Q7WH65 (NAGZ_BORBR) 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
Ordered Locus Names:	BB3344

Organism

Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

257310 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	353 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides By similarity. HAMAP MF_00364
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. HAMAP MF_00364
Pathway	Cell wall biogenesis; peptidoglycan recycling. HAMAP MF_00364
Subcellular location	Cytoplasm By similarity HAMAP MF_00364.
Sequence similarities	Belongs to the glycosyl hydrolase 3 family. NagZ subfamily.

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	Complete proteome
Gene Ontology (GO)
Biological process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW 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: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 353	353	Beta-hexosaminidase HAMAP MF_00364		PRO_0000210781
Sites
	Active site	263	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WH65 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 7553E72ED1F85824	FASTA	353	38,724
	10 20 30 40 50 60 MSSKKKTKPV LPPGPVMVDV AGTTLTKDEK RRLRNPLVGG VILFARNFTD RRQLCALTRA 70 80 90 100 110 120 IHKARKEPLL IAVDHEGGRV QRFRDDGFTA LPPMQELGKL WDRDPLAAMR LATEAGYVLA 130 140 150 160 170 180 AELRACGVDL SFTPVLDLDY GVSKVIGNRA FHHDARVVTM LSRALAQGLA LAGMAACGKH 190 200 210 220 230 240 FPGHGFVGAD SHHEIPVDPR PLARILKDDA APYAWLGDLV MPAVMPAHVI YPKVDAQPAG 250 260 270 280 290 300 FSRRWVSEIL RERLGYDGVV FSDDLTMEGA SVAGDILARA EAALGAGCDM VLVCNRPDLA 310 320 330 340 350 DELLDRLQVQ HPAASVERIR RLMPRFAAPD WDTLQNDSRY QHARRLQSQI VSG

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640447 Genomic DNA. Translation: CAE33836.1.
RefSeq	NP_889879.1. NC_002927.3.
3D structure databases
ProteinModelPortal	Q7WH65.
ModBase	Search...
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2661310.
GenomeReviews	Gene locus BB3344 in contig BX470250_GR.
KEGG	bbr:BB3344.
PATRIC	21140099. VBIBorBro124907_3414.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG617255.
OMA	DLTMEGA.
PhylomeDB	Q7WH65.
ProtClustDB	PRK05337.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3344-MONOMER.
Family and domain databases
HAMAP	MF_00364. NagZ. [Tree]
InterPro	IPR022956. Beta_hexosaminidase. IPR019800. Glyco_hydro_3_AS. IPR001764. Glyco_hydro_3_N. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:3.20.20.300. Glyco_hydro_3_N. 1 hit.
KO	K01207.
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_BORBR

Accession

Primary (citable) accession number: Q7WH65

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program