Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9KU37

- NAGZ_VIBCH

UniProt

Q9KU37 - NAGZ_VIBCH

Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.3 PublicationsUniRule annotation

    Catalytic activityi

    Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.3 PublicationsUniRule annotation

    Pathwayi

    Sites

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

    GO - Molecular functioni

    1. beta-N-acetylhexosaminidase activity Source: TIGR

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. peptidoglycan-based cell wall biogenesis Source: TIGR
    5. peptidoglycan biosynthetic process Source: UniProtKB-KW
    6. peptidoglycan turnover Source: TIGR
    7. regulation of cell shape Source: UniProtKB-KW
    8. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciVCHO:VC0692-MONOMER.
    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
    Ordered Locus Names:VC_0692
    OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
    Taxonomic identifieri243277 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
    ProteomesiUP000000584: Chromosome 1

    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 – 330330Beta-hexosaminidasePRO_0000210800Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer.Curated

    Protein-protein interaction databases

    STRINGi243277.VC0692.

    Structurei

    Secondary structure

    1
    330
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi9 – 124
    Helixi15 – 217
    Beta strandi26 – 316
    Helixi33 – 353
    Helixi39 – 5315
    Beta strandi58 – 614
    Beta strandi63 – 653
    Beta strandi68 – 703
    Helixi81 – 866
    Helixi90 – 10617
    Turni107 – 1093
    Turni125 – 1273
    Helixi128 – 1303
    Helixi136 – 15217
    Beta strandi158 – 1625
    Beta strandi173 – 1764
    Helixi185 – 19713
    Beta strandi201 – 2055
    Turni211 – 2133
    Beta strandi214 – 2163
    Helixi218 – 2203
    Helixi222 – 2254
    Helixi226 – 2327
    Beta strandi237 – 2437
    Helixi244 – 2463
    Helixi249 – 2524
    Helixi255 – 26511
    Beta strandi268 – 2714
    Helixi276 – 28510
    Helixi292 – 2976
    Helixi305 – 3095
    Helixi312 – 32817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TR9X-ray1.80A2-330[»]
    1Y65X-ray1.85A2-330[»]
    2OXNX-ray1.70A1-330[»]
    3GS6X-ray2.30A1-330[»]
    3GSMX-ray2.40A1-330[»]
    ProteinModelPortaliQ9KU37.
    SMRiQ9KU37. Positions 1-330.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9KU37.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG1472.
    KOiK01207.
    OMAiNHVVQAS.
    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.

    Q9KU37-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR    50
    QAAKRPILIG VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL 100
    MAAELIAHDV DLSFAPVLDM GFACKAIGNR AFGEDVQTVL KHSSAFLRGM 150
    KAVGMATTGK HFPGHGAVIA DSHLETPYDE RETIAQDMAI FRAQIEAGVL 200
    DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF SDDLSMEGAA 250
    VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK 300
    QQFSYSELKR LERWQQASAN MQRLIEQFSE 330
    Length:330
    Mass (Da):36,466
    Last modified:October 1, 2000 - v1
    Checksum:iA737BD82C149D3A2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93857.1.
    PIRiA82292.
    RefSeqiNP_230341.1. NC_002505.1.

    Genome annotation databases

    EnsemblBacteriaiAAF93857; AAF93857; VC_0692.
    GeneIDi2615481.
    KEGGivch:VC0692.
    PATRICi20080499. VBIVibCho83274_0663.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE003852 Genomic DNA. Translation: AAF93857.1 .
    PIRi A82292.
    RefSeqi NP_230341.1. NC_002505.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TR9 X-ray 1.80 A 2-330 [» ]
    1Y65 X-ray 1.85 A 2-330 [» ]
    2OXN X-ray 1.70 A 1-330 [» ]
    3GS6 X-ray 2.30 A 1-330 [» ]
    3GSM X-ray 2.40 A 1-330 [» ]
    ProteinModelPortali Q9KU37.
    SMRi Q9KU37. Positions 1-330.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243277.VC0692.

    Chemistry

    ChEMBLi CHEMBL1075035.

    Protein family/group databases

    CAZyi GH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    DNASUi 2615481.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAF93857 ; AAF93857 ; VC_0692 .
    GeneIDi 2615481.
    KEGGi vch:VC0692.
    PATRICi 20080499. VBIVibCho83274_0663.

    Phylogenomic databases

    eggNOGi COG1472.
    KOi K01207.
    OMAi NHVVQAS.
    OrthoDBi EOG6BCT06.

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    BioCyci VCHO:VC0692-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9KU37.
    PROi Q9KU37.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 39315 / El Tor Inaba N16961.
    2. "The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams."
      Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E., Gloster T.M., Vocadlo D.J., Mark B.L.
      ChemBioChem 14:1973-1981(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    3. "Structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine."
      Gorman J., Shapiro L.
      Submitted (DEC-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
    4. "Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance."
      Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J.
      J. Biol. Chem. 282:21382-21391(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.
    5. "Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ."
      Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J., Mark B.L.
      Protein Sci. 18:1541-1551(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, FUNCTION.

    Entry informationi

    Entry nameiNAGZ_VIBCH
    AccessioniPrimary (citable) accession number: Q9KU37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 4, 2001
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 95 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3