ID   BGAL_MOUSE              Reviewed;         647 AA.
AC   P23780;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Beta-galactosidase;
DE            EC=3.2.1.23 {ECO:0000269|PubMed:2124109};
DE   AltName: Full=Acid beta-galactosidase;
DE            Short=Lactase;
DE   Flags: Precursor;
GN   Name=Glb1; Synonyms=Bgl, Glb-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CATALYTIC ACTIVITY.
RC   TISSUE=Brain;
RX   PubMed=2124109; DOI=10.1016/s0006-291x(05)81033-2;
RA   Nanba E., Suzuki K.;
RT   "Molecular cloning of mouse acid beta-galactosidase cDNA: sequence,
RT   expression of catalytic activity and comparison with the human enzyme.";
RL   Biochem. Biophys. Res. Commun. 173:141-148(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J;
RX   PubMed=1906271; DOI=10.1016/0006-291x(91)91793-c;
RA   Nanba E., Suzuki K.;
RT   "Organization of the mouse acid beta-galactosidase gene.";
RL   Biochem. Biophys. Res. Commun. 178:158-164(1991).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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:0000269|PubMed:2124109};
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; M57734; AAA37293.1; -; mRNA.
DR   EMBL; M75122; AAA37292.1; -; Genomic_DNA.
DR   EMBL; M75137; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75107; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75108; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75109; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75111; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75112; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75113; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75114; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75115; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75116; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75117; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75118; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75119; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75120; AAA37292.1; JOINED; Genomic_DNA.
DR   EMBL; M75121; AAA37292.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS23593.1; -.
DR   PIR; A37086; A37086.
DR   RefSeq; NP_033882.1; NM_009752.2.
DR   PDB; 7KDV; EM; 4.59 A; A/C/E/G/I/K=28-647.
DR   PDBsum; 7KDV; -.
DR   AlphaFoldDB; P23780; -.
DR   SMR; P23780; -.
DR   BioGRID; 198341; 13.
DR   STRING; 10090.ENSMUSP00000055803; -.
DR   BindingDB; P23780; -.
DR   ChEMBL; CHEMBL1667667; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   GlyCosmos; P23780; 8 sites, No reported glycans.
DR   GlyGen; P23780; 9 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P23780; -.
DR   PhosphoSitePlus; P23780; -.
DR   SwissPalm; P23780; -.
DR   EPD; P23780; -.
DR   jPOST; P23780; -.
DR   PaxDb; 10090-ENSMUSP00000055803; -.
DR   PeptideAtlas; P23780; -.
DR   ProteomicsDB; 273486; -.
DR   Pumba; P23780; -.
DR   Antibodypedia; 3647; 839 antibodies from 38 providers.
DR   DNASU; 12091; -.
DR   Ensembl; ENSMUST00000063042.11; ENSMUSP00000055803.10; ENSMUSG00000045594.11.
DR   GeneID; 12091; -.
DR   KEGG; mmu:12091; -.
DR   UCSC; uc009rxj.3; mouse.
DR   AGR; MGI:88151; -.
DR   CTD; 2720; -.
DR   MGI; MGI:88151; Glb1.
DR   VEuPathDB; HostDB:ENSMUSG00000045594; -.
DR   eggNOG; KOG0496; Eukaryota.
DR   GeneTree; ENSGT00950000182942; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   InParanoid; P23780; -.
DR   OMA; RAHPDTW; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; P23780; -.
DR   TreeFam; TF314816; -.
DR   Reactome; R-MMU-2022857; Keratan sulfate degradation.
DR   Reactome; R-MMU-2024096; HS-GAG degradation.
DR   Reactome; R-MMU-4085001; Sialic acid metabolism.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9840310; Glycosphingolipid catabolism.
DR   SABIO-RK; P23780; -.
DR   BioGRID-ORCS; 12091; 3 hits in 82 CRISPR screens.
DR   ChiTaRS; Glb1; mouse.
DR   PRO; PR:P23780; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P23780; Protein.
DR   Bgee; ENSMUSG00000045594; Expressed in right kidney and 254 other cell types or tissues.
DR   ExpressionAtlas; P23780; baseline and differential.
DR   Genevisible; P23780; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR   GO; GO:0004565; F:beta-galactosidase activity; IDA:MGI.
DR   GO; GO:0016936; F:galactoside binding; ISO:MGI.
DR   GO; GO:0016787; F:hydrolase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; ISO:MGI.
DR   GO; GO:0019388; P:galactose catabolic process; ISO:MGI.
DR   GO; GO:0051413; P:response to cortisone; IEA:Ensembl.
