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Beta-galactosidase (Beta-gal) (EC 3.2.1.23) (Lactase)

 BGAL_ECOLI              Reviewed;        1024 AA.
P00722; Q2MC80;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 185.
RecName: Full=Beta-galactosidase;
Short=Beta-gal;
EC=3.2.1.23;
AltName: Full=Lactase;
Name=lacZ; OrderedLocusNames=b0344, JW0335;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6313347;
Kalnins A., Otto K., Ruether U., Mueller-Hill B.;
"Sequence of the lacZ gene of Escherichia coli.";
EMBO J. 2:593-597(1983).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-1024.
PubMed=97298;
Fowler A.V., Zabin I.;
"Amino acid sequence of beta-galactosidase. XI. Peptide ordering
procedures and the complete sequence.";
J. Biol. Chem. 253:5521-5525(1978).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476.
PubMed=6246435; DOI=10.1038/285038a0;
Calos M.P., Miller J.H.;
"Molecular consequences of deletion formation mediated by the
transposon Tn9.";
Nature 285:38-41(1980).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024.
PubMed=6444453; DOI=10.1038/283541a0;
Buechel D.E., Gronenborn B., Mueller-Hill B.;
"Sequence of the lactose permease gene.";
Nature 283:541-545(1980).
[8]
INDUCTION BY ALLOLACTOSE.
PubMed=4562709; DOI=10.1016/0022-2836(72)90253-7;
Jobe A., Bourgeois S.;
"lac repressor-operator interaction. VI. The natural inducer of the
lac operon.";
J. Mol. Biol. 69:397-408(1972).
[9]
BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=114210; DOI=10.1021/bi00586a005;
Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.;
"Interaction of divalent cations with beta-galactosidase (Escherichia
coli).";
Biochemistry 18:4090-4095(1979).
[10]
ACTIVE SITE REGIONS.
PubMed=6411710;
Fowler A.V., Smith P.J.;
"The active site regions of lacZ and ebg beta-galactosidases are
homologous.";
J. Biol. Chem. 258:10204-10207(1983).
[11]
ACTIVE SITE GLU-462.
PubMed=6420154; DOI=10.1111/j.1432-1033.1984.tb07947.x;
Herrchen M., Legler G.;
"Identification of an essential carboxylate group at the active site
of lacZ beta-galactosidase from Escherichia coli.";
Eur. J. Biochem. 138:527-531(1984).
[12]
ACTIVE SITE GLU-538.
PubMed=1350782;
Gebler J.C., Aebersold R., Withers S.G.;
"Glu-537, not Glu-461, is the nucleophile in the active site of (lac
Z) beta-galactosidase from Escherichia coli.";
J. Biol. Chem. 267:11126-11130(1992).
[13]
MUTAGENESIS OF GLU-462, AND COFACTOR.
PubMed=7577931; DOI=10.1021/bi00041a022;
Martinez-Bilbao M., Gaunt M.T., Huber R.E.;
"E461H-beta-galactosidase (Escherichia coli): altered divalent metal
specificity and slow but reversible metal inactivation.";
Biochemistry 34:13437-13442(1995).
[14]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-541.
PubMed=8662937; DOI=10.1074/jbc.271.24.14296;
Roth N.J., Huber R.E.;
"The beta-galactosidase (Escherichia coli) reaction is partly
facilitated by interactions of His-540 with the C6 hydroxyl of
galactose.";
J. Biol. Chem. 271:14296-14301(1996).
[15]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[16]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-358.
PubMed=9665715; DOI=10.1021/bi972796t;
Roth N.J., Rob B., Huber R.E.;
"His-357 of beta-galactosidase (Escherichia coli) interacts with the
C3 hydroxyl in the transition state and helps to mediate catalysis.";
Biochemistry 37:10099-10107(1998).
[17]
MUTAGENESIS OF HIS-392.
PubMed=11310566; DOI=10.1139/o00-101;
Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K.;
"His-391 of beta-galactosidase (Escherichia coli) promotes catalyses
by strong interactions with the transition state.";
Biochem. Cell Biol. 79:183-193(2001).
