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C4ZS47

- NAGZ_ECOBW

UniProt

C4ZS47 - NAGZ_ECOBW

Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.UniRule annotation

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621SubstrateUniRule annotation
    Binding sitei70 – 701SubstrateUniRule annotation
    Binding sitei133 – 1331SubstrateUniRule annotation
    Sitei174 – 1741Important for catalytic activityUniRule annotation
    Active sitei176 – 1761Proton donor/acceptorUniRule annotation
    Active sitei248 – 2481NucleophileUniRule annotation

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. peptidoglycan biosynthetic process Source: UniProtKB-KW
    5. peptidoglycan turnover Source: UniProtKB-HAMAP
    6. regulation of cell shape Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

    Enzyme and pathway databases

    BioCyciECOL595496:GI18-992-MONOMER.
    UniPathwayiUPA00544.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-hexosaminidaseUniRule annotation (EC:3.2.1.52UniRule annotation)
    Alternative name(s):
    Beta-N-acetylhexosaminidaseUniRule annotation
    N-acetyl-beta-glucosaminidaseUniRule annotation
    Gene namesi
    Name:nagZUniRule annotation
    Ordered Locus Names:BWG_0955
    OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
    Taxonomic identifieri595496 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000001478: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 341341Beta-hexosaminidasePRO_1000205459Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi595496.BWG_0955.

    Structurei

    3D structure databases

    ProteinModelPortaliC4ZS47.
    SMRiC4ZS47. Positions 1-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni163 – 1642Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1472.
    HOGENOMiHOG000248526.
    KOiK01207.
    OMAiAHDIDLS.
    OrthoDBiEOG6BCT06.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    HAMAPiMF_00364. NagZ.
    InterProiIPR022956. Beta_hexosaminidase_bac.
    IPR019800. Glyco_hydro_3_AS.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF00933. Glyco_hydro_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    C4ZS47-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR    50
    AASRNRLVVA VDQEGGRVQR FREGFTRLPA AQSFAALSGM EEGGKLAQEA 100
    GWLMASEMIA MDIDISFAPV LDVGHISAAI GERSYHADPQ KALAIASRFI 150
    DGMHEAGMKT TGKHFPGHGA VTADSHKETP CDPRPQAEIR AKDMSVFSSL 200
    IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG FDGVIFSDDL 250
    SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV 300
    TRLYHKGSFS RQELMDSARW KAISTRLNQL HERWQEEKAG H 341
    Length:341
    Mass (Da):37,595
    Last modified:July 28, 2009 - v1
    Checksum:i9E50C8E4DA87C7A4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR62054.1.
    RefSeqiYP_002926157.1. NC_012759.1.

    Genome annotation databases

    EnsemblBacteriaiACR62054; ACR62054; BWG_0955.
    GeneIDi7956126.
    KEGGiebw:BWG_0955.
    PATRICi18271031. VBIEscCol60876_1052.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001396 Genomic DNA. Translation: ACR62054.1 .
    RefSeqi YP_002926157.1. NC_012759.1.

    3D structure databases

    ProteinModelPortali C4ZS47.
    SMRi C4ZS47. Positions 1-340.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 595496.BWG_0955.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACR62054 ; ACR62054 ; BWG_0955 .
    GeneIDi 7956126.
    KEGGi ebw:BWG_0955.
    PATRICi 18271031. VBIEscCol60876_1052.

    Phylogenomic databases

    eggNOGi COG1472.
    HOGENOMi HOG000248526.
    KOi K01207.
    OMAi AHDIDLS.
    OrthoDBi EOG6BCT06.

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    BioCyci ECOL595496:GI18-992-MONOMER.

    Family and domain databases

    Gene3Di 3.20.20.300. 1 hit.
    HAMAPi MF_00364. NagZ.
    InterProi IPR022956. Beta_hexosaminidase_bac.
    IPR019800. Glyco_hydro_3_AS.
    IPR001764. Glyco_hydro_3_N.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF00933. Glyco_hydro_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
      Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
      J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MC4100 / BW2952.

    Entry informationi

    Entry nameiNAGZ_ECOBW
    AccessioniPrimary (citable) accession number: C4ZS47
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 36 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

    Complete proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3