ID A0A0D3CX00_BRAOL Unreviewed; 693 AA.
AC A0A0D3CX00;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-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};
GN Name=106296590 {ECO:0000313|EnsemblPlants:Bo6g088130.1};
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:Bo6g088130.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo6g088130.1, 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:Bo6g088130.1}
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_013588214.1; XM_013732760.1.
DR RefSeq; XP_013588215.1; XM_013732761.1.
DR RefSeq; XP_013588216.1; XM_013732762.1.
DR AlphaFoldDB; A0A0D3CX00; -.
DR STRING; 109376.A0A0D3CX00; -.
DR EnsemblPlants; Bo6g088130.1; Bo6g088130.1; Bo6g088130.
DR GeneID; 106296590; -.
DR Gramene; Bo6g088130.1; Bo6g088130.1; Bo6g088130.
DR eggNOG; KOG0496; Eukaryota.
DR HOGENOM; CLU_007853_7_2_1; -.
DR OMA; RAHPDTW; -.
DR OrthoDB; 5489808at2759; -.
DR Proteomes; UP000032141; Chromosome C6.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-KW.
DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR048912; BetaGal1-like_ABD1.
DR InterPro; IPR048913; BetaGal_gal-bd.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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 PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR Pfam; PF21317; BetaGal_ABD_1; 1.
DR Pfam; PF21467; BetaGal_gal-bd; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
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.
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 66..391
FT /note="Glycoside hydrolase 35 catalytic"
FT /evidence="ECO:0000259|Pfam:PF01301"
FT DOMAIN 438..559
FT /note="Beta-galactosidase 1-like first all-beta"
FT /evidence="ECO:0000259|Pfam:PF21317"
FT DOMAIN 595..657
FT /note="Beta-galactosidase galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21467"
FT ACT_SITE 214
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT ACT_SITE 297
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ SEQUENCE 693 AA; 77987 MW; F27DD701791B7A31 CRC64;
MAKISKPSTG GHHLAFVLLL VLVAVGICVP VFALLPSLTS HQSLPPALSR DEKMMSRIFY
IKDDKFWKDE NPFQIIGGDL HYFRVLPEYW EDRLMRAKAL GLNTIQTYVP WNLHEPKPGK
MVFEGIADLV SFIKLCQKLD LLVMLRAGPY ICGEWDLGGF PAWLLAVKPP LKLRTADPAY
LELVERWWNV LLRKVFPLLY SNGGPVIMVQ IENEYGSYGN DKAYLRNLVT MARGHLGNDI
ILYTTDGGTR ETLEKGNVPL YNVYSAVDFS TGDDPWPIFE LQRKFNAPGR SPPLSSEFYT
GWLTHWGEKI AKTDAEFTAA SLEKILSSNG SAVLYMVHGG TNFGFYSGAN TGSEEFDYKP
DLTSYDYDAP IKESGEIDNP KFKALRRVIK KYSAAPHTTT PYNTKRKAYG PIKMQRTISL
FDLMAMTDPV DVITSTNPIS MESAGHLFGF LVYESSYISK KSGNILRIPK VHDRAQVFVS
CLSQDVDGGV LRYIGTTERW NNQPVSIPTT ECTSNTSLFI LVENMGRVNY GPYIFDEKGI
LSPVYLDGEI LHGWKMIPIP FHNVNQMPHF SFKMQHTKKS SENLELTNDV GQKEPALFAG
EFSINSVEEI KDTYLSFNGW GKGVAFVNKF NIGRYWPSVG PQCNLYVPAP LLKPGRNSVV
IFELESPHVD LLLRSVDQED FTCGSNYSKV NQL
//
