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P96157 (NAGZ_VIBFU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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-hexosaminidase

EC=3.2.1.52
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene names
Name:nagZ
Synonyms:exo II
OrganismVibrio furnissii
Taxonomic identifier29494 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Hydrolyzes rapidly p-nitrophenyl-N-acetyl-beta-D-glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and slightly active on p-nitrophenyl-beta-GalNAc. May play a role in signal transduction between host and organism. Ref.1

Catalytic activity

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

Enzyme regulation

Inhibited by GlcNAc, 2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glucopyranosylamine (GlcNAc-Asn) and O-(2-acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate (PUGNAc). Ref.1

Pathway

Cell wall biogenesis; peptidoglycan recycling. Ref.1

Subunit structure

Monomer Potential.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00364.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_0000210801

Regions

Region160 – 1612Substrate binding By similarity

Sites

Active site1731Proton donor/acceptor By similarity
Active site2421Nucleophile By similarity
Binding site621Substrate By similarity
Binding site701Substrate By similarity
Binding site1301Substrate By similarity
Site1711Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P96157 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 440C6A9B18143C34

FASTA32936,181
        10         20         30         40         50         60 
MGPLWLDVEG CELTAEDREI LAHPTVGGVI LFARNYHDNQ QLLALNTAIR QAAKRPILIG 

        70         80         90        100        110        120 
VDQEGGRVQR FRDGFSKIPA AQLYARSDNG TQLAEDGGWL MAAELIAHDI DLSFAPVLDK 

       130        140        150        160        170        180 
GFDCRAIGNR AFGDDVQTVL TYSSAYMRGM KSVGMATTGK HFPGHGAVIA DSHLETPYDE 

       190        200        210        220        230        240 
RDSIADDMTI FRAQIEAGIL DAMMPAHVIY PHYDAQPASG SPYWLKQVLR QELGFQGIVF 

       250        260        270        280        290        300 
SDDLSMEGAA IMGGPAERAQ QSLDAGCDMV LMCNKRESAV AVLDQLPISV VPQAQSLLKQ 

       310        320 
QQFTYRELKA TERWKQAYQA LQRLIDAHS 

« Hide

References

[1]"Molecular cloning and characterization of a novel beta-N-acetyl-D-glucosaminidase from Vibrio furnissii."
Chitlaru E., Roseman S.
J. Biol. Chem. 271:33433-33439(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY.
Strain: 7225.
[2]Chitlaru E., Roseman S.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 70-80.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52818 Genomic DNA. Translation: AAC44686.2.

3D structure databases

ProteinModelPortalP96157.
SMRP96157. Positions 1-329.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP96157.
UniPathwayUPA00544.

Family and domain databases

Gene3D3.20.20.300. 1 hit.
HAMAPMF_00364. NagZ.
InterProIPR022956. Beta_hexosaminidase_bac.
IPR019800. 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 nameNAGZ_VIBFU
AccessionPrimary (citable) accession number: P96157
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 79 of the entry and version 2 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