BGAL_ECOLI
ID BGAL_ECOLI Reviewed; 1024 AA.
AC P00722; Q2MC80;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Beta-galactosidase;
DE Short=Beta-gal;
DE EC=3.2.1.23;
DE AltName: Full=Lactase;
GN Name=lacZ; OrderedLocusNames=b0344, JW0335;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6313347; DOI=10.1002/j.1460-2075.1983.tb01468.x;
RA Kalnins A., Otto K., Ruether U., Mueller-Hill B.;
RT "Sequence of the lacZ gene of Escherichia coli.";
RL EMBO J. 2:593-597(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-1024.
RX PubMed=97298; DOI=10.1016/s0021-9258(17)30405-2;
RA Fowler A.V., Zabin I.;
RT "Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures
RT and the complete sequence.";
RL J. Biol. Chem. 253:5521-5525(1978).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 356-476.
RX PubMed=6246435; DOI=10.1038/285038a0;
RA Calos M.P., Miller J.H.;
RT "Molecular consequences of deletion formation mediated by the transposon
RT Tn9.";
RL Nature 285:38-41(1980).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1008-1024.
RX PubMed=6444453; DOI=10.1038/283541a0;
RA Buechel D.E., Gronenborn B., Mueller-Hill B.;
RT "Sequence of the lactose permease gene.";
RL Nature 283:541-545(1980).
RN [8]
RP INDUCTION BY ALLOLACTOSE.
RX PubMed=4562709; DOI=10.1016/0022-2836(72)90253-7;
RA Jobe A., Bourgeois S.;
RT "lac repressor-operator interaction. VI. The natural inducer of the lac
RT operon.";
RL J. Mol. Biol. 69:397-408(1972).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RX PubMed=114210; DOI=10.1021/bi00586a005;
RA Huber R.E., Parfett C., Woulfe-Flanagan H., Thompson D.J.;
RT "Interaction of divalent cations with beta-galactosidase (Escherichia
RT coli).";
RL Biochemistry 18:4090-4095(1979).
RN [10]
RP ACTIVE SITE REGIONS.
RX PubMed=6411710; DOI=10.1016/s0021-9258(17)44440-1;
RA Fowler A.V., Smith P.J.;
RT "The active site regions of lacZ and ebg beta-galactosidases are
RT homologous.";
RL J. Biol. Chem. 258:10204-10207(1983).
RN [11]
RP ACTIVE SITE GLU-462.
RX PubMed=6420154; DOI=10.1111/j.1432-1033.1984.tb07947.x;
RA Herrchen M., Legler G.;
RT "Identification of an essential carboxylate group at the active site of
RT lacZ beta-galactosidase from Escherichia coli.";
RL Eur. J. Biochem. 138:527-531(1984).
RN [12]
RP ACTIVE SITE GLU-538.
RX PubMed=1350782; DOI=10.1016/s0021-9258(19)49884-0;
RA Gebler J.C., Aebersold R., Withers S.G.;
RT "Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z)
RT beta-galactosidase from Escherichia coli.";
RL J. Biol. Chem. 267:11126-11130(1992).
RN [13]
RP MUTAGENESIS OF GLU-462, AND COFACTOR.
RX PubMed=7577931; DOI=10.1021/bi00041a022;
RA Martinez-Bilbao M., Gaunt M.T., Huber R.E.;
RT "E461H-beta-galactosidase (Escherichia coli): altered divalent metal
RT specificity and slow but reversible metal inactivation.";
RL Biochemistry 34:13437-13442(1995).
RN [14]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-541.
RX PubMed=8662937; DOI=10.1074/jbc.271.24.14296;
RA Roth N.J., Huber R.E.;
RT "The beta-galactosidase (Escherichia coli) reaction is partly facilitated
RT by interactions of His-540 with the C6 hydroxyl of galactose.";
RL J. Biol. Chem. 271:14296-14301(1996).
RN [15]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [16]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-358.
RX PubMed=9665715; DOI=10.1021/bi972796t;
RA Roth N.J., Rob B., Huber R.E.;
RT "His-357 of beta-galactosidase (Escherichia coli) interacts with the C3
RT hydroxyl in the transition state and helps to mediate catalysis.";
RL Biochemistry 37:10099-10107(1998).
RN [17]
RP MUTAGENESIS OF HIS-392.
