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Database: UniProt
Entry: M5X5L2_PRUPE
LinkDB: M5X5L2_PRUPE
Original site: M5X5L2_PRUPE 
ID   M5X5L2_PRUPE            Unreviewed;       542 AA.
AC   M5X5L2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Beta-hexosaminidase {ECO:0000256|PIRNR:PIRNR001093};
DE            EC=3.2.1.52 {ECO:0000256|PIRNR:PIRNR001093};
GN   ORFNames=PRUPE_2G228000 {ECO:0000313|EMBL:ONI24170.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONI24170.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONI24170.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(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; CM007652; ONI24170.1; -; Genomic_DNA.
DR   RefSeq; XP_007220020.1; XM_007219958.1.
DR   AlphaFoldDB; M5X5L2; -.
DR   STRING; 3760.M5X5L2; -.
DR   EnsemblPlants; ONI24170; ONI24170; PRUPE_2G228000.
DR   GeneID; 18787548; -.
DR   Gramene; ONI24170; ONI24170; PRUPE_2G228000.
DR   KEGG; pper:18787548; -.
DR   eggNOG; KOG2499; Eukaryota.
DR   HOGENOM; CLU_007082_0_4_1; -.
DR   OMA; QNENECP; -.
DR   OrthoDB; 178991at2759; -.
DR   Proteomes; UP000006882; Chromosome g2.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase 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   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:SF40; BETA-HEXOSAMINIDASE 1; 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:UP000006882}.
FT   DOMAIN          36..161
FT                   /note="Beta-hexosaminidase eukaryotic type N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14845"
FT   DOMAIN          186..490
FT                   /note="Glycoside hydrolase family 20 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00728"
FT   ACT_SITE        333
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001093-1"
SQ   SEQUENCE   542 AA;  61298 MW;  F12E79BABFE04597 CRC64;
     MSTLFLILFV FSHSLCVLQT QGLNSADEVN DSLTYLWPLP SEFTFGNKTL SVHPQLSLVV
     GGNGGNSSIL RLGFDRYKAI IFKNSHGVSS FDRIRGRRLS YDVTKLKVVV HSDSEDLQLG
     VDESYTLFVL KKDGQSIVGE ATIEANTVYG ALRALETFSQ LCTFDYGSKS VQVYRAPWYI
     RDSPRFAYRG LLLDTSRHYL PVDVIKQVIE SMSYAKLNVL HWHVIDRESF PLEVPSYPKL
     WKGSYTKWER YTVEDAIEIV SFAKTRGINV MAEVDVPGHA ESWGAGYPNL WPSTSCKEPL
     DVSKSSTFDV VSGILTDMRK IFPFELFHLG GDEVNTTCWS STRHVKQWLE QHNMTTKDAY
     QYFVLKAQEI AISKNWTPVN WEETFNTFPT KLNPKTVVHN WLGPGVCPKA VAKGFRCIFS
     NQGVWYLDHL DVPWEDAYNA EPLEGIDDVS QQKLVLGGEV CMWGETADTS DVQQTIWPRA
     AAAAERLWSR REATSARNGN LTALPRLHYF RCLLNRRGVQ AAPVTNLIAR SPPIWSGSCY
     DQ
//
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