BGAL_BOVIN
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 03-AUG-2022, entry version 90.
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}.
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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 PaxDb; Q58D55; -.
DR PRIDE; Q58D55; -.
DR GeneID; 507188; -.
DR KEGG; bta:507188; -.
DR CTD; 2720; -.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; Q58D55; -.
DR OrthoDB; 179316at2759; -.
DR PRO; PR:Q58D55; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004565; F:beta-galactosidase activity; ISS:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR InterPro; IPR026283; B-gal_1-like.
DR InterPro; IPR025300; BetaGal_jelly_roll_dom.
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; PTHR23421; 1.
DR Pfam; PF13364; BetaGal_dom4_5; 1.
DR Pfam; PF01301; Glyco_hydro_35; 1.
DR PIRSF; PIRSF006336; B-gal; 1.
DR PRINTS; PR00742; GLHYDRLASE35.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 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
