ID   BGAL_ACTPL              Reviewed;        1005 AA.
AC   P70753;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Beta-galactosidase;
DE            Short=Beta-gal;
DE            EC=3.2.1.23;
DE   AltName: Full=Lactase;
GN   Name=lacZ;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CM5 / Serotype 1;
RX   PubMed=9228778; DOI=10.1111/j.1574-6968.1997.tb10417.x;
RA   Anderson T.J., Macinnes J.I.;
RT   "Expression and phylogenetic relationships of a novel lacZ homologue from
RT   Actinobacillus pleuropneumoniae.";
RL   FEMS Microbiol. Lett. 152:117-123(1997).
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; U62625; AAB17954.1; -; Genomic_DNA.
DR   PIR; T31333; T31333.
DR   AlphaFoldDB; P70753; -.
DR   SMR; P70753; -.
DR   CAZy; GH2; Glycoside Hydrolase Family 2.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 2.70.98.10; -; 1.
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; 2.
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   PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1.
DR   Pfam; PF02929; Bgal_small_N; 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   Pfam; PF16353; LacZ_4; 1.
DR   PRINTS; PR00132; GLHYDRLASE2.
DR   SMART; SM01038; Bgal_small_N; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 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   3: Inferred from homology;
KW   Glycosidase; Hydrolase.
FT   CHAIN           1..1005
FT                   /note="Beta-galactosidase"
FT                   /id="PRO_0000057654"
FT   ACT_SITE        455
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        526
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1005 AA;  117009 MW;  12254482581C710E CRC64;
     MILPNYFQDP NTLHVNTVEH HAYFIPHQQN ETALSGKREQ SDYFTLLNGQ WDFNYFQSYH
     DLPDNFLDIA FEHKIPVPAN WQNHGFDHHH YTNINYPFPF EPPFVPHQNP CGVYHRTLQL
     TPKHKRYLLN FEGVDSCLFV YVNKQFVGYS QISHNTSEFD VSDYLQAGTN HLTVVVLKWC
     DGSYLEDQDK FRMSGIFRDV YLLEREQNYL QDFFIQYELD DELRHANLKV ETLFSRQPQA
     IEYQLLNPNG FTVFNQTDTH LNIEVEDIQL WNAEKPQLYT LILHTAEEVI VQKIGFRKVE
     IKDGILLFNQ QPIKFKGVNR HDSDPKTGYA ITYAQAHKDL QLMKQHNINA IRTAHYPNAP
     WFSELCDQYG FYLIGESDVE SHGASMLTVK MPEPSILLNH QNDLQTERIR QDMIDNYCYF
     ARDPLFKKAI LDRQQANVER DKNRTSIIIW SLGNEAGYGA NFEAAAAWIK QRDKSRLVHY
     ESSIYQHSAD NNDLSNLDFY SEMYGSTEDI DRYCATAQRK PFVLCEYSHA MGNSNGDAED
     YWQAFHRHPQ SCGGFVWEWC DHAPYRANGQ FGYGGDFGES PHDGNFCMDG LVSPDRIPHS
     NLLELKNVNR PARAELIDNQ IVIHNYLDFT DLADYLTIDY EFVENGVVTS GGNLSVSCKP
     HSSVILPIEL PKNNGHLWLL NLDYRLNTAT ELLEAEHSLG FEQLNLFSEN KLVLPKFTIE
     KSTFEVQEDH FRINVHNGQF SYQLDKQKGI FSRIEKAGKA IIQQPLDFNI WRAPTDNDRL
     IREAWQNAGY DKAYTRAYEI QWQQSEQAVE FSVKSAIVSI SRGRILTLDI RYRIFNDGQI
     SVEINAIRPT ELPYLPRFGL RFWLAKAENT VEYFGYGEQE SYVDKHHLAN LGIYHTTAKQ
     NHTDYVKPQE NGSHYGCEYL KSENLFVSAS QPFSFNLSPY TQEELTEKKH YYELQESDYS
     VLCIDYKMSG IGSNSCGPNL KDQYRLMESE FKIRFDLIFD KTIRQ
//