Q0VQT2 (Q0VQT2_ALCBS) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Beta-hexosaminidase HAMAP-Rule MF_00364
EC=3.2.1.52 HAMAP-Rule MF_00364

Alternative name(s):
Beta-N-acetylhexosaminidase HAMAP-Rule MF_00364
N-acetyl-beta-glucosaminidase HAMAP-Rule MF_00364

Gene names

Name:	nagZ HAMAP-Rule MF_00364
Ordered Locus Names:	ABO_1018

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP] EMBL CAL16466.1

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax › Alcanivorax borkumensis

Protein attributes

Sequence length	345 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-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 SAAS SAAS022956
Pathway	Cell wall biogenesis; peptidoglycan recycling. HAMAP-Rule MF_00364 SAAS SAAS001764
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00364.
Sequence similarities	Belongs to the glycosyl hydrolase 3 family. NagZ subfamily. HAMAP-Rule MF_00364

Ontologies

Keywords
Biological process	Cell cycle Cell division HAMAP-Rule MF_00364 SAAS SAAS001764 Cell shape Cell wall biogenesis/degradation HAMAP-Rule MF_00364 SAAS SAAS001764 Peptidoglycan synthesis HAMAP-Rule MF_00364 SAAS SAAS001764
Cellular component	Cytoplasm HAMAP-Rule MF_00364 SAAS SAAS001764
Molecular function	Glycosidase HAMAP-Rule MF_00364 SAAS SAAS022956 EMBL CAL16466.1 Hydrolase
Technical term	Complete proteome
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
Sites
	Active site	261	1	By similarity HAMAP-Rule MF_00364

Sequences

	Sequence		Length	Mass (Da)
	Q0VQT2 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 358CF6114C414B4C	FASTA	345	36,802
	10 20 30 40 50 60 MSSVYKVAMS ASASPLLMLD LEGLEVSASE KDMLAHPGAG GLILFARNYV DRQQLAELVQ 70 80 90 100 110 120 QVRAVRPEML IAVDQEGGRV QRFRDGFVRL PPMAALGQRY DQAPAQAVGE ATLLGELMAS 130 140 150 160 170 180 ELTELDIDIS FAPVLDLDYG NSSVIGDRSF HGDADAMIAL AGAFIDGMSA AGMAATGKHF 190 200 210 220 230 240 PGHGHVGADS HLELPIDPRP LSELEAADMR PFMALAPKLD GIMPAHVIYS AVEQQTAGFS 250 260 270 280 290 300 RYWLQTQLRE RLGFRGVIFS DDLSMAGAHG VGGYPQRAQA ALEAGCDMVL ACNCCEGAEQ 310 320 330 340 VLDFLGTQNF SGQVPAAGLR ARPRLPMDAQ RRAVAADLAA ALREH

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SK2 / ATCC 700651 / DSM 11573.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM286690 Genomic DNA. Translation: CAL16466.1.
RefSeq	YP_692738.1. NC_008260.1.
3D structure databases
ProteinModelPortal	Q0VQT2.
ModBase	Search...
Protein-protein interaction databases
STRING	393595.ABO_1018.
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL16466; CAL16466; ABO_1018.
GeneID	4211415.
KEGG	abo:ABO_1018.
PATRIC	20839759. VBIAlcBor124741_1070.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1472.
HOGENOM	HOG000248526.
KO	K01207.
OMA	VVLHCNG.
Enzyme and pathway databases
BioCyc	ABOR393595:GHRI-1019-MONOMER.
UniPathway	UPA00544.
Family and domain databases
Gene3D	3.20.20.300. 1 hit.
HAMAP	MF_00364. NagZ.
InterPro	IPR022956. Beta_hexosaminidase_bac. 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.
ProtoNet	Search...

Entry information

Entry name

Q0VQT2_ALCBS

Accession

Primary (citable) accession number: Q0VQT2

Entry history

Integrated into UniProtKB/TrEMBL:	September 5, 2006
Last sequence update:	September 5, 2006
Last modified:	May 1, 2013
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)