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Q9KU37 (NAGZ_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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:VC_0692
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length330 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.4 Ref.5

Catalytic activity

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.2 Ref.4 Ref.5

Pathway

Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_00364

Subunit structure

Monomer Potential.

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 – 330330Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_0000210800

Regions

Region160 – 1612Substrate binding HAMAP-Rule MF_00364

Sites

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

Secondary structure

.............................................................. 330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KU37 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A737BD82C149D3A2

FASTA33036,466
        10         20         30         40         50         60 
MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR QAAKRPILIG 

        70         80         90        100        110        120 
VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL MAAELIAHDV DLSFAPVLDM 

       130        140        150        160        170        180 
GFACKAIGNR AFGEDVQTVL KHSSAFLRGM KAVGMATTGK HFPGHGAVIA DSHLETPYDE 

       190        200        210        220        230        240 
RETIAQDMAI FRAQIEAGVL DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF 

       250        260        270        280        290        300 
SDDLSMEGAA VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK 

       310        320        330 
QQFSYSELKR LERWQQASAN MQRLIEQFSE 

« Hide

References

« Hide 'large scale' references
[1]"DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae."
Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. expand/collapse author list , Qin H., Dragoi I., Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.
Nature 406:477-483(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39315 / El Tor Inaba N16961.
[2]"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: FUNCTION, CATALYTIC ACTIVITY.
[3]"Structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine."
Gorman J., Shapiro L.
Submitted (DEC-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
[4]"Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance."
Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J.
J. Biol. Chem. 282:21382-21391(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.
[5]"Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ."
Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J., Mark B.L.
Protein Sci. 18:1541-1551(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93857.1.
PIRA82292.
RefSeqNP_230341.1. NC_002505.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TR9X-ray1.80A2-330[»]
1Y65X-ray1.85A2-330[»]
2OXNX-ray1.70A1-330[»]
3GS6X-ray2.30A1-330[»]
3GSMX-ray2.40A1-330[»]
ProteinModelPortalQ9KU37.
SMRQ9KU37. Positions 1-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0692.

Chemistry

ChEMBLCHEMBL1075035.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

DNASU2615481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93857; AAF93857; VC_0692.
GeneID2615481.
KEGGvch:VC0692.
PATRIC20080499. VBIVibCho83274_0663.

Phylogenomic databases

eggNOGCOG1472.
KOK01207.
OMANHVVQAS.
OrthoDBEOG6BCT06.

Enzyme and pathway databases

BioCycVCHO:VC0692-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...

Other

EvolutionaryTraceQ9KU37.
PROQ9KU37.

Entry information

Entry nameNAGZ_VIBCH
AccessionPrimary (citable) accession number: Q9KU37
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 94 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