RX PubMed=11310566; DOI=10.1139/o00-101;
RA Huber R.E., Hlede I.Y., Roth N.J., McKenzie K.C., Ghumman K.K.;
RT "His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by
RT strong interactions with the transition state.";
RL Biochem. Cell Biol. 79:183-193(2001).
RN [18]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TRP-1000.
RX PubMed=12578395; DOI=10.1021/bi0270642;
RA Huber R.E., Hakda S., Cheng C., Cupples C.G., Edwards R.A.;
RT "Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for
RT binding, catalysis, and synthesis of allolactose, the natural lac operon
RT inducer.";
RL Biochemistry 42:1796-1803(2003).
RN [19]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-202.
RX PubMed=15060622; DOI=10.1139/o04-004;
RA Xu J., McRae M.A., Harron S., Rob B., Huber R.E.;
RT "A study of the relationships of interactions between Asp-201, Na+ or K+,
RT and galactosyl C6 hydroxyl and their effects on binding and reactivity of
RT beta-galactosidase.";
RL Biochem. Cell Biol. 82:275-284(2004).
RN [20]
RP REVIEW.
RX PubMed=15950161; DOI=10.1016/j.crvi.2005.03.006;
RA Matthews B.W.;
RT "The structure of E. coli beta-galactosidase.";
RL C. R. Biol. 328:549-556(2005).
RN [21]
RP COFACTOR, AND MUTAGENESIS OF GLU-798.
RX PubMed=17126292; DOI=10.1016/j.bbrc.2006.11.061;
RA Sutendra G., Wong S., Fraser M.E., Huber R.E.;
RT "Beta-galactosidase (Escherichia coli) has a second catalytically important
RT Mg2+ site.";
RL Biochem. Biophys. Res. Commun. 352:566-570(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS, AND
RP SUBUNIT.
RX PubMed=8008071; DOI=10.1038/369761a0;
RA Jacobson R.H., Zhang X.-J., Dubose R.F., Matthews B.W.;
RT "Three-dimensional structure of beta-galactosidase from E. coli.";
RL Nature 369:761-766(1994).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND SODIUM
RP IONS.
RX PubMed=11045615; DOI=10.1110/ps.9.9.1685;
RA Juers D.H., Jacobson R.H., Wigley D., Zhang X.-J., Huber R.E.,
RA Tronrud D.E., Matthews B.W.;
RT "High resolution refinement of beta-galactosidase in a new crystal form
RT reveals multiple metal-binding sites and provides a structural basis for
RT alpha-complementation.";
RL Protein Sci. 9:1685-1699(2000).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP MUTAGENESIS OF GLU-538 AND PHE-602, AND REACTION MECHANISM.
RX PubMed=11732897; DOI=10.1021/bi011727i;
RA Juers D.H., Heightman T.D., Vasella A., McCarter J.D., Mackenzie L.,
RA Withers S.G., Matthews B.W.;
RT "A structural view of the action of Escherichia coli (lacZ) beta-
RT galactosidase.";
RL Biochemistry 40:14781-14794(2001).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-1024 OF MUTANT ALA-795 IN
RP COMPLEX WITH MAGNESIUM IONS, SODIUM IONS AND SUBSTRATE ANALOGS,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP GLY-795.
RX PubMed=14621996; DOI=10.1021/bi035506j;
RA Juers D.H., Hakda S., Matthews B.W., Huber R.E.;
RT "Structural basis for the altered activity of Gly794 variants of
RT Escherichia coli beta-galactosidase.";
RL Biochemistry 42:13505-13511(2003).
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;
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 2 magnesium ions per monomer. Can also use manganese.;
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Note=Binds 1 sodium ion per monomer.;
CC -!- ACTIVITY REGULATION: Inhibited by phenylethyl thio-beta-D-galactoside
CC (PETG), isopropyl thio-beta-D-galactoside (IPTG), L-ribose, D-
CC galactonolactone, lactose and 2-amino-D-galactose.
