ID B2W8F8_PYRTR Unreviewed; 614 AA.
AC B2W8F8;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=PTRG_06266 {ECO:0000313|EMBL:EDU49186.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU49186.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
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; DS231620; EDU49186.1; -; Genomic_DNA.
DR RefSeq; XP_001936599.1; XM_001936564.1.
DR AlphaFoldDB; B2W8F8; -.
DR STRING; 426418.B2W8F8; -.
DR EnsemblFungi; EDU49186; EDU49186; PTRG_06266.
DR GeneID; 6344523; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; B2W8F8; -.
DR OMA; KMWPRAA; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000001471; 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: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:UP000001471};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..614
FT /note="Beta-hexosaminidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002784601"
FT DOMAIN 27..170
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 193..557
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT REGION 87..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 614 AA; 68324 MW; 6D2FA054F83754A5 CRC64;
MRDFILASVV TAAALFPGHA EAVAANPLPA PRNIVWGNSG CFSFDPSASF DVPESKLLSD
AVDRTKKSIT TLKWVPQAVE APVREFEPFP GSTTKASRRK HKRQYNAPPA GNCTGSVKSV
RITLVHPNAD LQHGVEESYT LNLKQGSDTL FITAQTVYGA LHALTTLQQI VISDGTGKLI
IEQPVSIVDW PLYPVRGIMI DTGRNFISKA KIEEQLNAMA LAKLNVLHWH LVDSQSWPVE
VKQYPTMTED AYSANEMFTQ DTLKEIVSYA AARGIRVIPE IDMPGHASSG WTQIDENIVT
CEDSWWSNDD WPKHTAVQPN PGQLDILNNK TYEVTGQVYK EMTSIFPDNW FHIGGDELFA
NCNNFSAPAL AFFNSGKSMG DLYQVWVDRA IPNFRSIANK TLVMWEDVKL SADVAATGNV
PKDIILQAWN NGLDHISNLT AQGYRVIVSS SDFMYLDCGY GGWVGNDPRY NVMVNPNAND
TSILNFNWGG GGGSWCAPYK TWQRIYDYDF TLNMTDAQKK LIQGAIAPLW SEQVDDAVVS
QKMWPRAAAL AELVWSGNRD SKGNKRTTEL TQRILNFREY LVANGVSASP LMPKYCLQHP
HECDLYLNQT ALWT
//
