ID Q0U7Z6_PHANO Unreviewed; 611 AA.
AC Q0U7Z6;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN ORFNames=SNOG_12118 {ECO:0000313|EMBL:EAT80530.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT80530.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
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; CH445345; EAT80530.2; -; Genomic_DNA.
DR RefSeq; XP_001802351.1; XM_001802299.1.
DR AlphaFoldDB; Q0U7Z6; -.
DR STRING; 321614.Q0U7Z6; -.
DR EnsemblFungi; SNOT_12118; SNOT_12118; SNOG_12118.
DR GeneID; 5979261; -.
DR KEGG; pno:SNOG_12118; -.
DR VEuPathDB; FungiDB:JI435_121180; -.
DR eggNOG; KOG2499; Eukaryota.
DR HOGENOM; CLU_007082_0_2_1; -.
DR InParanoid; Q0U7Z6; -.
DR OrthoDB; 178991at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; IBA:GO_Central.
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 GO; GO:0030203; P:glycosaminoglycan metabolic process; IBA:GO_Central.
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:UP000001055}.
FT DOMAIN 27..166
FT /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14845"
FT DOMAIN 189..552
FT /note="Glycoside hydrolase family 20 catalytic"
FT /evidence="ECO:0000259|Pfam:PF00728"
FT ACT_SITE 353
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ SEQUENCE 611 AA; 67638 MW; AE91C8696773F0E0 CRC64;
MHNFILASVA TASALFASHV DAVAVNPLPK PANMTWGNSG CLSVGSLSLE APEHAVLSAA
FDRTTKSITD LKWVPQAIEA PIRQFQPFPT PAAGSKKRRS KRQYGSGNCT STLGKVQVEI
ADTSAQLQHG VDESYKLDVT SDSDSIKISA KTVYGALHAM TTLQQIVIND GTGNMIIEQP
VSIDDKPLYP VRGIMIDTGR NYLSPKKIME QIDGMSLSKL NVLHWHMIDN QAWPIEIQAF
PEMTEDAYSE NEIFSQDSLK SLISYAAARG VRIIPEIDMP GHASSGWKQI DESILTCQNS
WWSNDDWPKH TAVQPNPGQL DILNNKTYEV TAKVYKEMAT IFPDNWFHIG GDELFANCNN
FSSLGLAWFN SGKSMGDLYQ YWVDKAIPNF RAQVNKTFVM WEDVKLSADV AATGEVPKDI
VLQAWTAGRE HISNLTSQGY RVIVSSSDFL YLDCGNGGYV SNDPRYNVQI NPNATDGGAN
FNWLGAGGSW CAPYKTWQRI YDYDFTANLT DTQKALVQGA IAPLFGEQID DTILSQKMWP
RAAALAELVW SGNRDASGKK RTTELTQRIL NFREYLLASG VQAAPLMPKY CAQHPHECDL
YLDQDVHKDA A
//