[18]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TRP-1000.
PubMed=12578395; DOI=10.1021/bi0270642;
Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.;
"Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for
binding, catalysis, and synthesis of allolactose, the natural lac
operon inducer.";
Biochemistry 42:1796-1803(2003).
[19]
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-202.
PubMed=15060622; DOI=10.1139/o04-004;
Xu J., McRae M.A., Harron S., Rob B., Huber R.E.;
"A study of the relationships of interactions between Asp-201, Na+ or
K+, and galactosyl C6 hydroxyl and their effects on binding and
reactivity of beta-galactosidase.";
Biochem. Cell Biol. 82:275-284(2004).
[20]
REVIEW.
PubMed=15950161; DOI=10.1016/j.crvi.2005.03.006;
Matthews B.W.;
"The structure of E. coli beta-galactosidase.";
C. R. Biol. 328:549-556(2005).
[21]
COFACTOR, AND MUTAGENESIS OF GLU-798.
PubMed=17126292; DOI=10.1016/j.bbrc.2006.11.061;
Sutendra G., Wong S., Fraser M.E., Huber R.E.;
"Beta-galactosidase (Escherichia coli) has a second catalytically
important Mg2+ site.";
Biochem. Biophys. Res. Commun. 352:566-570(2007).
[22]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
AND SUBUNIT.
PubMed=8008071; DOI=10.1038/369761a0;
Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.;
"Three-dimensional structure of beta-galactosidase from E. coli.";
Nature 369:761-766(1994).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
SODIUM IONS.
PubMed=11045615; DOI=10.1110/ps.9.9.1685;
Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E.,
Tronrud D.E., Matthews B.W.;
"High resolution refinement of beta-galactosidase in a new crystal
form reveals multiple metal-binding sites and provides a structural
basis for alpha-complementation.";
Protein Sci. 9:1685-1699(2000).
[24]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOGS, MUTAGENESIS OF GLU-538 AND PHE-602, AND REACTION MECHANISM.
PubMed=11732897; DOI=10.1021/bi011727i;
Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L.,
Withers S.G., Matthews B.W.;
"A structural view of the action of Escherichia coli (lacZ) beta-
galactosidase.";
Biochemistry 40:14781-14794(2001).
[25]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN
COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND MUTAGENESIS OF
GLY-795.
PubMed=14621996; DOI=10.1021/bi035506j;
Juers D.H., Hakda S., Matthews B.W., Huber R.E.;
"Structural basis for the altered activity of Gly794 variants of
Escherichia coli beta-galactosidase.";
Biochemistry 42:13505-13511(2003).
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Binds 2 magnesium ions per monomer. Can also use manganese.;
-!- COFACTOR:
Name=Na(+); Xref=ChEBI:CHEBI:29101;
Note=Binds 1 sodium ion per monomer.;
-!- ENZYME REGULATION: Inhibited by phenylethyl thio-beta-D-
galactoside (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-
ribose, D-galactonolactone, lactose and 2-amino-D-galactose.
{ECO:0000269|PubMed:14621996}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.04 mM for p-nitrophenyl beta-D-galactoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=0.12 mM for o-nitrophenyl beta-D-galactoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
KM=34 uM for p-nitrophenyl beta-D-galactoside (with magnesium as
cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
KM=140 uM for o-nitrophenyl beta-D-galactoside (with magnesium
as cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
KM=940 uM for allolactose (with magnesium as cofactor and 30
degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
KM=1350 uM for lactose (with magnesium as cofactor and 30
degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
Vmax=30.9 umol/min/mg enzyme with lactose as substrate (with
magnesium as cofactor and 30 degrees Celsius)
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
Vmax=49.7 umol/min/mg enzyme with allolactose as substrate (with
magnesium as cofactor and 30 degrees Celsius)
{ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
Vmax=59.7 umol/min/mg enzyme with p-nitrophenyl beta-D-
galactoside as substrate (with magnesium as cofactor and 30
degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
Vmax=360 umol/min/mg enzyme with o-nitrophenyl beta-D-
galactoside as substrate (with magnesium as cofactor and 30
degrees Celsius) {ECO:0000269|PubMed:114210,
ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
ECO:0000269|PubMed:9665715};
Note=The values for the enzymatic assays using manganese as
cofactor are very close.;
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11045615,
ECO:0000269|PubMed:11732897, ECO:0000269|PubMed:14621996,
ECO:0000269|PubMed:8008071}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-369998, EBI-369998;
-!- INDUCTION: By allolactose. {ECO:0000269|PubMed:4562709}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/BG/";
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EMBL; J01636; AAA24053.1; -; Genomic_DNA.
