ID   A0A2K6CMU5_MACNE        Unreviewed;       611 AA.
AC   A0A2K6CMU5;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303, ECO:0000256|RuleBase:RU000675};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756, ECO:0000256|RuleBase:RU000675};
GN   Name=GLB1 {ECO:0000313|Ensembl:ENSMNEP00000024968.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000024968.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000024968.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
CC       gangliosides, glycoproteins, and glycosaminoglycans.
CC       {ECO:0000256|ARBA:ARBA00002691}.
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:0000256|RuleBase:RU000675};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   AlphaFoldDB; A0A2K6CMU5; -.
DR   Ensembl; ENSMNET00000049241.1; ENSMNEP00000024968.1; ENSMNEG00000035974.1.
DR   GeneTree; ENSGT00950000182942; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000035974; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000675};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT   DOMAIN          1..285
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          332..444
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          478..539
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        197
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   611 AA;  68380 MW;  06A8236EE4E236EA CRC64;
     MKMAGLNTIQ TYVPWNFHEP WPGQYQFSED HDVEYFLRLA HELGLLVILR PGPYICAEWE
     MGGLPAWLLE KEAILLRSSD PDYLAAVDKW LGVLLPKMKP LLYQNGGPII TVQVENEYGS
     YFACDFDYLR FLQKRFHHHL GDDVVLFTTD GAHETFLQCG ALQGLYTTVD FGPGSNITDA
     FQIQRKCEPK GPLINSEFYT GWLDHWGQPH STIKTEVVAS SLYDILARGA SVNLYMFIGG
     TNFAYWNGAN SPYAAQPTSY DYDAPLSEAG DLTEKYFALR NVIQKFEKVP EGPIPPSTPK
     FAYGKVSLEK LKTVGAALDI LCPSGPIKSL YPLTFIQVKQ YYGFVLYRTT LPQDCSNSTP
     LSSPFNGVHD RAYVAVDGIP QGVLERNRVI TLNITGKAGA TLDLLVENMG RVNYGAYIND
     FKGLVSNLTL DSNILTGWTI FPLDTEDAVR SHLGGWEHRD SGRHDEAWAH SSSNYTLPAF
     YVGNFSIPSG IPDLPQDTFI QFPGWTKGQV WINGFNLGRY WPARGPQLTL FVPQHILMTS
     APNTITVLEL ERAPCSSDGP ELCAVEFVDR PVIGSSQIYD HLSKPVEQRL MAPPPKKTKI
     RGWSMYDDES L
//