Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

B7UYS5 (NAGZ_PSEA8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:PLES_20571
OrganismPseudomonas aeruginosa (strain LESB58) [Complete proteome] [HAMAP]
Taxonomic identifier557722 [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_1000121066

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
B7UYS5 [UniParc].

Last modified February 10, 2009. 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]"Newly introduced genomic prophage islands are critical determinants of in vivo competitiveness in the Liverpool epidemic strain of Pseudomonas aeruginosa."
Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.
Genome Res. 19:12-23(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LESB58.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM209186 Genomic DNA. Translation: CAW26784.1.
RefSeqYP_002439660.1. NC_011770.1.

3D structure databases

ProteinModelPortalB7UYS5.
SMRB7UYS5. Positions 3-325.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING557722.PLES_20571.

Chemistry

BindingDBB7UYS5.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW26784; CAW26784; PLES_20571.
GeneID7180781.
KEGGpag:PLES_20571.
PATRIC19813765. VBIPseAer113719_2129.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAAHDIDLS.
OrthoDBEOG6BCT06.

Enzyme and pathway databases

BioCycPAER557722:GHJW-2088-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_PSEA8
AccessionPrimary (citable) accession number: B7UYS5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 41 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