GenomeNet

Database: UniProt
Entry: BGAL_FELCA
LinkDB: BGAL_FELCA
Original site: 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   16-JAN-2019, entry version 98.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae;
OC   Felinae; Felis.
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Varadarajan G.S., Smith B.F., Foureman P., Martin D.R.,
RA   Varadarajan U., 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
CC         residues 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.
CC       {ECO:0000305}.
DR   EMBL; AF006749; AAB81350.1; -; mRNA.
DR   EMBL; AF029974; AAB86405.1; -; mRNA.
DR   RefSeq; NP_001009860.1; NM_001009860.1.
DR   ProteinModelPortal; O19015; -.
DR   SMR; O19015; -.
DR   STRING; 9685.ENSFCAP00000019661; -.
DR   ChEMBL; CHEMBL2331052; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   PRIDE; O19015; -.
DR   GeneID; 493927; -.
DR   KEGG; fca:493927; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   eggNOG; COG1874; LUCA.
DR   HOVERGEN; HBG004841; -.
DR   InParanoid; O19015; -.
DR   KO; K12309; -.
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   Gene3D; 2.60.120.260; -; 2.
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   Complete proteome; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   PROPEP       25     29       {ECO:0000250}.
FT                                /FTId=PRO_0000012183.
FT   CHAIN        30    669       Beta-galactosidase.
FT                                /FTId=PRO_0000012184.
FT   ACT_SITE    189    189       Proton donor.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   ACT_SITE    269    269       Nucleophile.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING      84     84       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     130    130       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     188    188       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   BINDING     334    334       Substrate.
FT                                {ECO:0000250|UniProtKB:P16278}.
FT   CARBOHYD     27     27       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    465    465       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    499    499       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    547    547       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    557    557       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    196    231       {ECO:0000250|UniProtKB:P16278}.
FT   DISULFID    628    636       {ECO:0000250|UniProtKB:P16278}.
FT   CONFLICT    483    483       R -> P (in Ref. 2; AAB86405).
FT                                {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
//
DBGET integrated database retrieval system