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P96157

- NAGZ_VIBFU

UniProt

P96157 - NAGZ_VIBFU

Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Vibrio furnissii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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 By similarity. Hydrolyzes rapidly p-nitrophenyl-N-acetyl-beta-D-glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and slightly active on p-nitrophenyl-beta-GalNAc. May play a role in signal transduction between host and organism.1 PublicationUniRule annotation

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 PublicationUniRule annotation

    Enzyme regulationi

    Inhibited by GlcNAc, 2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glucopyranosylamine (GlcNAc-Asn) and O-(2-acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate (PUGNAc).1 Publication

    pH dependencei

    Optimum pH is 7.0.1 Publication

    Temperature dependencei

    Optimum temperature is 45 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621SubstrateUniRule annotation
    Binding sitei70 – 701SubstrateUniRule annotation
    Binding sitei130 – 1301SubstrateUniRule annotation
    Sitei171 – 1711Important for catalytic activityUniRule annotation
    Active sitei173 – 1731Proton donor/acceptorUniRule annotation
    Active sitei242 – 2421NucleophileUniRule 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

    SABIO-RKP96157.
    UniPathwayiUPA00544.

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    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
    Synonyms:exo II
    OrganismiVibrio furnissii
    Taxonomic identifieri29494 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

    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 – 329329Beta-hexosaminidasePRO_0000210801Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliP96157.
    SMRiP96157. Positions 1-329.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni160 – 1612Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    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.

    P96157-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPLWLDVEG CELTAEDREI LAHPTVGGVI LFARNYHDNQ QLLALNTAIR    50
    QAAKRPILIG VDQEGGRVQR FRDGFSKIPA AQLYARSDNG TQLAEDGGWL 100
    MAAELIAHDI DLSFAPVLDK GFDCRAIGNR AFGDDVQTVL TYSSAYMRGM 150
    KSVGMATTGK HFPGHGAVIA DSHLETPYDE RDSIADDMTI FRAQIEAGIL 200
    DAMMPAHVIY PHYDAQPASG SPYWLKQVLR QELGFQGIVF SDDLSMEGAA 250
    IMGGPAERAQ QSLDAGCDMV LMCNKRESAV AVLDQLPISV VPQAQSLLKQ 300
    QQFTYRELKA TERWKQAYQA LQRLIDAHS 329
    Length:329
    Mass (Da):36,181
    Last modified:May 30, 2000 - v2
    Checksum:i440C6A9B18143C34
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52818 Genomic DNA. Translation: AAC44686.2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U52818 Genomic DNA. Translation: AAC44686.2 .

    3D structure databases

    ProteinModelPortali P96157.
    SMRi P96157. Positions 1-329.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    SABIO-RK P96157.

    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. "Molecular cloning and characterization of a novel beta-N-acetyl-D-glucosaminidase from Vibrio furnissii."
      Chitlaru E., Roseman S.
      J. Biol. Chem. 271:33433-33439(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
      Strain: 7225.
    2. Chitlaru E., Roseman S.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 70-80.

    Entry informationi

    Entry nameiNAGZ_VIBFU
    AccessioniPrimary (citable) accession number: P96157
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 80 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

    Direct protein sequencing

    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