CC {ECO:0000269|PubMed:14621996}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.04 mM for p-nitrophenyl beta-D-galactoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=0.12 mM for o-nitrophenyl beta-D-galactoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=0.15 mM for 2,3-dinitrophenyl beta-D-galactopyranoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=0.41 mM for 2,5-dinitrophenyl beta-D-galactopyranoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=11.6 mM for p-nitrophenol-alpha-L-arabinopyranoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=16.9 mM for p-nitrophenol-beta-D-fucopyranoside
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=34 uM for p-nitrophenyl beta-D-galactoside (with magnesium as
CC cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210,
CC ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
CC ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
CC ECO:0000269|PubMed:9665715};
CC KM=140 uM for o-nitrophenyl beta-D-galactoside (with magnesium as
CC cofactor and 30 degrees Celsius) {ECO:0000269|PubMed:114210,
CC ECO:0000269|PubMed:12578395, ECO:0000269|PubMed:14621996,
CC ECO:0000269|PubMed:15060622, ECO:0000269|PubMed:8662937,
CC ECO:0000269|PubMed:9665715};
CC KM=940 uM for allolactose (with magnesium as cofactor and 30 degrees
CC Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC KM=1350 uM for lactose (with magnesium as cofactor and 30 degrees
CC Celsius) {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC Vmax=30.9 umol/min/mg enzyme with lactose as substrate (with
CC magnesium as cofactor and 30 degrees Celsius)
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC Vmax=49.7 umol/min/mg enzyme with allolactose as substrate (with
CC magnesium as cofactor and 30 degrees Celsius)
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC Vmax=59.7 umol/min/mg enzyme with p-nitrophenyl beta-D-galactoside as
CC substrate (with magnesium as cofactor and 30 degrees Celsius)
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC Vmax=360 umol/min/mg enzyme with o-nitrophenyl beta-D-galactoside as
CC substrate (with magnesium as cofactor and 30 degrees Celsius)
CC {ECO:0000269|PubMed:114210, ECO:0000269|PubMed:12578395,
CC ECO:0000269|PubMed:14621996, ECO:0000269|PubMed:15060622,
CC ECO:0000269|PubMed:8662937, ECO:0000269|PubMed:9665715};
CC Note=The values for the enzymatic assays using manganese as cofactor
CC are very close.;
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11045615,
CC ECO:0000269|PubMed:11732897, ECO:0000269|PubMed:14621996,
CC ECO:0000269|PubMed:8008071}.
CC -!- INTERACTION:
CC P00722; P00722: lacZ; NbExp=3; IntAct=EBI-369998, EBI-369998;
CC -!- INDUCTION: By allolactose. {ECO:0000269|PubMed:4562709}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC URL="https://www.worthington-biochem.com/BG/";
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DR EMBL; J01636; AAA24053.1; -; Genomic_DNA.
DR EMBL; V00296; CAA23573.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18068.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73447.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76126.1; -; Genomic_DNA.
DR EMBL; V00295; CAA23570.1; -; Genomic_DNA.
DR PIR; A90981; GBEC.
DR RefSeq; NP_414878.1; NC_000913.3.
DR RefSeq; WP_000177906.1; NZ_SSZK01000061.1.
DR PDB; 1DP0; X-ray; 1.70 A; A/B/C/D=10-1024.
DR PDB; 1F4A; X-ray; 2.80 A; A/B/C/D=4-1024.
DR PDB; 1F4H; X-ray; 2.80 A; A/B/C/D=4-1024.
DR PDB; 1HN1; X-ray; 3.00 A; A/B/C/D=10-1024.
DR PDB; 1JYN; X-ray; 1.80 A; A/B/C/D=10-1024.
DR PDB; 1JYV; X-ray; 1.75 A; A/B/C/D=10-1024.
DR PDB; 1JYW; X-ray; 1.55 A; A/B/C/D=10-1024.
DR PDB; 1JYX; X-ray; 1.75 A; A/B/C/D=10-1024.
DR PDB; 1JZ2; X-ray; 2.10 A; A/B/C/D=2-1024.
DR PDB; 1JZ3; X-ray; 1.75 A; A/B/C/D=10-1024.
DR PDB; 1JZ4; X-ray; 2.10 A; A/B/C/D=10-1024.
DR PDB; 1JZ5; X-ray; 1.80 A; A/B/C/D=10-1024.
DR PDB; 1JZ6; X-ray; 2.10 A; A/B/C/D=10-1024.
DR PDB; 1JZ7; X-ray; 1.50 A; A/B/C/D=10-1024.
DR PDB; 1JZ8; X-ray; 1.50 A; A/B/C/D=10-1024.
DR PDB; 1PX3; X-ray; 1.60 A; A/B/C/D=10-1024.
DR PDB; 1PX4; X-ray; 1.60 A; A/B/C/D=10-1024.
