ID   BGAL_HORVU              Reviewed;          38 AA.
AC   P83252;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   11-DEC-2019, entry version 52.
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   Contains:
DE     RecName: Full=Beta-galactosidase large subunit;
DE   Contains:
DE     RecName: Full=Beta-galactosidase small subunit;
DE   Flags: Fragments;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, SUBUNIT, AND GLYCOSYLATION.
RC   STRAIN=cv. Sofia {ECO:0000269|PubMed:11838543};
RC   TISSUE=Seed {ECO:0000269|PubMed:11838543};
RX   PubMed=11838543; DOI=10.1023/a:1013369129751;
RA   Triantafillidou D., Georgatsos J.G.;
RT   "Barley beta-galactosidase: structure, function, heterogeneity, and gene
RT   origin.";
RL   J. Protein Chem. 20:551-562(2001).
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 (By similarity). {ECO:0000250|UniProtKB:P48981}.
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:0000250|UniProtKB:P48981};
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC       {ECO:0000269|PubMed:11838543}.
CC   -!- PTM: The small subunit is N-glycosylated.
CC       {ECO:0000269|PubMed:11838543}.
CC   -!- MISCELLANEOUS: There are three forms of the large subunit which have
CC       the same sequence but differ in charge. There are four forms of the
CC       small subunit which have the same sequence but differ in charge.
CC       {ECO:0000269|PubMed:11838543}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000255}.
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DR   BRENDA; 3.2.1.23; 2687.
DR   GO; GO:0004565; F:beta-galactosidase activity; NAS:UniProtKB.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; NAS:UniProtKB.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase.
FT   CHAIN           1..>28
FT                   /note="Beta-galactosidase large subunit"
FT                   /evidence="ECO:0000269|PubMed:11838543"
FT                   /id="PRO_0000271912"
FT   CHAIN           29..>38
FT                   /note="Beta-galactosidase small subunit"
FT                   /evidence="ECO:0000269|PubMed:11838543"
FT                   /id="PRO_0000271913"
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000303|PubMed:11838543"
FT   NON_TER         38
FT                   /evidence="ECO:0000303|PubMed:11838543"
SQ   SEQUENCE   38 AA;  4126 MW;  7138F328FA3EFFDE CRC64;
     TGVTYDHRAL VIDGXXXVLV SGSIHYPRAA SSWYAVET