ID BGAL1_KLEP7 Reviewed; 1035 AA. AC A6T8X0; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=Beta-galactosidase 1 {ECO:0000255|HAMAP-Rule:MF_01687}; DE Short=Beta-gal 1 {ECO:0000255|HAMAP-Rule:MF_01687}; DE EC=3.2.1.23 {ECO:0000255|HAMAP-Rule:MF_01687}; DE AltName: Full=Lactase 1 {ECO:0000255|HAMAP-Rule:MF_01687}; GN Name=lacZ1 {ECO:0000255|HAMAP-Rule:MF_01687}; GN OrderedLocusNames=KPN78578_15800; ORFNames=KPN_01610; OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella. OX NCBI_TaxID=272620; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700721 / MGH 78578; RG The Klebsiella pneumonia Genome Sequencing Project; RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.; RL Submitted (SEP-2006) 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; 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; CP000647; ABR77041.1; -; Genomic_DNA. DR RefSeq; WP_015958381.1; NC_009648.1. DR AlphaFoldDB; A6T8X0; -. DR SMR; A6T8X0; -. DR STRING; 272620.KPN_01610; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR PaxDb; 272620-KPN_01610; -. DR EnsemblBacteria; ABR77041; ABR77041; KPN_01610. DR KEGG; kpn:KPN_01610; -. DR HOGENOM; CLU_002346_0_2_6; -. DR Proteomes; UP000000265; 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..1035 FT /note="Beta-galactosidase 1" FT /id="PRO_0000367001" FT ACT_SITE 469 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 545 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 109 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 208 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 424 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 426 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 469 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 469 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 545..548 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 605 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 609 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 612 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 612 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 1011 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 365 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 399 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1035 AA; 117758 MW; C18A68CF81E14A6A CRC64; MQISDTGRSH TPDFHAVLAR EDWQNQTITH LNRLPAHPVF ASWRDELAAR DNLPSSRRRQ LDGEWQFSYA RSPFAVDAQW LTQDLPDCRG TPVPSNWQME GYDAPIYTNV RYPIDTTPPR VPEDNPTGCY SLHFTVEDTW RENGQTQIIF DGVNSAFHLW CNGVWVGYSQ DSRLPAAFDL SPFLRPGDNR LCVMVMRWSA GSWLEDQDMW RMSGIFRSVW LLNKPQQRLC DVQLTPALDA LYRDGTLQVQ ATIEATEAAL AGLSVGVSLW RGEEQIAAGR QPLGTPTVDE RGHYAERVDF SLAVATPAHW SAETPNCYRA VVTLWRGDEL LEAEAWDIGF RRIEIADGLL RLNGKPLLIR GVNRHEHHHL RGQVVTEADM VQDILLMKQN NFNAVRCSHY PNAPRWYELC NRYGLYVVDE ANIETHGMVP MNRLSDDPAW LPAFSARVTR MVQSNRNHPC IIIWSLGNES GGGGNHEALY HWLKRNDPSR PVQYEGGGAD TTATDIICPM YARVERDQPI PAVPKWGIKK WISLPGEQRP LILCEYAHAM GNSLGNFADY WQAFREYPRL QGGFIWDWAD QAIRKTFADG SVGWAYGGDF GDKPNDRQFC MNGLVFPDRT PHPSLVEAKH AQQYFQFTLL STSPLRVRII SEYLFRPTDN EVLRWQVQAA GEPLYHGDLT LALPPEGSDE ITLLDSLILP EGARAVWLTL EVTQPQATAW SEAEHRVAWQ QFPLPAPLAL PAPTVSAGAP DLIVSDEVWQ IRAGSQCWTI DRRTGLLSRW SVGGQEQLLT PLRDQFIRAP LDNDIGVSEV ERIDPNAWVE RWRSAGLYDL EAHCVQCDAQ RLANETLVDC RWHYLRGEEV VIVSHWRMHF TADGTLRLAV DGERAETLPP LPRVGLHFQV ADQQAPVSWL GLGPHENYPD RRSSACFARW EQPLAAMTTP YIFPTENGLR CDTQALDWGR WHISGHFHFS VQPWSTRQLM ETDHWHKMQA EDGVWITLDG LHMGVGGDDS WTPSVLPQWL LSQTRWHYEV SLRCL //