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Protein

Beta-N-acetylglucosaminidase/beta-glucosidase

Gene

nag3

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the cleavage of beta-N-acetyl-D-glucosaminides and beta-D-glucosides. Might be involved in the degradation of glucuronic acid-containing glycosaminoglycans such as hyaluronic acid.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Kineticsi

The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.

  1. KM=2.7 mM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide1 Publication

    pH dependencei

    Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei283 – 2831NucleophileBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation

    Enzyme and pathway databases

    SABIO-RKQ7WUL3.

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-N-acetylglucosaminidase/beta-glucosidase (EC:3.2.1.21, EC:3.2.1.52)
    Alternative name(s):
    3-beta-N-acetyl-D-glucosaminidase/beta-D-glucosidase
    Nag3
    Gene namesi
    Name:nag3
    Synonyms:nag3A
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 564564Beta-N-acetylglucosaminidase/beta-glucosidasePRO_0000252454Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi590998.Celf_2983.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7WUL3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 3 family.Curated

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    InterProiIPR019800. 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.

    Q7WUL3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY
    60 70 80 90 100
    LTRGLHVGGV MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ
    110 120 130 140 150
    EATHVGSNMA LAATGSTDHV RRAATVIGRE ARALGINWAF TPVVDIDLNF
    160 170 180 190 200
    RNPITNTRTF GADAATVAAM GAEYVEAIQA QGLAASAKHF PGDGVDERDQ
    210 220 230 240 250
    HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML PAYSRALRPG
    260 270 280 290 300
    VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV
    310 320 330 340 350
    PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA
    360 370 380 390 400
    SLGLHRGTNL PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR
    410 420 430 440 450
    ERYPRVLVYD LQNGGSPIGQ GARAGAVEQF VDALVEAGHD VTRFEPGGGW
    460 470 480 490 500
    EGMAAPTTDV TERHDLVLYL ANLSTRSNQT VVRIEWAEPM GANVPAYVHS
    510 520 530 540 550
    VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA LQGKAPFAGS
    560
    SPVDAFCGQW DTHL
    Length:564
    Mass (Da):59,993
    Last modified:October 1, 2003 - v1
    Checksum:i9B1428A4561F71D3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF478460 Genomic DNA. Translation: AAQ05801.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF478460 Genomic DNA. Translation: AAQ05801.1.

    3D structure databases

    ProteinModelPortaliQ7WUL3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi590998.Celf_2983.

    Protein family/group databases

    CAZyiGH3. Glycoside Hydrolase Family 3.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    SABIO-RKQ7WUL3.

    Family and domain databases

    Gene3Di3.20.20.300. 1 hit.
    InterProiIPR019800. 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]
    ProtoNetiSearch...

    Publicationsi

    1. "Characterization of a beta-N-acetylhexosaminidase and a beta-N-acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi."
      Mayer C., Vocadlo D.J., Mah M., Rupitz K., Stoll D., Warren R.A.J., Withers S.G.
      FEBS J. 273:2929-2941(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiNAG3_CELFI
    AccessioniPrimary (citable) accession number: Q7WUL3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 1, 2003
    Last modified: June 24, 2015
    This is version 38 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Catalyzes hydrolysis by a double-displacement mechanism via a covalent glycosyl-enzyme intermediate, involving the participation of a catalytic nucleophilic group in the enzyme active site.

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.