ID   A0A3B4YVX3_9TELE        Unreviewed;       650 AA.
AC   A0A3B4YVX3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
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|RefSeq:XP_008285146.1};
OS   Stegastes partitus (bicolor damselfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Stegastes.
OX   NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000000400.1, ECO:0000313|Proteomes:UP000261400};
RN   [1] {ECO:0000313|Ensembl:ENSSPAP00000000400.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_008285146.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_008285146.1; XM_008286924.1.
DR   AlphaFoldDB; A0A3B4YVX3; -.
DR   STRING; 144197.ENSSPAP00000000400; -.
DR   Ensembl; ENSSPAT00000000408.1; ENSSPAP00000000400.1; ENSSPAG00000000283.1.
DR   GeneID; 103360970; -.
DR   CTD; 2720; -.
DR   GeneTree; ENSGT00950000182942; -.
DR   OrthoDB; 5489808at2759; -.
DR   Proteomes; UP000261400; Unplaced.
DR   Proteomes; UP000694891; 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   Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..650
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041073988"
FT   DOMAIN          34..349
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          396..507
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          537..598
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        261
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   650 AA;  72090 MW;  F03447688BAD7C89 CRC64;
     MSPLRTGCMM LLLLVGQSLG ASPSFSLDYK NDCFRKDGER FRYISGSIHY SRIPRVYWKD
     RLLKMYMAGL NAIQTYIPWN YHEESPGRYN FSGDRDVEYF LKLAQEIGLL VILRPGPYIC
     GEWDMGGLPA WLLSKKNIVL RSSDPDYITA VDKWMGKLLP MMKPYLYQNG GPIITVQVEN
     EYGSYFACDY NYMRHLSKLF RSHLGDEVVL FTTDGAGVGY LKCGAIQGLY ATVDFGPGAN
     ITAAFDAQRH AEPHGPLVNS EFYTGWLDHW GSAHSVVSPA AVAKSLSEML ARGANVNLYM
     FIGGTNFGYW NGANDPFDAQ PTSYDYDAPL SEAGDLTEKY FAIRDVIKMY HKIPEGPIPP
     TTPKYAYGVV PMKKLQTLSD ALEKLSFSGP VKGVYPQTFI DLNQAFGYVL YRTTLPVNCT
     TPTPLSSPLN GVHDRAYVSV DGVAVGILER NKVITINVTG KAGSQVDILV ENMGRLNYGG
     YINDAKGLLS NLTLGKDTLT DWIMYSLSID EAVNQGLLGE KELTPKRPTQ GAGLSPPAFY
     GGSFIIPDGI PSLPQDTYIM LPNWRKGQIW INGFNLGRYW PTRGPQVTLF VPFNILSTTA
     PNNVTILELE GAPCSLKPCT VEFSSTPILN ATGQSDHKLH WGHYTKEDLL
//