ID   BGAL_PINPS              Reviewed;          44 AA.
AC   P81669;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Putative beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
DE   Flags: Fragments;
OS   Pinus pinaster (Maritime pine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Pinus;
OC   Pinus subgen. Pinus.
OX   NCBI_TaxID=71647;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Needle;
RX   PubMed=10344291;
RX   DOI=10.1002/(sici)1522-2683(19990101)20:4/5<1098::aid-elps1098>3.0.co;2-z;
RA   Costa P., Pionneau C., Bauw G., Dubos C., Bahrman N., Kremer A.,
RA   Frigerio J.-M., Plomion C.;
RT   "Separation and characterization of needle and xylem maritime pine
RT   proteins.";
RL   Electrophoresis 20:1098-1108(1999).
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   -!- INDUCTION: By water stress.
CC   -!- MISCELLANEOUS: On the 2D-gel the determined pI of this protein (spot
CC       N76) is: 5.8, its MW is: 32 kDa.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   AlphaFoldDB; P81669; -.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Stress response.
FT   CHAIN           <1..>44
FT                   /note="Putative beta-galactosidase"
FT                   /id="PRO_0000057686"
FT   NON_CONS        15..16
FT                   /evidence="ECO:0000305"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         44
SQ   SEQUENCE   44 AA;  4831 MW;  30886985FF48C9FA CRC64;
     VNIGVNYGML GNSYPTGPET ERHFGLNPDT LHVVRHAQGF HNLA
//