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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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. Plays a role in beta-lactam antibiotic resistance via its role in generating anhydro-N-acetylmuramic acid-linked peptides; these peptides function as signaling molecules that induce high-level expression of the beta-lactamase AmpC.2 PublicationsUniRule annotation

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.2 PublicationsUniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Substrate
Binding sitei70 – 701SubstrateUniRule annotation
Binding sitei133 – 1331Substrate
Sitei174 – 1741Important for catalytic activityUniRule annotation
Active sitei176 – 1761Proton donor/acceptor1 Publication
Active sitei248 – 2481Nucleophile1 PublicationUniRule 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: UniProtKB-HAMAP
  7. regulation of cell shape Source: UniProtKB-KW
  8. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciSENT99287:GCTI-1218-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
Ordered Locus Names:STM1209
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000001014: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761H → G: Reduced enzyme activity.
Mutagenesisi248 – 2481D → N: Abolishes enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Beta-hexosaminidasePRO_0000210797Add
BLAST

Proteomic databases

PaxDbiQ8ZQ06.
PRIDEiQ8ZQ06.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM1209.

Structurei

Secondary structure

1
341
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64Combined sources
Beta strandi9 – 124Combined sources
Helixi15 – 217Combined sources
Beta strandi26 – 316Combined sources
Helixi33 – 353Combined sources
Helixi39 – 5214Combined sources
Beta strandi58 – 614Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 703Combined sources
Helixi83 – 10927Combined sources
Turni110 – 1123Combined sources
Turni128 – 1303Combined sources
Helixi131 – 1333Combined sources
Helixi139 – 15618Combined sources
Beta strandi161 – 1655Combined sources
Beta strandi175 – 1784Combined sources
Helixi186 – 1916Combined sources
Helixi193 – 20210Combined sources
Beta strandi207 – 2115Combined sources
Turni217 – 2193Combined sources
Helixi224 – 2263Combined sources
Helixi228 – 2314Combined sources
Helixi232 – 2387Combined sources
Beta strandi243 – 2497Combined sources
Helixi250 – 2523Combined sources
Helixi256 – 2583Combined sources
Helixi261 – 27111Combined sources
Beta strandi274 – 2785Combined sources
Helixi282 – 29110Combined sources
Helixi298 – 3036Combined sources
Helixi311 – 3166Combined sources
Helixi318 – 33922Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GVFX-ray1.35A/B1-341[»]
4GVGX-ray1.70A/B1-341[»]
4GVHX-ray1.45A/B1-341[»]
4GVIX-ray1.55A/B1-341[»]
4HZMX-ray1.45A/B1-341[»]
ProteinModelPortaliQ8ZQ06.
SMRiQ8ZQ06. Positions 1-334.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
KOiK01207.
OMAiYTEADPR.
OrthoDBiEOG6BCT06.
PhylomeDBiQ8ZQ06.

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.

Q8ZQ06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPVMLNVEG CELDAEEREI LAHPLVGGLI LFTRNYHDPE QLRELVRQIR
60 70 80 90 100
AASRNHLVVA VDQEGGRVQR FREGFTRLPA AQSFFALHGL EEGGRLAQEA
110 120 130 140 150
GWLMASEMIA MDIDISFAPV LDVGHISAAI GERSYHADPA KALAMATRFI
160 170 180 190 200
DGMHDAGMKT TGKHFPGHGA VTADSHKETP CDPRPETDIR GKDMSVFRTL
210 220 230 240 250
ISENKLDAIM PAHVIYRAID PRPASGSPYW LKTVLRQELG FDGVIFSDDL
260 270 280 290 300
SMEGAAIMGS YAERAQASLD AGCDMILVCN NRKGAVSVLD NLSPIKAERV
310 320 330 340
TRLYHKGSFS RRELMDSARW KTASAQLNQL HERWQEEKAG H
Length:341
Mass (Da):37,698
Last modified:March 1, 2002 - v1
Checksum:iE07E83487336A300
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL20138.1.
RefSeqiNP_460179.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL20138; AAL20138; STM1209.
GeneIDi1252727.
KEGGistm:STM1209.
PATRICi32380867. VBISalEnt20916_1278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006468 Genomic DNA. Translation: AAL20138.1.
RefSeqiNP_460179.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GVFX-ray1.35A/B1-341[»]
4GVGX-ray1.70A/B1-341[»]
4GVHX-ray1.45A/B1-341[»]
4GVIX-ray1.55A/B1-341[»]
4HZMX-ray1.45A/B1-341[»]
ProteinModelPortaliQ8ZQ06.
SMRiQ8ZQ06. Positions 1-334.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM1209.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Proteomic databases

PaxDbiQ8ZQ06.
PRIDEiQ8ZQ06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL20138; AAL20138; STM1209.
GeneIDi1252727.
KEGGistm:STM1209.
PATRICi32380867. VBISalEnt20916_1278.

Phylogenomic databases

eggNOGiCOG1472.
HOGENOMiHOG000248526.
KOiK01207.
OMAiYTEADPR.
OrthoDBiEOG6BCT06.
PhylomeDBiQ8ZQ06.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciSENT99287:GCTI-1218-MONOMER.

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: LT2 / SGSC1412 / ATCC 700720.
  2. "Active site plasticity within the glycoside hydrolase NagZ underlies a dynamic mechanism of substrate distortion."
    Bacik J.P., Whitworth G.E., Stubbs K.A., Vocadlo D.J., Mark B.L.
    Chem. Biol. 19:1471-1482(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH DISACCHARIDE SUBSTRATE, CATALYTIC ACTIVITY, FUNCTION, ACTIVE SITE, MUTAGENESIS OF ASP-248.
  3. "The development of selective inhibitors of NagZ: increased susceptibility of Gram-negative bacteria to beta-lactams."
    Stubbs K.A., Bacik J.P., Perley-Robertson G.E., Whitworth G.E., Gloster T.M., Vocadlo D.J., Mark B.L.
    ChemBioChem 14:1973-1981(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiNAGZ_SALTY
AccessioniPrimary (citable) accession number: Q8ZQ06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: January 7, 2015
This is version 84 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.