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Protein

Beta-hexosaminidase

Gene

nagZ

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 (By similarity). Contributes to intrinsic fosfomycin resistance in P.aeruginosa (PubMed:24819062).UniRule annotation1 Publication

Catalytic activityi

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

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.UniRule annotation1 Publication
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 sitei62SubstrateUniRule annotation1
Binding sitei70SubstrateUniRule annotation1
Binding sitei131SubstrateUniRule annotation1
Sitei172Important for catalytic activityUniRule annotation1
Active sitei174Proton donor/acceptorUniRule annotation1
Active sitei244NucleophileUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processAntibiotic resistance, Cell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

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:PA3005
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3005.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Deletion of this gene increases fosfomycin sensitivity.1 Publication

Chemistry databases

ChEMBLiCHEMBL1667674.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002107951 – 332Beta-hexosaminidaseAdd BLAST332

Proteomic databases

PaxDbiQ9HZK0.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA3005.

Chemistry databases

BindingDBiQ9HZK0.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Beta strandi10 – 13Combined sources4
Helixi16 – 22Combined sources7
Beta strandi27 – 32Combined sources6
Helixi34 – 36Combined sources3
Helixi40 – 53Combined sources14
Beta strandi58 – 61Combined sources4
Turni64 – 66Combined sources3
Helixi67 – 71Combined sources5
Helixi81 – 85Combined sources5
Beta strandi86 – 88Combined sources3
Helixi90 – 107Combined sources18
Beta strandi111 – 113Combined sources3
Helixi116 – 118Combined sources3
Turni126 – 128Combined sources3
Turni131 – 133Combined sources3
Helixi137 – 153Combined sources17
Beta strandi159 – 163Combined sources5
Beta strandi166 – 169Combined sources4
Beta strandi173 – 176Combined sources4
Helixi184 – 189Combined sources6
Turni190 – 192Combined sources3
Helixi193 – 198Combined sources6
Turni199 – 201Combined sources3
Beta strandi203 – 207Combined sources5
Turni213 – 215Combined sources3
Beta strandi216 – 219Combined sources4
Helixi220 – 222Combined sources3
Helixi224 – 227Combined sources4
Helixi228 – 234Combined sources7
Beta strandi239 – 245Combined sources7
Beta strandi249 – 251Combined sources3
Turni252 – 254Combined sources3
Helixi257 – 267Combined sources11
Beta strandi270 – 273Combined sources4
Helixi278 – 290Combined sources13
Helixi299 – 302Combined sources4
Helixi312 – 314Combined sources3
Helixi316 – 327Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5G1MX-ray1.80A/B1-332[»]
5G2MX-ray3.00A/B1-332[»]
5G3RX-ray2.18A/B1-332[»]
5G5KX-ray3.10A/B1-332[»]
5G5UX-ray2.25A/B1-332[»]
5G6TX-ray2.15A/B1-332[»]
5LY7X-ray3.10A/B1-332[»]
ProteinModelPortaliQ9HZK0.
SMRiQ9HZK0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni161 – 162Substrate bindingUniRule annotation2

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4107QPA. Bacteria.
COG1472. LUCA.
HOGENOMiHOG000248526.
InParanoidiQ9HZK0.
KOiK01207.
OMAiHKETPRD.
PhylomeDBiQ9HZK0.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
HAMAPiMF_00364. NagZ. 1 hit.
InterProiView protein in InterPro
IPR022956. Beta_hexosaminidase_bac.
IPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
PfamiView protein in Pfam
PF00933. Glyco_hydro_3. 1 hit.
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00775. GLYCOSYL_HYDROL_F3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HZK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGSLMLDIG GTWLTAEDRQ ILRHPEVGGL IIFARNIEHP AQVRELCAAI
60 70 80 90 100
RAIRPDLLLA VDQEGGRVQR LRQGFVRLPA MRAIADNPNA EELAEHCGWL
110 120 130 140 150
MATEVQAVGL DLSFAPVLDL DHQRSAVVGS RAFEGDPERA ALLAGAFIRG
160 170 180 190 200
MHAAGMAATG KHFPGHGWAE ADSHVAIPED ARSLEEIRRS DLVPFARLAG
210 220 230 240 250
QLDALMPAHV IYPQVDPQPA GFSRRWLQEI LRGELKFDGV IFSDDLSMAG
260 270 280 290 300
AHVVGDAASR IEAALAAGCD MGLVCNDRAS AELALAALQR LKVTPPSRLQ
310 320 330
RMRGKGYANT DYRQQPRWLE ALSALRAAQL ID
Length:332
Mass (Da):36,101
Last modified:March 1, 2001 - v1
Checksum:iBA472E62B44A097A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG06393.1.
PIRiG83270.
RefSeqiNP_251695.1. NC_002516.2.
WP_003118092.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG06393; AAG06393; PA3005.
GeneIDi880216.
KEGGipae:PA3005.
PATRICifig|208964.12.peg.3153.

Similar proteinsi

Entry informationi

Entry nameiNAGZ_PSEAE
AccessioniPrimary (citable) accession number: Q9HZK0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: March 1, 2001
Last modified: September 27, 2017
This is version 110 of the entry and version 1 of the sequence. See 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