ID BGAL_CROS8 Reviewed; 1043 AA. AC A7MN76; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 93. 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=ESA_02977; OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Cronobacter. OX NCBI_TaxID=290339; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-894; RX PubMed=20221447; DOI=10.1371/journal.pone.0009556; RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L., RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A., RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K., RA McClelland M., Forsythe S.J.; RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic RT hybridization analysis with other Cronobacter species."; RL PLoS ONE 5:E9556-E9556(2010). 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; CP000783; ABU78206.1; -; Genomic_DNA. DR RefSeq; WP_012125561.1; NC_009778.1. DR AlphaFoldDB; A7MN76; -. DR SMR; A7MN76; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; esa:ESA_02977; -. DR PATRIC; fig|290339.8.peg.2666; -. DR HOGENOM; CLU_002346_0_2_6; -. DR Proteomes; UP000000260; 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; 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; PS00608; GLYCOSYL_HYDROL_F2_2; 1. PE 3: Inferred from homology; KW Glycosidase; Hydrolase; Magnesium; Metal-binding; Reference proteome; KW Sodium. FT CHAIN 1..1043 FT /note="Beta-galactosidase" FT /id="PRO_0000366984" FT REGION 33..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 471 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 547 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 113 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 212 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 212 FT /ligand="substrate" 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 428 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 471 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 471 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 547..550 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 607 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" 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 614 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 614 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 1017 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 367 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 401 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1043 AA; 117662 MW; 269BB0FA74F2772F CRC64; MTENPTTTAF NELQTRPLAT ILARNDWQNP AITSVNRLPS HTPLHGWRDA DRARRGEPSD AVLSLDGEWQ FSFFASPHQV PEVWLAADLS DARATPVPSN WQMEGYDTPI YTNVRYPIPV NPPFVPDDNP TGCYSRDIEV PQAWLETGRT RIIFGGVNSA FYLWCNGQWV GYSQDSRLPA EFDLTGVLHA GRNRLCVLVL RWSDGTYLED QDMWRMSGIF RPVSLLHLPE QALADVRVHT ELAPSLRHAT LFSEVEVTPA ACGLSVTLAL WHGENEIASQ TLPLGSAPID ERGNYAERVT LSLDVDNPLL WSAETPHLYR AVVTLLDADG MPLVSEAHDV GFRRVEINNG LLTLNGQPLL IRGVNRHEHH PEKGQAVDEA AMVQDILLMK QNNFNAVRCS HYPNQPRWYE LCSRYGLYVV DEANIETHGM EPMSRLSDDP VWLGAYSERV TRMVKCNRNH PSIIIWSLGN ESGNGATHTA LYNWIKHQDP TRPVQYEGGG ADTRATDIIC PMYARVETDQ LIPAVPKWSI KKWISMPGET RPLILCEYAH AMGNSLGNFA DYWAAFRQYP RLQGGFIWDW ADQAITRVEP DGSRWWAYGG DFGDTPNDRQ FCMNGLVFPD RTPHPALFEA KHQQQFFQFR LVSENPLQIE VTSEYLFRES DNERLLWSIE VRGETRLSGE LTLELGPQAS RVLTLSDTGF SARAGDEEIW LHVRVEQPQA TPWSPEGHLS AWAQWPLAAP LALPEPVAAG DAPQLEITDA EFVIRHGCQT WRVSRASGQL IQWSDDGVDQ ILTPLADQFI RAPIDNDIGV SEVERIDPNA WVERWKAAGL YNTEHRCLAC DAQTTRDGVE IVAQHAYFVK GVADGPAILS RWRMVVDNQG ALHCDIDIAR SAALPPLPRV GVVCQLRGGE ETASWLGLGP HENYPDRLSS ACFSRWTLPL SELTTPYIFP GENGLRCNTR ELNWNGWQAE GEFHFSLSPY GTRQLMETSH WHKLQPEAGI WLTIDGFHMG VGGDDSWTPS VHPEYLLTAR EYRYRFTLRR RQG //