ID A0A072P659_9EURO Unreviewed; 608 AA.
AC A0A072P659;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=A1O9_12833 {ECO:0000313|EMBL:KEF51110.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF51110.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF51110.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF51110.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) 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:KEF51110.1}.
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DR EMBL; AMGV01000028; KEF51110.1; -; Genomic_DNA.
DR RefSeq; XP_013253700.1; XM_013398246.1.
DR AlphaFoldDB; A0A072P659; -.
DR STRING; 1182545.A0A072P659; -.
DR GeneID; 25287727; -.
DR VEuPathDB; FungiDB:A1O9_12833; -.
DR HOGENOM; CLU_007082_0_2_1; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000027920; 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:UP000027920};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..608
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001681403"
FT DOMAIN 29..160
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 183..545
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 608 AA; 67497 MW; 1D405D01DCFA1E2A CRC64;
MQLARRVLRF LVLGVGICPS ASDAVAVNPL PAPQNITWGS SGPKQVAGYL ALNGAYNPIV
IDAWARAWTT ISTLQWVPAA VEAPISTFEA FPTGTVSRRT RGTSSYLSLI DLTVENSEAD
LQHGVDESYS LEITQNSPSV AIKANTIWGA LHAFTTLQQI IISDGNGGLL VEQPVSINDY
PNYPHRGILI DSGRNFISVK KFYEQIDGLA LSKLNVLHWH IVDSQSWPLQ IQAYPQMTQD
AYSTKEIYSP DDVQNLIAYA RARGVRVIPE IDMPGHASSG WTAVDPEIVA CANAWWSNDD
WALHTAVEPN PGQLDILNNK TYEVVANVYT ELSRVFSDNI FHIGADEVHS NCFNFSAAIR
NWFAANQSRT YNDLLQVWID RSFPLFSAVP NRRLMMWEDI LTAGDHANSL PKDVILQSWN
NGLENIQNLT ARGYDVVVSS SDFFYLDCGN GGWVTNDPRY NVPANPNATG PPTFNYLGMG
GSWCAPYKTW QRIYDYDFTL NLTDTQKSHI LGAEAPLWSE QVDDTVISSK LWPRAAALAE
LTWSGNKDPA TGSKRTTQMT QRILNFREYL VANGIQATAL VPKYCLQHPH ACDLYYNQSA
LADYFVAS
//
