ID A0A0L1IS02_ASPNO Unreviewed; 600 AA.
AC A0A0L1IS02;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=ANOM_010111 {ECO:0000313|EMBL:KNG82274.1};
OS Aspergillus nomiae NRRL 13137.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1509407 {ECO:0000313|EMBL:KNG82274.1, ECO:0000313|Proteomes:UP000037505};
RN [1] {ECO:0000313|EMBL:KNG82274.1, ECO:0000313|Proteomes:UP000037505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13137 {ECO:0000313|EMBL:KNG82274.1,
RC ECO:0000313|Proteomes:UP000037505};
RA Moore M.G., Shannon B.M., Brian M.M.;
RT "The Genome of the Aflatoxigenic Filamentous Fungus Aspergillus nomius.";
RL Submitted (JUN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNG82274.1}.
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DR EMBL; JNOM01000360; KNG82274.1; -; Genomic_DNA.
DR RefSeq; XP_015403197.1; XM_015555367.1.
DR AlphaFoldDB; A0A0L1IS02; -.
DR STRING; 1509407.A0A0L1IS02; -.
DR GeneID; 26811915; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000037505; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000037505};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..600
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005553010"
FT DOMAIN 23..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 600 AA; 67778 MW; 72C0FCF695ECB650 CRC64;
MRITRICTVL FTVSSAVAVS VNPLPAPREI SWGSSGPKSV AGELQLRIET DTQNGIVADA
WSRAWETIVA LRWVPAATEA PISSFEPFPT PTAGASRKTK RASNALQYVD VHVDDTEADL
QHGVDESYTL EVKEDSDSIT VNAQTVWGAL HAFTTLQQLV ISDGHGGLII EEPVSIKDSP
LYPYRGIMLD TGRNFITLPK IFEQLEGMAL SKLNVLHWHI DDAQSWPIWV DAYPEMVKDA
YSPHEIYSRN DVRNIVNYAR ARGIRVIPEI DMPSHSSSGW KQVDPEMVTC TDSWWSNDDW
PLHTAVEPNP GQLDIIYNKT YEVVGNVYKE LSDIFPDHWF HVGGDEIQPN CFNFSTHVTK
WFAEDPSRTY HDLAQYWIDH AVPIFQNYSK ERRLVMWEDI VLSAENAHDV PKNIVMQSWN
NGLEYISNLT ARGYDVIVSS SDFMYLDCGH GGFVTNDPRY NVMSNPDANT PNFNYGGNGG
SWCAPYKTWQ RIYDYDFTLN LTETQAKHVI GATAPLWGEQ VDDINVSSMF WPRAAALAEL
VWSGNRDADG KKRTTELTQR ILNFREYLVA NGVQAQALVP KYCLQHPHAC DLYRDQTAIH
//
