BGAL_ENTAG
ID BGAL_ENTAG Reviewed; 1028 AA.
AC A3FEW8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE Short=Bga;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
DE AltName: Full=Transglycosylating beta-galactosidase;
GN Name=lacZ;
OS Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea; Pantoea agglomerans group.
OX NCBI_TaxID=549;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION AS
RP TRANSGLYCOSYLATING BETA-GALACTOSIDASE, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=B1;
RX PubMed=17336932; DOI=10.1016/j.bbrc.2007.02.106;
RA Lu L., Xiao M., Xu X., Li Z., Li Y.;
RT "A novel beta-galactosidase capable of glycosyl transfer from Enterobacter
RT agglomerans B1.";
RL Biochem. Biophys. Res. Commun. 356:78-84(2007).
CC -!- FUNCTION: This beta-galactosidase is also able to catalyze glycosyl
CC transfer to a series of acceptors, including hexose, pentose, beta- or
CC alpha-disaccharides, hexahydroxy alcohol, cyclitol, and aromatic
CC glycosides, resulting in the production of galacto-oligosaccharides
CC (GOS). {ECO:0000269|PubMed:17336932}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
CC Note=Binds 2 magnesium ions per monomer. Can also use manganese and
CC iron. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000305};
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305};
CC Note=Binds 1 sodium ion per monomer. Can also use potassium.
CC {ECO:0000305};
CC -!- ACTIVITY REGULATION: Completely inhibited by Hg(2+), Cu(2+) Ag(2+), and
CC partially inhibited by Zn(2+), imidazole and EDTA. Activated by Ca(2+),
CC Co(2+), Ni(2+). {ECO:0000269|PubMed:17336932}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees
CC Celsius) {ECO:0000269|PubMed:17336932};
CC KM=114 mM for lactose (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17336932};
CC Vmax=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-
CC galactopyranoside (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17336932};
CC Vmax=2.9 mmol/min/mg enzyme for o-nitrophenyl-beta-D-
CC galactopyranoside (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:17336932};
CC pH dependence:
CC Optimum pH is 7.5-8.0. Stable between 7.5-10.0.
CC {ECO:0000269|PubMed:17336932};
CC Temperature dependence:
CC Optimum temperature is 37-40 degrees Celsius. Stable below 37 degrees
CC Celsius. {ECO:0000269|PubMed:17336932};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17336932}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABN42680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; EF371803; ABN42680.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A3FEW8; -.
DR SMR; A3FEW8; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR SABIO-RK; A3FEW8; -.
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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01687; Beta_gal; 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; IPR023933; Glyco_hydro_2_beta_Galsidase.
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 1: Evidence at protein level;
KW Direct protein sequencing; Glycosidase; Hydrolase; Magnesium;
KW Metal-binding; Sodium.
FT CHAIN 1..1028
FT /note="Beta-galactosidase"
FT /id="PRO_0000366982"
FT ACT_SITE 463
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 539
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 418
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 463
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 539..542
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 599
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000250"
FT BINDING 606
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1004
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 1004
FT /note="Important for ensuring that an appropriate
FT proportion of lactose is converted to allolactose"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1028 AA; 116394 MW; 5A72487AB243185D CRC64;
MFTASPMSLS KILARRDWEN PGVTQWHRLP AHAPFNSWRD EASARADDNA SRKRSLNGDW
QFSYYAAPEQ VPDSWVTEDC ADAVTTPVPS NWQMQGFDTP IYTNDTYPIP VNPPFVPAEN
PTGCYSLTFE VDEQWLESGQ TRIVFDGVNS AFYLWCNGKW MGYSQDSRLP AEFDLSAVLR
PGTNRLAVLV LRWCDGSYLE DQDMWRMSGI FRDVSLLHKP HTHIADYHAV TELNADYDRA
KLQVEVALAG EQFADCEVAV TLWRDGLSVA TVSAKPGSAI IDERGNWAER LNVTLPVKDP
ALWSAETPEL YRLTFALRDG QGEILDVEAC DVGFRCVEIS NGLLKVNGKP LLIRGVNRHE
HHPENGQVMD EATMCRDIEL MKQHNFNAVR CSHYPNHPLW YTLCDRYGLY VVDEANIETH
GMVPMSRLAD DPRWLPAMSE RVTRMVLRDR NHPSIIIWSL GNESGHGANH DALYRWVKTT
DPTRPVQYEG GGANTAATDI VCPMYARVDQ DQPFEAVPKW SLKKWIGMPD ETRPLILCEY
AHAMGNSFGG FAKYWQAFRN HPRLQGGFVW DWVDQALTKK DDNGNAFWAY GGDFGDTPND
RQFCLNGLVF PDRTPHPALF EAQRAQQFFT FTLVSTSPLV IDVHSDYLFR QCDNEQLRWN
IARDGEVLAS GEVALTIAPQ QTQRIEIDAP EFAAAAGEIW LNVDIVQTAA TAWSPADHRC
AWDQWQLPAP LYIAPPVEGT AKPDLKVKED VLEVSHQSQR WHFDRASGNL TQWWNNGTAT
LLAPLSDNFT RAPLDNDIGV SEATRIDPNA WVERWKAAGM YNLTPRLLLC EGEQLAQAVT
ITTLHAWESN GKALFLSRKV WKIDRAGVLH GDVQVQVAND IPQPARIGLS CQLAQTPQTA
SWLGLGPDEN YPDRKLAARQ GRWTLPLDAL HTAYIFPTDN GLRCDTRELT FDTHQMQGDF
HFSLSRYSQQ QLRDTSHHHL LEAEPGCWLN IDAFHMGVGG DDSWSPSVSP EFILQRREMR
YAFSWRQD