EMBL; V00296; CAA23573.1; -; Genomic_DNA.
EMBL; U73857; AAB18068.1; -; Genomic_DNA.
EMBL; U00096; AAC73447.1; -; Genomic_DNA.
EMBL; AP009048; BAE76126.1; -; Genomic_DNA.
EMBL; V00295; CAA23570.1; -; Genomic_DNA.
PIR; A90981; GBEC.
RefSeq; NP_414878.1; NC_000913.3.
RefSeq; WP_000177906.1; NZ_LN832404.1.
PDB; 1DP0; X-ray; 1.70 A; A/B/C/D=10-1024.
PDB; 1F4A; X-ray; 2.80 A; A/B/C/D=4-1024.
PDB; 1F4H; X-ray; 2.80 A; A/B/C/D=4-1024.
PDB; 1HN1; X-ray; 3.00 A; A/B/C/D=10-1024.
PDB; 1JYN; X-ray; 1.80 A; A/B/C/D=10-1024.
PDB; 1JYV; X-ray; 1.75 A; A/B/C/D=10-1024.
PDB; 1JYW; X-ray; 1.55 A; A/B/C/D=10-1024.
PDB; 1JYX; X-ray; 1.75 A; A/B/C/D=10-1024.
PDB; 1JZ2; X-ray; 2.10 A; A/B/C/D=2-1024.
PDB; 1JZ3; X-ray; 1.75 A; A/B/C/D=10-1024.
PDB; 1JZ4; X-ray; 2.10 A; A/B/C/D=10-1024.
PDB; 1JZ5; X-ray; 1.80 A; A/B/C/D=10-1024.
PDB; 1JZ6; X-ray; 2.10 A; A/B/C/D=10-1024.
PDB; 1JZ7; X-ray; 1.50 A; A/B/C/D=10-1024.
PDB; 1JZ8; X-ray; 1.50 A; A/B/C/D=10-1024.
PDB; 1PX3; X-ray; 1.60 A; A/B/C/D=10-1024.
PDB; 1PX4; X-ray; 1.60 A; A/B/C/D=10-1024.
PDB; 3CZJ; X-ray; 2.05 A; A/B/C/D=10-1024.
PDB; 3DYM; X-ray; 2.05 A; A/B/C/D=10-1024.
PDB; 3DYO; X-ray; 1.80 A; A/B/C/D=10-1024.
PDB; 3DYP; X-ray; 1.75 A; A/B/C/D=10-1024.
PDB; 3E1F; X-ray; 3.00 A; 1/2/3/4=10-1024.
PDB; 3I3B; X-ray; 2.20 A; A/B/C/D=10-1024.
PDB; 3I3D; X-ray; 2.20 A; A/B/C/D=10-1024.
PDB; 3I3E; X-ray; 2.10 A; A/B/C/D=10-1024.
PDB; 3IAP; X-ray; 2.00 A; A/B/C/D=10-1024.
PDB; 3IAQ; X-ray; 2.70 A; A/B/C/D=10-1024.
PDB; 3J7H; EM; 3.20 A; A/B/C/D=1-1024.
PDB; 3MUY; X-ray; 2.50 A; 1/2/3/4=10-1024.
PDB; 3MUZ; X-ray; 1.90 A; 1/2/3/4=10-1024.
PDB; 3MV0; X-ray; 2.20 A; 1/2/3/4=10-1024.
PDB; 3MV1; X-ray; 2.20 A; 1/2/3/4=10-1024.
