ID   BGAL_RHIML              Reviewed;         755 AA.
AC   Q59750;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, 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;
OS   Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=382;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=102F34;
RX   PubMed=8163182; DOI=10.1016/0378-1119(94)90133-3;
RA   Fanning S., Leahy M., Sheehan D.;
RT   "Nucleotide and deduced amino acid sequences of Rhizobium meliloti 102F34
RT   lacZ gene: comparison with prokaryotic beta-galactosidases and human beta-
RT   glucuronidase.";
RL   Gene 141:91-96(1994).
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}.
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DR   EMBL; L20757; AAA26296.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59750; -.
DR   SMR; Q59750; -.
DR   BindingDB; Q59750; -.
DR   ChEMBL; CHEMBL3484; -.
DR   DrugCentral; Q59750; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR040605; Glyco_hydro2_dom5.
DR   InterPro; IPR006103; Glyco_hydro_2_cat.
DR   InterPro; IPR023230; Glyco_hydro_2_CS.
DR   InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF18565; Glyco_hydro2_C5; 1.
DR   Pfam; PF00703; Glyco_hydro_2; 1.
DR   Pfam; PF02836; Glyco_hydro_2_C; 1.
DR   SUPFAM; SSF49303; SSF49303; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase.
FT   CHAIN           1..755
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057674"
FT   ACT_SITE        382
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        463
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   755 AA;  84149 MW;  09E339A92CC0D366 CRC64;
     MRSVTSFNDS WVFSEASTRD AERSGRVSRS ACRTNAVELP FNYFDERCYQ RAFTYQRVLA
     WRPDFSQGSR SSSTRQWPMR SCISTAKRSS RIRDGYTPFE ARLTDRLLEG DNLITVKIDG
     SENPEIPPFG AGIDYLTYAG IYRDVWLKVT DPVSIANIKI ETRDVLSDHK AVSLRCDLSN
     PQGLSFSGTI SALLKNAAGE VLAEVAGETT GQSLAFEMDG LRGLSLWDID DPVLYVIEVE
     LRTGQGFRLL RRAFRLPHGE FTTEGFRLNG RPLKIRGLNR HQSFPYVGLR MGRTAKGSAH
     ADIMNAHRLH CNLVRTSHYP QSKWFLDHCD RIGLLVFARN PRLAAYRWGG METGGNPERP
     PHRSSATGTT RLSYIWGVRI NESQDSHDFY AETNRLAREL DPTRQTGGVR YITDSEFLED
     VYTMNDFILG NEELPGANRP GTALRPQQEC TGLPRKVPYL ITEFGGHMYP TKIYDQEQRQ
     AEHVRRHLEV LNAAYARNPG ISGAIGWCMF DYNTTRISAP ATGSAITASW TCSASPKFAA
     YVYASQCDPS EEIVMKPVTF WARGDDDIGG VLPLIVLTNC DEIELKYGSL TKRVGPDREN
     FPHLPHPPVV IDHRHFTKDE LGVWGMKWES AEFTGFIAGK PVADLRMAAD PVPTTLQVEA
     DSKTLRREGR DTVRLILRAL DQAGNVLPFL NDAVDIEIHG PARLVGPARI VLQGGSGFLA
     GVHGRRRHAS SRSRRRGSAA AKLDLVALAD GAASA