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P33035 (GLNA_MICDP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 70. 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
OrganismMicrochaete diplosiphon (Fremyella diplosiphon)
Taxonomic identifier1197 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesMicrochaetaceaeMicrochaete

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

Initiator methionine11Removed By similarity
Chain2 – 471470Glutamine synthetase
PRO_0000153216

Amino acid modifications

Modified residue3991O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P33035 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4216D115B6EC7310

FASTA47153,050
        10         20         30         40         50         60 
MTTPQEVLKL IQDQKIQMID LKFIDTPGTW QHLTVYYNQI DESSFTDGVP FDGSSIRGWK 

        70         80         90        100        110        120 
GIEESDMTMV LDPNTAWIDP FMKEPTLSII CSIKEPRTGE WYNRCPRVIA QKAIDYLVST 

       130        140        150        160        170        180 
GLGDTAFFGP EAEFFIFDDA RFDQTANSGY YYVDSVEGRW NSGKDEGPNL AYKPRFKEGY 

       190        200        210        220        230        240 
FPVAPTDTFQ DMRTEMLLTM AACGVPIEKQ HHEVATGGQC ELGFRFGKLI EAADWLMTYK 

       250        260        270        280        290        300 
YVIKNVAKKY GRTVTFMPKP IFGDNGSGMH CHQSIWKDGK PLFGGDKYAG LSDMALYYIG 

       310        320        330        340        350        360 
GILKHAPALL GITNPTTNSY KRLVPGYEAP VNLAYSQGNR SASVRIPLSG TNPKAKRLEF 

       370        380        390        400        410        420 
RCPDATSNPY LAFAAMLCAG IDGIKNKIHP GEPLDRNIYE LSPEELAKVP STPGSLELAL 

       430        440        450        460        470 
EALENDHAFL TESGVFTEDF IQNWIEYKLV NEVKQLQLRP HPYEFYLYYD C 

« Hide

References

[1]"Molecular characterization of the gene encoding glutamine synthetase in the cyanobacterium Calothrix sp. PCC 7601."
Elmorjani K., Liotenberg S., Houmard J., de Marsac N.T.
Biochem. Biophys. Res. Commun. 189:1296-1302(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L05609 Genomic DNA. Translation: AAA23288.1.

3D structure databases

ProteinModelPortalP33035.
SMRP33035. Positions 2-470.
ModBaseSearch...
MobiDBSearch...

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_MICDP
AccessionPrimary (citable) accession number: P33035
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 70 of the entry and version 2 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