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Database: UniProt
Entry: A0A059DFQ3_EUCGR
LinkDB: A0A059DFQ3_EUCGR
Original site: A0A059DFQ3_EUCGR 
ID   A0A059DFQ3_EUCGR        Unreviewed;       837 AA.
AC   A0A059DFQ3;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=EUGRSUZ_A01583 {ECO:0000313|EMBL:KCW89294.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW89294.1};
RN   [1] {ECO:0000313|EMBL:KCW89294.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW89294.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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; KK198753; KCW89294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059DFQ3; -.
DR   EnsemblPlants; KCW89294; KCW89294; EUGRSUZ_A01583.
DR   Gramene; KCW89294; KCW89294; EUGRSUZ_A01583.
DR   eggNOG; KOG0496; Eukaryota.
DR   InParanoid; A0A059DFQ3; -.
DR   OMA; IQSAHEY; -.
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   CDD; cd22842; Gal_Rha_Lectin_BGal; 1.
DR   Gene3D; 2.60.120.740; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
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:SF160; 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..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..837
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001575319"
FT   DOMAIN          749..835
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   837 AA;  93680 MW;  50EB0758D8130AE7 CRC64;
     MAIFGPCFAA VFSVVSFLLV ASAVPLDVSY DERGIKLNGQ SRIIISGSIH YPRSTPEMWG
     DLIKKAKEGG LNAIETYVFW NAHEPLYRQY DFEGNKDLVR FIKTIQDAGL YAILRIGPYV
     CAEWNYGGFP VWLHNLPGVE LRTNNTVYQN EMKTFVTLIV DMMQKHGLFA IQGGPIIVAQ
     IENEYGNVEW AFGNNGKSYI NWCAQLAESY GVQVPWIMCQ QSDAPSPMIN TCNGYYCDQF
     SPNNPKSPKW WTENWSGWFK DWGMKDPHRT AEDLAFAVAR FFQYGGSLQN YYMYHGGTNF
     DRTAGGPYIT TSYDYDAPLD EYGNLNQPKW GHLKRLHELI MSMEEILTHG VKRDVDYGNM
     MSGTVYMYKG KQSCFLGNAN QNQDFTVNLM GSSYTVPAWS VSILPDCYTE VYNTAKINSQ
     QTVMVKLPNE ADDQTEPYEL QWDWRPEHPE SLHHGVAKGS VTTANELLDQ KTVTNDTSDY
     LWYLTSLDLS KDDSLAGKAI TLHVHTNGHI VHAFVNGKHV GSQWGTSDHL EFIMEKDIKL
     KHGKTNSISL LSVTVGLQNY GANFDTVNVG IHGPVKLIGN KGQSDEVTVD LSTNLWTYKV
     GLNGMEEKGL QLDNARHQHG WKSYNLPSNR LFVWYKTTFK APLGSDPVVV DLQGLGKGTA
     WVNGHNIGRF WPSFVASEDG CTATCDYRGA YNSNKCLTNC GDPSQRWYHI PRSFLQDDGN
     KLVLFEEFGG TPLHVRFQTI TAGTICATTD EKKQLELLCQ GGRIMSEIKF ASFGEPTGVC
     GSYARGSCEA PNTLSVIQKQ CLGQESCTLD VSENTFGPTG CHQNVYRLAV EATCDSP
//
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