ID BGAL1_KLEPN Reviewed; 1034 AA. AC P06219; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-SEP-2026, entry version 116. 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}; OS Klebsiella pneumoniae. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Klebsiella; OC Klebsiella pneumoniae complex. OX NCBI_TaxID=573; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3897196; DOI=10.1128/jb.163.3.850-857.1985; RA Buvinger W.E., Riley M.; RT "Nucleotide sequence of Klebsiella pneumoniae lac genes."; RL J. Bacteriol. 163:850-857(1985). 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. 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; M11441; AAA25082.1; -; Genomic_DNA. DR PIR; A24925; A24925. DR AlphaFoldDB; P06219; -. DR SMR; P06219; -. 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:0005990; P:lactose catabolic process; IEA:TreeGrafter. DR FunFam; 3.20.20.80:FF:000018; Beta-galactosidase; 1. 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; IPR050347; Bact_Beta-galactosidase. 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; IPR017853; GH_hydrolase_sf. 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; IPR006104; Glyco_hydro_2_N. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR006102; Ig-like_GH2. DR InterPro; IPR032312; LacZ_4. DR NCBIfam; NF007074; PRK09525.1; 1. 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..1034 FT /note="Beta-galactosidase" FT /id="PRO_0000057662" FT ACT_SITE 468 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 544 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 108 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 207 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 207 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 423 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 425 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 468 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 468 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 544..547 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 604 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 608 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 611 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 611 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 1010 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 364 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 398 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1034 AA; 117517 MW; 8F8B9DC7521EF649 CRC64; MQISDTGRSH TPDFHAVLAR EDWHNQTITH LNRLPAHPVF ASWRDELAAR DNLPSSRRRQ LDGSGSSLTP AARLPSMRVV TQDLPDCRGT PVPSNWQMEG YDAPIYTNVR YPIDTTPPRV PEDNPTGCYS LHFTVEDTWR ENGQTQIIFD GVNSAFHLWC NGVWVGYSQD SRLPAAFDLS PFLRPGDNRL CVMVMRWSAG SWLEDQDMWR MSGIFRSVWL LNKPQQRLCD VQLTPALDAL YRDGTLQVQA TIEATEAALA GLSVGVSLWR GEEQFAAGRQ PLGTPTVDER GHYAERVDFS LAVATPAHWS AETPNCYRAV VTLWRGDELL EAEAWDIGFR RIEIADGLLR LNGKPLLIRG VNRHEHHHLR GQVVTEADMV QDILLMKQNN FNAVRCSHYP NAPRWYELCN RYGLYVVDEA NIETHGMVPM NRLSDDPAWL PAFSARVTRM VQSNRNHPCI IIWSLGNESG GGGNHEALYH WLKRNDPSRP VQYEGGGADT TATDIICPMY ARVERDQPIP AVPKWGIKKW ISLPGEQRPL ILCEYAHAMG NSLGNFADYW QAFREYPRLQ GGFIWDWADQ AIRKTFADGS VGWAYGGDFG DKPNDRQFCM NGLVFPDRTP HPSLVEAKHA QQYFQFTLLS TSPLRVRIIS EYLFRPTDNE VVRWQVQAAG EPLYHGDLTL ALPPEGSDEI TLLDSLILPE GARAVWLTLE VTQPQATAWS EAEHRVAWQQ FPLPAPLGCR RPPCLPALPD LIVSDEVWQI RAGSQCWTID RRTGLLSRWS VGGQEQLLTP LRDQFIRAPL DNDIGVSEVE RIDPNAWVER WRSAGLYDLE AHCVQCDAQR LANETLVDCR WHYLRGEEVV IVSHWRMHFT ADGTLRLAVD GERAETLPPL PRVGLHFQVA DQQAPVSWLG LGPHENYPDR RSSACFARWE QPLAAMTTPY IFPTENGLRC DTQALDWGRW HISGHFHFSV QPWSTRQLME TDHWHKMQAE DGVWITLDGL HMGVGGDDSW TPSVLPQWLL SQTRWQYEVS LRSL //