ID A0A0D2E2A3_9EURO Unreviewed; 605 AA.
AC A0A0D2E2A3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=PV05_11231 {ECO:0000313|EMBL:KIW49563.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW49563.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW49563.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW49563.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) 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; KN847323; KIW49563.1; -; Genomic_DNA.
DR RefSeq; XP_013310147.1; XM_013454693.1.
DR AlphaFoldDB; A0A0D2E2A3; -.
DR STRING; 348802.A0A0D2E2A3; -.
DR GeneID; 25333139; -.
DR HOGENOM; CLU_007082_0_2_1; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000054342; 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:UP000054342};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..605
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002251918"
FT DOMAIN 27..158
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 181..542
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 345
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 605 AA; 67344 MW; 98C53178AECF34A4 CRC64;
MGRVGCRLAV FTVAILITLT NAIKVNPLPA PQSTTWGSSG PIAVGTDLML NTQSEQIITD
AWNRSWTTIS TLKWVPAAIE APIPKFQPFP TDAPSSRVKR WNSSLSQVDL TIADCAADLQ
HGVDESYTVD IIQSTQAVNI TAKTVWGALH AFTTLQQLII SDGNGGLMVE NPVSIIDHPN
YPYRGAMIDT GRNFISLPKI REQIDGMALS KMNVLHWHMA DAQSWPVQMQ VYPQMTQGAY
SPQSTYSQND IRDLIAYARA RGVRIIPEID MPGHASQGWT SVDPSILACA DSWWSNDDWA
LHTAVEPNPG QLDILNNKTY EVIKNVYGEL AGLFSDDIFH VGADELQTGC YNFSTAVQQY
FAHNKSRTYD DLVQVWVDRA IPTFRSAANK TLMMWEDILI ATPHAHTVPK NIILQTWNNG
LENIKNLTSQ GYDIVVSSAD FFYLDCGFGG WVSNDPRYNE MANPNASVPT FNYGGNGGSW
CAPYKSWQRI YDYDFTLNLT AQEKTHVLGT EVPLWSEQVD DTVISSKMWP RAAAMAELAW
SGNKDPKTGI KRTTQLTQRI LNFREYLVAN GIQAAPLVPK YCLQHPHACD LYYNQTALAT
YATTQ
//
