ID A0A2B7XE34_9EURO Unreviewed; 603 AA.
AC A0A2B7XE34;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=AJ79_06391 {ECO:0000313|EMBL:PGH06918.1};
OS Helicocarpus griseus UAMH5409.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Helicocarpus.
OX NCBI_TaxID=1447875 {ECO:0000313|EMBL:PGH06918.1, ECO:0000313|Proteomes:UP000223968};
RN [1] {ECO:0000313|EMBL:PGH06918.1, ECO:0000313|Proteomes:UP000223968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH5409 {ECO:0000313|EMBL:PGH06918.1,
RC ECO:0000313|Proteomes:UP000223968};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH06918.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PDNB01000113; PGH06918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7XE34; -.
DR STRING; 1447875.A0A2B7XE34; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000223968; 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:SF56; BETA-HEXOSAMINIDASE; 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:UP000223968};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..603
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013264984"
FT DOMAIN 18..188
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 213..557
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 374
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 603 AA; 67940 MW; 250792CBEF743AA7 CRC64;
MLLSAVAFLG FASLSLAVWP QPRDFKHGNT TVWLSPTAEF SYMPTGADEL REKSDYFSTF
VDLEEVFNFF QTPLLRRNKT SEKTLPSVAK LVKKAVKRTG KEIYRTKFVP WKFHPRNSSF
EPAVDGQHAV IRRVTINQNS TNQTKAETRD VIHEDESYDI EITADGEAEI TTKSAIGTIR
ALQTFRQLFY AHSSGSGVYT PYAPIAISDA PKWSYRGLNL DISRNAYMPA DVKRTIDAMS
SAKMNRLHIH ATDSQSWPLD IPAMPSLAAK GAYHPSLVWT SSNLRDVQMY GLENGVSVFI
EIDMPGHTGS IGYAFPELVS AFLAHDWEKY ALQPPSGQIK LNSPGVNEFL DKLMADLLPR
VSPFTRYFHT GGDEFNLNTY LLEESIRSNK EEVLRPLLQG VVTRLHTAIR EAGLTPIVWE
ELVADWNLTL SSDPAKKRDI IVQAWRNTTA VKHILEQGYR TIFGSGDFWY LDCGHGSYIN
PKPNSTAVKE PFLDWCSPLK NWKHMYIYNP LEGIPEDLHH LIEGGETHMW SENVDPIILD
KVVWPRAAAA AEVLWSGPRT ANQIQDASHR LSEWRERAVV DLGVGASLAQ MTYCLMKEGS
CEL
//
