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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides.

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.UniRule annotation

Enzyme regulationi

Slightly inhibited by GlcNAc and N-acetylmuramic acid and strongly inhibited by N-acetylglucosaminolactone.

pH dependencei

Optimum pH is 7.7.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621SubstrateUniRule annotation
Binding sitei70 – 701SubstrateUniRule annotation
Binding sitei133 – 1331SubstrateUniRule annotation
Sitei174 – 1741Important for catalytic activityUniRule annotation
Active sitei176 – 1761Proton donor/acceptorUniRule annotation
Active sitei248 – 2481NucleophileUniRule annotation

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. cell cycle Source: UniProtKB-KW
  3. cell division Source: UniProtKB-KW
  4. cell wall organization Source: UniProtKB-KW
  5. peptidoglycan biosynthetic process Source: UniProtKB-KW
  6. peptidoglycan turnover Source: EcoliWiki
  7. regulation of cell shape Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyciEcoCyc:G6567-MONOMER.
ECOL316407:JW1093-MONOMER.
MetaCyc:G6567-MONOMER.
UniPathwayiUPA00544.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-hexosaminidaseUniRule annotation (EC:3.2.1.52UniRule annotation)
Alternative name(s):
Beta-N-acetylhexosaminidaseUniRule annotation
N-acetyl-beta-glucosaminidaseUniRule annotation
Gene namesi
Name:nagZUniRule annotation
Synonyms:ycfO
Ordered Locus Names:b1107, JW1093
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG13433. nagZ.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Beta-hexosaminidasePRO_0000210785Add
BLAST

Proteomic databases

PaxDbiP75949.
PRIDEiP75949.

Expressioni

Gene expression databases

GenevestigatoriP75949.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

IntActiP75949. 8 interactions.
STRINGi511145.b1107.

Structurei

3D structure databases

ProteinModelPortaliP75949.
SMRiP75949. Positions 1-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 1642Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
InParanoidiP75949.
KOiK01207.
OMAiAGFSSYW.
OrthoDBiEOG6BCT06.
PhylomeDBiP75949.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P75949-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR
60 70 80 90 100
AASRNRLVVA VDQEGGRVQR FREGFTRLPA AQSFAALSGM EEGGKLAQEA
110 120 130 140 150
GWLMASEMIA MDIDISFAPV LDVGHISAAI GERSYHADPQ KALAIASRFI
160 170 180 190 200
DGMHEAGMKT TGKHFPGHGA VTADSHKETP CDPRPQAEIR AKDMSVFSSL
210 220 230 240 250
IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG FDGVIFSDDL
260 270 280 290 300
SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
310 320 330 340
TRLYHKGSFS RQELMDSARW KAISTRLNQL HERWQEEKAG H
Length:341
Mass (Da):37,595
Last modified:February 1, 1997 - v1
Checksum:i9E50C8E4DA87C7A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74191.1.
AP009048 Genomic DNA. Translation: BAA35914.1.
PIRiH64854.
RefSeqiNP_415625.1. NC_000913.3.
YP_489375.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74191; AAC74191; b1107.
BAA35914; BAA35914; BAA35914.
GeneIDi12930540.
945671.
KEGGiecj:Y75_p1077.
eco:b1107.
PATRICi32117457. VBIEscCol129921_1151.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74191.1.
AP009048 Genomic DNA. Translation: BAA35914.1.
PIRiH64854.
RefSeqiNP_415625.1. NC_000913.3.
YP_489375.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP75949.
SMRiP75949. Positions 1-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP75949. 8 interactions.
STRINGi511145.b1107.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbiP75949.
PRIDEiP75949.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74191; AAC74191; b1107.
BAA35914; BAA35914; BAA35914.
GeneIDi12930540.
945671.
KEGGiecj:Y75_p1077.
eco:b1107.
PATRICi32117457. VBIEscCol129921_1151.

Organism-specific databases

EchoBASEiEB3207.
EcoGeneiEG13433. nagZ.

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
InParanoidiP75949.
KOiK01207.
OMAiAGFSSYW.
OrthoDBiEOG6BCT06.
PhylomeDBiP75949.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciEcoCyc:G6567-MONOMER.
ECOL316407:JW1093-MONOMER.
MetaCyc:G6567-MONOMER.

Miscellaneous databases

PROiP75949.

Gene expression databases

GenevestigatoriP75949.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ.
InterProiIPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Purification and properties of beta-N-acetylglucosaminidase from Escherichia coli."
    Yem D.W., Wu H.C.
    J. Bacteriol. 125:324-331(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12.
  5. "Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling."
    Cheng Q., Li H., Merdek K., Park J.T.
    J. Bacteriol. 182:4836-4840(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: K12.

Entry informationi

Entry nameiNAGZ_ECOLI
AccessioniPrimary (citable) accession number: P75949
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: January 7, 2015
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.