PDB; 3SEP; X-ray; 2.05 A; A/B/C/D=10-1024.
PDB; 3T08; X-ray; 2.00 A; A/B/C/D=10-1024.
PDB; 3T09; X-ray; 1.75 A; A/B/C/D=10-1024.
PDB; 3T0A; X-ray; 1.90 A; A/B/C/D=10-1024.
PDB; 3T0B; X-ray; 2.40 A; A/B/C/D=10-1024.
PDB; 3T0D; X-ray; 1.93 A; A/B/C/D=10-1024.
PDB; 3T2O; X-ray; 1.85 A; A/B/C/D=10-1024.
PDB; 3T2P; X-ray; 2.60 A; A/B/C/D=10-1024.
PDB; 3T2Q; X-ray; 2.40 A; A/B/C/D=10-1024.
PDB; 3VD3; X-ray; 2.80 A; A/B/C/D=10-1024.
PDB; 3VD4; X-ray; 2.00 A; A/B/C/D=10-1024.
PDB; 3VD5; X-ray; 2.70 A; A/B/C/D=10-1024.
PDB; 3VD7; X-ray; 2.87 A; A/B/C/D=10-1024.
PDB; 3VD9; X-ray; 2.05 A; A/B/C/D=10-1024.
PDB; 3VDA; X-ray; 2.50 A; A/B/C/D=10-1024.
PDB; 3VDB; X-ray; 2.05 A; A/B/C/D=10-1024.
PDB; 3VDC; X-ray; 2.55 A; A/B/C/D=10-1024.
PDB; 4CKD; EM; 13.00 A; A/B/C/D=1-1024.
PDB; 4DUV; X-ray; 2.10 A; A/B/C/D=10-1024.
PDB; 4DUW; X-ray; 2.20 A; A/B/C/D=10-1024.
PDB; 4DUX; X-ray; 2.30 A; A/B/C/D=10-1024.
PDB; 4TTG; X-ray; 1.60 A; A/B/C/D=15-1024.
PDB; 4V40; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-1024.
PDB; 4V41; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-1024.
PDB; 4V44; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-1024.
PDB; 4V45; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=2-1024.
PDB; 5A1A; EM; 2.20 A; A/B/C/D=3-1024.
PDBsum; 1DP0; -.
PDBsum; 1F4A; -.
PDBsum; 1F4H; -.
PDBsum; 1HN1; -.
PDBsum; 1JYN; -.
PDBsum; 1JYV; -.
PDBsum; 1JYW; -.
PDBsum; 1JYX; -.
PDBsum; 1JZ2; -.
PDBsum; 1JZ3; -.
PDBsum; 1JZ4; -.
PDBsum; 1JZ5; -.
PDBsum; 1JZ6; -.
PDBsum; 1JZ7; -.
PDBsum; 1JZ8; -.
PDBsum; 1PX3; -.
PDBsum; 1PX4; -.
PDBsum; 3CZJ; -.
PDBsum; 3DYM; -.
PDBsum; 3DYO; -.
PDBsum; 3DYP; -.
PDBsum; 3E1F; -.
PDBsum; 3I3B; -.
PDBsum; 3I3D; -.
PDBsum; 3I3E; -.
PDBsum; 3IAP; -.
PDBsum; 3IAQ; -.
PDBsum; 3J7H; -.
PDBsum; 3MUY; -.
PDBsum; 3MUZ; -.
PDBsum; 3MV0; -.
PDBsum; 3MV1; -.
PDBsum; 3SEP; -.
PDBsum; 3T08; -.
PDBsum; 3T09; -.
PDBsum; 3T0A; -.
PDBsum; 3T0B; -.
PDBsum; 3T0D; -.
PDBsum; 3T2O; -.
PDBsum; 3T2P; -.
PDBsum; 3T2Q; -.
PDBsum; 3VD3; -.
PDBsum; 3VD4; -.
PDBsum; 3VD5; -.
PDBsum; 3VD7; -.
PDBsum; 3VD9; -.
PDBsum; 3VDA; -.
PDBsum; 3VDB; -.
PDBsum; 3VDC; -.
