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C3LSU7 (NAGZ_VIBCM) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 33. 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:VCM66_0650
OrganismVibrio cholerae serotype O1 (strain M66-2) [Complete proteome] [HAMAP]
Taxonomic identifier579112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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_1000133667

Regions

Region160 – 1612Substrate binding By similarity

Sites

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

Sequences

Sequence LengthMass (Da)Tools
C3LSU7 [UniParc].

Last modified June 16, 2009. 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

[1]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M66-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001233 Genomic DNA. Translation: ACP04973.1.
RefSeqYP_002809424.1. NC_012578.1.

3D structure databases

ProteinModelPortalC3LSU7.
SMRC3LSU7. Positions 1-330.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING579112.VCM66_0650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP04973; ACP04973; VCM66_0650.
GeneID7771934.
KEGGvcm:VCM66_0650.
PATRIC20065116. VBIVibCho108967_0623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycVCHO579112:GJAW-704-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_VIBCM
AccessionPrimary (citable) accession number: C3LSU7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 33 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