ID H6C3Q8_EXODN Unreviewed; 607 AA.
AC H6C3Q8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=HMPREF1120_06285 {ECO:0000313|EMBL:EHY58273.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY58273.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY58273.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY58273.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) 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; JH226134; EHY58273.1; -; Genomic_DNA.
DR RefSeq; XP_009158734.1; XM_009160486.1.
DR AlphaFoldDB; H6C3Q8; -.
DR STRING; 858893.H6C3Q8; -.
DR GeneID; 20310924; -.
DR VEuPathDB; FungiDB:HMPREF1120_06285; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; H6C3Q8; -.
DR OMA; KMWPRAA; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000007304; 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:UP000007304};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..607
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003603515"
FT DOMAIN 28..160
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 183..544
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 347
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 607 AA; 67291 MW; 163195AD154B4279 CRC64;
MFVPRGLQIV TFLASFLYEL ADAVAVNPLP APQSVAWGSS GPKQLAGYLV LNANIPNQII
SDAWNRAWTS INELKWTPAA IEASISTFEP FPTATASSRI KRADPVLTQV DLTVADTEAD
LQQGVDESYT IDITQTSQAV NITAQTVWGA LHAFTTLQQI IISDGNGGLV VEQPVSISDH
PNYPYRGVLI DTGRNFISLP KIYEQIDGMS LSKLNVFHWH MVDAQSWPVQ LQVYPQMTQD
AYLPKSVYSH DDIRVVIAYA RARGVRIVPE IDMPGHASAG WARVDPSIVT CGNSWWSNDV
WALHTAVEPN PGQLDILNNK TYEVVTNIYT ELSGLFADSI FHVGADEVHP NCFNFSSIVQ
EWLAANTSRT YDDLLQVWVD KAIPAFSAAA NRTLMMWEDI LLSAPHAHTL PNNIILQSWN
GGLTNIKNLT SQGYDVVVSS SDFFYLDCGS GGWVTNDPRY NEMANPNASV PNFNYGGGGG
SWCAPYKTWQ RIYDYDFTLN LTDTEKTHVL GPEVALWSEQ VDDTVISSKL WPRAAAMAEL
AWSGNRDPTT GLKRTTQMTQ RILNFREYLV ANGVQATPLV PKYCLQHPHA CDLYYNQTAL
ADYSTIQ
//
