BGAL_ACTPL
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 03-AUG-2022, entry version 90.
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; Proteobacteria; 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 STRING; 228399.appser1_11060; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PRIDE; P70753; -.
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.
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