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Q9KU37

- NAGZ_VIBCH

UniProt

Q9KU37 - NAGZ_VIBCH

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Protein
Beta-hexosaminidase
Gene
nagZ, VC_0692
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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. 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.3 Publications

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.3 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei62 – 621Substrate
Binding sitei70 – 701Substrate By similarity
Binding sitei130 – 1301Substrate
Sitei171 – 1711Important for catalytic activity By similarity
Active sitei173 – 1731Proton donor/acceptor By similarity
Active sitei242 – 2421Nucleophile

GO - Molecular functioni

  1. beta-N-acetylhexosaminidase activity Source: TIGR

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: TIGR
  6. peptidoglycan-based cell wall biogenesis Source: TIGR
  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

BioCyciVCHO:VC0692-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
Ordered Locus Names:VC_0692
OrganismiVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Taxonomic identifieri243277 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio
ProteomesiUP000000584: Chromosome 1

Subcellular locationi

Cytoplasm By similarity 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 – 330330Beta-hexosaminidaseUniRule annotation
PRO_0000210800Add
BLAST

Interactioni

Subunit structurei

Monomer Reviewed prediction.

Protein-protein interaction databases

STRINGi243277.VC0692.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 64
Beta strandi9 – 124
Helixi15 – 217
Beta strandi26 – 316
Helixi33 – 353
Helixi39 – 5315
Beta strandi58 – 614
Beta strandi63 – 653
Beta strandi68 – 703
Helixi81 – 866
Helixi90 – 10617
Turni107 – 1093
Turni125 – 1273
Helixi128 – 1303
Helixi136 – 15217
Beta strandi158 – 1625
Beta strandi173 – 1764
Helixi185 – 19713
Beta strandi201 – 2055
Turni211 – 2133
Beta strandi214 – 2163
Helixi218 – 2203
Helixi222 – 2254
Helixi226 – 2327
Beta strandi237 – 2437
Helixi244 – 2463
Helixi249 – 2524
Helixi255 – 26511
Beta strandi268 – 2714
Helixi276 – 28510
Helixi292 – 2976
Helixi305 – 3095
Helixi312 – 32817

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 1-330.

Miscellaneous databases

EvolutionaryTraceiQ9KU37.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 1612Substrate bindingUniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1472.
KOiK01207.
OMAiNHVVQAS.
OrthoDBiEOG6BCT06.

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.

Q9KU37-1 [UniParc]FASTAAdd to Basket

« Hide

MGPLWLDVAG YELSAEDREI LQHPTVGGVI LFGRNYHDNQ QLLALNKAIR    50
QAAKRPILIG VDQEGGRVQR FREGFSRIPP AQYYARAENG VELAEQGGWL 100
MAAELIAHDV DLSFAPVLDM GFACKAIGNR AFGEDVQTVL KHSSAFLRGM 150
KAVGMATTGK HFPGHGAVIA DSHLETPYDE RETIAQDMAI FRAQIEAGVL 200
DAMMPAHVVY PHYDAQPASG SSYWLKQVLR EELGFKGIVF SDDLSMEGAA 250
VMGGPVERSH QALVAGCDMI LICNKREAAV EVLDNLPIME VPQAEALLKK 300
QQFSYSELKR LERWQQASAN MQRLIEQFSE 330
Length:330
Mass (Da):36,466
Last modified:October 1, 2000 - v1
Checksum:iA737BD82C149D3A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93857.1.
PIRiA82292.
RefSeqiNP_230341.1. NC_002505.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE003852 Genomic DNA. Translation: AAF93857.1 .
PIRi A82292.
RefSeqi NP_230341.1. NC_002505.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1TR9 X-ray 1.80 A 2-330 [» ]
1Y65 X-ray 1.85 A 2-330 [» ]
2OXN X-ray 1.70 A 1-330 [» ]
3GS6 X-ray 2.30 A 1-330 [» ]
3GSM X-ray 2.40 A 1-330 [» ]
ProteinModelPortali Q9KU37.
SMRi Q9KU37. Positions 1-330.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243277.VC0692.

Chemistry

ChEMBLi CHEMBL1075035.

Protein family/group databases

CAZyi GH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

DNASUi 2615481.
Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF93857 ; AAF93857 ; VC_0692 .
GeneIDi 2615481.
KEGGi vch:VC0692.
PATRICi 20080499. VBIVibCho83274_0663.

Phylogenomic databases

eggNOGi COG1472.
KOi K01207.
OMAi NHVVQAS.
OrthoDBi EOG6BCT06.

Enzyme and pathway databases

UniPathwayi UPA00544 .
BioCyci VCHO:VC0692-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9KU37.
PROi Q9KU37.

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: ATCC 39315 / El Tor Inaba N16961.
  2. "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: FUNCTION, CATALYTIC ACTIVITY.
  3. "Structure of beta-hexosaminidase from Vibrio cholerae in complex with N-acetyl-D-glucosamine."
    Gorman J., Shapiro L.
    Submitted (DEC-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH N-ACETYL-D-GLUCOSAMINE.
  4. "Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta-lactam resistance."
    Stubbs K.A., Balcewich M., Mark B.L., Vocadlo D.J.
    J. Biol. Chem. 282:21382-21391(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, FUNCTION, CATALYTIC ACTIVITY.
  5. "Insight into a strategy for attenuating AmpC-mediated beta-lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ."
    Balcewich M.D., Stubbs K.A., He Y., James T.W., Davies G.J., Vocadlo D.J., Mark B.L.
    Protein Sci. 18:1541-1551(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, CATALYTIC ACTIVITY, FUNCTION.

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: June 11, 2014
This is version 94 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

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