ID   BGAL_MALDO              Reviewed;         731 AA.
AC   P48981;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Beta-galactosidase;
DE            EC=3.2.1.23;
DE   AltName: Full=Acid beta-galactosidase;
DE            Short=Lactase;
DE   AltName: Full=Exo-(1-->4)-beta-D-galactanase;
DE   Flags: Precursor;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Granny Smith; TISSUE=Fruit cortical tissue;
RX   PubMed=7991682; DOI=10.1104/pp.106.2.521;
RA   Ross G.S., Wegrzyn T., Macrae E.A., Redgwell R.J.;
RT   "Apple beta-galactosidase. Activity against cell wall polysaccharides and
RT   characterization of a related cDNA clone.";
RL   Plant Physiol. 106:521-528(1994).
CC   -!- FUNCTION: Involved in cell wall degradation. Degrades polysaccharides
CC       containing beta-(1-->4)-linked galactans, acting as an exo-(1-->4)-
CC       beta-D-galactanase.
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; L29451; AAA62324.1; -; mRNA.
DR   PIR; T17002; T17002.
DR   AlphaFoldDB; P48981; -.
DR   SMR; P48981; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR23421; 1.
DR   Pfam; PF17834; GHD; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF49785; SSF49785; 2.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
PE   1: Evidence at protein level;
KW   Apoplast; Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..731
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012197"
FT   ACT_SITE        182
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        251
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   731 AA;  80996 MW;  FAB65D24A0D30BD4 CRC64;
     MGVGIQTMWS ILLLFSCIFS AASASVSYDH KAIIINGQKR ILISGSIHYP RSTPEMWPDL
     IQKAKDGGLD VIQTYVFWNG HEPSPGNYYF EERYDLVKFI KLVQQEGLFV NLRIGPYVCA
     EWNFGGFPVW LKYVPGIAFR TDNEPFKAAM QKFTEKIVSM MKAEKLFQTQ GGPIILSQIE
     NEFGPVEWEI GAPGKAYTKW AAQMAVGLDT GVPWIMCKQE DAPDPVIDTC NGFYCENFKP
     NKDYKPKMWT EVWTGWYTEF GGAVPTRPAE DVAFSVARFI QSGGSFLNYY MYHGGTNFGR
     TAGGPFMATS YDYDAPLDEY GLPREPKWGH LRDLHKAIKS CESALVSVDP SVTKLGSNQE
     AHVFKSESDC AAFLANYDAK YSVKVSFGGG QYDLPPWSIS ILPDCKTEVY NTAKVGSQSS
     QVQMTPVHSG FPWQSFIEET TSSDETDTTT LDGLYEQINI TRDTTDYLWY MTDITIGSDE
     AFLKNGKSPL LTIFSAGHAL NVFINGQLSG TVYGSLENPK LSFSQNVNLR SGINKLALLS
     ISVGLPNVGT HFETWNAGVL GPITLKGLNS GTWDMSGWKW TYKTGLKGEA LGLHTVTGSS
     SVEWVEGPSM AEKQPLTWYK ATFNAPPGDA PLALDMGSMG KGQIWINGQS VGRHWPGYIA
     RGSCGDCSYA GTYDDKKCRT HCGEPSQRWY HIPRSWLTPT GNLLVVFEEW GGDPSRISLV
     ERGTALDAKK L