ID   A0A0B2R707_GLYSO        Unreviewed;       832 AA.
AC   A0A0B2R707;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN   ORFNames=glysoja_044382 {ECO:0000313|EMBL:KHN27597.1};
OS   Glycine soja (Wild soybean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3848 {ECO:0000313|EMBL:KHN27597.1};
RN   [1] {ECO:0000313|EMBL:KHN27597.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Root {ECO:0000313|EMBL:KHN27597.1};
RA   Lam H.-M., Qi X., Li M.-W., Liu X., Xie M., Ni M., Xu X.;
RT   "Identification of a novel salt tolerance gene in wild soybean by whole-
RT   genome sequencing.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001412,
CC         ECO:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; KN653308; KHN27597.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B2R707; -.
DR   Proteomes; UP000053555; Unassembled WGS sequence.
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   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR048913; BetaGal_gal-bd.
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:SF203; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF21467; BetaGal_gal-bd; 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; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR   PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..832
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002075088"
FT   DOMAIN          738..826
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   832 AA;  93970 MW;  3885290F3A89992D CRC64;
     MTWALLLLSF TLVNLAINAF EVSYDSRAIT IDGKRKVLFS GSIHYPRSTA EMWPSLINKA
     KEGGLDVIET YVFWNAHEPQ PRQYDFSGNL DLVKFIKTIQ KEGLYAMLRI GPYVCAEWNY
     GGFPVWLHNM PNMEFRTNNT AYMNEMQTFT TLIVDKMRHE NLFASQGGPI ILAQIENEYG
     NIMSEYGENG KQYVQWCAQL AESYKIGVPW VMCQQSDAPD PIINTCNGWY CDQFSPNSKS
     KPKMWTENWT GWFKNWGGPI PHRTARDVAY AVARFFQYGG TFQNYYMYHG GTNFGRTSGG
     PYITTSYDYD APLDEYGNKN QPKWGHLKQL HELLKSMEDV LTQGTTNHTD YGNLLTATVY
     NYSGKSACFL GNANSSNDAT IMFQSTQYIV PAWSVSILPN CVNEVYNTAK INAQTSIMVM
     KDNKSDNEEE PHSTLNWQWM HEPHVQMKDG QVLGSVSRKA AQLLDQKVVT NDTSDYLWYI
     TSVDISENDP IWSKIRVSTN GHVLHVFVNG AQAGYQYGQN GKYSFTYEAK IKLKKGTNEI
     SLLSGTVGLP NYGAHFSNVS VGVCGPVQLV TLQNNTEVVK DITNNTWNYK VGLHGEIVKL
     YCPENNKGWN TNGLPTNRVF VWYKTLFKSP KGTDPVVVDL RGLKKGQAWV NGNNIGRYWT
     RYLADDNGCT ATCNYRGPYS SDKCITKCGR PTQRWYHVPR SFLRQDNQNT LVLFEEFGGH
     PNEVKFATVM VEKICANSYE GNVLELSCRE EQVISEIKFS SFGVPEGECG SFKKSQCESP
     NALSILSKSC LGKQSCSVQV SQRMLGPTGC RMPQNQNKLA IEAVCESIAK KY
//