PDBsum; 4CKD; -.
PDBsum; 4DUV; -.
PDBsum; 4DUW; -.
PDBsum; 4DUX; -.
PDBsum; 4TTG; -.
PDBsum; 4V40; -.
PDBsum; 4V41; -.
PDBsum; 4V44; -.
PDBsum; 4V45; -.
PDBsum; 5A1A; -.
ProteinModelPortal; P00722; -.
SMR; P00722; -.
DIP; DIP-10081N; -.
IntAct; P00722; 76.
STRING; 316407.85674486; -.
BindingDB; P00722; -.
ChEMBL; CHEMBL4603; -.
DrugBank; DB01920; 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose.
DrugBank; DB02228; 2-deoxy-2-fluoro-Beta-D-galactose.
DrugBank; DB04382; 2-Deoxy-Beta-D-Galactose.
DrugBank; DB04155; 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose.
DrugBank; DB02632; 4-nitrophenyl-beta-D-galactoside.
DrugBank; DB04116; Allolactose.
DrugBank; DB01885; D-Galctopyranosyl-1-On.
DrugBank; DB01862; Isopropyl beta-D-thiogalactopyranoside.
DrugBank; DB04465; Lactose.
CAZy; GH2; Glycoside Hydrolase Family 2.
PaxDb; P00722; -.
PRIDE; P00722; -.
EnsemblBacteria; AAC73447; AAC73447; b0344.
EnsemblBacteria; BAE76126; BAE76126; BAE76126.
GeneID; 945006; -.
KEGG; ecj:JW0335; -.
KEGG; eco:b0344; -.
EchoBASE; EB0522; -.
EcoGene; EG10527; lacZ.
eggNOG; ENOG4105CNT; Bacteria.
eggNOG; COG3250; LUCA.
HOGENOM; HOG000252443; -.
InParanoid; P00722; -.
KO; K01190; -.
PhylomeDB; P00722; -.
BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -.
BioCyc; MetaCyc:BETAGALACTOSID-MONOMER; -.
BRENDA; 3.2.1.23; 2026.
SABIO-RK; P00722; -.
EvolutionaryTrace; P00722; -.
PRO; PR:P00722; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0009341; C:beta-galactosidase complex; IDA:EcoCyc.
GO; GO:0031420; F:alkali metal ion binding; IDA:EcoCyc.
GO; GO:0004565; F:beta-galactosidase activity; IDA:EcoCyc.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
GO; GO:0005990; P:lactose catabolic process; IMP:CACAO.
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.
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;
3D-structure; Complete proteome; Direct protein sequencing;
Glycosidase; Hydrolase; Magnesium; Manganese; Metal-binding;
Reference proteome; Sodium.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:97298}.
CHAIN 2 1024 Beta-galactosidase.
/FTId=PRO_0000057650.
REGION 538 541 Substrate binding.
ACT_SITE 462 462 Proton donor.
{ECO:0000269|PubMed:6420154}.
ACT_SITE 538 538 Nucleophile.
{ECO:0000269|PubMed:1350782}.
METAL 202 202 Sodium.
METAL 417 417 Magnesium 1.
{ECO:0000269|PubMed:11045615}.
METAL 419 419 Magnesium 1.
{ECO:0000269|PubMed:11045615}.
METAL 462 462 Magnesium 1.
{ECO:0000269|PubMed:11045615}.
METAL 598 598 Magnesium 2.
{ECO:0000269|PubMed:11045615}.
METAL 602 602 Sodium; via carbonyl oxygen.
METAL 605 605 Sodium.
BINDING 103 103 Substrate.
BINDING 202 202 Substrate.
BINDING 462 462 Substrate.
BINDING 605 605 Substrate.
BINDING 1000 1000 Substrate.
SITE 358 358 Transition state stabilizer.
SITE 392 392 Transition state stabilizer.
SITE 1000 1000 Important for ensuring that an
appropriate proportion of lactose is
converted to allolactose.
MUTAGEN 202 202 D->E,N: Causes a significant decrease in
binding affinity in the absence of
monovalent cations or in the presence of
potassium ions, but only a moderate
decrease in the presence of sodium ions.
