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Database: UniProt
Entry: A0A3B4BLL7_9GOBI
LinkDB: A0A3B4BLL7_9GOBI
Original site: A0A3B4BLL7_9GOBI 
ID   A0A3B4BLL7_9GOBI        Unreviewed;       553 AA.
AC   A0A3B4BLL7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Beta-galactosidase {ECO:0000256|ARBA:ARBA00013303};
DE            EC=3.2.1.23 {ECO:0000256|ARBA:ARBA00012756};
DE   AltName: Full=Acid beta-galactosidase {ECO:0000256|ARBA:ARBA00031635};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000029412.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000029412.1}
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809}.
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DR   AlphaFoldDB; A0A3B4BLL7; -.
DR   STRING; 409849.ENSPMGP00000029412; -.
DR   Ensembl; ENSPMGT00000031302.1; ENSPMGP00000029412.1; ENSPMGG00000023663.1.
DR   Proteomes; UP000261520; Unplaced.
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; 3.
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; 2.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..553
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017395853"
FT   DOMAIN          35..343
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          358..431
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          472..504
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        181
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        256
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   553 AA;  61485 MW;  C4434C2A679E26C3 CRC64;
     ALRSLSARRF KFSSLLFLLS FSPRTFSVDY QKNCFQKDGQ PFRYISGSIH YNRIPRVYWK
     DRLLKMYMAG LNAIQTYIPW NYHEESPGQY NFSGDRDLMY FLKLAQDIGL LVILRPGPYI
     CGEWEMGGLP AWLLNKKDIV LRSSDKGEGA VDRWMGKLLP MIKPYLYENG GPIITVQVEN
     EYGSYFACDF DYLRHLTGLF REHLGQTVVL FTTDGGSVGF LKCGSIQGLY ATVDFGPGKF
     VFRLVNQYLG VFVNSEFYTG WLDHWGSHHS VVSTDAVTKT LTEMLQIGAN VNLYMFIGGT
     NFGYWNGANE PYSAQPTSYD YDAPLTEAGD LTKKYFAIQN FHKIPDGIIP PTTPKFAYGS
     ITLQKVPAGI LERFQTITIN ITGKAGSRVD ILVENMGRIN YGKGINDFKG LVSNMTLGAD
     VLTGWTMYSL NIDEAVSQGV LGKSVSSDPP QPSTLSLPTF YGGSFVIPDG IPGQIWINGF
     NLGRYWPARG PQVTLFVPSS ILSTAAPNNI TVLELEAAPC SSGPCSVEFT DTPILGVTLH
     SKPISRLFSK DLL
//
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