Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q7WUL4 (HEX20_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-N-acetylhexosaminidase

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylgalactosaminidase
Beta-N-acetylglucosaminidase
Hex20
Gene names
Name:hex20
Synonyms:hex20A
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Pathway

Glycan degradation; chitin degradation.

Miscellaneous

The reaction mechanism involves an oxazolinium ion intermediate.

Sequence similarities

Belongs to the glycosyl hydrolase 20 family.

Biophysicochemical properties

Kinetic parameters:

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

KM=53 µM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide Ref.1

KM=66 µM for 4'-nitrophenyl beta-N-acetyl-D-galactosaminide

pH dependence:

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Beta-N-acetylhexosaminidase
PRO_0000252455

Sites

Active site2981Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WUL4 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 7D514C614991706C

FASTA49653,326
        10         20         30         40         50         60 
MPDVAVIPRP VLLETTDGPP FVLTAATILV VDSAPELVAV GVLAADLLGR LSGRPVEVRY 

        70         80         90        100        110        120 
TEGGAPSVVR LRLSEDLPAG DEAYRLVVSE HRVDIDARSA AGLVRAVVTL RQTVSSLGDG 

       130        140        150        160        170        180 
TLTVPALRVE DHPRYAWRGL SIDVARHFFT VDDLKAIIGL LAHYKLNVLH LHLTDDQGWR 

       190        200        210        220        230        240 
VHLPSRPHLT RASAGTSVGG GPGGFYNPAQ LAEIVVARAA RGIRVVPEID VPGHVNAATH 

       250        260        270        280        290        300 
AYGDLTPSGE PTDVYTGIEV GFSRLHDDLP ATRPFLRDVF TDLAAMTPGE YVHIGGDEVL 

       310        320        330        340        350        360 
TMDHDKYARL VGYAASVVRD AGKKVVGWQE ISSTPLEPGT VVQYWDINAD PAPFVAAAQA 

       370        380        390        400        410        420 
GAHVLMSPGS RAYLDMKYDA TTELGLEWAG HIELRDAYDW EPSTLIPGVP PESVIGVEAA 

       430        440        450        460        470        480 
VWTETLTDLG ELTSMLLPRL AAVAEVAWTA PQDRDWDDFS GRVAQHAPFW DRVGFRWHAS 

       490 
PQVSWPGPGS APGAAF 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF478459 Genomic DNA. Translation: AAQ05800.1.

3D structure databases

ProteinModelPortalQ7WUL4.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH20. Glycoside Hydrolase Family 20.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ7WUL4.
UniPathwayUPA00349.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR025705. Beta_hexosaminidase_sua/sub.
IPR015883. Glyco_hydro_20_cat-core.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR015882. HEX_bac_N.
[Graphical view]
PfamPF00728. Glyco_hydro_20. 1 hit.
PF02838. Glyco_hydro_20b. 1 hit.
[Graphical view]
PRINTSPR00738. GLHYDRLASE20.
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameHEX20_CELFI
AccessionPrimary (citable) accession number: Q7WUL4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 1, 2003
Last modified: April 16, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries