ID   NAG3_CELFI              Reviewed;         564 AA.
AC   Q7WUL3;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Beta-N-acetylglucosaminidase/beta-glucosidase;
DE            EC=3.2.1.21;
DE            EC=3.2.1.52;
DE   AltName: Full=3-beta-N-acetyl-D-glucosaminidase/beta-D-glucosidase;
DE   AltName: Full=Nag3;
GN   Name=nag3; Synonyms=nag3A;
OS   Cellulomonas fimi.
OC   Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas.
OX   NCBI_TaxID=1708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP   CATALYTIC ACTIVITY, REACTION MECHANISM, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16762038; DOI=10.1111/j.1742-4658.2006.05308.x;
RA   Mayer C., Vocadlo D.J., Mah M., Rupitz K., Stoll D., Warren R.A.J.,
RA   Withers S.G.;
RT   "Characterization of a beta-N-acetylhexosaminidase and a beta-N-
RT   acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi.";
RL   FEBS J. 273:2929-2941(2006).
CC   -!- FUNCTION: Catalyzes the cleavage of beta-N-acetyl-D-glucosaminides and
CC       beta-D-glucosides. Might be involved in the degradation of glucuronic
CC       acid-containing glycosaminoglycans such as hyaluronic acid.
CC       {ECO:0000269|PubMed:16762038}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine
CC         residues in N-acetyl-beta-D-hexosaminides.; EC=3.2.1.52;
CC         Evidence={ECO:0000269|PubMed:16762038};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal, non-reducing beta-D-glucosyl residues
CC         with release of beta-D-glucose.; EC=3.2.1.21;
CC         Evidence={ECO:0000269|PubMed:16762038};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.7 mM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide
CC         {ECO:0000269|PubMed:16762038};
CC         Note=The catalytic efficiencies against 4'-nitrophenyl beta-N-acetyl-
CC         D-glucosaminide and 4'-nitrophenyl beta-D-glucopyranoside are
CC         similar.;
CC       pH dependence:
CC         Optimum pH is 7.3 with 4'-nitrophenyl beta-D-glucopyranoside as
CC         substrate. Precipitates below pH 6 and stable from pH 6.8 to 8.4.
CC         {ECO:0000269|PubMed:16762038};
CC   -!- MISCELLANEOUS: Catalyzes hydrolysis by a double-displacement mechanism
CC       via a covalent glycosyl-enzyme intermediate, involving the
CC       participation of a catalytic nucleophilic group in the enzyme active
CC       site.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 3 family. {ECO:0000305}.
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DR   EMBL; AF478460; AAQ05801.1; -; Genomic_DNA.
DR   RefSeq; WP_013772128.1; NZ_LR134387.1.
DR   AlphaFoldDB; Q7WUL3; -.
DR   SMR; Q7WUL3; -.
DR   CAZy; GH3; Glycoside Hydrolase Family 3.
DR   OMA; WAFAPIV; -.
DR   SABIO-RK; Q7WUL3; -.
DR   GO; GO:0008422; F:beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.300; -; 1.
DR   Gene3D; 3.40.50.1700; -; 1.
DR   InterPro; IPR019800; Glyco_hydro_3_AS.
DR   InterPro; IPR036881; Glyco_hydro_3_C_sf.
DR   InterPro; IPR001764; Glyco_hydro_3_N.
DR   InterPro; IPR036962; Glyco_hydro_3_N_sf.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00933; Glyco_hydro_3; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00775; GLYCOSYL_HYDROL_F3; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycosidase; Hydrolase;
KW   Polysaccharide degradation.
FT   CHAIN           1..564
FT                   /note="Beta-N-acetylglucosaminidase/beta-glucosidase"
FT                   /id="PRO_0000252454"
FT   ACT_SITE        283
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   564 AA;  59993 MW;  9B1428A4561F71D3 CRC64;
     MIDLTAAPFS LDDDGIAWVR TTLAEMGEDE KLGQLFCLIT YTSDPEYLGY LTRGLHVGGV
     MLRTMTAADA AATVTTLQST ATVPLLISAN LEGGASQTVQ EATHVGSNMA LAATGSTDHV
     RRAATVIGRE ARALGINWAF TPVVDIDLNF RNPITNTRTF GADAATVAAM GAEYVEAIQA
     QGLAASAKHF PGDGVDERDQ HLLASVNTMS VEEWDDSFGV VYRAAIAAGV KTVMVGHIML
     PAYSRALRPG VADRDILPGV VAEELLNDLL RDRLGFNGLV VSDSTTMAGL ASVLPRSQAV
     PRVIAAGCDM FLFTKNLDED FGYMRAGIRD GVITPERLDE AVTRILALKA SLGLHRGTNL
     PAQGAAGVLA DPDHSATARE VAASSITLVK EEPGVLPITR ERYPRVLVYD LQNGGSPIGQ
     GARAGAVEQF VDALVEAGHD VTRFEPGGGW EGMAAPTTDV TERHDLVLYL ANLSTRSNQT
     VVRIEWAEPM GANVPAYVHS VPTVFVSFEN PYHLFDVPRV RTLINTYGSS PVVLETLLAA
     LQGKAPFAGS SPVDAFCGQW DTHL