{ECO:0000269|PubMed:15060622}.
MUTAGEN 202 202 D->F: Obliterates all binding and
catalysis. {ECO:0000269|PubMed:15060622}.
MUTAGEN 358 358 H->D,F,L,N: Less stable to heat than
wild-type. Causes significant
destabilizations of the first transition
state. {ECO:0000269|PubMed:9665715}.
MUTAGEN 392 392 H->E,F,K: Essentially inactive unless
very rapid purification. Causes very
large destabilizations of the transition
state. {ECO:0000269|PubMed:11310566}.
MUTAGEN 462 462 E->H: Slowly inactivates galactosidase
activity by reducing the binding of
magnesium. It increases binding
specificity.
{ECO:0000269|PubMed:7577931}.
MUTAGEN 538 538 E->Q: 10000-fold decrease in the beta-
galactosidase activity.
{ECO:0000269|PubMed:11732897}.
MUTAGEN 541 541 H->E,F,N: Poorly reactive with galactosyl
substrates. Less stable to heat than
wild-type. {ECO:0000269|PubMed:8662937}.
MUTAGEN 602 602 F->A: Decreases the stability of the loop
794-804. {ECO:0000269|PubMed:11732897}.
MUTAGEN 795 795 G->A: It forces the apoenzyme to adopt
the closed rather than the open
conformation. Reduces the binding
affinity. {ECO:0000269|PubMed:14621996}.
MUTAGEN 798 798 E->A,L: The catalytic efficiency is not
increased, when the sodium concentration
increases. {ECO:0000269|PubMed:17126292}.
MUTAGEN 798 798 E->D,Q: Small increase of the catalytic
efficiency, when the sodium concentration
increases. {ECO:0000269|PubMed:17126292}.
MUTAGEN 1000 1000 W->F,G,L,T: Decreases affinity for
substrate. {ECO:0000269|PubMed:12578395}.
STRAND 5 7 {ECO:0000244|PDB:5A1A}.
HELIX 11 14 {ECO:0000244|PDB:3T09}.
HELIX 16 18 {ECO:0000244|PDB:1JZ7}.
STRAND 23 26 {ECO:0000244|PDB:1JZ7}.
STRAND 37 39 {ECO:0000244|PDB:1JZ7}.
HELIX 40 45 {ECO:0000244|PDB:1JZ7}.
STRAND 52 54 {ECO:0000244|PDB:1JZ7}.
STRAND 57 66 {ECO:0000244|PDB:1JZ7}.
HELIX 67 69 {ECO:0000244|PDB:1JZ7}.
HELIX 73 76 {ECO:0000244|PDB:1JZ7}.
STRAND 83 88 {ECO:0000244|PDB:1JZ7}.
HELIX 91 94 {ECO:0000244|PDB:1JZ7}.
STRAND 100 105 {ECO:0000244|PDB:1JZ7}.
STRAND 121 130 {ECO:0000244|PDB:1JZ7}.
HELIX 132 136 {ECO:0000244|PDB:1JZ7}.
STRAND 137 145 {ECO:0000244|PDB:1JZ7}.
STRAND 147 155 {ECO:0000244|PDB:1JZ7}.
STRAND 158 164 {ECO:0000244|PDB:1JZ7}.
STRAND 166 168 {ECO:0000244|PDB:3J7H}.
STRAND 170 173 {ECO:0000244|PDB:1JZ7}.
TURN 175 177 {ECO:0000244|PDB:1JZ7}.
STRAND 180 191 {ECO:0000244|PDB:1JZ7}.
HELIX 194 198 {ECO:0000244|PDB:1JZ7}.
STRAND 202 205 {ECO:0000244|PDB:1JZ7}.
STRAND 213 218 {ECO:0000244|PDB:1JZ7}.
STRAND 220 232 {ECO:0000244|PDB:1JZ7}.
STRAND 236 249 {ECO:0000244|PDB:1JZ7}.
STRAND 255 263 {ECO:0000244|PDB:1JZ7}.
