ID   BGAL_PYRWO              Reviewed;         510 AA.
AC   O52629;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Lactase;
DE            EC=3.2.1.23;
OS   Pyrococcus woesei.
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=2262;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 49860 / DSM 3773 / JCM 8421 / Vul4;
RX   PubMed=10833397; DOI=10.1006/prep.2000.1231;
RA   Daabrowski S., Sobiewska G., Maciunska J., Synowiecki J., Kur J.;
RT   "Cloning, expression, and purification of the His(6)-tagged thermostable
RT   beta-galactosidase from Pyrococcus woesei in Escherichia coli and some
RT   properties of the isolated enzyme.";
RL   Protein Expr. Purif. 19:107-112(2000).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         This enzyme is thermostable.;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. {ECO:0000305}.
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DR   EMBL; AF043283; AAB97862.1; -; Genomic_DNA.
DR   AlphaFoldDB; O52629; -.
DR   SMR; O52629; -.
DR   CAZy; GH1; Glycoside Hydrolase Family 1.
DR   BRENDA; 3.2.1.23; 5249.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
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   NCBIfam; NF041004; Beta_gal_BgaS; 1.
DR   PANTHER; PTHR10353; GLYCOSYL HYDROLASE; 1.
DR   PANTHER; PTHR10353:SF36; KLOTHO (MAMMALIAN AGING-ASSOCIATED PROTEIN) HOMOLOG; 1.
DR   Pfam; PF00232; Glyco_hydro_1; 2.
DR   PRINTS; PR00131; GLHYDRLASE1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00572; GLYCOSYL_HYDROL_F1_1; 1.
DR   PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..510
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000063865"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10055"
SQ   SEQUENCE   510 AA;  59057 MW;  10D0D3B8D9F26545 CRC64;
     MFPEKFLWGV AQSGFQFEMG DKLRRNIDTN TDWWHWVRDK TNIEKGLVSG DLPEEGINNY
     ELYEKDHEIA RKLGLNAYRI GIEWSRIFPW PTTFIDVDYS YNESYNLIED VKITKDTLEE
     LDEIANKREV AYYRSVINSL RSKGFKVIVN LNHFTLPYWL HDPIEARERA LTNKRNGWVN
     PRTVIEFAKY AAYIAYKFGD IVDMWSTFNE PMVVVELGYL APYSGFPPGV LNPEAAKLAI
     LHMINAHALA YRQIKKFDTE KADKDSKEPA EVGIIYNNIG VAYPKDPNDS KDVKAAENDN
     FFHSGLFFEA IHKGKLNIEF DGETFIDAPY LKGNDWIGVN YYTREVVTYQ EPMFPSIPLI
     TFKGVQGYGY ACRPGTLSKD DRPVSDIGWE LYPEGMYDSI VEAHKYGVPV YVTENGIADS
     KDILRPYYIA SHIKMTEKAF EDGYEVKGYF HWALTDNFEW ALGFRMRFGL YEVNLITKER
     IPREKSVSIF REIVANNGVT KKIEEELLRG
//