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P19904 (GLNA_VIBAL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 72. 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

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
OrganismVibrio alginolyticus
Taxonomic identifier663 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

Subunit structure

Oligomer of 12 subunits arranged in the form of two hexagons.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

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 – 468468Glutamine synthetase
PRO_0000153275

Amino acid modifications

Modified residue3971O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P19904 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: ABB66AA9C072D856

FASTA46851,556
        10         20         30         40         50         60 
MSVEKVLSLI QENEVKFVDL RFTDTKGKEQ HISIPAHQID ADFFEEGKMF DGSSVAGWKG 

        70         80         90        100        110        120 
INESDMVMMP DASSAVLDPF TEDATLNIRC DILEPATMQG YDRDPRSIAK RAEDFMRSTG 

       130        140        150        160        170        180 
VADTVLIGPE PEFFLFDDVK FATDMSGSFF KIDDVEAAWN TGSDYEEGNK GHRPGVKGGY 

       190        200        210        220        230        240 
FPVAPVDSSQ DIRSAMCLVM EEMGLVVEAH HHEATAGQNE IATRFNTLTT KADEIQIYKY 

       250        260        270        280        290        300 
VVHNVAHAFG KTATFMPKPL VGDNGSGMHV HQSLAKDGVN LFAGDKYGGL SEMALYYIGG 

       310        320        330        340        350        360 
IIKHARAINA FANPSTNSYK RLVPGFEAPV MLAYSARNRS ASIRIPVVPS PKARRIEVRF 

       370        380        390        400        410        420 
GDPAANPYLC FASMLMAGLD GIKNKIHPGE AMDKDLYDLP AEESAEIPTV AYSLKDALAE 

       430        440        450        460 
LDADREFLTA GGVFSDDFID SYIELKSQDV ERVNMTTHPV EFELYYSV 

« Hide

References

[1]"Nucleotide sequence of the Vibrio alginolyticus glnA region."
Maharaj R., Rumbak E., Jones W.A., Robb S.M., Robb F.T., Woods D.R.
Arch. Microbiol. 152:542-549(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L08499 Genomic DNA. Translation: AAA27523.1.
PIRAJVCQA. JL0113.

3D structure databases

ProteinModelPortalP19904.
SMRP19904. Positions 2-468.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP19904.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_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.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_VIBAL
AccessionPrimary (citable) accession number: P19904
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: October 16, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families