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Q5QUZ5 (NAGZ_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 62. 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:IL0915
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length330 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 – 330330Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_0000234914

Regions

Region163 – 1642Substrate binding By similarity

Sites

Active site1761Proton donor/acceptor By similarity
Active site2461Nucleophile 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
Q5QUZ5 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: D19231584F462851

FASTA33036,118
        10         20         30         40         50         60 
MAQLMIDIAG TELTAEDKKL LAAPAVNGLI LFTRNFASLE QLQELIREAR AAAAKPLLIA 

        70         80         90        100        110        120 
VDHEGGRVQR FREGFSAIPS MGSLQKIENE DERQRAARDL GWLMAAEVQA VGIDISFAPV 

       130        140        150        160        170        180 
LDVDDCSDVI GDRAFSAVPS EISKLASSFI EGMHEAGMAC TGKHFPGHGS VQADSHIAIP 

       190        200        210        220        230        240 
EDDRTLEQIR AHDLKPFLSL IQKLDGIMPA HVIYPQIDPQ PAGFSEFWLQ QILRSELQFN 

       250        260        270        280        290        300 
GTIFSDDLSM QGATVAGDME QRAVAALKAG CDMILVCNDR AGAVQVLDAD LPATEPESAQ 

       310        320        330 
RVNRMLMSSN AVSLEELKRT QRWEQAQRWL 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81755.1.
RefSeqYP_155304.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QUZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0915.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81755; AAV81755; IL0915.
GeneID3173409.
KEGGilo:IL0915.
PATRIC22139861. VBIIdiLoi21852_0916.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAAHDIDLS.
OrthoDBEOG6BCT06.

Enzyme and pathway databases

BioCycILOI283942:GI0U-915-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_IDILO
AccessionPrimary (citable) accession number: Q5QUZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 4, 2005
Last modified: May 14, 2014
This is version 62 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