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Protein

Glutamine synthetase

Gene

GLUL

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential for proliferation of fetal skin fibroblasts. 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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.2. 1153.
ReactomeiR-CFA-210455. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
R-CFA-70614. Amino acid synthesis and interconversion (transamination).
SABIO-RKQ8HZM5.

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
Gene namesi
Name:GLUL
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Chromosome 7

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001531372 – 373Glutamine synthetaseAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei104PhosphotyrosineBy similarity1
Modified residuei343PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ8HZM5.
PRIDEiQ8HZM5.

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD (By similarity).By similarity

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000032533.

Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Helixi11 – 18Combined sources8
Beta strandi26 – 33Combined sources8
Beta strandi40 – 49Combined sources10
Helixi54 – 56Combined sources3
Beta strandi60 – 63Combined sources4
Helixi64 – 67Combined sources4
Beta strandi76 – 86Combined sources11
Turni88 – 90Combined sources3
Beta strandi95 – 102Combined sources8
Helixi114 – 122Combined sources9
Helixi123 – 127Combined sources5
Beta strandi130 – 140Combined sources11
Beta strandi144 – 146Combined sources3
Beta strandi158 – 160Combined sources3
Turni167 – 169Combined sources3
Helixi173 – 186Combined sources14
Beta strandi190 – 195Combined sources6
Beta strandi201 – 210Combined sources10
Helixi213 – 232Combined sources20
Beta strandi235 – 237Combined sources3
Beta strandi245 – 247Combined sources3
Beta strandi251 – 257Combined sources7
Helixi259 – 262Combined sources4
Turni264 – 266Combined sources3
Helixi267 – 278Combined sources12
Helixi281 – 287Combined sources7
Turni290 – 295Combined sources6
Helixi296 – 298Combined sources3
Turni303 – 305Combined sources3
Beta strandi314 – 316Combined sources3
Beta strandi321 – 325Combined sources5
Helixi327 – 332Combined sources6
Beta strandi337 – 339Combined sources3
Helixi348 – 359Combined sources12
Beta strandi365 – 367Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UU7X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-373[»]
ProteinModelPortaliQ8HZM5.
SMRiQ8HZM5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8HZM5.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiKOG0683. Eukaryota.
COG0174. LUCA.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiQ8HZM5.
KOiK01915.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_b-grasp.
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]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8HZM5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE
60 70 80 90 100
PKGVEELPEW NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE
110 120 130 140 150
VFKYNRKPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI AGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLKYI EESIEKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPFS
360 370
VTEALIRTCL LNETGDEPFQ YKN
Length:373
Mass (Da):42,028
Last modified:January 23, 2007 - v3
Checksum:iE5AD18AEED3F0C52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF544242 mRNA. Translation: AAN41001.1.
AF544243 Genomic DNA. Translation: AAN41002.1.
RefSeqiNP_001002965.2. NM_001002965.2.
NP_001280153.1. NM_001293224.1.
UniGeneiCfa.1407.

Genome annotation databases

EnsembliENSCAFT00000020795; ENSCAFP00000019307; ENSCAFG00000013102.
GeneIDi403443.
KEGGicfa:403443.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF544242 mRNA. Translation: AAN41001.1.
AF544243 Genomic DNA. Translation: AAN41002.1.
RefSeqiNP_001002965.2. NM_001002965.2.
NP_001280153.1. NM_001293224.1.
UniGeneiCfa.1407.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UU7X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-373[»]
ProteinModelPortaliQ8HZM5.
SMRiQ8HZM5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000032533.

Proteomic databases

PaxDbiQ8HZM5.
PRIDEiQ8HZM5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCAFT00000020795; ENSCAFP00000019307; ENSCAFG00000013102.
GeneIDi403443.
KEGGicfa:403443.

Organism-specific databases

CTDi2752.

Phylogenomic databases

eggNOGiKOG0683. Eukaryota.
COG0174. LUCA.
GeneTreeiENSGT00390000010047.
HOGENOMiHOG000061500.
HOVERGENiHBG005847.
InParanoidiQ8HZM5.
KOiK01915.

Enzyme and pathway databases

BRENDAi6.3.1.2. 1153.
ReactomeiR-CFA-210455. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
R-CFA-70614. Amino acid synthesis and interconversion (transamination).
SABIO-RKQ8HZM5.

Miscellaneous databases

EvolutionaryTraceiQ8HZM5.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_b-grasp.
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]
SMARTiSM01230. Gln-synt_C. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLNA_CANLF
AccessioniPrimary (citable) accession number: Q8HZM5
Secondary accession number(s): Q8HZM4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 94 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.