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B5QXC7 (NAGZ_SALEP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 42. 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:SEN1840
OrganismSalmonella enteritidis PT4 (strain P125109) [Complete proteome] [HAMAP]
Taxonomic identifier550537 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length341 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_1000121069

Regions

Region163 – 1642Substrate binding By similarity

Sites

Active site1761Proton donor/acceptor By similarity
Active site2481Nucleophile By similarity
Binding site621Substrate By similarity
Binding site701Substrate By similarity
Binding site1331Substrate By similarity
Site1741Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B5QXC7 [UniParc].

Last modified November 4, 2008. Version 1.
Checksum: E07E83487336A300

FASTA34137,698
        10         20         30         40         50         60 
MGPVMLNVEG CELDAEEREI LAHPLVGGLI LFTRNYHDPE QLRELVRQIR AASRNHLVVA 

        70         80         90        100        110        120 
VDQEGGRVQR FREGFTRLPA AQSFFALHGL EEGGRLAQEA GWLMASEMIA MDIDISFAPV 

       130        140        150        160        170        180 
LDVGHISAAI GERSYHADPA KALAMATRFI DGMHDAGMKT TGKHFPGHGA VTADSHKETP 

       190        200        210        220        230        240 
CDPRPETDIR GKDMSVFRTL ISENKLDAIM PAHVIYRAID PRPASGSPYW LKTVLRQELG 

       250        260        270        280        290        300 
FDGVIFSDDL SMEGAAIMGS YAERAQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV 

       310        320        330        340 
TRLYHKGSFS RRELMDSARW KTASAQLNQL HERWQEEKAG H 

« Hide

References

[1]"Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella gallinarum 287/91 provides insights into evolutionary and host adaptation pathways."
Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., Ormond D. expand/collapse author list , Abdellah Z., Brooks K., Cherevach I., Chillingworth T., Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.
Genome Res. 18:1624-1637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P125109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM933172 Genomic DNA. Translation: CAR33420.1.
RefSeqYP_002243935.1. NC_011294.1.

3D structure databases

ProteinModelPortalB5QXC7.
SMRB5QXC7. Positions 1-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING550537.SEN1840.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PRIDEB5QXC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR33420; CAR33420; SEN1840.
PATRIC32334183. VBISalEnt14964_1872.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
OMAYTEADPR.
OrthoDBEOG6BCT06.

Enzyme and pathway databases

BioCycSENT550537:GJFI-1858-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_SALEP
AccessionPrimary (citable) accession number: B5QXC7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 4, 2008
Last modified: June 11, 2014
This is version 42 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