Q7WUL3 (NAG3_CELFI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-N-acetylglucosaminidase/beta-glucosidase
EC=3.2.1.21
EC=3.2.1.52

Alternative name(s):
3-beta-N-acetyl-D-glucosaminidase/beta-D-glucosidase
Nag3

Gene names

Name:	nag3
Synonyms:	nag3A

Organism

Cellulomonas fimi

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	564 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the cleavage of beta-N-acetyl-D-glucosaminides and beta-D-glucosides. Might be involved in the degradation of glucuronic acid-containing glycosaminoglycans such as hyaluronic acid. Ref.1
Catalytic activity	Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. Ref.1 Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. Ref.1
Miscellaneous	Catalyzes hydrolysis by a double-displacement mechanism via a covalent glycosyl-enzyme intermediate, involving the participation of a catalytic nucleophilic group in the enzyme active site.
Sequence similarities	Belongs to the glycosyl hydrolase 3 family.
Biophysicochemical properties	Kinetic parameters: The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar. KM=2.7 mM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide Ref.1 pH dependence: Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Polysaccharide degradation
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	beta-N-acetylhexosaminidase activity Inferred from electronic annotation. Source: EC beta-glucosidase 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 – 564	564	Beta-N-acetylglucosaminidase/beta-glucosidase		PRO_0000252454
Sites
	Active site	283	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7WUL3 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 9B1428A4561F71D3	FASTA	564	59,993
	10 20 30 40 50 60 MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY LTRGLHVGGV 70 80 90 100 110 120 MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ EATHVGSNMA LAATGSTDHV 130 140 150 160 170 180 RRAATVIGRE ARALGINWAF TPVVDIDLNF RNPITNTRTF GADAATVAAM GAEYVEAIQA 190 200 210 220 230 240 QGLAASAKHF PGDGVDERDQ HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML 250 260 270 280 290 300 PAYSRALRPG VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV 310 320 330 340 350 360 PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA SLGLHRGTNL 370 380 390 400 410 420 PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR ERYPRVLVYD LQNGGSPIGQ 430 440 450 460 470 480 GARAGAVEQF VDALVEAGHD VTRFEPGGGW EGMAAPTTDV TERHDLVLYL ANLSTRSNQT 490 500 510 520 530 540 VVRIEWAEPM GANVPAYVHS VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA 550 560 LQGKAPFAGS SPVDAFCGQW DTHL

References

[1]

"Characterization of a beta-N-acetylhexosaminidase and a beta-N-acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi." Mayer C., Vocadlo D.J., Mah M., Rupitz K., Stoll D., Warren R.A.J., Withers S.G. FEBS J. 273:2929-2941(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF478460 Genomic DNA. Translation: AAQ05801.1.
3D structure databases
ProteinModelPortal	Q7WUL3.
ModBase	Search...
Protein family/group databases
CAZy	GH3. Glycoside Hydrolase Family 3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
SABIO-RK	Q7WUL3.
Family and domain databases
Gene3D	3.20.20.300. 1 hit.
InterPro	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

NAG3_CELFI

Accession

Primary (citable) accession number: Q7WUL3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 17, 2006
Last sequence update:	October 1, 2003
Last modified:	March 6, 2013
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program