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C6DKR8

- NAGZ_PECCP

UniProt

C6DKR8 - NAGZ_PECCP

Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
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 (01 Sep 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

    BioCyciPCAR561230:GKCK-2535-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:PC1_2488
    OrganismiPectobacterium carotovorum subsp. carotovorum (strain PC1)
    Taxonomic identifieri561230 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium
    ProteomesiUP000002736: 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 – 342342Beta-hexosaminidasePRO_1000205461Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi561230.PC1_2488.

    Structurei

    3D structure databases

    ProteinModelPortaliC6DKR8.
    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.
    OMAiYTEADPR.
    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.

    C6DKR8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPVMLDVAS YELDAEDREV LEHPLVGGVI LFTRNFHDAA QLRELVRQIR    50
    AASRERLVVS VDQEGGRVQR FRDGFTRLPA AQAFAALNSE PEALRLAEEG 100
    GWLMAAEMIS MDIDISFAPV LDIGHQSAAI GERSFHANPE TALAVAQSFI 150
    RGMHSAGMKV TGKHFPGHGA VSADSHKETP RDPRPLAEIR AHDMLIFKAL 200
    IQRQQLDAIM PAHVIYTEAD PRPASGSPYW LKTVLREELG FDGIIFSDDL 250
    SMEGAAVMGS YPERAQATLQ AGCDMILVCN HREGAVSVLD NLSPVKAEQL 300
    TRLYHQGSFS RRELLDSPRW KLANQALTSL SERWQAHKNG EK 342
    Length:342
    Mass (Da):37,780
    Last modified:September 1, 2009 - v1
    Checksum:iBA452047B7355209
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT13519.1.
    RefSeqiWP_015840699.1. NC_012917.1.
    YP_003018055.1. NC_012917.1.

    Genome annotation databases

    EnsemblBacteriaiACT13519; ACT13519; PC1_2488.
    GeneIDi8133434.
    KEGGipct:PC1_2488.
    PATRICi20489642. VBIPecCar70489_2505.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001657 Genomic DNA. Translation: ACT13519.1 .
    RefSeqi WP_015840699.1. NC_012917.1.
    YP_003018055.1. NC_012917.1.

    3D structure databases

    ProteinModelPortali C6DKR8.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 561230.PC1_2488.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACT13519 ; ACT13519 ; PC1_2488 .
    GeneIDi 8133434.
    KEGGi pct:PC1_2488.
    PATRICi 20489642. VBIPecCar70489_2505.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00544 .
    BioCyci PCAR561230:GKCK-2535-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. "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
      US DOE Joint Genome Institute
      Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.
      , Balakrishnan V., Glasner J., Perna N.T.
      Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: PC1.

    Entry informationi

    Entry nameiNAGZ_PECCP
    AccessioniPrimary (citable) accession number: C6DKR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: September 1, 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