ID   E3NYM0_PENOX            Unreviewed;       601 AA.
AC   E3NYM0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
OS   Penicillium oxalicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69781 {ECO:0000313|EMBL:ABY57948.1};
RN   [1] {ECO:0000313|EMBL:ABY57948.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bezouska K., Ryslava H., Kumar V., Kalendova A., Slamova K., Bojarova P.,
RA   Pompach P., Novak P., Hofbauerova K., Kren V.;
RT   "Unique substrate specificity of beta-N-acetylhexosaminidase from
RT   Penicillium oxalicum is explained by a rapid evolution within the family of
RT   fungal hexosaminidases.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001231,
CC         ECO:0000256|PIRNR:PIRNR001093};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC       {ECO:0000256|ARBA:ARBA00006285, ECO:0000256|PIRNR:PIRNR001093}.
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DR   EMBL; EU189026; ABY57948.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3NYM0; -.
DR   SMR; E3NYM0; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   CLAE; HEX20A_PENOX; -.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd06562; GH20_HexA_HexB-like; 1.
DR   Gene3D; 3.30.379.10; Chitobiase/beta-hexosaminidase domain 2-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR025705; Beta_hexosaminidase_sua/sub.
DR   InterPro; IPR015883; Glyco_hydro_20_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR029018; Hex-like_dom2.
DR   InterPro; IPR029019; HEX_eukaryotic_N.
DR   PANTHER; PTHR22600; BETA-HEXOSAMINIDASE; 1.
DR   PANTHER; PTHR22600:SF21; BETA-HEXOSAMINIDASE A; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF14845; Glycohydro_20b2; 1.
DR   PIRSF; PIRSF001093; B-hxosamndse_ab_euk; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF55545; beta-N-acetylhexosaminidase-like domain; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001093};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR001093};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..601
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003178297"
FT   DOMAIN          24..159
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          182..544
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        346
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   601 AA;  67098 MW;  76A8554F41DBD6EA CRC64;
     MKCTALFGGL ALSASLATAV KVNPLPAPRN ITWGSSGPIS ITKPALHLEN HHGQNQDILH
     HAWDRTWATI TNLEWVPAAI EAPIPSFRPF PTPADQVKRD TAATAIHSVH LSVVDAAADL
     QHGVDESYTL EVTADSGTIQ IHAQTVWGAI HAMTTLQQLV ITDGHGNLII EQPVKIQDAP
     LYPYRGIMID TGRNFISVPK ILEQIDGMAL SKLNVLHWHL DDTQSWPVQI RSYPQMTKDA
     YSSREIYTET DLRRVLAYAR ARGVRVIPEV DMPGHSASGW KQVDPDVVTC TDTWWSNDDW
     PKHTAVEPNP GQLDIIYNKT YEVVGNVYKD LSAIFSDNWF HVGGDELQNN CFNFSTHITK
     WFAEDPSRTY NDLSQYWLDH ALPIFHGTGG PQRRLMMWED IFINTDAAHH VPRDIVMQSW
     NNGIDNIKNL TASGFDVVVS SADFLYLDCG FAGFVGNDPR YNVMSNPGGD VTFNYGGSGG
     SWCAPYKSWQ RIYDYDFTTN LTASEAKHVI GAEAPLWSEQ VDDVTISSKM WPRAAALGEL
     VWSGNRDASG HKRTTQLTQR LLNFREYLVA NGVMATNLAP KYCLQHPHAC DLYYNQSVIT
     P
//