SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P75949

- NAGZ_ECOLI

UniProt

P75949 - NAGZ_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-hexosaminidase

Gene
nagZ, ycfO, b1107, JW1093
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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.UniRule annotation

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.UniRule annotation

pH dependencei

Optimum pH is 7.7.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Substrate By similarity
Binding sitei70 – 701Substrate By similarity
Binding sitei133 – 1331Substrate By similarity
Sitei174 – 1741Important for catalytic activity By similarity
Active sitei176 – 1761Proton donor/acceptor By similarity
Active sitei248 – 2481Nucleophile By similarity

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. peptidoglycan biosynthetic process Source: UniProtKB-KW
  5. peptidoglycan turnover Source: EcoliWiki
  6. 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-hexosaminidase (EC:3.2.1.52)
Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase
Gene namesi
Name:nagZ
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

Cytoplasm UniRule annotation

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-hexosaminidaseUniRule annotationPRO_0000210785Add
BLAST

Proteomic databases

PaxDbiP75949.
PRIDEiP75949.

Expressioni

Gene expression databases

GenevestigatoriP75949.

Interactioni

Subunit structurei

Monomer Reviewed prediction.

Protein-protein interaction databases

IntActiP75949. 8 interactions.
STRINGi511145.b1107.

Structurei

3D structure databases

ProteinModelPortaliP75949.
SMRiP75949. Positions 1-340.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni163 – 1642Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
KOiK01207.
OMAiAHDIDLS.
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

MGPVMLDVEG YELDAEEREI LAHPLVGGLI LFTRNYHDPA QLRELVRQIR    50
AASRNRLVVA VDQEGGRVQR FREGFTRLPA AQSFAALSGM EEGGKLAQEA 100
GWLMASEMIA MDIDISFAPV LDVGHISAAI GERSYHADPQ KALAIASRFI 150
DGMHEAGMKT TGKHFPGHGA VTADSHKETP CDPRPQAEIR AKDMSVFSSL 200
IRENKLDAIM PAHVIYSDVD PRPASGSPYW LKTVLRQELG FDGVIFSDDL 250
SMEGAAIMGS YAERGQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV 300
TRLYHKGSFS RQELMDSARW KAISTRLNQL HERWQEEKAG H 341
Length:341
Mass (Da):37,595
Last modified:February 1, 1997 - v1
Checksum:i9E50C8E4DA87C7A4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U00096 Genomic DNA. Translation: AAC74191.1 .
AP009048 Genomic DNA. Translation: BAA35914.1 .
PIRi H64854.
RefSeqi NP_415625.1. NC_000913.3.
YP_489375.1. NC_007779.1.

3D structure databases

ProteinModelPortali P75949.
SMRi P75949. Positions 1-340.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P75949. 8 interactions.
STRINGi 511145.b1107.

Protein family/group databases

CAZyi GH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbi P75949.
PRIDEi P75949.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74191 ; AAC74191 ; b1107 .
BAA35914 ; BAA35914 ; BAA35914 .
GeneIDi 12930540.
945671.
KEGGi ecj:Y75_p1077.
eco:b1107.
PATRICi 32117457. VBIEscCol129921_1151.

Organism-specific databases

EchoBASEi EB3207.
EcoGenei EG13433. nagZ.

Phylogenomic databases

eggNOGi COG1472.
HOGENOMi HOG000248526.
KOi K01207.
OMAi AHDIDLS.
OrthoDBi EOG6BCT06.
PhylomeDBi P75949.

Enzyme and pathway databases

UniPathwayi UPA00544 .
BioCyci EcoCyc:G6567-MONOMER.
ECOL316407:JW1093-MONOMER.
MetaCyc:G6567-MONOMER.

Miscellaneous databases

PROi P75949.

Gene expression databases

Genevestigatori P75949.

Family and domain databases

Gene3Di 3.20.20.300. 1 hit.
HAMAPi MF_00364. NagZ.
InterProi IPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00933. Glyco_hydro_3. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 115 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