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P51121 (GLNA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 65. 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
Gene names
Name:glul
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity. May play an important role in the early stages of vertebrate neural development.

Catalytic activity

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

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Biotin By similarity.

Magnesium or manganese By similarity.

Subunit structure

Homooctamer and homotetramer By similarity.

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity.

Developmental stage

Up-regulated during early neural development. Maternally transmitted and abundantly expressed in neuroectoderm-derived tissues during the gastrula and neurula stages.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Lyase
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 – 392392Glutamine synthetase
PRO_0000153146

Sequences

Sequence LengthMass (Da)Tools
P51121 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D69C175E95FA8D2F

FASTA39243,985
        10         20         30         40         50         60 
MSVSHSSRLN KGVREQYMKL PQGEKVQVTY VWIDGTGEGV RCKTRTLDQE PKTIDEIPEW 

        70         80         90        100        110        120 
NFDGSSTHQA EGSNSDMYLI PVQMFRDPFC LDPNKLVMCE VLKYNRKSAE TNLRHTCKKI 

       130        140        150        160        170        180 
MEMVNDHRPW FGMEQEYTLL GINGHPYGWP ENGFPGPQGP YYCGVGADKV YGRDVVESHY 

       190        200        210        220        230        240 
KACLYAGIKI CGTNAEVMPS QWEFQVGPCE GIDMGDHLWM ARFILHRVCE DFGVVATLDP 

       250        260        270        280        290        300 
KPMTGNWNGA GCHTNYSTES MRVEGGLKHI EDAIEKLGKR HDYHICVYDP RGGKDNSRRL 

       310        320        330        340        350        360 
TGQHETSSIH EFSAGVANRG ASIRIPRQVG QEGYGYFEDR RPAANCDPYA VTEALVRTTI 

       370        380        390 
LNETGSETKD YKNGAGFSRA IGMASPRDAA VF 

« Hide

References

[1]"Identification of a Xenopus glutamine synthetase gene abundantly expressed in the embryonic nervous system but not in adult brain."
Hatada S., Kinoshita M., Noda M., Asashima M.
FEBS Lett. 371:287-292(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D50062 mRNA. Translation: BAA08779.1.
PIRI51422.
RefSeqNP_001082548.1. NM_001089079.1.
UniGeneXl.47270.

3D structure databases

ProteinModelPortalP51121.
SMRP51121. Positions 4-372.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID398556.
KEGGxla:398556.

Organism-specific databases

CTD398556.
XenbaseXB-GENE-6256042. glul.

Phylogenomic databases

HOVERGENHBG005847.
KOK01915.

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...

Entry information

Entry nameGLNA_XENLA
AccessionPrimary (citable) accession number: P51121
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 65 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