STRAND 266 275 {ECO:0000244|PDB:1JZ7}.
STRAND 279 281 {ECO:0000244|PDB:3MUZ}.
STRAND 289 298 {ECO:0000244|PDB:1JZ7}.
STRAND 304 307 {ECO:0000244|PDB:1JZ7}.
STRAND 310 318 {ECO:0000244|PDB:1JZ7}.
TURN 319 321 {ECO:0000244|PDB:3IAQ}.
STRAND 323 331 {ECO:0000244|PDB:1JZ7}.
STRAND 336 339 {ECO:0000244|PDB:1JZ7}.
STRAND 342 345 {ECO:0000244|PDB:1JZ7}.
STRAND 352 356 {ECO:0000244|PDB:1JZ7}.
TURN 362 364 {ECO:0000244|PDB:1JZ7}.
HELIX 370 382 {ECO:0000244|PDB:1JZ7}.
STRAND 387 389 {ECO:0000244|PDB:1JZ7}.
HELIX 397 406 {ECO:0000244|PDB:1JZ7}.
STRAND 409 413 {ECO:0000244|PDB:1JZ7}.
STRAND 421 423 {ECO:0000244|PDB:1JZ7}.
TURN 424 429 {ECO:0000244|PDB:1JZ7}.
HELIX 431 433 {ECO:0000244|PDB:1JZ7}.
HELIX 434 448 {ECO:0000244|PDB:1JZ7}.
STRAND 454 458 {ECO:0000244|PDB:1JZ7}.
STRAND 461 463 {ECO:0000244|PDB:1JYW}.
HELIX 467 479 {ECO:0000244|PDB:1JZ7}.
TURN 489 491 {ECO:0000244|PDB:1JZ7}.
STRAND 492 494 {ECO:0000244|PDB:1JZ7}.
STRAND 498 500 {ECO:0000244|PDB:1JZ7}.
STRAND 507 509 {ECO:0000244|PDB:5A1A}.
STRAND 514 516 {ECO:0000244|PDB:1JZ7}.
HELIX 521 525 {ECO:0000244|PDB:1JZ7}.
STRAND 534 540 {ECO:0000244|PDB:1JZ7}.
STRAND 543 545 {ECO:0000244|PDB:1JZ6}.
HELIX 550 559 {ECO:0000244|PDB:1JZ7}.
STRAND 563 569 {ECO:0000244|PDB:1JZ7}.
STRAND 576 579 {ECO:0000244|PDB:1JZ7}.
STRAND 585 588 {ECO:0000244|PDB:1JZ7}.
TURN 590 593 {ECO:0000244|PDB:1JZ7}.
HELIX 600 603 {ECO:0000244|PDB:1JZ7}.
HELIX 617 624 {ECO:0000244|PDB:1JZ7}.
STRAND 627 633 {ECO:0000244|PDB:1JZ7}.
STRAND 636 641 {ECO:0000244|PDB:1JZ7}.
STRAND 652 659 {ECO:0000244|PDB:1JZ7}.
STRAND 662 670 {ECO:0000244|PDB:1JZ7}.
STRAND 678 682 {ECO:0000244|PDB:1JZ7}.
STRAND 691 703 {ECO:0000244|PDB:1JZ7}.
STRAND 708 710 {ECO:0000244|PDB:1JZ8}.
STRAND 714 726 {ECO:0000244|PDB:1JZ7}.
STRAND 740 743 {ECO:0000244|PDB:1JZ7}.
STRAND 745 752 {ECO:0000244|PDB:1JZ7}.
STRAND 755 760 {ECO:0000244|PDB:1JZ7}.
TURN 761 763 {ECO:0000244|PDB:1JZ7}.
STRAND 765 771 {ECO:0000244|PDB:1JZ7}.
STRAND 777 784 {ECO:0000244|PDB:1JZ7}.
HELIX 791 794 {ECO:0000244|PDB:1JZ7}.
STRAND 799 801 {ECO:0000244|PDB:1PX4}.
STRAND 804 806 {ECO:0000244|PDB:3J7H}.
