ID B8BGB0_ORYSI Unreviewed; 828 AA.
AC B8BGB0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 81.
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=OsI_33138 {ECO:0000313|EMBL:EEC66762.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC66762.1, ECO:0000313|Proteomes:UP000007015};
RN [1] {ECO:0000313|EMBL:EEC66762.1, ECO:0000313|Proteomes:UP000007015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA Samudrala R., Wang J., Wong G.K., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
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 EMBL; CM000135; EEC66762.1; -; Genomic_DNA.
DR AlphaFoldDB; B8BGB0; -.
DR STRING; 39946.B8BGB0; -.
DR EnsemblPlants; BGIOSGA032117-TA; BGIOSGA032117-PA; BGIOSGA032117.
DR Gramene; BGIOSGA032117-TA; BGIOSGA032117-PA; BGIOSGA032117.
DR HOGENOM; CLU_007853_4_0_1; -.
DR OMA; IQSAHEY; -.
DR Proteomes; UP000007015; Chromosome 10.
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; 2.
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:SF174; BETA-GALACTOSIDASE 7; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000007015};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..828
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002868603"
FT DOMAIN 746..828
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 828 AA; 92320 MW; 47D40FE1D478392B CRC64;
MAKAMCSLGA CLAVMLVVLA AAVAGVGCSI VSYDGRSLIL DGERRIVISG SIHYPRSTPE
MWPDLIKKAK EGGLNAIETY VFWNGHEPRR REFNFEGNYD VVRFFKEIQN AGMYAILRIG
PYICGEWNYG GLPVWLRDIP GIKFRLHNKP FENEMEAFTT LIVKKMKDAN MFAGQGGPII
LAQIENEYGY TMLQPENIQS AHEYIHWCAD MANKQNVGVP WIMCQQDNDV PPNVVNTCNG
FYCHEWFSNR TSIPKMWTEN WTGWYRDWDQ PEFRRPTEDI AFAVAMFFQM RGSLQNYYMY
HGGTNFGRTA GGPYITTSYD YDAPLDEYGN LRQPKYGHLK ELHSVLMSME KILLHGDYID
TNYGDNVTVT KYTLNATSAC FINNRFDDRD VNVTLDGTTH FLPAWSVSIL PDCKTVAFNS
AKIKTQTTVM VNKTSMVEQQ TEHFKWSWMP ENLRPFMTDE KGNFRKNELL EQIVTTTDQS
DYLWYRTSLE HKGEGSYVLY VNTTGHELYA FVNGKLVGQQ YSPNENFTFQ LKSPVKLHDG
KNYISLLSGT VGLRNYGGSF ELLPAGIVGG PVKLIDSSGS AIDLSNNSWS YKAGLAGEYR
KIYLDKPGNK WRSHNSTIPI NRPFTWYKTT FQAPAGEDSV VVDLHGLNKG VAWVNGNSLG
RYWPSYVAAD MPGCHHCDYR GVFKAEVEAQ KCLTGCGEPS QQLYHVPRSF LHKGEPNTLI
LFEEAGGDPS EVAVRTVVEG SVCASAELGD TVTLSCGAHG RTISSVDVAS FGVARGRCGS
YDGGCDSKVA YDAFAAACVG KESCTVLVTD AFANAGCVSG VLTVQATC
//
