ID BGAL_PRIM3 Reviewed; 1034 AA. AC O52847; D5DFH9; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 115. DE RecName: Full=Beta-galactosidase; DE Short=Beta-gal; DE EC=3.2.1.23; DE AltName: Full=Lactase; GN Name=bgaM; OrderedLocusNames=BMD_2126; OS Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia. OX NCBI_TaxID=592022; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Strey J.; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 319 / IMG 1521; RX PubMed=21705586; DOI=10.1128/jb.00449-11; RA Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., RA Koenig S.S., Creasy H.H., Rosovitz M.J., Riley D.R., Daugherty S., RA Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C., RA Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J., RA Bremer E., Jahn D., Ravel J., Vary P.S.; RT "Genome sequences of the biotechnologically important Bacillus megaterium RT strains QM B1551 and DSM319."; RL J. Bacteriol. 193:4199-4213(2011). CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues CC in beta-D-galactosides.; EC=3.2.1.23; CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}. 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; AJ000733; CAA04267.1; -; Genomic_DNA. DR EMBL; CP001982; ADF38979.1; -; Genomic_DNA. DR PIR; T30574; T30574. DR RefSeq; WP_013082993.1; NZ_CP120609.1. DR AlphaFoldDB; O52847; -. DR SMR; O52847; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; bmd:BMD_2126; -. DR PATRIC; fig|592022.4.peg.2076; -. DR HOGENOM; CLU_002346_0_2_9; -. DR Proteomes; UP000002365; 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: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 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; 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. FT CHAIN 1..1034 FT /note="Beta-galactosidase" FT /id="PRO_0000057659" FT ACT_SITE 481 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 547 FT /note="Nucleophile" FT /evidence="ECO:0000250" SQ SEQUENCE 1034 AA; 118674 MW; 38644C9A649415E9 CRC64; MLKTGKKFHY TAPANGYPEW NNNPEIFQLN RSKAHALLMP YQTVEEALKN DRKSSVYYQS LNGSWYFHFA ENADGRVKNF FAPEFSYEKW DSISVPSHWQ LQGYDYPQYT NVTYPWVENE ELEPPFAPTK YNPVGQYVRT FTPKSEWKDQ PVYISFQGVE SAFYVWINGE FVGYSEDSFT PAEFDITSYL QEGENTIAVE VYRWSDASWL EDQDFWRMSG IFRDVYLYST PQVHIYDFSV RSSLDNNYED GELSVSADIL NYFEHDTQDL TFEVMLYDAN AQEVLQAPLQ TNLSVSDQRT VSLRTHIKSP AKWSAESPNL YTLVLSLKNA AGSIIETESC KVGFRTFEIK NGLMTINGKR IVLRGVNRHE FDSVKGRAGI TREDMIHDIL LMKQHNINAV RTSHYPNDSV WYELCNEYGL YVIDETNLET HGTWTYLQEG EQKAVPGSKP EWKENVLDRC RSMYERDKNH PSIIIWSLGN ESFGGENFQH MYTFFKEKDS TRLVHYEGIF HHRDYDASDI ESTMYVKPAD VERYALMNPK KPYILCEYSH AMGNSCGNLY KYWELFDQYP ILQGGFIWDW KDQALQATAE DGTSYLAYGG DFGDTPNDGN FCGNGLIFAD GTASPKIAEV KKCYQPVKWT AVDPAKGKFA VQNKHLFTNL NAYDFVWTVE KNGELVEKHA SLLNVAPDGT DELTLSYPLY EQENETDEFV LTLSLRLSKD TAWASAGYEV AYEQFVLPAK AAMPSVKAAH PALTVDQNEQ TLTVTGTNFT AIFDKRKGQF ISYNYERTEL LASGFRPNFW RAVTDNDLGN KLHERCQTWR QASLEQHVKK VTVQPQVDFV IISVELALDN SLASCYVTYT LYNDGEMKIE QSLAPSETMP EIPEIGMLFT MNAAFDSLTW YGRGPHENYW DRKTGAKLAL HKGSVKEQVT PYLRPQECGN KTDVRWATIT NDQGRGFLIK GLPTVELNAL PYSPFELEAY DHFYKLPASD SVTVRVNYKQ MGVGGDDSWQ AKTHPNYTLY ANRSYTNTFT LKPL //