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Protein

Glutaminase 1

Gene

glsA1

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

Functioni

Catalytic activityi

L-glutamine + H2O = L-glutamate + NH3.UniRule annotation1 Publication

Kineticsi

  1. KM=7.3 mM for glutamine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei66 – 661SubstrateUniRule annotation
    Binding sitei117 – 1171SubstrateUniRule annotation
    Binding sitei161 – 1611SubstrateUniRule annotation
    Binding sitei168 – 1681SubstrateUniRule annotation
    Binding sitei192 – 1921SubstrateUniRule annotation
    Binding sitei244 – 2441SubstrateUniRule annotation
    Binding sitei262 – 2621Substrate; via amide nitrogenUniRule annotation

    GO - Molecular functioni

    • glutaminase activity Source: EcoCyc

    GO - Biological processi

    • glutamine metabolic process Source: InterPro
    • negative regulation of growth Source: EcoliWiki
    • response to acidic pH Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6261-MONOMER.
    ECOL316407:JW0474-MONOMER.
    MetaCyc:G6261-MONOMER.
    BRENDAi3.5.1.2. 2026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutaminase 1UniRule annotation (EC:3.5.1.2UniRule annotation)
    Gene namesi
    Name:glsA1UniRule annotation
    Synonyms:ybaS
    Ordered Locus Names:b0485, JW0474
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13247. glsA1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691K → A: Loss of activity. 1 Publication
    Mutagenesisi117 – 1171N → A: Loss of activity. 1 Publication
    Mutagenesisi160 – 1601S → A: Loss of activity. 1 Publication
    Mutagenesisi161 – 1611E → A: Strongly reduced activity. 1 Publication
    Mutagenesisi162 – 1621Q → A: No effect. 1 Publication
    Mutagenesisi168 – 1681N → A: Loss of activity. 1 Publication
    Mutagenesisi192 – 1921Y → A: Loss of activity. 1 Publication
    Mutagenesisi244 – 2441Y → A: Loss of activity. 1 Publication
    Mutagenesisi260 – 2601S → A: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 310310Glutaminase 1PRO_0000110607Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei294 – 2941N6-acetyllysineUniRule annotation1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP77454.
    PRIDEiP77454.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation1 Publication

    Protein-protein interaction databases

    DIPiDIP-11307N.
    IntActiP77454. 2 interactions.
    STRINGi511145.b0485.

    Structurei

    Secondary structure

    1
    310
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1815Combined sources
    Helixi31 – 344Combined sources
    Beta strandi42 – 476Combined sources
    Beta strandi52 – 576Combined sources
    Helixi65 – 673Combined sources
    Helixi68 – 8013Combined sources
    Helixi82 – 887Combined sources
    Helixi101 – 1066Combined sources
    Turni107 – 1093Combined sources
    Helixi117 – 12610Combined sources
    Helixi132 – 14716Combined sources
    Helixi155 – 1628Combined sources
    Helixi166 – 17813Combined sources
    Helixi185 – 19511Combined sources
    Beta strandi198 – 2003Combined sources
    Helixi202 – 21312Combined sources
    Beta strandi216 – 2183Combined sources
    Turni219 – 2224Combined sources
    Helixi228 – 2303Combined sources
    Helixi231 – 24111Combined sources
    Helixi244 – 2463Combined sources
    Helixi247 – 2537Combined sources
    Beta strandi258 – 2603Combined sources
    Beta strandi264 – 2707Combined sources
    Turni271 – 2733Combined sources
    Beta strandi274 – 2796Combined sources
    Helixi290 – 30314Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U60X-ray1.61A/B/C/D1-310[»]
    ProteinModelPortaliP77454.
    SMRiP77454. Positions 2-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP77454.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutaminase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216890.
    InParanoidiP77454.
    KOiK01425.
    OMAiPMNPMVN.
    OrthoDBiEOG6N94BK.
    PhylomeDBiP77454.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    HAMAPiMF_00313. Glutaminase.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view]
    PANTHERiPTHR12544. PTHR12544. 1 hit.
    PfamiPF04960. Glutaminase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    TIGRFAMsiTIGR03814. Gln_ase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P77454-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG
    60 70 80 90 100
    NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS
    110 120 130 140 150
    VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ
    160 170 180 190 200
    VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL
    210 220 230 240 250
    NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW
    260 270 280 290 300
    AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA
    310
    KQLGYNVFKG
    Length:310
    Mass (Da):32,903
    Last modified:February 1, 1997 - v1
    Checksum:i4448BA0549E3C851
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82664 Genomic DNA. Translation: AAB40239.1.
    U00096 Genomic DNA. Translation: AAC73587.1.
    AP009048 Genomic DNA. Translation: BAE76264.1.
    PIRiD64779.
    RefSeqiNP_415018.1. NC_000913.3.
    WP_000883034.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73587; AAC73587; b0485.
    BAE76264; BAE76264; BAE76264.
    GeneIDi946187.
    KEGGieco:b0485.
    PATRICi32116129. VBIEscCol129921_0506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U82664 Genomic DNA. Translation: AAB40239.1.
    U00096 Genomic DNA. Translation: AAC73587.1.
    AP009048 Genomic DNA. Translation: BAE76264.1.
    PIRiD64779.
    RefSeqiNP_415018.1. NC_000913.3.
    WP_000883034.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U60X-ray1.61A/B/C/D1-310[»]
    ProteinModelPortaliP77454.
    SMRiP77454. Positions 2-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-11307N.
    IntActiP77454. 2 interactions.
    STRINGi511145.b0485.

    Proteomic databases

    PaxDbiP77454.
    PRIDEiP77454.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73587; AAC73587; b0485.
    BAE76264; BAE76264; BAE76264.
    GeneIDi946187.
    KEGGieco:b0485.
    PATRICi32116129. VBIEscCol129921_0506.

    Organism-specific databases

    EchoBASEiEB3036.
    EcoGeneiEG13247. glsA1.

    Phylogenomic databases

    eggNOGiCOG2066.
    HOGENOMiHOG000216890.
    InParanoidiP77454.
    KOiK01425.
    OMAiPMNPMVN.
    OrthoDBiEOG6N94BK.
    PhylomeDBiP77454.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6261-MONOMER.
    ECOL316407:JW0474-MONOMER.
    MetaCyc:G6261-MONOMER.
    BRENDAi3.5.1.2. 2026.

    Miscellaneous databases

    EvolutionaryTraceiP77454.
    PROiP77454.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    HAMAPiMF_00313. Glutaminase.
    InterProiIPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view]
    PANTHERiPTHR12544. PTHR12544. 1 hit.
    PfamiPF04960. Glutaminase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    TIGRFAMsiTIGR03814. Gln_ase. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    5. "Functional and structural characterization of four glutaminases from Escherichia coli and Bacillus subtilis."
      Brown G., Singer A., Proudfoot M., Skarina T., Kim Y., Chang C., Dementieva I., Kuznetsova E., Gonzalez C.F., Joachimiak A., Savchenko A., Yakunin A.F.
      Biochemistry 47:5724-5735(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.61 ANGSTROMS), CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-69; ASN-117; SER-160; GLU-161; GLN-162; ASN-168; TYR-192; TYR-244 AND SER-260, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiGLSA1_ECOLI
    AccessioniPrimary (citable) accession number: P77454
    Secondary accession number(s): Q2MBU2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: July 22, 2015
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.