ID   BGAL_PONAB              Reviewed;         677 AA.
AC   Q5R7P4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 81.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860068; CAH92216.1; -; mRNA.
DR   RefSeq; NP_001126295.1; NM_001132823.1.
DR   AlphaFoldDB; Q5R7P4; -.
DR   SMR; Q5R7P4; -.
DR   STRING; 9601.ENSPPYP00000015702; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; Q5R7P4; 6 sites, No reported glycans.
DR   GeneID; 100173272; -.
DR   KEGG; pon:100173272; -.
DR   CTD; 2720; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   InParanoid; Q5R7P4; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000001595; 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   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..23
FT                   /evidence="ECO:0000250"
FT   PROPEP          24..28
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000283037"
FT   CHAIN           29..677
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000283038"
FT   REGION          654..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   677 AA;  75932 MW;  F918E217E84BC7B5 CRC64;
     MPGFLVRILP LLLALLLLGP TRGLRNATQR MFEIDYSRDC FLKDGQPFRY ISGSIHYSRV
     PRFYWKDRLL KMKMAGLNAI QTYVPWNFHE PWPGQYQFSE DHDVEYFLQL AHELGLLVIL
     RPGPYICAEW EMGGLPAWLL EKESILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPV
     ITVQVENEYG SYFACDFDYL RFLQKCFRHH LGDDVVLFTT DGAHKTFLKC GALQGLYTTV
     DFGTGSNITD AFLSQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEAVA SSLYDILARG
     ASVNLYMFIG GTNFAYWNGA NTPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNIIQKFEKV
     PEGPIPPSTP KFAYGKVALE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QHYGFVLYRT
     TLPQDCSNPA PLSSPFNGVH DRAYVAVDGI PQGVLERNNV ITLNITGKAG ATLDLLVENM
     GRVNYGAYIN DFKGLVSNLT LSSNILTDWT IFPLDTEDAV RSHLGGWGHR DSGHHDEAWA
     HSSSNYTLPA FYVGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT
     LFVPQHILMT SAPNTITMLE LERAPCSNDD PELCAVTFVD RPVIGSSVTY DHPSKPVEKK
     LMPSPPQKNK DSWLDHV
//