ID BGAL_ECOL5 Reviewed; 1024 AA. AC Q0TKT1; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 27-MAR-2024, entry version 101. DE RecName: Full=Beta-galactosidase {ECO:0000255|HAMAP-Rule:MF_01687}; DE Short=Beta-gal {ECO:0000255|HAMAP-Rule:MF_01687}; DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687}; DE AltName: Full=Lactase {ECO:0000255|HAMAP-Rule:MF_01687}; GN Name=lacZ {ECO:0000255|HAMAP-Rule:MF_01687}; GN OrderedLocusNames=ECP_0417; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=536 / UPEC; RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues CC in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01687}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01687}; CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_01687}; CC -!- COFACTOR: CC Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01687}; CC Note=Binds 1 sodium ion per monomer. {ECO:0000255|HAMAP-Rule:MF_01687}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01687}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. CC {ECO:0000255|HAMAP-Rule:MF_01687}. 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; CP000247; ABG68450.1; -; Genomic_DNA. DR RefSeq; WP_000177876.1; NC_008253.1. DR AlphaFoldDB; Q0TKT1; -. DR SMR; Q0TKT1; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; ecp:ECP_0417; -. DR HOGENOM; CLU_002346_0_2_6; -. DR Proteomes; UP000009182; Chromosome. DR GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro. DR GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. DR HAMAP; MF_01687; Beta_gal; 1. DR InterPro; IPR004199; B-gal_small/dom_5. DR InterPro; IPR036156; Beta-gal/glucu_dom_sf. DR InterPro; IPR011013; Gal_mutarotase_sf_dom. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR014718; GH-type_carb-bd. DR InterPro; IPR006101; Glyco_hydro_2. DR InterPro; IPR023232; Glyco_hydro_2_AS. DR InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase. DR InterPro; IPR006103; Glyco_hydro_2_cat. DR InterPro; IPR023230; Glyco_hydro_2_CS. DR InterPro; IPR006102; Glyco_hydro_2_Ig-like. DR InterPro; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR032312; LacZ_4. DR PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1. DR Pfam; PF02929; Bgal_small_N; 1. DR Pfam; PF00703; Glyco_hydro_2; 1. DR Pfam; PF02836; Glyco_hydro_2_C; 1. DR Pfam; PF02837; Glyco_hydro_2_N; 1. DR Pfam; PF16353; LacZ_4; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SMART; SM01038; Bgal_small_N; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 1. DR PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1. DR PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Sodium. FT CHAIN 1..1024 FT /note="Beta-galactosidase" FT /id="PRO_0000366997" FT ACT_SITE 462 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 538 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 103 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 202 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 202 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 417 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 419 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 462 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 538..541 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 598 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 602 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 605 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 605 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 1000 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 358 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 392 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1024 AA; 116473 MW; 1596932C64CC1EB5 CRC64; MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR FAWFPAPEAV PESWLECDLP DADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPAENP TGCYSLTFNI DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFQVTT RFNDDFSRAV LEAEVQMYGE LRDELRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPE LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE MRPLILCEYA HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGRTIEVT SEYLFRHSDN EFLHWMVALD GKPLASGEVP LDVGPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ WRLAENLSVT LPSASHAIPQ LTTSGTDFCI ELGNKRWQFN RQSGFLSQMW IGDEKQLLTP LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA HAWQHQGKTL FISRKTYRID GHGEMVINVD VAVASDTPHP ARVGLTCQLA QVAERVNWLG LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGHYHYQLV WCQK //