ID A0A0D3EDP9_BRAOL Unreviewed; 828 AA.
AC A0A0D3EDP9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-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};
GN Name=106315383 {ECO:0000313|EnsemblPlants:Bo9g151560.1};
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:Bo9g151560.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo9g151560.1, 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:Bo9g151560.1}
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_013608565.1; XM_013753111.1.
DR AlphaFoldDB; A0A0D3EDP9; -.
DR STRING; 109376.A0A0D3EDP9; -.
DR EnsemblPlants; Bo9g151560.1; Bo9g151560.1; Bo9g151560.
DR GeneID; 106315383; -.
DR Gramene; Bo9g151560.1; Bo9g151560.1; Bo9g151560.
DR KEGG; boe:106315383; -.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_4_0_1; -.
DR OMA; IQSAHEY; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000032141; Chromosome C9.
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: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; 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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..828
FT /note="Beta-galactosidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002261071"
FT DOMAIN 742..828
FT /note="SUEL-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50228"
SQ SEQUENCE 828 AA; 92975 MW; 3F0098489F6046D5 CRC64;
MKMKQFNLLS LFLILINSFG SANSTIVSHD ERAITIDGQR RILLSGSIHY PRSTSDMWPD
LISKAKDGGL DTIETYVFWN AHEPSRRQYD FSGNLDLVRF IKTIQGAGLY SVLRIGPYVC
AEWNYGGFPV WLHNMPDMKF RTINPGFMNE MQNFTTKIVN MMKEESLFAS QGGPIILAQI
ENEYGNVISS YGAEGKAYID WCANMANSLD IGVPWIMCQQ PHAPQPMIET CNGFYCDQYK
PSNPSSPKMW TENWTGWFKN WGGKHPYRTA EDLAFSVARF FQTGGTFQNY YMYHGGTNFG
RVAGGPYITT SYDYDAPLDE YGNLNQPKWG HLKQLHTLLK SMEKPLTYGN ISTIDLGNSV
TATVYSTNEK SSCFIGNVNA TADALVNFKG KDYNVPAWSV SVLPDCDKEA YNTARVNTQT
SIITEDSCDE PEKLKWTWRP EFTTQKTILK GSGDLIAKGL VDQKDVTNDA SDYLWYMTRV
HLDKKDPIWS RNMSLRVHSN AHVLHAYANG KYVGNEIVRD NKFDYRFEKK VNLVHGTNHL
ALLSVSVGLQ NYGPFFESGP TGINGPVKLV GYKGDETIEK DLSKHQWDYK IGLNGFNHKL
FSMKSAGHHH RKWSTEKLPA DRMLSWYKAN FKAPLGKDPV IVDLNGLGKG EVWINGQSIG
RYWPSFNSSD EGCTEECDYR GEYGSDKCAF MCGKPTQRWY HVPRSFLNDK GHNTITLFEE
MGGDPSMVKF KTVVTGRVCA KAHEHNKVEL SCNNRPISAV KFASFGNPSG QCGSFAAGSC
EGAKDAVKVV AKECVGKLNC TMNVSSHKFG SNLDCGDSPK RLFVEVEC
//
