BGAL_FELCA
ID BGAL_FELCA Reviewed; 669 AA.
AC O19015; O18898;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
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; Synonyms=BGAL;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Varadarajan G.S., Smith B.F., Foureman P., Martin D.R., Varadarajan U.,
RA Georgeson M., Baker H.J.;
RT "The sequence of feline lysosomal beta-galactosidase.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Smith B.F., Foureman P., Georgeson M., Martin D.R., Baker H.J.;
RT "The mutation in feline beta-galactosidase deficiency (GM1
RT gangliosidosis).";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
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; AF006749; AAB81350.1; -; mRNA.
DR EMBL; AF029974; AAB86405.1; -; mRNA.
DR RefSeq; NP_001009860.1; NM_001009860.1.
DR AlphaFoldDB; O19015; -.
DR SMR; O19015; -.
DR STRING; 9685.ENSFCAP00000019661; -.
DR ChEMBL; CHEMBL2331052; -.
DR CAZy; GH35; Glycoside Hydrolase Family 35.
DR GeneID; 493927; -.
DR KEGG; fca:493927; -.
DR CTD; 2720; -.
DR eggNOG; KOG0496; Eukaryota.
DR InParanoid; O19015; -.
DR OrthoDB; 179316at2759; -.
DR BRENDA; 3.2.1.23; 2235.
DR PRO; PR:O19015; -.
DR Proteomes; UP000011712; 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 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..24
FT /evidence="ECO:0000255"
FT PROPEP 25..29
FT /evidence="ECO:0000250"
FT /id="PRO_0000012183"
FT CHAIN 30..669
FT /note="Beta-galactosidase"
FT /id="PRO_0000012184"
FT REGION 649..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 189
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT ACT_SITE 269
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 196..231
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT DISULFID 628..636
FT /evidence="ECO:0000250|UniProtKB:P16278"
FT CONFLICT 483
FT /note="R -> P (in Ref. 2; AAB86405)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 75230 MW; 35B84933BB5E2F76 CRC64;
MDFPGAARLL SLLLVPLLLG PARGLRNASQ RTFKIDYGHN RFLKDGQPFR YISGSIHYFR
VPRFYWKDRL LKMKMAGLNA IQTYVPWNFH EPQPGQYQFS GEHDVEYFLK LAHELGLLVI
LRPGPYICAE WDMGGLPAWL LLKESIILRS SDPDYLAAVD KWLGVLLPKM KPLLYQNGGP
IITVQVENEY GSYFTCDYDY LRFLQRRFRD HLGGDVLLFT TDGAHEKFLQ CGALQGIYAT
VDFGPDANIT AAFQIQRKSE PRGPLVNSEF YTGWLDHWGQ PHSRVRTEVV ASSLHDVLAH
GANVNLYMFI GGTNFAYWNG ANIPYQPQPT SYDYDAPLSE AGDLTDKYFA LRDVIRKFEK
VPEGFIPPST PKFAYGKVAL QKLKTVEDAL NVLCPAGPIK SLYPLTFIQV KQYFGFVLYR
TTLPQDCSNP TPLSSPLNGV RDRAYVAVDG VPQGVLERSY VITLNITGQA GATLDLLVEN
MGRVNYGRYI NDFKGLISNL TLGSSVLTDW MIFPLDTEDA VRSHLGGWHG RNHGRQDNKA
FAHHSSNYTL PAFYAGNFSI PSGIPDLPQD TFIQFSGWTK GQVWINGFNL GRYWPGRGPQ
VTLFVPRHIL VTSAPNTIMV LELERAPCDD NGPELCTVEF VDRPLISATP TSSHPLPDLS
DRDSGWDRV
