P16580 (GLNA_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate decarboxylase activity Inferred from electronic annotation. Source: EC glutamate-ammonia ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 373	373	Glutamine synthetase		PRO_0000153144

Sequences

	Sequence		Length	Mass (Da)
	P16580 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 505254A25E8733DB	FASTA	373	42,146
	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

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.
IPI	IPI00587415.
PIR	AJCHQ. JQ0025.
RefSeq	NP_990824.1. NM_205493.1.
UniGene	Gga.2464.
3D structure databases
ProteinModelPortal	P16580.
SMR	P16580. Positions 3-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	P16580. 1 interaction.
STRING	9031.ENSGALP00000005819.
Proteomic databases
PaxDb	P16580.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	396489.
KEGG	gga:396489.
Organism-specific databases
CTD	2752.
Phylogenomic databases
eggNOG	COG0174.
HOGENOM	HOG000061500.
HOVERGEN	HBG005847.
InParanoid	P16580.
KO	K01915.
OrthoDB	EOG444KKD.
Family and domain databases
Gene3D	3.30.590.10. 1 hit.
InterPro	IPR008147. 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]
Pfam	PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit. [Graphical view]
SUPFAM	SSF54368. Gln_synt_beta. 1 hit.
PROSITE	PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20816528.

Entry information

Entry name

GLNA_CHICK

Accession

Primary (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:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program