HELIX 807 814 {ECO:0000244|PDB:1JZ7}.
TURN 815 818 {ECO:0000244|PDB:1JZ7}.
STRAND 820 830 {ECO:0000244|PDB:1JZ7}.
STRAND 832 845 {ECO:0000244|PDB:1JZ7}.
STRAND 848 860 {ECO:0000244|PDB:1JZ7}.
TURN 861 863 {ECO:0000244|PDB:1F4H}.
STRAND 865 873 {ECO:0000244|PDB:1JZ7}.
STRAND 875 877 {ECO:0000244|PDB:5A1A}.
STRAND 881 890 {ECO:0000244|PDB:1JZ7}.
STRAND 894 904 {ECO:0000244|PDB:1JZ7}.
STRAND 915 922 {ECO:0000244|PDB:1JZ7}.
HELIX 923 926 {ECO:0000244|PDB:1JZ7}.
STRAND 939 947 {ECO:0000244|PDB:1JZ7}.
STRAND 950 963 {ECO:0000244|PDB:1JZ7}.
HELIX 965 970 {ECO:0000244|PDB:1JZ7}.
HELIX 974 976 {ECO:0000244|PDB:1JZ7}.
STRAND 981 991 {ECO:0000244|PDB:1JZ7}.
STRAND 999 1001 {ECO:0000244|PDB:1JZ7}.
HELIX 1006 1008 {ECO:0000244|PDB:1JZ7}.
STRAND 1013 1022 {ECO:0000244|PDB:1JZ7}.
SEQUENCE 1024 AA; 116483 MW; 9D295EF4CEF90B08 CRC64;
MTMITDSLAV VLQRRDWENP GVTQLNRLAA HPPFASWRNS EEARTDRPSQ QLRSLNGEWR
FAWFPAPEAV PESWLECDLP EADTVVVPSN WQMHGYDAPI YTNVTYPITV NPPFVPTENP
TGCYSLTFNV DESWLQEGQT RIIFDGVNSA FHLWCNGRWV GYGQDSRLPS EFDLSAFLRA
GENRLAVMVL RWSDGSYLED QDMWRMSGIF RDVSLLHKPT TQISDFHVAT RFNDDFSRAV
LEAEVQMCGE LRDYLRVTVS LWQGETQVAS GTAPFGGEII DERGGYADRV TLRLNVENPK
LWSAEIPNLY RAVVELHTAD GTLIEAEACD VGFREVRIEN GLLLLNGKPL LIRGVNRHEH
HPLHGQVMDE QTMVQDILLM KQNNFNAVRC SHYPNHPLWY TLCDRYGLYV VDEANIETHG
MVPMNRLTDD PRWLPAMSER VTRMVQRDRN HPSVIIWSLG NESGHGANHD ALYRWIKSVD
PSRPVQYEGG GADTTATDII CPMYARVDED QPFPAVPKWS IKKWLSLPGE TRPLILCEYA
HAMGNSLGGF AKYWQAFRQY PRLQGGFVWD WVDQSLIKYD ENGNPWSAYG GDFGDTPNDR
QFCMNGLVFA DRTPHPALTE AKHQQQFFQF RLSGQTIEVT SEYLFRHSDN ELLHWMVALD
GKPLASGEVP LDVAPQGKQL IELPELPQPE SAGQLWLTVR VVQPNATAWS EAGHISAWQQ
WRLAENLSVT LPAASHAIPH LTTSEMDFCI ELGNKRWQFN RQSGFLSQMW IGDKKQLLTP
LRDQFTRAPL DNDIGVSEAT RIDPNAWVER WKAAGHYQAE AALLQCTADT LADAVLITTA
HAWQHQGKTL FISRKTYRID GSGQMAITVD VEVASDTPHP ARIGLNCQLA QVAERVNWLG
LGPQENYPDR LTAACFDRWD LPLSDMYTPY VFPSENGLRC GTRELNYGPH QWRGDFQFNI
SRYSQQQLME TSHRHLLHAE EGTWLNIDGF HMGIGGDDSW SPSVSAEFQL SAGRYHYQLV
WCQK


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