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Beta-N-acetylhexosaminidase (EC 3.2.1.52) (Beta-N-acetylgalactosaminidase) (Beta-N-acetylglucosaminidase) (Hex20)

 HEX20_CELFI             Reviewed;         496 AA.
Q7WUL4;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
28-FEB-2018, entry version 63.
RecName: Full=Beta-N-acetylhexosaminidase;
EC=3.2.1.52;
AltName: Full=Beta-N-acetylgalactosaminidase;
AltName: Full=Beta-N-acetylglucosaminidase;
AltName: Full=Hex20;
Name=hex20; Synonyms=hex20A;
Cellulomonas fimi.
Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae;
Cellulomonas.
NCBI_TaxID=1708;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16762038; DOI=10.1111/j.1742-4658.2006.05308.x;
Mayer C., Vocadlo D.J., Mah M., Rupitz K., Stoll D., Warren R.A.J.,
Withers S.G.;
"Characterization of a beta-N-acetylhexosaminidase and a beta-N-
acetylglucosaminidase/beta-glucosidase from Cellulomonas fimi.";
FEBS J. 273:2929-2941(2006).
-!- FUNCTION: Catalyzes the cleavage of beta-N-acetylglucosaminides
and beta-N-acetylgalactosaminides. Also catalyzes the hydrolysis
of N-acetylchitooligomers. May be involved in chitin degradation.
It is not able to cleave beta-glucosides.
{ECO:0000269|PubMed:16762038}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000269|PubMed:16762038}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=53 uM for 4'-nitrophenyl beta-N-acetyl-D-glucosaminide
{ECO:0000269|PubMed:16762038};
KM=66 uM for 4'-nitrophenyl beta-N-acetyl-D-galactosaminide
{ECO:0000269|PubMed:16762038};
Note=There is a 4-fold greater activity on 4'-nitrophenyl beta-
N-acetyl-D-glucosaminide than on 4'-nitrophenyl beta-N-acetyl-D-
galactosaminide.;
pH dependence:
Optimum pH is 7.3-8.7 with 4'-nitrophenyl beta-N-acetyl-D-
glucosaminide as substrate. Rapidly inactivated above pH 9.5 and
stable from pH 6.0 to 9.5. {ECO:0000269|PubMed:16762038};
-!- PATHWAY: Glycan degradation; chitin degradation.
-!- MISCELLANEOUS: The reaction mechanism involves an oxazolinium ion
intermediate.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
{ECO:0000305}.
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EMBL; AF478459; AAQ05800.1; -; Genomic_DNA.
ProteinModelPortal; Q7WUL4; -.
SMR; Q7WUL4; -.
CAZy; GH20; Glycoside Hydrolase Family 20.
eggNOG; ENOG4105E2D; Bacteria.
eggNOG; COG3525; LUCA.
SABIO-RK; Q7WUL4; -.
UniPathway; UPA00349; -.
GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
Gene3D; 3.30.379.10; -; 1.
InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
InterPro; IPR015883; Glyco_hydro_20_cat.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR029018; Hex-like_dom2.
InterPro; IPR015882; HEX_bac_N.
Pfam; PF00728; Glyco_hydro_20; 1.
Pfam; PF02838; Glyco_hydro_20b; 1.
PRINTS; PR00738; GLHYDRLASE20.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55545; SSF55545; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Chitin degradation;
Direct protein sequencing; Glycosidase; Hydrolase;
Polysaccharide degradation.
CHAIN 1 496 Beta-N-acetylhexosaminidase.
/FTId=PRO_0000252455.
ACT_SITE 298 298 Proton donor. {ECO:0000250}.
SEQUENCE 496 AA; 53326 MW; 7D514C614991706C CRC64;
MPDVAVIPRP VLLETTDGPP FVLTAATILV VDSAPELVAV GVLAADLLGR LSGRPVEVRY
TEGGAPSVVR LRLSEDLPAG DEAYRLVVSE HRVDIDARSA AGLVRAVVTL RQTVSSLGDG
TLTVPALRVE DHPRYAWRGL SIDVARHFFT VDDLKAIIGL LAHYKLNVLH LHLTDDQGWR
VHLPSRPHLT RASAGTSVGG GPGGFYNPAQ LAEIVVARAA RGIRVVPEID VPGHVNAATH
AYGDLTPSGE PTDVYTGIEV GFSRLHDDLP ATRPFLRDVF TDLAAMTPGE YVHIGGDEVL
TMDHDKYARL VGYAASVVRD AGKKVVGWQE ISSTPLEPGT VVQYWDINAD PAPFVAAAQA
GAHVLMSPGS RAYLDMKYDA TTELGLEWAG HIELRDAYDW EPSTLIPGVP PESVIGVEAA
VWTETLTDLG ELTSMLLPRL AAVAEVAWTA PQDRDWDDFS GRVAQHAPFW DRVGFRWHAS
PQVSWPGPGS APGAAF


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