Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P16580 (GLNA_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate decarboxylase
EC=4.1.1.15
Glutamate--ammonia ligase
p42
Gene names
Name:GLUL
Synonyms:GLNS
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.6

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine. Ref.6

L-glutamate = 4-aminobutanoate + CO2. Ref.6

Cofactor

Biotin. Ref.5 Ref.6

Magnesium or manganese. Ref.5 Ref.6

Enzyme regulation

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. Ref.6

Subunit structure

Homooctamer and homotetramer. Ref.6

Subcellular location

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. Ref.4 Ref.5

Tissue specificity

Expressed in retina, brain and liver. Little or no detectable expression in breast muscle, pancreas and spleen. Ref.2

Developmental stage

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). Ref.5

Induction

In the retina, down-regulated upon application of glutamate concentrations of 15 µmol/eye or higher. Ref.5 Ref.6

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373Glutamine synthetase
PRO_0000153144

Sequences

Sequence LengthMass (Da)Tools
P16580 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 505254A25E8733DB

FASTA37342,146
        10         20         30         40         50         60 
MATSASSHLS KAIKHMYMKL PQGEKVQAMY IWIDGTGEHL RCKTRTLDHE PKSLEDLPEW 

        70         80         90        100        110        120 
NFDGSSTFQA EGSNSDMYLR PAAMFRDPFR KDPNKLVLCE VFKYNRQSAD TNLRHTCRRI 

       130        140        150        160        170        180 
MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP SNCFPGPQGP YYCGVGADKA YGRDIVEAHY 

       190        200        210        220        230        240 
RACLYAGVKI GGTNAEVMPA QWEFQVGPCE GIEMGDHLWI ARFILHRVCE DFGVIVSFDP 

       250        260        270        280        290        300 
KPIPGNWNGA GCHTNFSTKN MREDGGLKHI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL 

       310        320        330        340        350        360 
TGFHETSSIH EFSAGVANRG ASIRIPRNVG HEKKGYFEDR GPSANCDPYA VTEALVRTCL 

       370 
LNETGDEPFE YKN 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M29076 mRNA. Translation: AAA48783.1.
S45408 mRNA. Translation: AAC69361.1.
EU369427 Genomic DNA. Translation: ABY71840.1.
PIRAJCHQ. JQ0025.
RefSeqNP_990824.1. NM_205493.1.
UniGeneGga.2464.

3D structure databases

ProteinModelPortalP16580.
SMRP16580. Positions 3-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676736. 1 interaction.
IntActP16580. 1 interaction.
STRING9031.ENSGALP00000005819.

Proteomic databases

PaxDbP16580.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396489.
KEGGgga:396489.

Organism-specific databases

CTD2752.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
HOVERGENHBG005847.
InParanoidP16580.
KOK01915.
PhylomeDBP16580.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. 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]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816528.
PROP16580.

Entry information

Entry nameGLNA_CHICK
AccessionPrimary (citable) accession number: P16580
Secondary accession number(s): B0FZC2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families