ID A0A7U6I4Q7_9ENTE Unreviewed; 686 AA. AC A0A7U6I4Q7; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 5. DE RecName: Full=Beta-galactosidase {ECO:0000256|PIRNR:PIRNR001084}; DE Short=Beta-gal {ECO:0000256|PIRNR:PIRNR001084}; DE EC=3.2.1.23 {ECO:0000256|PIRNR:PIRNR001084}; GN ORFNames=EGX73_00705 {ECO:0000313|EMBL:AYY08480.1}; OS Enterococcus sp. FDAARGOS_553. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=2420313 {ECO:0000313|EMBL:AYY08480.1, ECO:0000313|Proteomes:UP000271079}; RN [1] {ECO:0000313|Proteomes:UP000271079} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=FDAARGOS_553 {ECO:0000313|Proteomes:UP000271079}; RA Plongla R., Gilligan P., Tallon L., Sadzewicz L., Zhao X., Vavikolanu K., RA Mehta A., Aluvathingal J., Nadendla S., Geyer C., Nandy P., Yan Y., RA Sichtig H.; RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): RT Supporting development and validation of Infectious Disease Dx tests."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00001412, CC ECO:0000256|PIRNR:PIRNR001084}; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. CC {ECO:0000256|ARBA:ARBA00005940, ECO:0000256|PIRNR:PIRNR001084}. 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 EMBL; CP033740; AYY08480.1; -; Genomic_DNA. DR RefSeq; WP_005470856.1; NZ_CP033740.1. DR AlphaFoldDB; A0A7U6I4Q7; -. DR Proteomes; UP000271079; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006012; P:galactose metabolic process; IEA:InterPro. DR Gene3D; 2.60.40.1180; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR013739; Beta_galactosidase_C. DR InterPro; IPR013738; Beta_galactosidase_Trimer. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR003476; Glyco_hydro_42. DR InterPro; IPR013529; Glyco_hydro_42_N. DR InterPro; IPR013780; Glyco_hydro_b. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR PANTHER; PTHR36447; BETA-GALACTOSIDASE GANA; 1. DR Pfam; PF02449; Glyco_hydro_42; 1. DR Pfam; PF08533; Glyco_hydro_42C; 1. DR Pfam; PF08532; Glyco_hydro_42M; 1. DR PIRSF; PIRSF001084; B-galactosidase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1. PE 3: Inferred from homology; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|PIRNR:PIRNR001084}; KW Hydrolase {ECO:0000256|PIRNR:PIRNR001084}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR001084-3}; KW Zinc {ECO:0000256|PIRSR:PIRSR001084-3}. FT DOMAIN 15..398 FT /note="Glyco_hydro_42" FT /evidence="ECO:0000259|Pfam:PF02449" FT DOMAIN 409..613 FT /note="Glyco_hydro_42M" FT /evidence="ECO:0000259|Pfam:PF08532" FT DOMAIN 625..679 FT /note="Glyco_hydro_42C" FT /evidence="ECO:0000259|Pfam:PF08533" FT ACT_SITE 153 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1" FT ACT_SITE 319 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-1" FT BINDING 114 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2" FT BINDING 118 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2" FT BINDING 158 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3" FT BINDING 160 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3" FT BINDING 163 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-3" FT BINDING 327 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR001084-2" SQ SEQUENCE 686 AA; 79792 MW; 0536FFAABD19C4AA CRC64; MTNYFFDQRF LHGGDYNPDQ WLDYPEILKK DLAYMQKAHV NTVTLGVFAW SALEPTEGVY QFDWLDEQFD AIHAMGGNVI LATPSGGRPQ WLSQKYPEVN RTNAYGQKHT HGFRHNHCYS SPIYREKVRQ INTKLAERYG DHPALAMWHM SNEYSGECFC EYCQENWRDW LKKKYKNLEA LNHAWWMSFW GNRYSDWEQV LPPSPLGEHK VHGMDLDWKR FVTDQTIDFY LNEIVPIRER TPDIPVTTNF MAEGHATQDF IPLEGIDYGK FSQYVDVVSW DSYPDWNNRF EAIATTAMKS AYVHDQYWSL KKQPFLVMEC TPSYVNWHQY DKSKRPGVHI LSSMQQLAHG SDSTLYFQWR QSRGNSEKFH GAVVSHDDST NNRVFKEVAE YGARLEKISE IKGTTRKKEV AILFDWESNW ALKRGGGFGR PTRRYPQTLQ EHYQVFWEQD IPVDILTPEQ DFSDYQLVIA PMLYMMTEKT MLKLTSYVEK GGILVSSYFT GMVNETDLLY IGGLPQPLKA LFGIEVLELE TLLEDEHNQI DFQDQRFVTK DYSAIIDVLD AEVLSHYQTD FYQGTPAVTK KPFGAGASYY LAARTNSDFL AAFYQKLIEK LGLRRTAIAE ALPEVSIQTR VGTQRDYSFI MNFSEEEQQL VLKQPVTDLE TNEHLVGAIT LAPYEVRIVY HPSEVH //