ID   BGAL_ASPOF              Reviewed;         832 AA.
AC   P45582;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
DE   Flags: Precursor;
OS   Asparagus officinalis (Garden asparagus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asparagaceae;
OC   Asparagoideae; Asparagus.
OX   NCBI_TaxID=4686;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Limbras 10; TISSUE=Spear;
RX   PubMed=7784512; DOI=10.1104/pp.108.1.419;
RA   King G.A., Davies K.M.;
RT   "Cloning of a harvest-induced beta-galactosidase from tips of harvested
RT   asparagus spears.";
RL   Plant Physiol. 108:419-420(1995).
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; X77319; CAA54525.1; -; mRNA.
DR   PIR; S41889; S41889.
DR   AlphaFoldDB; P45582; -.
DR   SMR; P45582; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PRIDE; P45582; -.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.740; -; 1.
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   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR043159; Lectin_gal-bd_sf.
DR   PANTHER; PTHR23421; PTHR23421; 1.
DR   Pfam; PF02140; Gal_Lectin; 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.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..832
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012193"
FT   DOMAIN          741..832
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        183
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        252
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   832 AA;  92214 MW;  94ABDC61EC4164AE CRC64;
     MALKLVLMLM VALLAAVWSP PAVTASVTYD HKSVIINGQR RILISGSIHY PRSTPEMWPD
     LIQKAKDGGL DVIQTYVFWN GHEPSPGQYY FGGRYDLVRF LKLVKQAGLY AHLRIGPYVC
     AEWNFGGFPV WLKYVPGIHF RTDNGPFKAA MGKFTEKIVS MMKAEGLYET QGGPIILSQI
     ENEYGPVEYY DGAAGKSYTN WAAKMAVGLN TGVPWVMCKQ DDAPDPVINT CNGFYCDYFS
     PNKDNKPKMW TEAWTGWFTG FGGAVPQRPA EDMAFAVARF IQKGGSFINY YMYHGGTNFG
     RTAGGPFIST SYDYDAPIDE YGLLRQPKWG HLRDLHKAIK LCEPALVSGE PTITSLGQNQ
     ESYVYRSKSS CAAFLANFNS RYYATVTFNG MHYNLPPWSV SILPDCKTTV FNTARVGAQT
     TTMKMQYLGG FSWKAYTEDT DALNDNTFTK DGLVEQLSTT WDRSDYLWYT TYVDIAKNEE
     FLKTGKYPYL TVMSAGHAVH VFINGQLSGT AYGSLDNPKL TYSGSAKLWA GSNKISILSV
     SVGLPNVGNH FETWNTGVLG PVTLTGLNEG KRDLSLQKWT YQIGLHGETL SLHSLTGSSN
     VEWGEASQKQ PLTWYKTFFN APPGNEPLAL DMNTMGKGQI WINGQSIGRY WPAYKASGSC
     GSCDYRGTYN EKKCLSNCGE ASQRWYHVPR SWLIPTGNFL VVLEEWGGDP TGISMVKRSV
     ASVCAEVEEL QPTMDNWRTK AYGRPKVHLS CDPGQKMSKI KFASFGTPQG TCGSFSEGSC
     HAHKSYDAFE QEGLMQNCVG QEFCSVNVAP EVFGGDPCPG TMKKLAVEAI CE