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Database: UniProt
Entry: B9RR87_RICCO
LinkDB: B9RR87_RICCO
Original site: B9RR87_RICCO 
ID   B9RR87_RICCO            Unreviewed;       848 AA.
AC   B9RR87;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 70.
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=RCOM_0711410 {ECO:0000313|EMBL:EEF46258.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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; EQ973802; EEF46258.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9RR87; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   InParanoid; B9RR87; -.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IBA:GO_Central.
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; 2.
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:UP000008311}.
FT   DOMAIN          762..848
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   848 AA;  94191 MW;  E202C168733689CE CRC64;
     MSHMFSYKYS VPVLFNTILC SFNRMASSKS VVAIFFCLFT FVSATIVSHD GRAITIDGKR
     RVLISGSIHY PRSTAEMWPD LIKKSKEGGL DAIETYVFWN SHEPSRRQYD FSGNLDLVRF
     IKTIQAEGLY AVLRIGPYVC AEWNYGGFPM WLHNLPGCEL RTANSVFMNE MQNFTSLIVD
     MMKDENLFAS QGGPIILAQV ENEYGNVMSA YGAAGKTYID WCSNMAESLD IGVPWIMCQQ
     SDAPQPMINT CNGWYCDQFT PNNANSPKMW TENWTGWFKS WGGKDPHRTA EDVAFAVARF
     FQTGGTFQNY YMYHGGTNFG RTAGGPYITT SYDYDAPLDE YGNLNQPKWG HLKQLHDILH
     SMEYTLTHGN ISTIDYDNSV TATIYATDKE SACFFGNANE TSDATIVFKG TEYNVPAWSV
     SILPDCENVG YNTAKVKTQT AIMVKQKNEA EDQPSSLKWS WIPENTHTTS LLGKGHAHAR
     QLIDQKAAAN DASDYLWYMT SLHIKKDDPV WSSDMSLRVN GSGHVLHAYV NGKHLGSQFA
     KYGVFSYVFE KSLKLRPGKN VISLLSATVG LQNYGPMFDL VQTGIPGPVE IIGHRGDEKV
     VKDLSSHKWS YSVGLNGFHN ELYSSNSRHA SRWVEQDLPT NKMMIWYKTT FKAPLGKDPV
     VLDLQGMGKG FAWVNGNNIG RYWPSFLAEE DGCSTEVCDY RGAYDNNKCV TNCGKPTQRW
     YHVPRSFFND YENTLVLFEE FGGNPAGVNF QTVTVGKVSG SAGEGETIEL SCNGKSISAI
     EFASFGDPQG TSGAYVKGTC EGSNDAFSIV QKACVGKETC KLEASKDVFG PTSCGSDVVN
     TLAVQATC
//
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