ID   Q9AYS1_PYRPY            Unreviewed;       731 AA.
AC   Q9AYS1;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN   Name=JP-GAL {ECO:0000313|EMBL:BAB21492.1};
OS   Pyrus pyrifolia (Chinese pear) (Pyrus serotina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX   NCBI_TaxID=3767 {ECO:0000313|EMBL:BAB21492.1};
RN   [1] {ECO:0000313|EMBL:BAB21492.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fruit {ECO:0000313|EMBL:BAB21492.1};
RX   PubMed=11382815; DOI=10.1093/pcp/pce059;
RA   Tateishi A., Inoue H., Shiba H., Yamaki S.;
RT   "Molecular cloning of beta-galactosidase from Japanese pear (Pyrus
RT   pyrifolia) and its gene expression with fruit ripening.";
RL   Plant Cell Physiol. 42:492-498(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues
CC         in beta-D-galactosides.; EC=3.2.1.23;
CC         Evidence={ECO:0000256|ARBA:ARBA00001412,
CC         ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; AB046543; BAB21492.1; -; mRNA.
DR   AlphaFoldDB; Q9AYS1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR041392; GHD.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR019801; Glyco_hydro_35_CS.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF63; BETA-GALACTOSIDASE 12; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 2.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..731
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004324141"
FT   DOMAIN          33..337
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          360..415
FT                   /note="Beta-galactosidase beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF17834"
FT   DOMAIN          467..534
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   DOMAIN          616..702
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
SQ   SEQUENCE   731 AA;  80923 MW;  E069ACA689511514 CRC64;
     MGVGIQTMWS ILLLFSCIFS AASASVSYDH KAIIINGQKR ILISGSIHYP RSTPEMWPDL
     IQKAKDGGLD VIQTYVFWNG HEPSPGKYYF EDRYDLVKFI KLVQQAGLFV NLRIGPYVCA
     EWNFGGFPVW LKYVPGIAFR TDNEPFKAAM QKFTEKIVSM MKAEKLFQTQ GGPIILSQIE
     NEFGPVEWEI GAPGKAYTKW AAQMAVGLDT GVPWIMCKQE DAPDPVIDTC NGFYCENFKP
     NKDYKPKMWT EVWTGWYTEF GGAVPTRPAE DVAFSVARFI QSGGSFLNYY MYHGGTNFGR
     TAGGPFMATS YDYDAPLDEY GLLREPKWGH LRDLHKAIKS CESALVSVDP SVTKLGSNQE
     AHVFKSESDC AAFLANYDAK YSVKVSFGGG QYDLPPWSIS ILPDCKTEVY STAKVGSQSS
     QVQMTPVHSG FPWQSFIEET TSSDETDTTT LDGLYEQINI TRDTTDYLWY MTDITIGSDE
     AFLKNGKSPL LTIFSAGHAL NVFINGQLSG TVYGSLENPK LSFSQNVNLR SGINKLALLS
     ISVGLPNVGT HFETWNAGVL GPITLKGLNS GTWDMSGWKW TYKTGLKGEA LGLHTVTGSS
     SVEWVEGPSM AKKQPLTWYK ATFNAPPGDA PLALDMGSMG KGQIWINGQS VGRHWPGYIA
     RGSCGDCSYA GTYDDKKCRT HCGEPSQRWY HIPRSWLTPN GNLLVVFEEW GGDPSRISLV
     ERGTALDAKK P
//