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Protein

Glutamine synthetase

Gene

glnA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: EcoCyc
  3. identical protein binding Source: IntAct

GO - Biological processi

  1. ammonia assimilation cycle Source: EcoCyc
  2. glutamine biosynthetic process Source: InterPro
  3. nitrogen fixation Source: InterPro
  4. nitrogen utilization Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:glnA
Ordered Locus Names:b3870, JW3841
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10383. glnA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 469468Glutamine synthetasePRO_0000153235Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei398 – 3981O-AMP-tyrosine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0A9C5.
PRIDEiP0A9C5.

2D gel databases

SWISS-2DPAGEP0A9C5.

Expressioni

Gene expression databases

GenevestigatoriP0A9C5.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-909063,EBI-909063

Protein-protein interaction databases

DIPiDIP-9777N.
IntActiP0A9C5. 10 interactions.
STRINGi511145.b3870.

Structurei

3D structure databases

ProteinModelPortaliP0A9C5.
SMRiP0A9C5. Positions 2-469.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005157.
InParanoidiP0A9C5.
KOiK01915.
OMAiACFMPKP.
OrthoDBiEOG6B360N.
PhylomeDBiP0A9C5.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. 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]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF
60 70 80 90 100
DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG
110 120 130 140 150
YDRDPRSIAK RAEDYLRSTG IADTVLFGPE PEFFLFDDIR FGSSISGSHV
160 170 180 190 200
AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY FPVPPVDSAQ DIRSEMCLVM
210 220 230 240 250
EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF
260 270 280 290 300
GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG
310 320 330 340 350
GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS
360 370 380 390 400
SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL
410 420 430 440 450
PPEEAKEIPQ VAGSLEEALN ELDLDREFLK AGGVFTDEAI DAYIALRREE
460
DDRVRMTPHP VEFELYYSV
Length:469
Mass (Da):51,904
Last modified:January 22, 2007 - v2
Checksum:i0AFC05724CDEBA36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901C → S in AAA23879 (PubMed:2874141).Curated
Sequence conflicti108 – 1092IA → MS in AAA23879 (PubMed:2874141).Curated
Sequence conflicti197 – 1971C → S in AAA23879 (PubMed:2874141).Curated
Sequence conflicti228 – 2281T → I in CAA28806 (PubMed:2882477).Curated
Sequence conflicti247 – 2482AH → VRN in CAA28806 (PubMed:2882477).Curated
Sequence conflicti305 – 3062HA → QP in CAA28806 (PubMed:2882477).Curated
Sequence conflicti394 – 3952DK → KD AA sequence (PubMed:5543675).Curated
Sequence conflicti394 – 3952DK → KD AA sequence (PubMed:4904088).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS40815. AJECQ.
RefSeqiNP_418306.1. NC_000913.3.
YP_491580.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76867; AAC76867; b3870.
BAE77439; BAE77439; BAE77439.
GeneIDi12933636.
948370.
KEGGiecj:Y75_p3316.
eco:b3870.
PATRICi32123243. VBIEscCol129921_3982.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS40815. AJECQ.
RefSeqiNP_418306.1. NC_000913.3.
YP_491580.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP0A9C5.
SMRiP0A9C5. Positions 2-469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-9777N.
IntActiP0A9C5. 10 interactions.
STRINGi511145.b3870.

Chemistry

BindingDBiP0A9C5.
ChEMBLiCHEMBL3789.

2D gel databases

SWISS-2DPAGEP0A9C5.

Proteomic databases

PaxDbiP0A9C5.
PRIDEiP0A9C5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76867; AAC76867; b3870.
BAE77439; BAE77439; BAE77439.
GeneIDi12933636.
948370.
KEGGiecj:Y75_p3316.
eco:b3870.
PATRICi32123243. VBIEscCol129921_3982.

Organism-specific databases

EchoBASEiEB0378.
EcoGeneiEG10383. glnA.

Phylogenomic databases

eggNOGiCOG0174.
HOGENOMiHOG000005157.
InParanoidiP0A9C5.
KOiK01915.
OMAiACFMPKP.
OrthoDBiEOG6B360N.
PhylomeDBiP0A9C5.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP0A9C5.

Gene expression databases

GenevestigatoriP0A9C5.

Family and domain databases

Gene3Di3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProiIPR008147. 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]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
TIGRFAMsiTIGR00653. GlnA. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [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(1985) [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(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. 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(2005) [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(1982) [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(1984) [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(1996) [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(1984) [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(1970) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 387-406, SEQUENCE REVISION, AMPYLATION 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(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 394-406, AMPYLATION AT TYR-398.
  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(1983) [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(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.

Entry informationi

Entry nameiGLNA_ECOLI
AccessioniPrimary (citable) accession number: P0A9C5
Secondary accession number(s): P06711, Q2M8G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 31, 1987
Last sequence update: January 22, 2007
Last modified: January 6, 2015
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.