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Protein

Glutamine synthetase

Gene

GLUL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner. When expressed in liver, it may be involved in detoxifying intramitochondrially generated ammonia.2 Publications

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.1 Publication
L-glutamate = 4-aminobutanoate + CO2.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Glutamate to glutamine ratio influences catalytic activity. At glutamate to glutamine ratios greater than 4, decarboxylase activity ceases. In the presence of manganese, synthetase activity is limited to concentrations between 10 mM and 20 mM, whereas decarboxylase activity is not affected. Both catalytic activities are inhibited by avidin.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
p42
Gene namesi
Name:GLUL
Synonyms:GLNS
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

  • Cytoplasm
  • Mitochondrion

  • Note: In the liver found in mitochondria, in brain and retina in the cytoplasm. In retinal cells found in the outer part of the inner nuclear layer and in the bacillary layer of the photoreceptor, and is probably associated with the cell membrane.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Glutamine synthetasePRO_0000153144Add
BLAST

Proteomic databases

PaxDbiP16580.

Expressioni

Tissue specificityi

Expressed in retina, brain and liver. Little or no detectable expression in breast muscle, pancreas and spleen.1 Publication

Developmental stagei

Weakly expressed in retina on embryonic day 18, with levels increasing until day 6 after hatching and then remaining high until day 21 (at protein level).1 Publication

Inductioni

In the retina, down-regulated upon application of glutamate concentrations of 15 µmol/eye or higher.1 Publication

Interactioni

Subunit structurei

Homooctamer and homotetramer.1 Publication

Protein-protein interaction databases

BioGridi676736. 1 interaction.
IntActiP16580. 1 interaction.
STRINGi9031.ENSGALP00000005819.

Structurei

3D structure databases

ProteinModelPortaliP16580.
SMRiP16580. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiP16580.
KOiK01915.
PhylomeDBiP16580.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16580-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSASSHLS KAIKHMYMKL PQGEKVQAMY IWIDGTGEHL RCKTRTLDHE
60 70 80 90 100
PKSLEDLPEW NFDGSSTFQA EGSNSDMYLR PAAMFRDPFR KDPNKLVLCE
110 120 130 140 150
VFKYNRQSAD TNLRHTCRRI MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP
160 170 180 190 200
SNCFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGVKI GGTNAEVMPA
210 220 230 240 250
QWEFQVGPCE GIEMGDHLWI ARFILHRVCE DFGVIVSFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKN MREDGGLKHI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSSIH EFSAGVANRG ASIRIPRNVG HEKKGYFEDR GPSANCDPYA
360 370
VTEALVRTCL LNETGDEPFE YKN
Length:373
Mass (Da):42,146
Last modified:August 1, 1990 - v1
Checksum:i505254A25E8733DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29076 mRNA. Translation: AAA48783.1.
S45408 mRNA. Translation: AAC69361.1.
EU369427 Genomic DNA. Translation: ABY71840.1.
PIRiJQ0025. AJCHQ.
RefSeqiNP_990824.1. NM_205493.1.
UniGeneiGga.2464.

Genome annotation databases

GeneIDi396489.
KEGGigga:396489.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29076 mRNA. Translation: AAA48783.1.
S45408 mRNA. Translation: AAC69361.1.
EU369427 Genomic DNA. Translation: ABY71840.1.
PIRiJQ0025. AJCHQ.
RefSeqiNP_990824.1. NM_205493.1.
UniGeneiGga.2464.

3D structure databases

ProteinModelPortaliP16580.
SMRiP16580. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676736. 1 interaction.
IntActiP16580. 1 interaction.
STRINGi9031.ENSGALP00000005819.

Proteomic databases

PaxDbiP16580.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396489.
KEGGigga:396489.

Organism-specific databases

CTDi2752.

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiP16580.
KOiK01915.
PhylomeDBiP16580.

Miscellaneous databases

NextBioi20816528.
PROiP16580.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The structure of the chicken glutamine synthetase-encoding gene."
    Pu H., Young A.P.
    Gene 81:169-175(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Metabolic compartmentation of vertebrate glutamine synthetase: putative mitochondrial targeting signal in avian liver glutamine synthetase."
    Campbell J.W., Smith D.D. Jr.
    Mol. Biol. Evol. 9:787-805(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Liver.
  3. "Evolution of mitochondrial targeting mechanisms: tissue-specific subcellular localization of glutamine synthetase."
    Matthews G.D., Gur N., Pines O., Vardimon L.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
  4. "Glutamine synthetase. A mitochondrial enzyme in uricotelic species."
    Vorhaben J.E., Campbell J.W.
    J. Biol. Chem. 247:2763-2767(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "A non-mitochondrial carboxylase, related to glutamate action is synthesized in the retina of the chick embryo."
    Sattayasai N., Sattayasai J., Daduang S., Chahomchuen T., Ketkaew S., Puchongkavarin H.
    J. Neuroimmunol. 141:104-111(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
  6. "A biotin-coupled bifunctional enzyme exhibiting both glutamine synthetase activity and glutamate decarboxylase activity."
    Arunchaipong K., Sattayasai N., Sattayasai J., Svasti J., Rimlumduan T.
    Curr. Eye Res. 34:809-818(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, SUBUNIT.

Entry informationi

Entry nameiGLNA_CHICK
AccessioniPrimary (citable) accession number: P16580
Secondary accession number(s): B0FZC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 1, 2015
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.