ID BGAL_LACDA Reviewed; 1008 AA. AC Q1G9Z4; P20043; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 92. DE RecName: Full=Beta-galactosidase; DE Short=Beta-gal; DE EC=3.2.1.23; DE AltName: Full=Lactase; GN Name=lacZ; OrderedLocusNames=Ldb1201; OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081 OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM OS 00102 / Lb 14). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=390333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1705929; DOI=10.1128/jb.173.6.1951-1957.1991; RA Leong-Morgenthaler P.M., Zwahlen M.-C., Hottinger H.; RT "Lactose metabolism in Lactobacillus bulgaricus: analysis of the primary RT structure and expression of the genes involved."; RL J. Bacteriol. 173:1951-1957(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / RC NCIMB 11778 / NCTC 12712 / WDCM 00102 / Lb 14; RX PubMed=16754859; DOI=10.1073/pnas.0603024103; RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P., RA Weissenbach J., Ehrlich S.D., Maguin E.; RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive RT and ongoing reductive evolution."; RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006). 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 -!- SUBUNIT: Monomer. {ECO:0000250}. 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; M55068; AAA25244.1; -; Genomic_DNA. DR EMBL; CR954253; CAI98003.1; -; Genomic_DNA. DR RefSeq; WP_003619632.1; NZ_JQAV01000039.1. DR AlphaFoldDB; Q1G9Z4; -. DR SMR; Q1G9Z4; -. DR STRING; 390333.Ldb1201; -. DR CAZy; GH2; Glycoside Hydrolase Family 2. DR KEGG; ldb:Ldb1201; -. DR PATRIC; fig|390333.13.peg.1439; -. DR eggNOG; COG3250; Bacteria. DR HOGENOM; CLU_002346_0_2_9; -. DR BioCyc; LDEL390333:LDB_RS05145-MONOMER; -. DR BRENDA; 3.2.1.23; 2861. DR SABIO-RK; Q1G9Z4; -. DR Proteomes; UP000001259; 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; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..1008 FT /note="Beta-galactosidase" FT /id="PRO_0000250751" FT REGION 29..48 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 465 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 532 FT /note="Nucleophile" FT /evidence="ECO:0000250" SQ SEQUENCE 1008 AA; 114160 MW; 4681BFCA448F731F CRC64; MSNKLVKEKR VDQADLAWLT DPEVYEVNTI PPHSDHESFQ SQEELEEGKS SLVQSLDGDW LIDYAENGQG PVNFYAEDFD DSNFKSVKVP GNLELQGFGQ PQYVNVQYPW DGSEEIFPPQ IPSKNPLASY VRYFDLDEAF WDKEVSLKFD GAATAIYVWL NGHFVGYGED SFTPSEFMVT KFLKKENNRL AVALYKYSSA SWLEDQDFWR MSGLFRSVTL QAKPRLHLED LKLTASLTDN YQKGKLEVEA NIAYRLPNAS FKLEVRDSEG DLVAEKLGPI RSEQLEFTLA DLPVAAWSAE KPNLYQVRLY LYQAGSLLEV SRQEVGFRNF ELKDGIMYLN GQRIVFKGAN RHEFDSKLGR AITEEDMIWD IKTMKRSNIN AVRCSHYPNQ SLFYRLCDKY GLYVIDEANL ESHGTWEKVG GHEDPSFNVP GDDQHWLGAS LSRVKNMMAR DKNHASILIW SLGNESYAGT VFAQMADYVR KADPTRVQHY EGVTHNRKFD DATQIESRMY APAKVIEEYL TNKPAKPFIS VEYAHAMGNS VGDLAAYTAL EKYPHYQGGF IWDWIDQGLE KDGHLLYGGD FDDRPTDYEF CGNGLVFADR TESPKLANVK ALYANLKLEV KDGQLFLKND NLFTNSSSYY FLTSLLVDGK LTYQSRPLTF GLEPGESGTF ALPWPEVADE KGEVVYRVTA HLKEDLPWAD EGFTVAEAEE VAQKLPEFKP EGRPDLVDSD YNLGLKGNNF QILFSKVKGW PVSLKYAGRE YLKRLPEFTF WRALTDNDRG AGYGYDLARW ENAGKYARLK DISCEVKEDS VLVKTAFTLP VALKGDLTVT YEVDGRGKIA VTADFPGAEE AGLLPAFGLN LALPKELTDY RYYGLGPNES YPDRLEGNYL GIYQGAVKKN FSPYLRPQET GNRSKVRWYQ LFDEKGGLEF TANGADLNLS ALPYSAAQIE AADHAFELTN NYTWVRALSA QMGVGGDDSW GQKVHPEFCL DAQKARQLRL VIQPLLLK //