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Beta-galactosidase (Beta-gal) (Bga) (EC 3.2.1.23) (Lactase) (Transglycosylating beta-galactosidase)

 BGAL_ENTAG              Reviewed;        1028 AA.
A3FEW8;
24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
24-MAR-2009, sequence version 2.
22-NOV-2017, entry version 43.
RecName: Full=Beta-galactosidase;
Short=Beta-gal;
Short=Bga;
EC=3.2.1.23;
AltName: Full=Lactase;
AltName: Full=Transglycosylating beta-galactosidase;
Name=lacZ;
Enterobacter agglomerans (Erwinia herbicola) (Pantoea agglomerans).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Erwiniaceae; Pantoea; Pantoea agglomerans group.
NCBI_TaxID=549;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9, FUNCTION
AS TRANSGLYCOSYLATING BETA-GALACTOSIDASE, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND SUBUNIT.
STRAIN=B1;
PubMed=17336932; DOI=10.1016/j.bbrc.2007.02.106;
Lu L., Xiao M., Xu X., Li Z., Li Y.;
"A novel beta-galactosidase capable of glycosyl transfer from
Enterobacter agglomerans B1.";
Biochem. Biophys. Res. Commun. 356:78-84(2007).
-!- FUNCTION: This beta-galactosidase is also able to catalyze
glycosyl transfer to a series of acceptors, including hexose,
pentose, beta- or alpha-disaccharides, hexahydroxy alcohol,
cyclitol, and aromatic glycosides, resulting in the production of
galacto-oligosaccharides (GOS). {ECO:0000269|PubMed:17336932}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000305};
Note=Binds 2 magnesium ions per monomer. Can also use manganese
and iron. {ECO:0000305};
-!- COFACTOR:
Name=Na(+); Xref=ChEBI:CHEBI:29101; Evidence={ECO:0000305};
Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305};
Note=Binds 1 sodium ion per monomer. Can also use potassium.
{ECO:0000305};
-!- ENZYME REGULATION: Completely inhibited by Hg(2+), Cu(2+) Ag(2+),
and partially inhibited by Zn(2+), imidazole and EDTA. Activated
by Ca(2+), Co(2+), Ni(2+). {ECO:0000269|PubMed:17336932}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.06 mM for o-nitrophenyl-beta-D-galactopyranoside (at 37
degrees Celsius) {ECO:0000269|PubMed:17336932};
KM=114 mM for lactose (at 37 degrees Celsius)
{ECO:0000269|PubMed:17336932};
Vmax=0.43 mmol/min/mg enzyme for o-nitrophenyl-beta-D-
galactopyranoside (at 37 degrees Celsius)
{ECO:0000269|PubMed:17336932};
Vmax=2.9 mmol/min/mg enzyme for o-nitrophenyl-beta-D-
galactopyranoside (at 37 degrees Celsius)
{ECO:0000269|PubMed:17336932};
pH dependence:
Optimum pH is 7.5-8.0. Stable between 7.5-10.0.
{ECO:0000269|PubMed:17336932};
Temperature dependence:
Optimum temperature is 37-40 degrees Celsius. Stable below 37
degrees Celsius. {ECO:0000269|PubMed:17336932};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17336932}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ABN42680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; EF371803; ABN42680.1; ALT_INIT; Genomic_DNA.
ProteinModelPortal; A3FEW8; -.
SMR; A3FEW8; -.
CAZy; GH2; Glycoside Hydrolase Family 2.
PRIDE; A3FEW8; -.
SABIO-RK; A3FEW8; -.
GO; GO:0009341; C:beta-galactosidase complex; IEA:InterPro.
GO; GO:0004565; F:beta-galactosidase activity; IEA:UniProtKB-EC.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.70.98.10; -; 1.
HAMAP; MF_01687; Beta_gal; 1.
InterPro; IPR004199; B-gal_small/dom_5.
InterPro; IPR036156; Beta-gal/glucu_dom_sf.
InterPro; IPR011013; Gal_mutarotase_sf_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR014718; GH-type_carb-bd.
InterPro; IPR006101; Glyco_hydro_2.
InterPro; IPR023232; Glyco_hydro_2_AS.
InterPro; IPR023933; Glyco_hydro_2_beta_Galsidase.
InterPro; IPR006103; Glyco_hydro_2_cat.
InterPro; IPR023230; Glyco_hydro_2_CS.
InterPro; IPR006102; Glyco_hydro_2_Ig-like.
InterPro; IPR006104; Glyco_hydro_2_N.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR032312; LacZ_4.
PANTHER; PTHR10066:SF76; PTHR10066:SF76; 1.
Pfam; PF02929; Bgal_small_N; 1.
Pfam; PF16353; DUF4981; 1.
Pfam; PF00703; Glyco_hydro_2; 1.
Pfam; PF02836; Glyco_hydro_2_C; 1.
Pfam; PF02837; Glyco_hydro_2_N; 1.
PRINTS; PR00132; GLHYDRLASE2.
SMART; SM01038; Bgal_small_N; 1.
SUPFAM; SSF49303; SSF49303; 2.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF74650; SSF74650; 1.
PROSITE; PS00719; GLYCOSYL_HYDROL_F2_1; 1.
PROSITE; PS00608; GLYCOSYL_HYDROL_F2_2; 1.
1: Evidence at protein level;
Direct protein sequencing; Glycosidase; Hydrolase; Magnesium;
Metal-binding; Sodium.
CHAIN 1 1028 Beta-galactosidase.
/FTId=PRO_0000366982.
REGION 539 542 Substrate binding. {ECO:0000250}.
ACT_SITE 463 463 Proton donor. {ECO:0000250}.
ACT_SITE 539 539 Nucleophile. {ECO:0000250}.
METAL 203 203 Sodium. {ECO:0000250}.
METAL 418 418 Magnesium 1. {ECO:0000250}.
METAL 420 420 Magnesium 1. {ECO:0000250}.
METAL 463 463 Magnesium 1. {ECO:0000250}.
METAL 599 599 Magnesium 2. {ECO:0000250}.
METAL 603 603 Sodium; via carbonyl oxygen.
{ECO:0000250}.
METAL 606 606 Sodium. {ECO:0000250}.
BINDING 104 104 Substrate. {ECO:0000250}.
BINDING 203 203 Substrate. {ECO:0000250}.
BINDING 463 463 Substrate. {ECO:0000250}.
BINDING 606 606 Substrate. {ECO:0000250}.
BINDING 1004 1004 Substrate. {ECO:0000250}.
SITE 359 359 Transition state stabilizer.
{ECO:0000250}.
SITE 393 393 Transition state stabilizer.
{ECO:0000250}.
SITE 1004 1004 Important for ensuring that an
appropriate proportion of lactose is
converted to allolactose. {ECO:0000250}.
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


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