ID   BGAL_LEULA              Reviewed;         626 AA.
AC   Q02603;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Beta-galactosidase large subunit {ECO:0000305|PubMed:1624440};
DE            Short=Beta-gal large subunit {ECO:0000305|PubMed:1624440};
DE            EC=3.2.1.23 {ECO:0000269|PubMed:1624440};
GN   Name=lacL {ECO:0000303|PubMed:1624440};
OS   Leuconostoc lactis.
OG   Plasmid pNZ63.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Leuconostoc.
OX   NCBI_TaxID=1246;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6, FUNCTION,
RP   CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=NZ6009;
RX   PubMed=1624440; DOI=10.1128/jb.174.13.4475-4481.1992;
RA   David S., Stevens H., van Riel M., Simons G., de Vos W.M.;
RT   "Leuconostoc lactis beta-galactosidase is encoded by two overlapping
RT   genes.";
RL   J. Bacteriol. 174:4475-4481(1992).
CC   -!- FUNCTION: Component of a beta-galactosidase that displays activity with
CC       the artificial chromogenic substrate o-nitrophenyl-beta-D-
CC       galactopyranoside (ONPG). {ECO:0000269|PubMed:1624440}.
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:0000269|PubMed:1624440};
CC   -!- SUBUNIT: Heterodimer of a large (LacL) and a small subunit (LacM).
CC       {ECO:0000269|PubMed:1624440}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; M92281; AAA25267.1; -; Genomic_DNA.
DR   PIR; A42891; A42891.
DR   AlphaFoldDB; Q02603; -.
DR   SMR; Q02603; -.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 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   PRINTS; PR00132; GLHYDRLASE2.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Plasmid.
FT   CHAIN           1..626
FT                   /note="Beta-galactosidase large subunit"
FT                   /id="PRO_0000057672"
FT   ACT_SITE        466
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        534
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   SITE            318
FT                   /note="Has an effect on thermostability"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   626 AA;  72113 MW;  E9CEA154B992CF7D CRC64;
     MQANLQWLDD PEVFRVNQLP AHSDHHYYHD TAEFKTGSRF IKSLNGAWRF NFAKTPAERP
     VDFYQPDFDA TDFDTIQVPG HIELAGYGQI QYINTLYPWE GKIYRRPPYT LNQDQLTPGL
     FSDAADNTVG SYLKTFDLDD VFKGQRIIIQ FQGVEEALYV WLNGHFIGYS EDSFTPSEFD
     LTPYIQDQGN VLAVRVYKHS TAAFIEDQDM FRFSGIFRDV NILAEPASHI TDLDIRPVPN
     ANLKSGELNI TTKVTGEPAT LALTVKDHDG RVLTSQTQTG SGSVTFDTML FDQLHLWSPQ
     TPYLYQLTIE VYDADHQLLE VVPYQFGFRT VELRDDKVIY VNNKRLVING VNRHEWNAHT
     GRVISMADMR ADIQTMLANN INADRTCHYP DQLPWYQLCD EAGIYLMAET NLESHGSWQK
     MGAIEPSYNV PGDNPHWPAA VIDRARSNYE WFKNHPSIIF WSLGNESYAG EDIAAMQAFY
     KEHDDSRLVH YEGVFYTPEL KDRISDVESR MYEKPQNIVA YLEDNPTKPF LNCEYMHDMG
     NSLGGMQSYN DLIDKYPMYQ GGFIWDFIDQ ALFVHDPITD QDVLRYGGDF DERHSDYAFS
     GNGLMFADRT PKPAMQEVKY YYGLHK
//