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Q7N397 (NAGZ_PHOLL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:plu2822
OrganismPhotorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP]
Taxonomic identifier243265 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePhotorhabdus

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides 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 – 340340Beta-hexosaminidase HAMAP-Rule MF_00364
PRO_0000210794

Sites

Active site2481 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7N397 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 0150EE572B011C65

FASTA34038,018
        10         20         30         40         50         60 
MGPVMLDVVG YELDNEEKEI LQHPLVGGLI LFTRNFYDVE QLRELVRQIR KASRHRLVIA 

        70         80         90        100        110        120 
VDQEGGRVQR FREGFTCLPA AQSFAGLSDN LNGTQLAEEA GWLMASEMIA MDIDISFAPV 

       130        140        150        160        170        180 
LDLGHQCAAI GERSFHEDPE QAKMMAEHFI KGMHSAGMKS TGKHFPGHGA VNADSHKETP 

       190        200        210        220        230        240 
CDDRPLEVIC HHDMSIFRDF IQRNLLDAIM PAHVIYPQVD KHPASGSSYW LKSVLRQQLG 

       250        260        270        280        290        300 
FNGVIFSDDL SMEGAAMMGS YVERGQTALN AGCDMILICN NRDGAVSALD NLPLTKVEKL 

       310        320        330        340 
SELYHRGGQY SLNELKNSER WQQANKALTA LYEQWQDCAR 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX571868 Genomic DNA. Translation: CAE15196.1.
RefSeqNP_930056.1. NC_005126.1.

3D structure databases

ProteinModelPortalQ7N397.
SMRQ7N397. Positions 1-336.
ModBaseSearch...

Protein-protein interaction databases

STRING243265.plu2822.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE15196; CAE15196; plu2822.
GeneID2802830.
KEGGplu:plu2822.
PATRIC20509935. VBIPhoLum48522_3207.

Organism-specific databases

GenoListplu2822.
CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAVVLHCNG.
ProtClustDBPRK05337.

Enzyme and pathway databases

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. Glyco_hydro_cat. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNAGZ_PHOLL
AccessionPrimary (citable) accession number: Q7N397
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: December 15, 2003
Last modified: May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families