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Q7WUL4

- HEX20_CELFI

UniProt

Q7WUL4 - HEX20_CELFI

Protein

Beta-N-acetylhexosaminidase

Gene

hex20

Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 53 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Catalyzes the cleavage of beta-N-acetylglucosaminides and beta-N-acetylgalactosaminides. Also catalyzes the hydrolysis of N-acetylchitooligomers. May be involved in chitin degradation. It is not able to cleave beta-glucosides.1 Publication

    Catalytic activityi

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

    Kineticsi

    There is a 4-fold greater activity on 4'-nitrophenyl beta-N-acetyl-D-glucosaminide than on 4'-nitrophenyl beta-N-acetyl-D-galactosaminide.

    1. KM=53 µM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide1 Publication
    2. KM=66 µM for 4'-nitrophenyl beta-N-acetyl-D-galactosaminide1 Publication

    pH dependencei

    Optimum pH is 7.3-8.7 with 4'-nitrophenyl beta-N-acetyl-D-glucosaminide as substrate. Rapidly inactivated above pH 9.5 and stable from pH 6.0 to 9.5.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei298 – 2981Proton donorBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. chitin catabolic process Source: UniProtKB-UniPathway
    2. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Polysaccharide degradation

    Enzyme and pathway databases

    SABIO-RKQ7WUL4.
    UniPathwayiUPA00349.

    Protein family/group databases

    CAZyiGH20. Glycoside Hydrolase Family 20.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-N-acetylhexosaminidase (EC:3.2.1.52)
    Alternative name(s):
    Beta-N-acetylgalactosaminidase
    Beta-N-acetylglucosaminidase
    Hex20
    Gene namesi
    Name:hex20
    Synonyms:hex20A
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 496496Beta-N-acetylhexosaminidasePRO_0000252455Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ7WUL4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 20 family.Curated

    Family and domain databases

    Gene3Di3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProiIPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    [Graphical view]
    PfamiPF00728. Glyco_hydro_20. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    [Graphical view]
    PRINTSiPR00738. GLHYDRLASE20.
    SUPFAMiSSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q7WUL4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPDVAVIPRP VLLETTDGPP FVLTAATILV VDSAPELVAV GVLAADLLGR    50
    LSGRPVEVRY TEGGAPSVVR LRLSEDLPAG DEAYRLVVSE HRVDIDARSA 100
    AGLVRAVVTL RQTVSSLGDG TLTVPALRVE DHPRYAWRGL SIDVARHFFT 150
    VDDLKAIIGL LAHYKLNVLH LHLTDDQGWR VHLPSRPHLT RASAGTSVGG 200
    GPGGFYNPAQ LAEIVVARAA RGIRVVPEID VPGHVNAATH AYGDLTPSGE 250
    PTDVYTGIEV GFSRLHDDLP ATRPFLRDVF TDLAAMTPGE YVHIGGDEVL 300
    TMDHDKYARL VGYAASVVRD AGKKVVGWQE ISSTPLEPGT VVQYWDINAD 350
    PAPFVAAAQA GAHVLMSPGS RAYLDMKYDA TTELGLEWAG HIELRDAYDW 400
    EPSTLIPGVP PESVIGVEAA VWTETLTDLG ELTSMLLPRL AAVAEVAWTA 450
    PQDRDWDDFS GRVAQHAPFW DRVGFRWHAS PQVSWPGPGS APGAAF 496
    Length:496
    Mass (Da):53,326
    Last modified:October 1, 2003 - v1
    Checksum:i7D514C614991706C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478459 Genomic DNA. Translation: AAQ05800.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF478459 Genomic DNA. Translation: AAQ05800.1 .

    3D structure databases

    ProteinModelPortali Q7WUL4.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH20. Glycoside Hydrolase Family 20.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00349 .
    SABIO-RK Q7WUL4.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    3.30.379.10. 1 hit.
    InterProi IPR025705. Beta_hexosaminidase_sua/sub.
    IPR029018. Chitobiase/Hex_dom_2-like.
    IPR015883. Glyco_hydro_20_cat-core.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR015882. HEX_bac_N.
    [Graphical view ]
    Pfami PF00728. Glyco_hydro_20. 1 hit.
    PF02838. Glyco_hydro_20b. 1 hit.
    [Graphical view ]
    PRINTSi PR00738. GLHYDRLASE20.
    SUPFAMi SSF51445. SSF51445. 1 hit.
    SSF55545. SSF55545. 1 hit.
    ProtoNeti Search...

    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 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiHEX20_CELFI
    AccessioniPrimary (citable) accession number: Q7WUL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 53 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The reaction mechanism involves an oxazolinium ion intermediate.

    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