ID   BGAL_SACSH              Reviewed;         489 AA.
AC   P50388;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
GN   Name=bglY;
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RA   Connaris H., Charalambous B.M.;
RT   "The development and application of genetical techniques for the extremely
RT   thermoacidophilic archaeon Sulfolobus shibatae.";
RL   Submitted (OCT-1995) 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   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; L47841; AAA79030.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50388; -.
DR   SMR; P50388; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   BRENDA; 3.2.1.B33; 6162.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR001360; Glyco_hydro_1.
DR   InterPro; IPR018120; Glyco_hydro_1_AS.
DR   InterPro; IPR033132; Glyco_hydro_1_N_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR10353; PTHR10353; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 2.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Methylation.
FT   CHAIN           1..489
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000063868"
FT   ACT_SITE        206
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        387
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
FT   MOD_RES         135
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         273
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         332
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   489 AA;  56565 MW;  32412B88F478842E CRC64;
     MYSFPKNFRF GWSQAGFQSE MGTPGSEDPN TDWYKWVHDP ENISAGLVSG DLPENGPGYW
     GNYKTFHDNA QKMGLKIARL NVEWSRIFPN QLPKPQNFDD SKQDVTEVEI NQNELRRLDE
     HANKDALNHY REIFKDLKSR GIYFILNMYH WPLPLWLHDP IRVRRGDLSG PTGWLSTRTV
     YEFARFSAYI AWKFDDLVDE YSTMNEPNVV GGLGYVGVKS GFPPGYLSFE LSRKAMYNII
     QAHARAYDGI KSVSKKPIGI IYANSSFQPL TEKDVEAVEM AEYDNRWAFF DAIIRGEIMR
     GSEKVVRDDL RGRLDWIGVN YYTRTVVKKT EKGYTSLGGY GHGCERNSVS LAGLPTSDFG
     WEFFPEGLYD VLTKYWNRYH LYMYVTENGI ADDADYQRPY YLVSHVYQVH RAINSGADVR
     GYLHWSLADN YEWASGFSMR FGLLKVDYGT KRLYWRPSAL VYREIATNGG ITDEIEHLNT
     VPPIRPLRH