ID   A0A3B4C0W3_PYGNA        Unreviewed;       653 AA.
AC   A0A3B4C0W3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000004466.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000004466.1}
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   RefSeq; XP_017539285.1; XM_017683796.1.
DR   AlphaFoldDB; A0A3B4C0W3; -.
DR   Ensembl; ENSPNAT00000006970.1; ENSPNAP00000004466.1; ENSPNAG00000010957.1.
DR   GeneID; 108411970; -.
DR   CTD; 2720; -.
DR   GeneTree; ENSGT00950000182942; -.
DR   OMA; RAHPDTW; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000261440; 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; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..653
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017428279"
FT   DOMAIN          36..351
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          398..509
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          540..601
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        183
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        263
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   653 AA;  72898 MW;  E42EDBEDBAD6BFA4 CRC64;
     MGFPRAAAGL LFLAVIPVSL ATSSSNFTVD YKNNCFLKDG QPFRYISGSI HYSRIPQVYW
     KDRLLKMYMA GLNAIQTYIP WNFHEPIPGR YDFSGDRNLT HFLQLCKDLD LLVILRPGPY
     ICGEWDMGGL PSWLLKKKDI VLRSSDADYI AAVDRWMGKL LPMIKPYLYQ NGGPIITVQV
     ENEYGSYFAC DFDYLRHLVK LFRSHLGEEV VLFSTDGAGV GYLKCGSLQG VYATVDFGPG
     GNVTAAFEAQ RHAEPHGPLV NSEFYTGWLD HWGSPHSVTS TAVLVKSLNE ILEIDANVNL
     YMFIGGTNFE YWNGANTPYA PQPTSYDYDA PLTEAGDLTE KYFAIRDVIK KYRKIPEGAV
     PPSTPKFAYG QVTMKKLQTV SESLDILSFS GPVKSPYPLT FEDLNQAFGF MLYQITLPVD
     CPKPTPLSSP LNGVHDRAYV TIDGVAAGVL ERDKTISINI TGKIGSRLDI LVENMGRVNY
     GKDINDFKGL VSNLTLGADT LSNWTVYSLS IDEAVKKGLF WKNSSPRTPD NAPTTTLSPP
     AFYAGSFNIP DDIPDLPQDT YIQFPDWRKG QVWINGFNLG RYWPSRGPQI TLFVPEYLLS
     TRAPNNITVL ELEASPCSPG PCVVEFISTP IINATTRYTK PFMREPFSKQ DLL
//