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

P0A9C5 (GLNA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Ordered Locus Names:b3870, JW3841
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subunit structure

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutamine synthetase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-909063,EBI-909063

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 469468Glutamine synthetase
PRO_0000153235

Amino acid modifications

Modified residue3981O-AMP-tyrosine

Experimental info

Sequence conflict901C → S in AAA23879. Ref.2
Sequence conflict108 – 1092IA → MS in AAA23879. Ref.2
Sequence conflict1971C → S in AAA23879. Ref.2
Sequence conflict2281T → I in CAA28806. Ref.1
Sequence conflict247 – 2482AH → VRN in CAA28806. Ref.1
Sequence conflict305 – 3062HA → QP in CAA28806. Ref.1
Sequence conflict394 – 3952DK → KD AA sequence Ref.10
Sequence conflict394 – 3952DK → KD AA sequence Ref.11

Sequences

Sequence LengthMass (Da)Tools
P0A9C5 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0AFC05724CDEBA36

FASTA46951,904
        10         20         30         40         50         60 
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF DGSSIGGWKG 

        70         80         90        100        110        120 
INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG YDRDPRSIAK RAEDYLRSTG 

       130        140        150        160        170        180 
IADTVLFGPE PEFFLFDDIR FGSSISGSHV AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY 

       190        200        210        220        230        240 
FPVPPVDSAQ DIRSEMCLVM EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK 

       250        260        270        280        290        300 
YVVHNVAHRF GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG 

       310        320        330        340        350        360 
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS SPKARRIEVR 

       370        380        390        400        410        420 
FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL PPEEAKEIPQ VAGSLEEALN 

       430        440        450        460 
ELDLDREFLK AGGVFTDEAI DAYIALRREE DDRVRMTPHP VEFELYYSV 

« Hide

References

« Hide 'large scale' references
[1]"The complete nucleotide sequence of the glnALG operon of Escherichia coli K12."
Miranda-Rios J., Sanchez-Pescador R., Urdea M., Covarrubias A.A.
Nucleic Acids Res. 15:2757-2770(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Amino acid sequence of Escherichia coli glutamine synthetase deduced from the DNA nucleotide sequence."
Colombo G., Villafranca J.J.
J. Biol. Chem. 261:10587-10591(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Nucleotide sequence of the glnA control region of Escherichia coli."
Covarrubias A.A., Bastarrachea F.
Mol. Gen. Genet. 190:171-175(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
[7]"Expression of glnA in Escherichia coli is regulated at tandem promoters."
Reitzer L.J., Magasanik B.
Proc. Natl. Acad. Sci. U.S.A. 82:1979-1983(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-12.
Strain: K12 / EMG2.
[9]"Nucleotide sequence of the glnA-glnL intercistronic region of Escherichia coli."
Rocha M., Vazquez M., Garciarrubio A., Covarrubias A.A.
Gene 37:91-99(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 363-469.
[10]"Primary structure of Escherichia coli glutamine synthetase. II. The complete amino acid sequence of a tryptic heneicosapeptide containing covalently bound adenylic acid."
Heinrikson R.L., Kingdon H.S.
J. Biol. Chem. 246:1099-1106(1971) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 387-406, SEQUENCE REVISION, AMP-BINDING AT TYR-398.
[11]"The amino acid sequence in the vicinity of the covalently bound adenylic acid in glutamine synthetase from Escherichia coli."
Heinrikson R.L., Kingdon H.S.
J. Biol. Chem. 245:138-142(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 394-406, AMP-BINDING.
[12]"Identification and regulation of the glnL operator-promoter of the complex glnALG operon of Escherichia coli."
Ueno-Nishio S., Mango S., Reitzer L.J., Magasanik B.
J. Bacteriol. 160:379-384(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-469.
[13]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05173 Genomic DNA. Translation: CAA28806.1.
M13746 Genomic DNA. Translation: AAA23879.1.
L19201 Genomic DNA. Translation: AAB03004.1.
U00096 Genomic DNA. Translation: AAC76867.1.
AP009048 Genomic DNA. Translation: BAE77439.1.
J01618 Genomic DNA. Translation: AAA98066.1.
M10421 Genomic DNA. Translation: AAA23882.1.
K02176 Genomic DNA. Translation: AAA23880.1.
PIRAJECQ. S40815.
RefSeqNP_418306.1. NC_000913.3.
YP_491580.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0A9C5.
SMRP0A9C5. Positions 2-469.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9777N.
IntActP0A9C5. 10 interactions.
STRING511145.b3870.

Chemistry

BindingDBP0A9C5.
ChEMBLCHEMBL3789.

2D gel databases

SWISS-2DPAGEP0A9C5.

Proteomic databases

PaxDbP0A9C5.
PRIDEP0A9C5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76867; AAC76867; b3870.
BAE77439; BAE77439; BAE77439.
GeneID12933636.
948370.
KEGGecj:Y75_p3316.
eco:b3870.
PATRIC32123243. VBIEscCol129921_3982.

Organism-specific databases

EchoBASEEB0378.
EcoGeneEG10383. glnA.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005157.
KOK01915.
OMARAHHEVG.
OrthoDBEOG6B360N.
PhylomeDBP0A9C5.
ProtClustDBPRK09469.

Enzyme and pathway databases

BioCycEcoCyc:GLUTAMINESYN-MONOMER.
ECOL316407:JW3841-MONOMER.
MetaCyc:GLUTAMINESYN-MONOMER.
SABIO-RKP0A9C5.

Gene expression databases

GenevestigatorP0A9C5.

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...

Other

PROP0A9C5.

Entry information

Entry nameGLNA_ECOLI
AccessionPrimary (citable) accession number: P0A9C5
Secondary accession number(s): P06711, Q2M8G7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 81 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene