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Database: UniProt
Entry: A0A0E0JKF1_ORYPU
LinkDB: A0A0E0JKF1_ORYPU
Original site: A0A0E0JKF1_ORYPU 
ID   A0A0E0JKF1_ORYPU        Unreviewed;       779 AA.
AC   A0A0E0JKF1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 40.
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};
OS   Oryza punctata (Red rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC01G20770.1};
RN   [1] {ECO:0000313|EnsemblPlants:OPUNC01G20770.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wing R.;
RT   "Oryza genome evolution.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OPUNC01G20770.1}
RP   IDENTIFICATION.
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         ECO:0000256|RuleBase:RU000675};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   AlphaFoldDB; A0A0E0JKF1; -.
DR   STRING; 4537.A0A0E0JKF1; -.
DR   EnsemblPlants; OPUNC01G20770.1; OPUNC01G20770.1; OPUNC01G20770.
DR   Gramene; OPUNC01G20770.1; OPUNC01G20770.1; OPUNC01G20770.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_0_1; -.
DR   OMA; SYEMQAS; -.
DR   Proteomes; UP000026962; Chromosome 1.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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:SF153; BETA-GALACTOSIDASE 2; 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   Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..779
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002364041"
FT   DOMAIN          693..779
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   779 AA;  85913 MW;  DF8E6C03EB29AAF1 CRC64;
     MAMAASAAAV AVAAVVAVAV LASAVSAAVT YDRKAVVMWP DLIEKAKDGG LDVVQTYVFW
     NGHEPSPGQY YFEGQYDLVH FIKLVKQAGL YVHLRIGPYV CAEWNFGGFP VWLKYAEMQK
     FTTKIVEMMK SEGLFEWQGG PIILSQIENE FGPLEWDQGE PAKAYASWAA NMAVALNTGV
     PWIMCKEDDA PDPIINTCNG FYCDWFSPNK PHKPTMWTEA WTAWYTGFGI PVPHRPVEDL
     AYGVAKFIQK GGSFVNYYMY HGGTNFGRTA GGPFIATSYD YDAPIDEYGL LREPKWGHLK
     QLHKAIKFCE PALVAGDPIV TSLGNAQKSS VFRSSTGACA AFLENKDKVS YARVAFNGMH
     YDLPPWSISI LPDCKTTVFN TARVGSQISQ MKMEWAGGFA WQSYNEEINS FGEDPFTTVG
     LLEQINVTRD NTDYLCVDVA QDEQFLSNGE NPKLTVMSAG HALHIFINGQ LTGTVYGSVD
     NPKLTYTGNV KLWAGSNTIS CLSIAVGLPN VGEHFETWNA GILGPVTLDG LNEGRRDLTW
     QKWTYQVGLK GESMSLHSLS GSSTVEWGEP VQKQPLTWYK AFFNAPDGDE PLALDMSSMG
     KGQIWINGQG IGRYWPGYKA SGNCETCDYR GEYNETKYHV PRSWLSPTGN LLVIFEEWGG
     DPTGISMVKR SIGSICADVS EWQPSMKNWR TKDYEKAKVH LQCDNGKKIT EIKFASFGTP
     QGSCGSYSEG GCHAHKSYDI FWKNCVGQER CGVSVVPEVF GGDPCPGTMK RAVVEATCG
//
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