme has 2 functions: it catalyzes the production
CC       of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA),
CC       the latter in a pyridoxal phosphate-independent manner. When
CC       expressed in liver, it may be involved in detoxifying
CC       intramitochondrially generated ammonia.
CC       {ECO:0000269|PubMed:19895308, ECO:0000269|PubMed:4401992}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine. {ECO:0000269|PubMed:19895308}.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC       {ECO:0000269|PubMed:19895308}.
CC   -!- COFACTOR: Biotin.
CC   -!- COFACTOR: Magnesium or manganese.
CC   -!- ENZYME REGULATION: Glutamate to glutamine ratio influences
CC       catalytic activity. At glutamate to glutamine ratios greater than
CC       4, decarboxylase activity ceases. In the presence of manganese,
CC       synthetase activity is limited to concentrations between 10 mM and
CC       20 mM, whereas decarboxylase activity is not affected. Both
CC       catalytic activities are inhibited by avidin.
CC       {ECO:0000269|PubMed:19895308}.
CC   -!- SUBUNIT: Homooctamer and homotetramer.
CC       {ECO:0000269|PubMed:19895308}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Note=In the liver
CC       found in mitochondria, in brain and retina in the cytoplasm. In
CC       retinal cells found in the outer part of the inner nuclear layer
CC       and in the bacillary layer of the photoreceptor, and is probably
CC       associated with the cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in retina, brain and liver. Little
CC       or no detectable expression in breast muscle, pancreas and spleen.
CC       {ECO:0000269|PubMed:1356223}.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed in retina on embryonic day
CC       18, with levels increasing until day 6 after hatching and then
CC       remaining high until day 21 (at protein level).
CC       {ECO:0000269|PubMed:12965260}.
CC   -!- INDUCTION: In the retina, down-regulated upon application of
CC       glutamate concentrations of 15 umol/eye or higher.
CC       {ECO:0000269|PubMed:12965260}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {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   UniGene; Gga.2464; -.
DR   ProteinModelPortal; P16580; -.
DR   SMR; P16580; 3-372.
DR   BioGrid; 676736; 1.
DR   IntAct; P16580; 1.
DR   STRING; 9031.ENSGALP00000005819; -.
DR   PaxDb; P16580; -.
DR   GeneID; 396489; -.
DR   KEGG; gga:396489; -.
DR   CTD; 2752; -.
DR   eggNOG; COG0174; -.
DR   HOGENOM; HOG000061500; -.
DR   HOVERGEN; HBG005847; -.
DR   InParanoid; P16580; -.
DR   KO; K01915; -.
DR   PhylomeDB; P16580; -.
DR   NextBio; 20816528; -.
DR   PRO; PR:P16580; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; -; 1.
DR   InterPro; IPR008147; Gln_synt_beta.
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   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Ligase; Lyase;
KW   Mitochondrion; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    373       Glutamine synthetase.
FT                                /FTId=PRO_0000153144.
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
//
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