ID BGAL_BOVIN Reviewed; 653 AA. AC Q58D55; A5LIP2; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 1. DT 24-JAN-2024, entry version 96. DE RecName: Full=Beta-galactosidase; DE EC=3.2.1.23 {ECO:0000250|UniProtKB:P16278}; DE AltName: Full=Acid beta-galactosidase; DE Short=Lactase; DE Flags: Precursor; GN Name=GLB1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RA Satoh Y., Yajima A., Uda Y.; RT "Molecular cloning and characterization of lysosomal beta-galactosidase RT from bovine liver."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). CC -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from CC gangliosides, glycoproteins, and glycosaminoglycans. CC {ECO:0000250|UniProtKB:P16278}. 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:0000250|UniProtKB:P16278}; CC -!- SUBUNIT: Homodimer. May form higher multimers. CC {ECO:0000250|UniProtKB:P16278}. CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P16278}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB325580; BAF64285.1; -; mRNA. DR EMBL; BT021742; AAX46589.1; -; mRNA. DR RefSeq; NP_001030215.1; NM_001035043.1. DR AlphaFoldDB; Q58D55; -. DR SMR; Q58D55; -. DR STRING; 9913.ENSBTAP00000020296; -. DR BindingDB; Q58D55; -. DR ChEMBL; CHEMBL3482; -. DR DrugCentral; Q58D55; -. DR CAZy; GH35; Glycoside Hydrolase Family 35. DR GlyCosmos; Q58D55; 6 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000020296; -. DR GeneID; 507188; -. DR KEGG; bta:507188; -. DR CTD; 2720; -. DR eggNOG; KOG0496; Eukaryota. DR InParanoid; Q58D55; -. DR OrthoDB; 5489808at2759; -. DR PRO; PR:Q58D55; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0005773; C:vacuole; IBA:GO_Central. DR GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB. 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:SF172; 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 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome; KW Reference proteome; Signal; Zymogen. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT PROPEP 23..27 FT /evidence="ECO:0000250" FT /id="PRO_0000283035" FT CHAIN 28..653 FT /note="Beta-galactosidase" FT /id="PRO_0000283036" FT ACT_SITE 187 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P16278" FT ACT_SITE 267 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:P16278" FT BINDING 82 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P16278" FT BINDING 128 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P16278" FT BINDING 186 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P16278" FT BINDING 332 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:P16278" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 96 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 246 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 463 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 497 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 554 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 194..229 FT /evidence="ECO:0000250|UniProtKB:P16278" FT DISULFID 625..633 FT /evidence="ECO:0000250|UniProtKB:P16278" SQ SEQUENCE 653 AA; 73413 MW; 37ED2284A4EB4F97 CRC64; MPGVVRLLAL LLVPLLLGSA RGLHNATQRT FQIDYRRNRF LKDGQPFRYI SGSIHYFRVP RFYWKDRLLK MKMAGLNAIQ TYVAWNFHEL QPGRYNFSGD HDVEHFIQLA HELGLLVILR PGPYICAEWD MGGLPAWLLE KKSIVLRSSD PDYLAAVDKW LGVLLPKMRP LLYKNGGPII TVQVENEYGS YLSCDYDYLR FLQKRFHDHL GEDVLLFTTD GVNERLLQCG ALQGLYATVD FSPGTNLTAA FMLQRKFEPT GPLVNSEFYT GWLDHWGQRH STVSSKAVAF TLHDMLALGA NVNMYMFIGG TNFAYWNGAN IPYQPQPTSY DYDAPLSEAG DLTEKYFALR DIIQKFAKVP EGPIPPSTPK FAYGKVALNK LKTVEDALNI LCPSGPIKSV YPLTFIDVKQ YFGFVLYRTM LPEDCSDPTP LSSPLSGVHD RAYVSVNGVA QGILERESVI TLNITGKAGA TLDLLVENMG RVNYGSSIND FKGLVSNLTL GSKILTNWEI FPLDMEDAVR SHLGTWGGRD RGYHNKARAH SPPTYALPTF YVGNFTIPSG IADLPQDTFI QFPGWTKGQV WINGFNLGRY WPVRGPQMTL FVPQHILVTS TPNTIVVLEL EHAPCQDGGP ELCTVEFVDK PVFRTVQTHR HAN //