DR   GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
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   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW   Lysosome; Reference proteome; Signal; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..29
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000012190"
FT   CHAIN           30..647
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000012191"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   BINDING         334
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        248
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        500
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        510
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        617
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        196..231
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   DISULFID        628..636
FT                   /evidence="ECO:0000250|UniProtKB:P16278"
FT   CONFLICT        517
FT                   /note="N -> D (in Ref. 2; AAA37292)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        539
FT                   /note="G -> R (in Ref. 2; AAA37292)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   647 AA;  73121 MW;  0E68EAA66A10803A CRC64;
     MLRVPLCTPL PLLALLQLLG AAHGIYNVTQ RTFKLDYSRD RFLKDGQPFR YISGSIHYFR
     IPRFYWEDRL LKMKMAGLNA IQMYVPWNFH EPQPGQYEFS GDRDVEHFIQ LAHELGLLVI
     LRPGPYICAE WDMGGLPAWL LEKQSIVLRS SDPDYLVAVD KWLAVLLPKM KPLLYQNGGP
     IITVQVENEY GSYFACDYDY LRFLVHRFRY HLGNDVILFT TDGASEKMLK CGTLQDLYAT
     VDFGTGNNIT QAFLVQRKFE PKGPLINSEF YTGWLDHWGK PHSTVKTKTL ATSLYNLLAR
     GANVNLYMFI GGTNFAYWNG ANTPYEPQPT SYDYDAPLSE AGDLTKKYFA LREVIQMFKE
     VPEGPIPPST PKFAYGKVAL RKFKTVAEAL GILCPNGPVK SLYPLTFTQV KQYFGYVLYR
     TTLPQDCSNP KPIFSSPFNG VRDRAYVSVD GVPQGILDRN LMTALNIRGK AGATLDILVE
     NMGRVNYGRF INDFKGLISN MTINSTVLTN WTVFPLNTEA MVRNHLWGRE ASDEGHLDGR
     STSNSSDLIL PTFYVGNFSI PSGIPDLPQD TFIQFPGWSK GQVWINGFNL GRYWPTMGPQ
     KTLFVPRNIL TTSAPNNITV LELEFAPCSE GTPELCTVEF VDTPVIS
//

ID   Q3TAW7_MOUSE            Unreviewed;       647 AA.
AC   Q3TAW7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   24-JAN-2024, entry version 141.
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|MGI:MGI:88151};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE42549.1};
RN   [1] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [6] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8] {ECO:0000313|EMBL:BAE42549.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE42549.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [9] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   EMBL; AK171593; BAE42549.1; -; mRNA.
DR   RefSeq; NP_033882.1; NM_009752.2.
DR   AlphaFoldDB; Q3TAW7; -.
DR   SMR; Q3TAW7; -.
DR   CAZy; GH35; Glycoside Hydrolase Family 35.
DR   EPD; Q3TAW7; -.
DR   MaxQB; Q3TAW7; -.
DR   Antibodypedia; 3647; 839 antibodies from 38 providers.
DR   DNASU; 12091; -.
DR   GeneID; 12091; -.
DR   KEGG; mmu:12091; -.
DR   AGR; MGI:88151; -.
DR   CTD; 2720; -.
DR   MGI; MGI:88151; Glb1.
DR   VEuPathDB; HostDB:ENSMUSG00000045594; -.
DR   HOGENOM; CLU_007853_7_2_1; -.
DR   OMA; RAHPDTW; -.
DR   OrthoDB; 5489808at2759; -.
DR   PhylomeDB; Q3TAW7; -.
DR   BioGRID-ORCS; 12091; 3 hits in 82 CRISPR screens.
DR   ChiTaRS; Glb1; mouse.
DR   ExpressionAtlas; Q3TAW7; baseline and differential.
DR   Genevisible; Q3TAW7; MM.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016936; F:galactoside binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0019388; P:galactose catabolic process; IEA:Ensembl.
DR   GO; GO:0051413; P:response to cortisone; IEA:Ensembl.
DR   GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
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   1: Evidence at protein level;
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..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..647
FT                   /note="Beta-galactosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009970779"
FT   DOMAIN          42..357
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   DOMAIN          404..517
FT                   /note="Beta-galactosidase 1-like first all-beta"
FT                   /evidence="ECO:0000259|Pfam:PF21317"
FT   DOMAIN          551..612
FT                   /note="Beta-galactosidase galactose-binding"
FT                   /evidence="ECO:0000259|Pfam:PF21467"
FT   ACT_SITE        189
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
FT   ACT_SITE        269
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006336-1"
SQ   SEQUENCE   647 AA;  73121 MW;  0E68EAA66A10803A CRC64;
     MLRVPLCTPL PLLALLQLLG AAHGIYNVTQ RTFKLDYSRD RFLKDGQPFR YISGSIHYFR
     IPRFYWEDRL LKMKMAGLNA IQMYVPWNFH EPQPGQYEFS GDRDVEHFIQ LAHELGLLVI
     LRPGPYICAE WDMGGLPAWL LEKQSIVLRS SDPDYLVAVD KWLAVLLPKM KPLLYQNGGP
     IITVQVENEY GSYFACDYDY LRFLVHRFRY HLGNDVILFT TDGASEKMLK CGTLQDLYAT
     VDFGTGNNIT QAFLVQRKFE PKGPLINSEF YTGWLDHWGK PHSTVKTKTL ATSLYNLLAR
     GANVNLYMFI GGTNFAYWNG ANTPYEPQPT SYDYDAPLSE AGDLTKKYFA LREVIQMFKE
     VPEGPIPPST PKFAYGKVAL RKFKTVAEAL GILCPNGPVK SLYPLTFTQV KQYFGYVLYR
     TTLPQDCSNP KPIFSSPFNG VRDRAYVSVD GVPQGILDRN LMTALNIRGK AGATLDILVE
     NMGRVNYGRF INDFKGLISN MTINSTVLTN WTVFPLNTEA MVRNHLWGRE ASDEGHLDGR
     STSNSSDLIL PTFYVGNFSI PSGIPDLPQD TFIQFPGWSK GQVWINGFNL GRYWPTMGPQ
     KTLFVPRNIL TTSAPNNITV LELEFAPCSE GTPELCTVEF VDTPVIS
//