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P0A9C5

- GLNA_ECOLI

UniProt

P0A9C5 - GLNA_ECOLI

Protein

Glutamine synthetase

Gene

glnA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10383. glnA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000005157.
    KOiK01915.
    OMAiDMLLMPI.
    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

    MSAEHVLTML NEHEVKFVDL RFTDTKGKEQ HVTIPAHQVN AEFFEEGKMF    50
    DGSSIGGWKG INESDMVLMP DASTAVIDPF FADSTLIIRC DILEPGTLQG 100
    YDRDPRSIAK RAEDYLRSTG IADTVLFGPE PEFFLFDDIR FGSSISGSHV 150
    AIDDIEGAWN SSTQYEGGNK GHRPAVKGGY FPVPPVDSAQ DIRSEMCLVM 200
    EQMGLVVEAH HHEVATAGQN EVATRFNTMT KKADEIQIYK YVVHNVAHRF 250
    GKTATFMPKP MFGDNGSGMH CHMSLSKNGV NLFAGDKYAG LSEQALYYIG 300
    GVIKHAKAIN ALANPTTNSY KRLVPGYEAP VMLAYSARNR SASIRIPVVS 350
    SPKARRIEVR FPDPAANPYL CFAALLMAGL DGIKNKIHPG EAMDKNLYDL 400
    PPEEAKEIPQ VAGSLEEALN ELDLDREFLK AGGVFTDEAI DAYIALRREE 450
    DDRVRMTPHP VEFELYYSV 469
    Length:469
    Mass (Da):51,904
    Last modified:January 23, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi S40815. AJECQ.
    RefSeqi NP_418306.1. NC_000913.3.
    YP_491580.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A9C5.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9777N.
    IntActi P0A9C5. 10 interactions.
    STRINGi 511145.b3870.

    Chemistry

    BindingDBi P0A9C5.
    ChEMBLi CHEMBL3789.

    2D gel databases

    SWISS-2DPAGE P0A9C5.

    Proteomic databases

    PaxDbi P0A9C5.
    PRIDEi P0A9C5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC76867 ; AAC76867 ; b3870 .
    BAE77439 ; BAE77439 ; BAE77439 .
    GeneIDi 12933636.
    948370.
    KEGGi ecj:Y75_p3316.
    eco:b3870.
    PATRICi 32123243. VBIEscCol129921_3982.

    Organism-specific databases

    EchoBASEi EB0378.
    EcoGenei EG10383. glnA.

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000005157.
    KOi K01915.
    OMAi DMLLMPI.
    OrthoDBi EOG6B360N.
    PhylomeDBi P0A9C5.

    Enzyme and pathway databases

    BioCyci EcoCyc:GLUTAMINESYN-MONOMER.
    ECOL316407:JW3841-MONOMER.
    MetaCyc:GLUTAMINESYN-MONOMER.
    SABIO-RK P0A9C5.

    Miscellaneous databases

    PROi P0A9C5.

    Gene expression databases

    Genevestigatori P0A9C5.

    Family and domain databases

    Gene3Di 3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR008147. 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 ]
    Pfami PF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54368. SSF54368. 1 hit.
    TIGRFAMsi TIGR00653. GlnA. 1 hit.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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, 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(1970) [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(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.

    Entry informationi

    Entry nameiGLNA_ECOLI
    AccessioniPrimary (citable) accession number: P0A9C5
    Secondary accession number(s): P06711, Q2M8G7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 85 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