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Q02PG9 (NAGZ_PSEAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:PA14_25195
OrganismPseudomonas aeruginosa (strain UCBPP-PA14) [Complete proteome] [HAMAP]
Taxonomic identifier208963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length332 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 – 332332Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_1000005659

Regions

Region161 – 1622Substrate binding By similarity

Sites

Active site1741Proton donor/acceptor By similarity
Active site2441Nucleophile By similarity
Binding site621Substrate By similarity
Binding site701Substrate By similarity
Binding site1311Substrate By similarity
Site1721Important for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02PG9 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: BA472E62B44A097A

FASTA33236,101
        10         20         30         40         50         60 
MQGSLMLDIG GTWLTAEDRQ ILRHPEVGGL IIFARNIEHP AQVRELCAAI RAIRPDLLLA 

        70         80         90        100        110        120 
VDQEGGRVQR LRQGFVRLPA MRAIADNPNA EELAEHCGWL MATEVQAVGL DLSFAPVLDL 

       130        140        150        160        170        180 
DHQRSAVVGS RAFEGDPERA ALLAGAFIRG MHAAGMAATG KHFPGHGWAE ADSHVAIPED 

       190        200        210        220        230        240 
ARSLEEIRRS DLVPFARLAG QLDALMPAHV IYPQVDPQPA GFSRRWLQEI LRGELKFDGV 

       250        260        270        280        290        300 
IFSDDLSMAG AHVVGDAASR IEAALAAGCD MGLVCNDRAS AELALAALQR LKVTPPSRLQ 

       310        320        330 
RMRGKGYANT DYRQQPRWLE ALSALRAAQL ID 

« Hide

References

[1]"Genomic analysis reveals that Pseudomonas aeruginosa virulence is combinatorial."
Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.
Genome Biol. 7:R90.1-R90.14(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UCBPP-PA14.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000438 Genomic DNA. Translation: ABJ15648.1.
RefSeqYP_790167.1. NC_008463.1.

3D structure databases

ProteinModelPortalQ02PG9.
SMRQ02PG9. Positions 3-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208963.PA14_25195.

Chemistry

BindingDBQ02PG9.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ15648; ABJ15648; PA14_25195.
GeneID4384185.
KEGGpau:PA14_25195.
PATRIC19850172. VBIPseAer79785_2045.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAAGFSSYW.
OrthoDBEOG6BCT06.
ProtClustDBPRK05337.

Enzyme and pathway databases

BioCycPAER208963:GI5K-2041-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_PSEAB
AccessionPrimary (citable) accession number: Q02PG9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: April 16, 2014
This is version 51 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