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P77454

- GLSA1_ECOLI

UniProt

P77454 - GLSA1_ECOLI

Protein

Glutaminase 1

Gene

glsA1

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 108 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    L-glutamine + H2O = L-glutamate + NH3.1 PublicationUniRule annotation

    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

    1. glutaminase activity Source: EcoCyc

    GO - Biological processi

    1. glutamine metabolic process Source: InterPro
    2. negative regulation of growth Source: EcoliWiki
    3. response to acidic pH Source: EcoCyc

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BioCyciEcoCyc:G6261-MONOMER.
    ECOL316407:JW0474-MONOMER.
    MetaCyc:G6261-MONOMER.

    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: Chromosome, UP000000625: 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-acetyllysine1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP77454.
    PRIDEiP77454.

    Expressioni

    Gene expression databases

    GenevestigatoriP77454.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    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 – 1815
    Helixi31 – 344
    Beta strandi42 – 476
    Beta strandi52 – 576
    Helixi65 – 673
    Helixi68 – 8013
    Helixi82 – 887
    Helixi101 – 1066
    Turni107 – 1093
    Helixi117 – 12610
    Helixi132 – 14716
    Helixi155 – 1628
    Helixi166 – 17813
    Helixi185 – 19511
    Beta strandi198 – 2003
    Helixi202 – 21312
    Beta strandi216 – 2183
    Turni219 – 2224
    Helixi228 – 2303
    Helixi231 – 24111
    Helixi244 – 2463
    Helixi247 – 2537
    Beta strandi258 – 2603
    Beta strandi264 – 2707
    Turni271 – 2733
    Beta strandi274 – 2796
    Helixi290 – 30314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01425.
    OMAiQCSVGVT.
    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

    MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG    50
    NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS 100
    VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ 150
    VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL 200
    NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW 250
    AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA 300
    KQLGYNVFKG 310
    Length:310
    Mass (Da):32,903
    Last modified:February 1, 1997 - v1
    Checksum:i4448BA0549E3C851
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_488776.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73587; AAC73587; b0485.
    BAE76264; BAE76264; BAE76264.
    GeneIDi12932991.
    946187.
    KEGGiecj:Y75_p0472.
    eco:b0485.
    PATRICi32116129. VBIEscCol129921_0506.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U82664 Genomic DNA. Translation: AAB40239.1 .
    U00096 Genomic DNA. Translation: AAC73587.1 .
    AP009048 Genomic DNA. Translation: BAE76264.1 .
    PIRi D64779.
    RefSeqi NP_415018.1. NC_000913.3.
    YP_488776.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U60 X-ray 1.61 A/B/C/D 1-310 [» ]
    ProteinModelPortali P77454.
    SMRi P77454. Positions 2-310.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11307N.
    IntActi P77454. 2 interactions.
    STRINGi 511145.b0485.

    Proteomic databases

    PaxDbi P77454.
    PRIDEi P77454.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73587 ; AAC73587 ; b0485 .
    BAE76264 ; BAE76264 ; BAE76264 .
    GeneIDi 12932991.
    946187.
    KEGGi ecj:Y75_p0472.
    eco:b0485.
    PATRICi 32116129. VBIEscCol129921_0506.

    Organism-specific databases

    EchoBASEi EB3036.
    EcoGenei EG13247. glsA1.

    Phylogenomic databases

    eggNOGi COG2066.
    HOGENOMi HOG000216890.
    KOi K01425.
    OMAi QCSVGVT.
    OrthoDBi EOG6N94BK.
    PhylomeDBi P77454.

    Enzyme and pathway databases

    BioCyci EcoCyc:G6261-MONOMER.
    ECOL316407:JW0474-MONOMER.
    MetaCyc:G6261-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P77454.
    PROi P77454.

    Gene expression databases

    Genevestigatori P77454.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    HAMAPi MF_00313. Glutaminase.
    InterProi IPR012338. Beta-lactam/transpept-like.
    IPR015868. Glutaminase.
    [Graphical view ]
    PANTHERi PTHR12544. PTHR12544. 1 hit.
    Pfami PF04960. Glutaminase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56601. SSF56601. 1 hit.
    TIGRFAMsi TIGR03814. Gln_ase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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