ID   BGAL_MACFA              Reviewed;         682 AA.
AC   Q60HF6; Q4R564;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 75.
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; ORFNames=QccE-15801, QccE-17236;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.;
RT   "Isolation and characterization of cDNA for macaque neurological disease
RT   genes.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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; AB125171; BAD51959.1; -; mRNA.
DR   EMBL; AB169680; BAE01761.1; -; mRNA.
DR   RefSeq; NP_001306360.1; NM_001319431.1.
DR   AlphaFoldDB; Q60HF6; -.
DR   SMR; Q60HF6; -.
DR   STRING; 9541.XP_005545588.1; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GeneID; 102119163; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   Proteomes; UP000233100; 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..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012188"
FT   CHAIN           29..682
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012189"
FT   ACT_SITE        188
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   ACT_SITE        268
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         187
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         333
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        464
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        498
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        555
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        195..230
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   DISULFID        626..634
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
SQ   SEQUENCE   682 AA;  76826 MW;  FDF97A8B8DC8B680 CRC64;
     MPGFLVRILP LLLPLLLLGP TRGLRNATRR VFEIAYSQDR FLKDGQPFRY ISGSIHYSRV
     PRFYWKDRLL KMKMAGLNTI QTYVPWNFHE PWPGQYQFSE DHDVEYFLRL AHELGLLVIL
     RPGPYICAEW EMGGLPAWLL EKEAILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPI
     ITVQVENEYG SYFACDFDYL RFLQKRFHHH LGDDVVLFTT DGAHETFLQC GALQGLYTTV
     DFGPGSNITD AFQIQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEVVA SSLYDILARG
     ASVNLYMFIG GTNFAYWNGA NSPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNVIQKFEKV
     PEGPIPPSTP KFAYGKVSLE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QYYGFVLYRT
     TLPQDCSNST PLSSPFNGVH DRAYVAVDGI PQGVLERNRV ITLNITGKTG ATLDLLVENM
     GRVNYGAYIN DFKGLVSNLT LDSNILTGWT IFPLDTEDAV RSHLGGWEHR DSGRHDEAWA
     HSSSNYTLPA FYVGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT
     LFVPQHILMT SAPNTITVLE LERAPCSSDG PELCAVEFVD RPVIGSSQIY DHLSKPVEQR
     LMAPPPKKTK IRGWSMYDDE SL