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 01-MAY-2013, entry version 86.
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 Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC Neognathae; Galliformes; Phasianidae; 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 -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC L-glutamine.
CC -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
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 -!- SUBUNIT: Homooctamer and homotetramer.
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 -!- 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 -!- INDUCTION: In the retina, down-regulated upon application of
CC glutamate concentrations of 15 umol/eye or higher.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
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DR EMBL; M29076; AAA48783.1; -; mRNA.
DR EMBL; S45408; AAC69361.1; -; mRNA.
DR EMBL; EU369427; ABY71840.1; -; Genomic_DNA.
DR IPI; IPI00587415; -.
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 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 OrthoDB; EOG444KKD; -.
DR NextBio; 20816528; -.
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:EC.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA: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; Gln_synt_beta; 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
//
