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Database: UniProt
Entry: G7XZP3_ASPKW
LinkDB: G7XZP3_ASPKW
Original site: G7XZP3_ASPKW 
ID   G7XZP3_ASPKW            Unreviewed;       601 AA.
AC   G7XZP3;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=AKAW_10516 {ECO:0000313|EMBL:GAA92402.1};
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177 {ECO:0000313|EMBL:GAA92402.1};
RN   [1] {ECO:0000313|EMBL:GAA92402.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFO 4308 {ECO:0000313|EMBL:GAA92402.1};
RX   PubMed=22045919; DOI=10.1128/EC.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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; DF126493; GAA92402.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7XZP3; -.
DR   STRING; 1033177.G7XZP3; -.
DR   VEuPathDB; FungiDB:AKAW_10516; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   InParanoid; G7XZP3; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
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   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..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..601
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003506053"
FT   DOMAIN          25..161
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          184..546
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        348
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   601 AA;  67370 MW;  E40C56B90B04ED51 CRC64;
     MLLHHLWLAC LTLLVAGAAA VKVNPLPAPR NITWASSGPK QLADFVSLRT SRDTSDFILA
     NGWNRAWNSI VSLQWVPAAT QGPVPSYQPF PTGTAGATKR SPQALPSLQF VDVNVLDVAA
     DLQHGVDESY TLEVTEGSTS VVIEAPTVWG ALHAFTTLQQ LVIADGQGGL IIEQPVKIQD
     APLYPYRGIM IDTGRNFISV NKIYEQLDGM SLSKLNVLHW HMEDTQSWPV EIDAHPEMIY
     DAYSPREVYS HADMRNVVAY ARARGVRVIP ELDMPSHSAS GWKQVDPQMV TCVDSWWSND
     NYALHTAVEP PPGQMDIIYN GTYEVVRQVY NELSSIFPDN WFHVGADEIQ PNCFNFSSYV
     TEWFAQDPSR TYNDLAQYWI DHAVPIFQNY STSRQLVMWE DIVLSTEHAH DVPTNIVMQT
     WNNGLDYINQ LTAKGYDVIV SSADFMYLDC GIGGFLTNDP RYDVMSNPDA STPNFNYGGN
     GGSWCAPYKT WQRIYDYDFT QNLTATQAQH IIGAEAPLWS EQVDDVTVSS LIWPRAAALA
     ELVWSGNREN GQKRTTLMTQ RILNFREYLV ANGVQATALV PKYCVQRPHA CDLYLNQSVI
     Q
//
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