ID A0A059AJJ6_EUCGR Unreviewed; 713 AA.
AC A0A059AJJ6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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_J02852 {ECO:0000313|EMBL:KCW53580.1};
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:KCW53580.1};
RN [1] {ECO:0000313|EMBL:KCW53580.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW53580.1};
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; KK198762; KCW53580.1; -; Genomic_DNA.
DR RefSeq; XP_018719731.1; XM_018864186.1.
DR AlphaFoldDB; A0A059AJJ6; -.
DR STRING; 71139.A0A059AJJ6; -.
DR EnsemblPlants; KCW53580; KCW53580; EUGRSUZ_J02852.
DR GeneID; 104424130; -.
DR Gramene; KCW53580; KCW53580; EUGRSUZ_J02852.
DR KEGG; egr:104424130; -.
DR eggNOG; KOG0496; Eukaryota.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; A0A059AJJ6; -.
DR OMA; RAHPDTW; -.
DR OrthoDB; 5489808at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 83..409
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 456..574
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 615..677
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 232
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 713 AA; 78935 MW; 0F122D1CF8E721F7 CRC64;
MPVRTATSNA LPLHRAAPAA SRAAAMARKR GLRATTVVFF GLLSLAAFGA FVPALAPLPS
LSSPHPSLPR KSSSRKFEID SDKFWKDGSP FQIIGGDVHY FRVLPEYWED RLLRAKALGL
NTIQTYVPWN LHEPKPGETV FEGIADIISF LNLCKKLDLL VMLRVGPYIC AEWDFGGFPY
WLLAIKPALT LRSSDPAFVK LVEQWWSILL PKVSSLLYAN GGPIIMVQIE NEYGSYGDDK
TYLRHLVKLA RGYLGNEVIL YTTDGGSKET LQKGTVGGED VFSAVDFDTG AEAWPIFNLQ
KQFNAPGKSP PLAAEFYTGW LTHWGEKLAQ TDAEFTAAAL EKILSRNGSA VLYMAHGGTN
FGFYNGANTG GSESEYKPDL TSYDYDAPIK ESGDVDNPKY KAIRKVVEQY SIVPLPSVPY
NNAKTSYGRI QLQRTSFLFD LLNVLGPHDV VESESPLSME LVGQMFGFLL YATKFASTDD
GSMLTIPKVH DRGQVFVSCA SRKDRPLYAG AIERWSNKPL HLPVTKCASR INLYVLVENM
GRVNYGSYMF DMKGILSSVY LNGRVLLGWK MFSIPLHNLN EATTINSVVQ VRHSGIMRVL
SNRSINKSDG VTREPAFYAG SFHVNEVAQI KDTFISFQGW GKGVAYVNDF NIGRFWPSFG
PQCNLYVPAP VLRVGVNSLV VLELESPKPD LALHSVDEPD FSCGKSKSSV HHL
//
