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Database: UniProt
Entry: A0A0E0HHH7_ORYNI
LinkDB: A0A0E0HHH7_ORYNI
Original site: A0A0E0HHH7_ORYNI 
ID   A0A0E0HHH7_ORYNI        Unreviewed;       671 AA.
AC   A0A0E0HHH7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=beta-galactosidase {ECO:0000256|ARBA:ARBA00012756};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
OS   Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA05G25220.1};
RN   [1] {ECO:0000313|EnsemblPlants:ONIVA05G25220.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G25220.1};
RA   Wing R.A., Hsing Y.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ONIVA05G25220.1}
RP   IDENTIFICATION.
RC   STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA05G25220.1};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A0E0HHH7; -.
DR   STRING; 4536.A0A0E0HHH7; -.
DR   EnsemblPlants; ONIVA05G25220.1; ONIVA05G25220.1; ONIVA05G25220.
DR   Gramene; ONIVA05G25220.1; ONIVA05G25220.1; ONIVA05G25220.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   OMA; RAHPDTW; -.
DR   Proteomes; UP000006591; Unassembled WGS sequence.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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; 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.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..671
FT                   /note="beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002361593"
FT   DOMAIN          41..364
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          412..531
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          581..643
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        270
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   671 AA;  75447 MW;  13B90C5F0D98E36D CRC64;
     MGPSRSFQNL LLLLLPLALA LCSAAASGEA SRRFWVENDT FWKDGAPFQI VGGDVHYFRI
     VPEYWKDRLL RAKALGLNTI QTYVPWNLHE PKPLSWEFKG FTDIESYLRL AHELDMLVML
     RVGPYICGEW DLGGFPPWLL TIEPTIELRS SDSTYLSLVD RWWGVLLPKI APLLYSNGGP
     IIMIENEFGS FGDDKNYLHY LVEVARRYLG NDIMLYTTDG GAIGNLKNGT ILQDDVFAAV
     DFDTGSNPWP IFQLQKEYNL PGKSAPLSSE FYTGWLTHWG ERIATTDASS TAKALKRILC
     RNGSAVLYMA HGGTNFGFYN GANTGQNESD YKADLTSYDY DAPIREYGDV HNAKYKALRR
     VIHECTGIPL LQLPSKIERA SYGLVEVQKV ASLFDVIHNI SDALKVAFSE QPLSMELMGQ
     MFGFLLYTSE YQEKHSSSIL SIPKVHDRAQ VFVSCSHGDV RKPRYVGIVE RWSSKTLQIP
     SLSCSSNVSL YILVENMGRV NYGPYIFDQK GILSSVEIDG IILRHWKMHP VSLNAVGNLS
     KLQLIMQMTD AEASKVSIYG DSENKLQDVS LYLNEGISEE PAFYEGHFHI DSESEKKDTF
     ISFRGWNKGV AFVNNFNIGR FWPAIGPQCA LYVPAPILKP GDNVIVIFEL HSPNPELTIK
     LVKDPDFTCG Q
//
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