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

O27612 (GLNA_METTH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 84. 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--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:MTH_1570
OrganismMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum) [Reference proteome] [HAMAP]
Taxonomic identifier187420 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length442 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.

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
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 – 442442Glutamine synthetase
PRO_0000153206

Amino acid modifications

Modified residue3721O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
O27612 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: B907928AAD8960A6

FASTA44250,248
        10         20         30         40         50         60 
MSDKIGRIIA KMDECGVKFV RLQFVDIHGK PKNMAIPLVR PDQIEDIIKD GLLFDGSSVE 

        70         80         90        100        110        120 
GFVDINESDL VLKPDPDTFS TLPWRPEEKG VCRFICDIYW PDGKPFEGDP RYVLKRALDK 

       130        140        150        160        170        180 
YAHLGYEYNV GPEPEFFILD QDEDGNIIPH DCGAYFDVEP VDQGTDFRRK LVMDLEALNF 

       190        200        210        220        230        240 
DVEVSHHEVA PGQHEIDFKF DKALKTADAV ITFKQAIKAI VDKIGYMVTF MPKPFFGENG 

       250        260        270        280        290        300 
SGMHCHQSLF KDGENVFYDP DTETQLSEEA LYFIGGLLKH APALTAVCAP TVNSYKRLVP 

       310        320        330        340        350        360 
GYEAPVYIAY GLKNRSTLIR IPASRGKGTR VELRMPDPSC NPYLAFAAML EAGMNGIQNK 

       370        380        390        400        410        420 
IDPGEPTEID VYEKSMSELR EMGIETLPSS LWEAYHALEE DDVIKGALGG HVYEKFMEIK 

       430        440 
HREWDDYRVR VFKYELERYL DI 

« Hide

References

[1]"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics."
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. expand/collapse author list , Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.
J. Bacteriol. 179:7135-7155(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000666 Genomic DNA. Translation: AAB86044.1.
PIRF69076.
RefSeqNP_276683.1. NC_000916.1.

3D structure databases

ProteinModelPortalO27612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING187420.MTH1570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB86044; AAB86044; MTH_1570.
GeneID1471839.
KEGGmth:MTH1570.

Phylogenomic databases

eggNOGCOG0174.
KOK01915.
OMAAYKIQLK.

Enzyme and pathway databases

BioCycMTHE187420:GJNM-1572-MONOMER.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_METTH
AccessionPrimary (citable) accession number: O27612
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: May 14, 2014
This is version 84 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