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Q7WUL3 (NAG3_CELFI) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-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 names
Name:nag3
Synonyms:nag3A
OrganismCellulomonas fimi
Taxonomic identifier1708 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length564 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

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

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Ref.1

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.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family.

Biophysicochemical properties

Kinetic parameters:

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

KM=2.7 mM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide Ref.1

pH dependence:

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 564564Beta-N-acetylglucosaminidase/beta-glucosidase
PRO_0000252454

Sites

Active site2831Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7WUL3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9B1428A4561F71D3

FASTA56459,993
        10         20         30         40         50         60 
MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY LTRGLHVGGV 

        70         80         90        100        110        120 
MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ EATHVGSNMA LAATGSTDHV 

       130        140        150        160        170        180 
RRAATVIGRE ARALGINWAF TPVVDIDLNF RNPITNTRTF GADAATVAAM GAEYVEAIQA 

       190        200        210        220        230        240 
QGLAASAKHF PGDGVDERDQ HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML 

       250        260        270        280        290        300 
PAYSRALRPG VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV 

       310        320        330        340        350        360 
PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA SLGLHRGTNL 

       370        380        390        400        410        420 
PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR ERYPRVLVYD LQNGGSPIGQ 

       430        440        450        460        470        480 
GARAGAVEQF VDALVEAGHD VTRFEPGGGW EGMAAPTTDV TERHDLVLYL ANLSTRSNQT 

       490        500        510        520        530        540 
VVRIEWAEPM GANVPAYVHS VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA 

       550        560 
LQGKAPFAGS SPVDAFCGQW DTHL 

« 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 1-11, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF478460 Genomic DNA. Translation: AAQ05801.1.

3D structure databases

ProteinModelPortalQ7WUL3.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ7WUL3.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
InterProIPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNAG3_CELFI
AccessionPrimary (citable) accession number: Q7WUL3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 1, 2003
Last modified: October 16, 2013
This is version 36 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

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries