ID   I1NU59_ORYGL            Unreviewed;       526 AA.
AC   I1NU59;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
OS   Oryza glaberrima (African rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4538 {ECO:0000313|EnsemblPlants:ORGLA01G0339900.1, ECO:0000313|Proteomes:UP000007306};
RN   [1] {ECO:0000313|Proteomes:UP000007306}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 96717 {ECO:0000313|Proteomes:UP000007306};
RA   Wing R.A., Yu Y., Rounsley S., Reddy-Marri P., Goicoechea J.L.,
RA   Sisneros N., Lee S., Song X., Angelova A., Kudrna D.P., de Baynast K.,
RA   Zuccolo A.;
RT   "The complete genome of Oryza glaberrima.";
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORGLA01G0339900.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
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   AlphaFoldDB; I1NU59; -.
DR   SMR; I1NU59; -.
DR   STRING; 4538.I1NU59; -.
DR   EnsemblPlants; ORGLA01G0339900.1; ORGLA01G0339900.1; ORGLA01G0339900.
DR   Gramene; ORGLA01G0339900.1; ORGLA01G0339900.1; ORGLA01G0339900.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   OMA; HYLPVTN; -.
DR   Proteomes; UP000007306; 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:SF57; BETA-HEXOSAMINIDASE; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..526
FT                   /note="Beta-hexosaminidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003649213"
FT   DOMAIN          30..148
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          173..477
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        320
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   526 AA;  59024 MW;  3E33F5558033BCEF CRC64;
     MAQALSLGLL LAFLAIQSCI AIELTDHIDL WPMPTSVSHG TQRLYVSKDI TMSMEGSTYP
     DGKGILKDAF QRVVDLMKLN HVVDGANPSS FVLTGVNVVV HSPEDELKFG VDESYNLSVP
     TAGYPLRVQI EAQTVFGALH ALQTFSQLCY FDFTSKLIEL ISAPWRISDT PRFPYRGLLI
     DTSRHYLPVT VIKKVIDTMA YSKLNVLHWH IVDAQSFPIE IPSYPKLWNG SYSFSERYTT
     SDAVDIVRYA ENRGVNVMAE IDVPGHALSW GVGYPSLWPS DSCKEPLDVS NNFTFGVIDG
     ILSDFSKVFK FKFVHLGGDE VNTSCWTATP HIKKWLDDNQ MNVSDAYRYF VLRSQKLAIS
     HGYDVINWEE TFNNFGDKLD RRTVVHNWLG EDVAPKVVAA GLRCIVSNQD KWYLDHLDAT
     WEGFYTNEPL KGIDDPEQQS LVIGGEVCMW GEQIDASDIE QTIWPRAAAA AERLWTPIEK
     IAEDPRLVTS RLARFRCLLN QRGVAAAPVA GYGRTAPYEP GPCVRQ
//