ID A0A0E0CY79_9ORYZ Unreviewed; 716 AA.
AC A0A0E0CY79;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI03G10280.4};
RN [1] {ECO:0000313|EnsemblPlants:OMERI03G10280.4}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI03G10280.4};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI03G10280.4}
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; A0A0E0CY79; -.
DR EnsemblPlants; OMERI03G10280.4; OMERI03G10280.4; OMERI03G10280.
DR Gramene; OMERI03G10280.4; OMERI03G10280.4; OMERI03G10280.
DR HOGENOM; CLU_007853_4_0_1; -.
DR Proteomes; UP000008021; Chromosome 3.
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; 3.20.20.80; Glycosidases; 1.
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:SF124; BETA-GALACTOSIDASE 2-RELATED; 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; 2.
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.
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:UP000008021};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..716
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002356314"
FT DOMAIN 630..716
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 716 AA; 78006 MW; C275EF3A45C266CE CRC64;
MAAAATAAAP LLRLRLRLLP VLVVVSLLVG ASRAANVTYD HRAVVIDGVR RVLVSGSIHY
PRSTPDMWPG LIQKSKDGGL DVIETYVFWD IHEPVRGQAR TTLSQLLLST TARSVVLHLI
YDFEGRKDLV RFVKAVADAG LYVHLRIGPY VCAEWNYGGF PVWLHFVPGI KFRTDNEAFK
AEMQRFTEKV VDTMKGAGLY ASQGGPIILS QIENEYGNID SAYGAAGKAY MRWAAGMAVS
LDTGVPWVMC QQSDAPDPLI NTCNGFYCDQ FTPNSKSKPK MWTENWSGWF LSFGGAVPYR
PAEDLAFAVA RFYQRGGTFQ NYYMYHGGTN FGRSTGGPFI ATSYDYDAPI DEYGMVRQPK
WGHLRDVHKA IKLCEPALIA AEPSYSSLGQ NTEATVYQTA DNSICAAFLA NVDAQSDKTV
KFNGNTYKLP AWSVSILPDC KNVVLNTAQI NSQVTTSEMR SLGSSAQDTD DSSITPELAT
AGWSYAIEPV GITKENALTK PGLMEQINTT ADASDFLWYS TSIVVKGDEP YLNGSQSNLL
VNSLGHVLQE VLRAVLAARS SHCRHQLHLY HVPRSFLQPG SNDLVLFEQF GGDPSMISFT
TRQTSSICAH VSEMHPAQID SWISPQQTSQ TPGPALRLEC PREGQVISNI KFASFGTPSG
TCGNYNHGEC SSSQALAVVQ EACVGMTNCS VPVSSNNFGD PCSGVTKSLV VEAACS
//
