ID   BGAL_SOLLC              Reviewed;         835 AA.
AC   P48980;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
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   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Ailsa Craig; TISSUE=Pericarp;
RX   PubMed=7630937; DOI=10.1104/pp.108.3.1099;
RA   Carey A.T., Holt K., Picard S., Wilde R., Tucker G.A., Bird C.R.,
RA   Schuch W., Seymour G.B.;
RT   "Tomato exo-(1-->4)-beta-D-galactanase. Isolation, changes during ripening
RT   in normal and mutant tomato fruit, and characterization of a related cDNA
RT   clone.";
RL   Plant Physiol. 108:1099-1107(1995).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.5.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}.
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DR   EMBL; X83854; CAA58734.1; -; mRNA.
DR   PIR; T06590; T06590.
DR   RefSeq; NP_001234465.1; NM_001247536.2.
DR   AlphaFoldDB; P48980; -.
DR   SMR; P48980; -.
DR   STRING; 4081.Solyc12g044880.1.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PaxDb; P48980; -.
DR   PRIDE; P48980; -.
DR   EnsemblPlants; Solyc12g044880.2.1; Solyc12g044880.2.1; Solyc12g044880.2.
DR   GeneID; 544167; -.
DR   Gramene; Solyc12g044880.2.1; Solyc12g044880.2.1; Solyc12g044880.2.
DR   KEGG; sly:544167; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   InParanoid; P48980; -.
DR   OMA; SPSVEWV; -.
DR   OrthoDB; 179316at2759; -.
DR   PhylomeDB; P48980; -.
DR   Proteomes; UP000004994; Chromosome 12.
DR   ExpressionAtlas; P48980; baseline and differential.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT   CHAIN           23..835
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012195"
FT   DOMAIN          749..835
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00260"
FT   ACT_SITE        180
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        249
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   835 AA;  93336 MW;  94C9685F95C4A646 CRC64;
     MGFWMAMLLM LLLCLWVSCG IASVSYDHKA IIVNGQRKIL ISGSIHYPRS TPEMWPDLIQ
     KAKEGGVDVI QTYVFWNGHE PEEGKYYFEE RYDLVKFIKV VQEAGLYVHL RIGPYACAEW
     NFGGFPVWLK YVPGISFRTN NEPFKAAMQK FTTKIVDMMK AEKLYETQGG PIILSQIENE
     YGPMEWELGE PGKVYSEWAA KMAVDLGTGV PWIMCKQDDV PDPIINTCNG FYCDYFTPNK
     ANKPKMWTEA WTAWFTEFGG PVPYRPAEDM AFAVARFIQT GGSFINYYMY HGGTNFGRTS
     GGPFIATSYD YDAPLDEFGS LRQPKWGHLK DLHRAIKLCE PALVSVDPTV TSLGNYQEAR
     VFKSESGACA AFLANYNQHS FAKVAFGNMH YNLPPWSISI LPDCKNTVYN TARVGAQSAQ
     MKMTPVSRGF SWESFNEDAA SHEDDTFTVV GLLEQINITR DVSDYLWYMT DIEIDPTEGF
     LNSGNWPWLT VFSAGHALHV FVNGQLAGTV YGSLENPKLT FSNGINLRAG VNKISLLSIA
     VGLPNVGPHF ETWNAGVLGP VSLNGLNEGT RDLTWQKWFY KVGLKGEALS LHSLSGSPSV
     EWVEGSLVAQ KQPLSWYKTT FNAPDGNEPL ALDMNTMGKG QVWINGQSLG RHWPAYKSSG
     SCSVCNYTGW FDEKKCLTNC GEGSQRWYHV PRSWLYPTGN LLVVFEEWGG DPYGITLVKR
     EIGSVCADIY EWQPQLLNWQ RLVSGKFDRP LRPKAHLKCA PGQKISSIKF ASFGTPEGVC
     GNFQQGSCHA PRSYDAFKKN CVGKESCSVQ VTPENFGGDP CRNVLKKLSV EAICS