ID   BGAL_GEOSY              Reviewed;         672 AA.
AC   C9S0R2;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Beta-galactosidase BgaB;
DE            Short=Beta-gal {ECO:0000250|UniProtKB:P19668};
DE            EC=3.2.1.23;
DE   AltName: Full=Beta-galactosidase I {ECO:0000250|UniProtKB:P19668};
DE   AltName: Full=Lactase {ECO:0000250|UniProtKB:P19668};
GN   Name=bgaB {ECO:0000250|UniProtKB:P19668}; OrderedLocusNames=GYMC61_0530;
OS   Geobacillus sp. (strain Y412MC61).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=544556;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y412MC61 {ECO:0000312|EMBL:ACX77212.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Brumm P.,
RA   Mead D.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y412MC61.";
RL   Submitted (OCT-2009) 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;
CC         Evidence={ECO:0000250|UniProtKB:P19668};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 42 family. {ECO:0000255}.
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DR   EMBL; CP001794; ACX77212.1; -; Genomic_DNA.
DR   RefSeq; WP_013524100.1; NC_013411.1.
DR   AlphaFoldDB; C9S0R2; -.
DR   SMR; C9S0R2; -.
DR   CAZy; GH42; Glycoside Hydrolase Family 42.
DR   KEGG; gyc:GYMC61_0530; -.
DR   HOGENOM; CLU_012430_1_1_9; -.
DR   OMA; SRRHYCF; -.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006012; P:galactose metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR013739; Beta_galactosidase_C.
DR   InterPro; IPR013738; Beta_galactosidase_Trimer.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR003476; Glyco_hydro_42.
DR   InterPro; IPR013529; Glyco_hydro_42_N.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR36447; PTHR36447; 1.
DR   Pfam; PF02449; Glyco_hydro_42; 1.
DR   Pfam; PF08533; Glyco_hydro_42C; 1.
DR   Pfam; PF08532; Glyco_hydro_42M; 1.
DR   PIRSF; PIRSF001084; B-galactosidase; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..672
FT                   /note="Beta-galactosidase BgaB"
FT                   /id="PRO_0000407689"
FT   ACT_SITE        148
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         158
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         161
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
FT   BINDING         351..354
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O69315"
SQ   SEQUENCE   672 AA;  78015 MW;  5B4573522E398425 CRC64;
     MNVLSSICYG GDYNPEQWPE EIWYEDAKLM QKAGVNLVSL GIFSWSKIEP SDGVFDFEWL
     DKVIDILYDH GVYINLGTAT ATTPAWFVKK YPDSLPIDES GVIFSFGSRQ HYCPNHPQLI
     THIKRLVRAI AERYKNHPAL KMWHVNNEYA CHVSKCFCEN CAVAFRKWLK ERYKTIDELN
     ERWGTNFWGQ RYNHWDEINP PRKAPTFINP SQELDYYRFM NDSILKLFLT EKEILRGVTP
     DIPVSTNFMG SFKPLNYFQW AQHVDIVTWD SYPDPREGLP IQHAMMNDLM RSLRKGQPFI
     LMEQVTSHVN WRDINVPKPP GVMRLWSYAT IARGADGIMF FQWRQSRAGA EKFHGAMVPH
     FLNENNRIYR EVTQLGQELK KLDCLVGSRI KAEVAIIFDW ENWWAVELSS KPHNKLRYIP
     IVEAYYRELY KRNIAVDFVR PSDDLTKYKV VIAPMLYMVK EGEDENLRQF VANGGTLIVS
     FFSGIVDEND RVHLGGYPGP LRDILGIFVE EFVPYPETKV NKIYSNDGEY DCTTWADIIR
     LEGAEPLATF KGDWYAGLPA VTRNCYGKGE GIYVGTYPDS NYLGRLLEQV FAKHHINPIL
     EVAENVEVQQ RETDEWKYLI IINHNDYEVT LSLPEDKIYQ NMIDGKCFRG GELRIQGVDV
     AVLREHDEAG KV