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Database: UniProt
Entry: A0A0D3C3S7_BRAOL
LinkDB: A0A0D3C3S7_BRAOL
Original site: A0A0D3C3S7_BRAOL 
ID   A0A0D3C3S7_BRAOL        Unreviewed;       898 AA.
AC   A0A0D3C3S7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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   Name=106341920 {ECO:0000313|EnsemblPlants:Bo4g179470.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo4g179470.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo4g179470.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo4g179470.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   RefSeq; XP_013636126.1; XM_013780672.1.
DR   AlphaFoldDB; A0A0D3C3S7; -.
DR   STRING; 109376.A0A0D3C3S7; -.
DR   EnsemblPlants; Bo4g179470.1; Bo4g179470.1; Bo4g179470.
DR   GeneID; 106341920; -.
DR   Gramene; Bo4g179470.1; Bo4g179470.1; Bo4g179470.
DR   KEGG; boe:106341920; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   HOGENOM; CLU_007853_4_1_1; -.
DR   OMA; NFFEPFN; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000032141; Chromosome C4.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-KW.
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:SF13; BETA-GALACTOSIDASE 2-RELATED; 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   Apoplast {ECO:0000256|ARBA:ARBA00022523};
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:UP000032141}.
FT   DOMAIN          796..882
FT                   /note="SUEL-type lectin"
FT                   /evidence="ECO:0000259|PROSITE:PS50228"
SQ   SEQUENCE   898 AA;  99897 MW;  367B4E8FAD7830D0 CRC64;
     MSFASMAEST RNASLQWRKL PPIIALLLIL PIVSGSYFKP FNVSYDHRAL IVAGKRRMLV
     SAGVHYPRAT PQMWPDLIAK SKEGGADVVQ TYVFWSGHEP VKGQYNFEGR YDLVKFVKLV
     GSSGLYLHLR IGPYVCAEWN FGGFPVWLRD VPGIEFRTDN EPFKKEMQKF VTKIVGLMRE
     AKMFCWQGGP VIMLQIENEY GDVEKSYGQK GKDYVKWAAS MALGLGAGVP WVMCKQTDAP
     ENILDACNGY YCDGFKPNSK TKPVLWTEDW DGWYTKWGGS LPHRPAEDLA FAVARFYQRG
     GSFQNYYMYF GGTNFGRTSG GPFYITSYDY DAPLDEYGLR SEPKWGHLKD LHAAIKLCEP
     ALVAADAPQY KKLGSNQEAH IYHGDGETGG KVCAAFLANI DEHKSAYVKF NGQSYTLPPW
     SVSILPDCRH VAYNTAKVGA QTSVKTVEPA RPPLGSMSIL QKVVSQDSAS YISKSWMALK
     EPIGIWGENN FTAQGLLEHL NVTKDQSDYL WHKTRISVTE DDISFWKKNG ANPTLSVDSM
     RDVLRVFVNK QLSGSIVGHW VKAEQPVRFV QGNNDLLLLT QTVGLQNYGA FLEKDGAGFR
     GKAKLTGFKN GDVDLSKSSW TYQVGLKGEA EKVYTVEYNE KAEWSTLDTE ASPSIFMWYK
     TYFNTPDGTD PVVLDLGSMG KGQAWVNGHH IGRYWSIIAQ KDGCDKTCDY RGAYTSDKCT
     TNCGKPTQTR YHVPRSWLKP DSNLLVLFEE TGGNPFKISV KTVTAGVLCG QVSESHYPPL
     RKWSTPGFMD GTMSINSVAP EMHLRCEEGH VISSIEFASY GTPRGSCEKF STGKCHASKS
     LSVVSEACKG RNSCFIEVSN AAFQSDPCKG TLKTLAVMAR CSPSQNTSCL RQRETASD
//
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