ID A0A059ANH0_EUCGR Unreviewed; 830 AA.
AC A0A059ANH0;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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_I01412 {ECO:0000313|EMBL:KCW55522.1};
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:KCW55522.1};
RN [1] {ECO:0000313|EMBL:KCW55522.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW55522.1};
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; KK198761; KCW55522.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059ANH0; -.
DR EnsemblPlants; KCW55522; KCW55522; EUGRSUZ_I01412.
DR Gramene; KCW55522; KCW55522; EUGRSUZ_I01412.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; A0A059ANH0; -.
DR OMA; FEYHIPR; -.
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; 1.
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:SF52; BETA-GALACTOSIDASE 14; 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; PS51257; PROKAR_LIPOPROTEIN; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..830
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001572546"
FT DOMAIN 746..829
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 830 AA; 93413 MW; D90D86CE8CD3CCCA CRC64;
MRIAMKRLVI LSALFSLLLS VACAKKKVQG VTYDGTSLII NGKRELLFSG SIHYPRSTPE
MWPDLIRKAK QGGLNVIQTY VFWNAHEPVQ GQYNFEGNYD LVKFIKLIGE HKMYVTLRVG
PFIQAEWNHG GLPYWLREVQ NITFRSDNPP FKYHMKKYVK MIIQKMKDEK LFASQGGPII
ISQIENEYNS IQLAYRDAGT RYVQWAGNMA VGLKTGVPWI MCKQKDAPDP VINACNGRHC
GDTFTGPNKP YKPTLWTENW TAQYRVFGDP PSQRSAEDLA FSVARFFAKN GTLTNYYMYH
GGTNLGRTSA VFTTTRYYDE APLDEYGLQR EPKWGHLKDL HKALRLCRKA LLWGSPKVQR
LSKDLEARYY EIPGTKVCAA FLTNNSTLSA QVVKFRGQEY YLPQHSISIL PDCKTVVYNT
QRIVSQHNSR NLVKSEKANK LKWEMSLEII PDTNRVPVNA KIPAELYSLL KDTTDYAWFT
TSLDLGVRDL PMRKNIKPVL RVASLGHAML AFVNGEFIGS AHGSHIDKSF VLQQPIDLKP
GVNHISLLGS TVGLPDSGAY MEHRYAGPRL VTILGLNTGT LDLTLNGWGH QVGLDGEKVR
VYTQSGSHRA QWTEATKGVG RALTWYKTYF DAPEGDQPVA IHLPQMTKGM VWVNGKSIGR
YWYTYLSPLG QPSQSEYHIP RSFIKPTDNL LVVLDEDGGN PESIEILNVD RDTICSYITE
NHPPSVKSWA RKNSHFITVL DEVKTAAHLK CPNHKKIVAI EFASFGDPYG ICGNFKYGNC
TSPISKDIVE KHCLGKTSCA VPIERGLLDK GNDGCPSIMK TLAIQAKCSH
//
