ID BGAL_PECAS Reviewed; 1040 AA. AC Q6D736; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 107. 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=ECA1490; OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia OS carotovora subsp. atroseptica). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=218491; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SCRI 1043 / ATCC BAA-672; RX PubMed=15263089; DOI=10.1073/pnas.0402424101; RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J., RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K., RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J., RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H., RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S., RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.; RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora RT subsp. atroseptica and characterization of virulence factors."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004). 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; BX950851; CAG74399.1; -; Genomic_DNA. DR RefSeq; WP_011093073.1; NC_004547.2. DR AlphaFoldDB; Q6D736; -. DR SMR; Q6D736; -. DR STRING; 218491.ECA1490; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; eca:ECA1490; -. DR PATRIC; fig|218491.5.peg.1529; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_002346_0_2_6; -. DR OrthoDB; 9758603at2; -. DR Proteomes; UP000007966; 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; Reference proteome; KW Sodium. FT CHAIN 1..1040 FT /note="Beta-galactosidase" FT /id="PRO_0000366986" FT ACT_SITE 472 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT ACT_SITE 548 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 111 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 210 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 210 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 427 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 429 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 472 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 472 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 548..551 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 608 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" 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 615 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 615 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT BINDING 1016 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 368 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" FT SITE 402 FT /note="Transition state stabilizer" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01687" SQ SEQUENCE 1040 AA; 119655 MW; 040D728F9B080D06 CRC64; MSDSVLSNPT RQHATLREIL ARRDWENPAC TNYQRLPAHP PFNSWRNVAA AHQDEPSQRL RRLNGEWKFS YFTRPEAVPE SWLQQDLPDS ATIPVPSNWQ LQGYDTPIYT NVKYPIPVNP PYVPEDNPTG CYSLTFKVNH DWLSCGQTRV IFDGVNSAFY LWCNGHWVGY SQDSRLPAEF DISRYLTTGE NRLAVMVLRW SDGSYLEDQD MWRMSGIFRD VTLLHKPTVH LGDIQLTTPL SADFRHGTLD IQVKATLSES EAKNYRVHAQ LWRGNNLIGE TRQAFGSDIV DERGTYHDRA SLRLDVTRPD LWSAELPHLY RAVIALETAE GELLEAEAYD VGFRKVEISN GLLLLNGKPL LIRGVNRHEH HPQNGQVMDE ETMRRDIMLM KQHNFNAVRC SHYPNHPLWY RLCDRYGLYV VDEANIETHG MQPMNRLSDD PMWLPAYSER VSRMVQRDRN HPCIIIWSLG NESGYGANHD ALYQWIKRHD PTRPVHYEGG GANSRATDIV CPMYARVDED QPFPNVPKWS ISKWISMPNE HRPLILCEYA HAMGNSLGGF ARYWKAFRQY PRLQGGFIWD WVDQALIRHD EQGNAYWAYG GDFGDMPNDR QFCLDGLLFP DRTPHPSLYE AQRAQQHIQF VWQAESPCEL RVTSEYLFRH TDNEQLNWHI TLDDKTLVEG SLPLKLAPQA TQTLTLLESL PTVDRAGEIW LNVEVVQPKE TAWSKANHRC AWDQWQLPIP LHLPEASCSK QKIPPVLRAS DIYFDVVQGE QHWRFNRQSG LLEQWWTADT PALLTPLQDQ FVRAPLDNDI GISEVDRIDP HAWAERWKSA GLYQLQTQCV AIQADQLADA VHIVTEHVFR HAGQILLRSK KRWQIDAYGV MTVDVDVDVA TVLPSLARVG LSCQLADVAP QVSWIGLGPH ENYPDRQLAA QHGHWNLPLD DLHTPYIFPS ENGLRCNTRA LTYGKWAITG NFHFGLSRYG LTQLMTCTHH HLLEKEKGVW LNLDGFHMGI GGDDSWSPSV HCDDLLTATH YHYRVAIQRH //