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Q8ZQ06 (NAGZ_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:STM1209
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length341 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. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC. Ref.2 Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.2 Ref.3

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_0000210797

Regions

Region163 – 1642Substrate binding HAMAP-Rule MF_00364

Sites

Active site1761Proton donor/acceptor Probable
Active site2481Nucleophile Ref.2
Binding site621Substrate
Binding site701Substrate By similarity
Binding site1331Substrate
Site1741Important for catalytic activity By similarity

Experimental info

Mutagenesis1761H → G: Reduced enzyme activity.
Mutagenesis2481D → N: Abolishes enzyme activity. Ref.2

Secondary structure

............................................................. 341
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8ZQ06 [UniParc].

Last modified March 1, 2002. 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

« Hide 'large scale' references
[1]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion."
Bacik J.P., Whitworth G.E., Stubbs K.A., Vocadlo D.J., Mark B.L.
Chem. Biol. 19:1471-1482(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH DISACCHARIDE SUBSTRATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF ASP-248.
[3]"The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams."
Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E., Gloster T.M., Vocadlo D.J., Mark B.L.
ChemBioChem 14:1973-1981(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006468 Genomic DNA. Translation: AAL20138.1.
RefSeqNP_460179.1. NC_003197.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4GVFX-ray1.35A/B1-341[»]
4GVGX-ray1.70A/B1-341[»]
4GVHX-ray1.45A/B1-341[»]
4GVIX-ray1.55A/B1-341[»]
4HZMX-ray1.45A/B1-341[»]
ProteinModelPortalQ8ZQ06.
SMRQ8ZQ06. Positions 1-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM1209.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbQ8ZQ06.
PRIDEQ8ZQ06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL20138; AAL20138; STM1209.
GeneID1252727.
KEGGstm:STM1209.
PATRIC32380867. VBISalEnt20916_1278.

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAYTEADPR.
OrthoDBEOG6BCT06.
PhylomeDBQ8ZQ06.

Enzyme and pathway databases

BioCycSENT99287:GCTI-1218-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_SALTY
AccessionPrimary (citable) accession number: Q8ZQ06
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 80 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries