ID   BGAL_ALKHC              Reviewed;        1014 AA.
AC   Q9K9C6;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ; OrderedLocusNames=BH2723;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
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DR   EMBL; BA000004; BAB06442.1; -; Genomic_DNA.
DR   PIR; C83990; C83990.
DR   RefSeq; WP_010898871.1; NC_002570.2.
DR   AlphaFoldDB; Q9K9C6; -.
DR   SMR; Q9K9C6; -.
DR   STRING; 272558.10175344; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
DR   PRIDE; Q9K9C6; -.
DR   EnsemblBacteria; BAB06442; BAB06442; BAB06442.
DR   KEGG; bha:BH2723; -.
DR   eggNOG; COG3250; Bacteria.
DR   HOGENOM; CLU_002346_0_2_9; -.
DR   OMA; WCDHGIL; -.
DR   OrthoDB; 245411at2; -.
DR   Proteomes; UP000001258; Chromosome.
DR   GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
DR   GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016052; P:carbohydrate catabolic process; IEA:UniProt.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 2.70.98.10; -; 1.
DR   InterPro; IPR004199; B-gal_small/dom_5.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR014718; GH-type_carb-bd.
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   InterPro; IPR032312; LacZ_4.
DR   Pfam; PF02929; Bgal_small_N; 1.
DR   Pfam; PF16353; DUF4981; 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   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF49303; SSF49303; 2.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF74650; SSF74650; 1.
DR   PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
DR   PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..1014
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057658"
FT   ACT_SITE        460
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        527
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1014 AA;  116656 MW;  30405EB697C72798 CRC64;
     MKTHSNVSWL RDVNVFAVNR LPAHSDHVYY ETVEEAKKEP PMSMRHSLNG HWKFHYAINP
     NTRPKEFYQL GFDCKCWDDI LVPGHIQLQG YGKPQYVNTM YPWDGHHHLR PPEIPEDDNP
     VGSYVKYFDI PNNMSNHPLF ISFQGVETAF YVWLNGEFVG YSEDSFTPAE FDLTPYAVEG
     ENKLCVEVYQ RSTGSWLEDQ DFWRFSGIFR DVYLYTIPNI HVYDMHVRAD LDRSLQTGIL
     ETTLELKRSQ EKEVMIVAEL YDAEGAVVAT ADMKTNQDQA TVSMSVDSPA LWSAEDPYLY
     KLFLKLFDEN GTLVEVVPQK IGFRRFELVN NIMTLNGKRI VFKGVNRHEF NGRTGRVVTK
     EDMLEDIKTM KKHNINAVRT SHYPNNSEWY QLCDEYGLYV IDEMNLETHG SWQKLGKVEP
     SWNIPGNHLE WEPIVMDRAV SMFERDKNHP SILIWSCGNE SYAGEVILNV SRYFKSVDPS
     RLVHYEGVFH ARAYDATSDM ESRMYAKPKD IEDYLTNDPK KPYISCEYMH AMGNSLGGMH
     KYTELEQKYP MYQGGFIWDY IDQALLKKDR YGKEYFAYGG DFGDRPTDYS FCANGIVYAD
     RKPSPKMQEV KFLYQNIKLV PDREGVLVKN ENLFTDTSAY QLEYVLYWEG TELYRKKQDV
     FVAPQEEVYL PFDWLEQGMN ESGEYCIHTM LTLKQDQLWA EKGHEVAFGQ HVYRMGAIQK
     ERNARGALKV VHGDVNIGIH GEDFSVLFSK AVGSLVSLHY AGKEMIEQPP MPLFWRATTD
     NDKGCSQLYH SGIWYAASLA RKCVNMEVEE KPGHVSVLFT YHFAISDRVE VKVGYTVFPD
     GSLRVRSTYQ ASKGGETLPQ LPMFALSFKL PADYEQLEWY ALGPEENYAD RATGARLCTF
     KNKVEDSLSQ YVTPQESGNR TGVRTVKILD ANGQGIEVCS VEEPIECQIS PYTAFELEQA
     SHPYELPNVH YTVVNVAGKQ MGVGGDDSWG APVHDEYVLK ADQDLEFVFD INRV