ID A0A059DEF6_EUCGR Unreviewed; 669 AA.
AC A0A059DEF6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE Flags: Fragment;
GN ORFNames=EUGRSUZ_A01181 {ECO:0000313|EMBL:KCW88854.1};
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:KCW88854.1};
RN [1] {ECO:0000313|EMBL:KCW88854.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW88854.1};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KK198753; KCW88854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059DEF6; -.
DR EnsemblPlants; KCW88854; KCW88854; EUGRSUZ_A01181.
DR Gramene; KCW88854; KCW88854; EUGRSUZ_A01181.
DR InParanoid; A0A059DEF6; -.
DR OMA; DANINFQ; -.
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; 2.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041392; GHD.
DR InterPro; IPR031330; Gly_Hdrlase_35_cat.
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; 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; PS50228; SUEL_LECTIN; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 581..653
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KCW88854.1"
SQ SEQUENCE 669 AA; 76182 MW; C687D6E6465F2BDC CRC64;
KEGGLNAIET YVFWNAHEPL YRQYDFEGNK DLVRFIKTIQ DAGLHAILRI GPYVCAEWNY
GGFPVWLHNL PGVELRTNNT VYQGGPIIVA RIENEYENVE WAYGNNGNYG VQVPWIMCQQ
SDAPSPMMNT CNGYYCDQFS PNNPKSPKWW TENWSGWFKD WGMKDPHRTA EDLAFAVARF
FQYGGSLQNY YMYHGGTNFD RTAGGPYITT SYDYDAPLDE YGNLNQTKWG HLKRLHELIM
SMEEILTHGV KRDVDYGNMM SGTVYMYKGK QSCFLGNANQ NQDFTVNLMG SSHTVPAWSV
SILPDCYTEV YNTAKINSQQ TVMVKLPNEA DDQTEPYELK WDWRPEHLES LHHGVAKGSA
MTANELLDQK TVTNDTSDYL WYLTSLDLSK NDSLAGKVIT LHVHTNGHIV HAFVNGKHVG
ESSSHLYNLH LIRLIDVKYS NRYHIKLKHG KTNWISLLSV TVGLQILFVW YKTTFKAPLG
SDPWWWTWQR HCLGQWPQHG RFWPSYVASE DGCIATYDYC GAYKSDKCLT NCGKPSQRWY
HIPCSFLQDD GNKLVLFEEF GGTPLHVRFQ TVTAGTICAT TDEKMKLELS CQDGRVMSEI
KFASFSEPIG VYGSYARGSC EAPNTLSVIQ KQCLGQKSCT LDVSENTFGP TGCHQNVSFS
IDFISLVSF
//
