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Q3BVU6 (NAGZ_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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
Ordered Locus Names:XCV1386
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length334 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP-Rule MF_00364

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. HAMAP-Rule MF_00364

Pathway

Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_00364

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00364.

Sequence similarities

Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.

Sequence caution

The sequence CAJ23017.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 334334Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_0000234929

Regions

Region163 – 1642Substrate binding By similarity

Sites

Active site1761Proton donor/acceptor By similarity
Active site2471Nucleophile By similarity
Binding site601Substrate By similarity
Binding site681Substrate By similarity
Binding site1331Substrate By similarity
Site1741Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3BVU6 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 7F81413243693110

FASTA33434,931
        10         20         30         40         50         60 
MLLIGVAGTE LSAQERDWLQ HDAVAGVVLF KRNFASRTQV AELSAAIRAA APRPVLVCVD 

        70         80         90        100        110        120 
QEGGRVQRFR EGFSALAPLQ SFGAQYAHDP ESALAAARAH AQLMASEVRA SGVDLSFAPV 

       130        140        150        160        170        180 
VDLGRGNRAI GDRAFSDDPQ IVATFTRAYV QALHGAGMAA TLKHFPGHGT VLEDTHVDHA 

       190        200        210        220        230        240 
SDPRPLEVLQ AEDLVPFVAG IEAGADAVMM AHVVYPQVAP EPAGYSQRWI EQILRGQMGF 

       250        260        270        280        290        300 
CGVVFSDDIG MAASFSAGGV AGRVHAHLDA GCDVVLVCHP ELVAESLQAV QGRSLNTAAL 

       310        320        330 
IGLIGRGALG WDGLLAGTDA SFTTPPSAHF GTTA 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ23017.1. Different initiation.
RefSeqYP_363117.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BVU6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1386.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ23017; CAJ23017; XCV1386.
GeneID3731455.
KEGGxcv:XCV1386.
PATRIC24092236. VBIXanCam71633_1613.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OrthoDBEOG6BCT06.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1426-MONOMER.
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_XANC5
AccessionPrimary (citable) accession number: Q3BVU6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: May 14, 2014
This is version 62 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