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A5F8Y1 (NAGZ_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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
Synonyms:exoII
Ordered Locus Names:VC0395_A0223, VC395_0709
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [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_1000072096

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
A5F8Y1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: A8002629ABFC67A2

FASTA33036,382
        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 LMCNKREAAV EVLDNLPIMV VPQATALLKK 

       310        320        330 
QQFSYSELKR LDRWQQASAN MQRLIEQFSV 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"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: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ20198.1.
CP001235 Genomic DNA. Translation: ACP08727.1.
RefSeqYP_001216186.1. NC_009457.1.
YP_002818963.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F8Y1.
SMRA5F8Y1. Positions 1-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A0223.

Protein family/group databases

CAZyGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ20198; ABQ20198; VC0395_A0223.
ACP08727; ACP08727; VC395_0709.
GeneID5137813.
7774728.
KEGGvco:VC0395_A0223.
vcr:VC395_0709.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1472.
HOGENOMHOG000248526.
KOK01207.
OMAAHDIDLS.

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. SSF51445. 1 hit.
PROSITEPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNAGZ_VIBC3
AccessionPrimary (citable) accession number: A5F8Y1
Secondary accession number(s): C3LY03
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 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