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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Vibrio furnissii
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.UniRule annotation1 Publication

Enzyme regulationi

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).1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 45 degrees Celsius.1 Publication

Pathway:ipeptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.UniRule annotation1 Publication
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateUniRule annotation
Binding sitei70 – 701SubstrateUniRule annotation
Binding sitei130 – 1301SubstrateUniRule annotation
Sitei171 – 1711Important for catalytic activityUniRule annotation
Active sitei173 – 1731Proton donor/acceptorUniRule annotation
Active sitei242 – 2421NucleophileUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

SABIO-RKP96157.
UniPathwayiUPA00544.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidaseUniRule annotation (EC:3.2.1.52UniRule annotation)
Alternative name(s):
Beta-N-acetylhexosaminidaseUniRule annotation
N-acetyl-beta-glucosaminidaseUniRule annotation
Gene namesi
Name:nagZUniRule annotation
Synonyms:exo II
OrganismiVibrio furnissii
Taxonomic identifieri29494 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 329329Beta-hexosaminidasePRO_0000210801Add
BLAST

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

STRINGi903510.vfu_A00990.

Structurei

3D structure databases

ProteinModelPortaliP96157.
SMRiP96157. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1612Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.UniRule annotation

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. 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.

P96157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPLWLDVEG CELTAEDREI LAHPTVGGVI LFARNYHDNQ QLLALNTAIR
60 70 80 90 100
QAAKRPILIG VDQEGGRVQR FRDGFSKIPA AQLYARSDNG TQLAEDGGWL
110 120 130 140 150
MAAELIAHDI DLSFAPVLDK GFDCRAIGNR AFGDDVQTVL TYSSAYMRGM
160 170 180 190 200
KSVGMATTGK HFPGHGAVIA DSHLETPYDE RDSIADDMTI FRAQIEAGIL
210 220 230 240 250
DAMMPAHVIY PHYDAQPASG SPYWLKQVLR QELGFQGIVF SDDLSMEGAA
260 270 280 290 300
IMGGPAERAQ QSLDAGCDMV LMCNKRESAV AVLDQLPISV VPQAQSLLKQ
310 320
QQFTYRELKA TERWKQAYQA LQRLIDAHS
Length:329
Mass (Da):36,181
Last modified:May 30, 2000 - v2
Checksum:i440C6A9B18143C34
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52818 Genomic DNA. Translation: AAC44686.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52818 Genomic DNA. Translation: AAC44686.2.

3D structure databases

ProteinModelPortaliP96157.
SMRiP96157. Positions 1-329.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi903510.vfu_A00990.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00544.
SABIO-RKP96157.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. 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. "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.

Entry informationi

Entry nameiNAGZ_VIBFU
AccessioniPrimary (citable) accession number: P96157
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: June 24, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

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.