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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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.UniRule annotation3 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.UniRule annotation3 Publications

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei62Substrate1
Binding sitei70SubstrateUniRule annotation1
Binding sitei130Substrate1
Sitei171Important for catalytic activityUniRule annotation1
Active sitei173Proton donor/acceptorUniRule annotation1
Active sitei242Nucleophile1

GO - Molecular functioni

  • beta-N-acetylhexosaminidase activity Source: TIGR

GO - Biological processi

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

BioCyciVCHO:VC0692-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:VC_0692
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
Proteomesi
  • UP000000584 Componenti: Chromosome 1

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075035.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002108001 – 330Beta-hexosaminidaseAdd BLAST330

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

STRINGi243277.VC0692.

Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Beta strandi9 – 12Combined sources4
Helixi15 – 21Combined sources7
Beta strandi26 – 31Combined sources6
Helixi33 – 35Combined sources3
Helixi39 – 53Combined sources15
Beta strandi58 – 61Combined sources4
Beta strandi63 – 65Combined sources3
Beta strandi68 – 70Combined sources3
Helixi81 – 86Combined sources6
Helixi90 – 106Combined sources17
Turni107 – 109Combined sources3
Turni125 – 127Combined sources3
Helixi128 – 130Combined sources3
Helixi136 – 152Combined sources17
Beta strandi158 – 162Combined sources5
Beta strandi173 – 176Combined sources4
Helixi185 – 197Combined sources13
Beta strandi201 – 205Combined sources5
Turni211 – 213Combined sources3
Beta strandi214 – 216Combined sources3
Helixi218 – 220Combined sources3
Helixi222 – 225Combined sources4
Helixi226 – 232Combined sources7
Beta strandi237 – 243Combined sources7
Helixi244 – 246Combined sources3
Helixi249 – 252Combined sources4
Helixi255 – 265Combined sources11
Beta strandi268 – 271Combined sources4
Helixi276 – 285Combined sources10
Helixi292 – 297Combined sources6
Helixi305 – 309Combined sources5
Helixi312 – 328Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TR9X-ray1.80A2-330[»]
1Y65X-ray1.85A2-330[»]
2OXNX-ray1.70A1-330[»]
3GS6X-ray2.30A1-330[»]
3GSMX-ray2.40A1-330[»]
ProteinModelPortaliQ9KU37.
SMRiQ9KU37.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9KU37.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni160 – 161Substrate binding2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QPA. Bacteria.
COG1472. LUCA.
KOiK01207.
OMAiDMVLICN.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ. 1 hit.
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.

Q9KU37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR
60 70 80 90 100
QAAKRPILIG VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL
110 120 130 140 150
MAAELIAHDV DLSFAPVLDM GFACKAIGNR AFGEDVQTVL KHSSAFLRGM
160 170 180 190 200
KAVGMATTGK HFPGHGAVIA DSHLETPYDE RETIAQDMAI FRAQIEAGVL
210 220 230 240 250
DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF SDDLSMEGAA
260 270 280 290 300
VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK
310 320 330
QQFSYSELKR LERWQQASAN MQRLIEQFSE
Length:330
Mass (Da):36,466
Last modified:October 1, 2000 - v1
Checksum:iA737BD82C149D3A2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93857.1.
PIRiA82292.
RefSeqiNP_230341.1. NC_002505.1.
WP_000529115.1. NC_002505.1.

Genome annotation databases

EnsemblBacteriaiAAF93857; AAF93857; VC_0692.
GeneIDi2615481.
KEGGivch:VC0692.
PATRICi20080499. VBIVibCho83274_0663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE003852 Genomic DNA. Translation: AAF93857.1.
PIRiA82292.
RefSeqiNP_230341.1. NC_002505.1.
WP_000529115.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TR9X-ray1.80A2-330[»]
1Y65X-ray1.85A2-330[»]
2OXNX-ray1.70A1-330[»]
3GS6X-ray2.30A1-330[»]
3GSMX-ray2.40A1-330[»]
ProteinModelPortaliQ9KU37.
SMRiQ9KU37.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243277.VC0692.

Chemistry databases

ChEMBLiCHEMBL1075035.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

DNASUi2615481.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF93857; AAF93857; VC_0692.
GeneIDi2615481.
KEGGivch:VC0692.
PATRICi20080499. VBIVibCho83274_0663.

Phylogenomic databases

eggNOGiENOG4107QPA. Bacteria.
COG1472. LUCA.
KOiK01207.
OMAiDMVLICN.

Enzyme and pathway databases

UniPathwayiUPA00544.
BioCyciVCHO:VC0692-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9KU37.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ. 1 hit.
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...

Entry informationi

Entry nameiNAGZ_VIBCH
AccessioniPrimary (citable) accession number: Q9KU37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: October 1, 2000
Last modified: November 2, 2016
This is version 108 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

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 one 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.