P96157 (NAGZ_VIBFU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase
EC=3.2.1.52

Alternative name(s):
Beta-N-acetylhexosaminidase
N-acetyl-beta-glucosaminidase

Gene names

Name:	nagZ
Synonyms:	exo II

Organism

Vibrio furnissii

Taxonomic identifier

29494 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides By similarity. Hydrolyzes rapidly p-nitrophenyl-N-acetyl-beta-D-glucosaminide (PNP-beta-GlcNAc) and 4-methylumbelliferyl-beta-GlcNAc, and slightly active on p-nitrophenyl-beta-GalNAc. May play a role in signal transduction between host and organism. HAMAP-Rule MF_00364
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. HAMAP-Rule MF_00364
Enzyme regulation	Inhibited by GlcNAc, 2-acetamido-1-N-(4-L-aspartyl)-2-deoxy-beta-D-glucopyranosylamine (GlcNAc-Asn) and O-(2-acetamido-2-deoxy-D-glucopyranosylidene)-amino-N-phenylcarbamate (PUGNAc). HAMAP-Rule MF_00364
Pathway	Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_00364
Subunit structure	Monomer Potential.
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00364.
Sequence similarities	Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 7.0. HAMAP-Rule MF_00364 Temperature dependence: Optimum temperature is 45 degrees Celsius.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cytoplasm
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan turnover Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 329	329	Beta-hexosaminidase HAMAP-Rule MF_00364		PRO_0000210801
Sites
	Active site	242	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P96157 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 440C6A9B18143C34	FASTA	329	36,181
	10 20 30 40 50 60 MGPLWLDVEG CELTAEDREI LAHPTVGGVI LFARNYHDNQ QLLALNTAIR QAAKRPILIG 70 80 90 100 110 120 VDQEGGRVQR FRDGFSKIPA AQLYARSDNG TQLAEDGGWL MAAELIAHDI DLSFAPVLDK 130 140 150 160 170 180 GFDCRAIGNR AFGDDVQTVL TYSSAYMRGM KSVGMATTGK HFPGHGAVIA DSHLETPYDE 190 200 210 220 230 240 RDSIADDMTI FRAQIEAGIL DAMMPAHVIY PHYDAQPASG SPYWLKQVLR QELGFQGIVF 250 260 270 280 290 300 SDDLSMEGAA IMGGPAERAQ QSLDAGCDMV LMCNKRESAV AVLDQLPISV VPQAQSLLKQ 310 320 QQFTYRELKA TERWKQAYQA LQRLIDAHS

References

[1]	"Molecular cloning and characterization of a novel beta-N-acetyl-D-glucosaminidase from Vibrio furnissii." Chitlaru E., Roseman S. J. Biol. Chem. 271:33433-33439(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-16. Strain: 7225.
[2]	Chitlaru E., Roseman S. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 70-80.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U52818 Genomic DNA. Translation: AAC44686.2.
3D structure databases
ProteinModelPortal	P96157.
SMR	P96157. Positions 1-329.
ModBase	Search...
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	P96157.
UniPathway	UPA00544.
Family and domain databases
Gene3D	3.20.20.300. 1 hit.
HAMAP	MF_00364. NagZ.
InterPro	IPR022956. Beta_hexosaminidase_bac. IPR019800. Glyco_hydro_3_AS. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF00933. Glyco_hydro_3. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00775. GLYCOSYL_HYDROL_F3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NAGZ_VIBFU

Accession

Primary (citable) accession number: P96157

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 30, 2000
Last modified:	April 3, 2013
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program