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Protein

Beta-N-acetylglucosaminidase/beta-glucosidase

Gene

nag3

Organism
Cellulomonas fimi
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.1 Publication
Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.1 Publication

Kineticsi

The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are similar.

  1. KM=2.7 mM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide1 Publication

pH dependencei

Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei283 – 2831NucleophileBy similarity

GO - Molecular functioni

  1. beta-glucosidase activity Source: UniProtKB-EC
  2. beta-N-acetylhexosaminidase activity Source: UniProtKB-EC

GO - Biological processi

  1. polysaccharide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

SABIO-RKQ7WUL3.

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Names & Taxonomyi

Protein namesi
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 namesi
Name:nag3
Synonyms:nag3A
OrganismiCellulomonas fimi
Taxonomic identifieri1708 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 564564Beta-N-acetylglucosaminidase/beta-glucosidasePRO_0000252454Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ7WUL3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
InterProiIPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7WUL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY
60 70 80 90 100
LTRGLHVGGV MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ
110 120 130 140 150
EATHVGSNMA LAATGSTDHV RRAATVIGRE ARALGINWAF TPVVDIDLNF
160 170 180 190 200
RNPITNTRTF GADAATVAAM GAEYVEAIQA QGLAASAKHF PGDGVDERDQ
210 220 230 240 250
HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML PAYSRALRPG
260 270 280 290 300
VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV
310 320 330 340 350
PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA
360 370 380 390 400
SLGLHRGTNL PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR
410 420 430 440 450
ERYPRVLVYD LQNGGSPIGQ GARAGAVEQF VDALVEAGHD VTRFEPGGGW
460 470 480 490 500
EGMAAPTTDV TERHDLVLYL ANLSTRSNQT VVRIEWAEPM GANVPAYVHS
510 520 530 540 550
VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA LQGKAPFAGS
560
SPVDAFCGQW DTHL
Length:564
Mass (Da):59,993
Last modified:October 1, 2003 - v1
Checksum:i9B1428A4561F71D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478460 Genomic DNA. Translation: AAQ05801.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF478460 Genomic DNA. Translation: AAQ05801.1.

3D structure databases

ProteinModelPortaliQ7WUL3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKQ7WUL3.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
InterProiIPR019800. Glyco_hydro_3_AS.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00933. Glyco_hydro_3. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00775. GLYCOSYL_HYDROL_F3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiNAG3_CELFI
AccessioniPrimary (citable) accession number: Q7WUL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 1, 2003
Last modified: October 1, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.