DR PDB; 3CZJ; X-ray; 2.05 A; A/B/C/D=10-1024.
DR PDB; 3DYM; X-ray; 2.05 A; A/B/C/D=10-1024.
DR PDB; 3DYO; X-ray; 1.80 A; A/B/C/D=10-1024.
DR PDB; 3DYP; X-ray; 1.75 A; A/B/C/D=10-1024.
DR PDB; 3E1F; X-ray; 3.00 A; 1/2/3/4=10-1024.
DR PDB; 3I3B; X-ray; 2.20 A; A/B/C/D=10-1024.
DR PDB; 3I3D; X-ray; 2.20 A; A/B/C/D=10-1024.
DR PDB; 3I3E; X-ray; 2.10 A; A/B/C/D=10-1024.
DR PDB; 3IAP; X-ray; 2.00 A; A/B/C/D=10-1024.
DR PDB; 3IAQ; X-ray; 2.70 A; A/B/C/D=10-1024.
DR PDB; 3J7H; EM; 3.20 A; A/B/C/D=1-1024.
DR PDB; 3MUY; X-ray; 2.50 A; 1/2/3/4=10-1024.
DR PDB; 3MUZ; X-ray; 1.90 A; 1/2/3/4=10-1024.
DR PDB; 3MV0; X-ray; 2.20 A; 1/2/3/4=10-1024.
DR PDB; 3MV1; X-ray; 2.20 A; 1/2/3/4=10-1024.
DR PDB; 3SEP; X-ray; 2.05 A; A/B/C/D=10-1024.
DR PDB; 3T08; X-ray; 2.00 A; A/B/C/D=10-1024.
DR PDB; 3T09; X-ray; 1.75 A; A/B/C/D=10-1024.
DR PDB; 3T0A; X-ray; 1.90 A; A/B/C/D=10-1024.
DR PDB; 3T0B; X-ray; 2.40 A; A/B/C/D=10-1024.
DR PDB; 3T0D; X-ray; 1.93 A; A/B/C/D=10-1024.
DR PDB; 3T2O; X-ray; 1.85 A; A/B/C/D=10-1024.
DR PDB; 3T2P; X-ray; 2.60 A; A/B/C/D=10-1024.
DR PDB; 3T2Q; X-ray; 2.40 A; A/B/C/D=10-1024.
DR PDB; 3VD3; X-ray; 2.80 A; A/B/C/D=10-1024.
DR PDB; 3VD4; X-ray; 2.00 A; A/B/C/D=10-1024.
DR PDB; 3VD5; X-ray; 2.70 A; A/B/C/D=10-1024.
DR PDB; 3VD7; X-ray; 2.87 A; A/B/C/D=10-1024.
DR PDB; 3VD9; X-ray; 2.05 A; A/B/C/D=10-1024.
DR PDB; 3VDA; X-ray; 2.50 A; A/B/C/D=10-1024.
DR PDB; 3VDB; X-ray; 2.05 A; A/B/C/D=10-1024.
DR PDB; 3VDC; X-ray; 2.55 A; A/B/C/D=10-1024.
DR PDB; 4CKD; EM; 13.00 A; A/B/C/D=1-1024.
DR PDB; 4DUV; X-ray; 2.10 A; A/B/C/D=10-1024.
DR PDB; 4DUW; X-ray; 2.20 A; A/B/C/D=10-1024.
DR PDB; 4DUX; X-ray; 2.30 A; A/B/C/D=10-1024.
DR PDB; 4TTG; X-ray; 1.60 A; A/B/C/D=15-1024.
DR 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.
DR 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.
DR 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.
DR 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.
DR PDB; 5A1A; EM; 2.20 A; A/B/C/D=3-1024.
DR PDB; 6CVM; EM; 1.90 A; A/B/C/D=3-1023.
DR PDB; 6DRV; EM; 2.20 A; A/B/C/D=1-1024.
DR PDB; 6KUZ; X-ray; 2.83 A; A/B/C/D=1-1024.
DR PDB; 6TSH; EM; 2.30 A; A/B/C/D=10-1024.
DR PDB; 6TSK; EM; 2.30 A; A/B/C/D=10-1024.
DR PDB; 6TTE; EM; 2.20 A; A/B/C/D=10-1024.
DR PDB; 6X1Q; EM; 1.80 A; A/B/C/D=3-1023.
DR PDB; 7BRS; X-ray; 2.67 A; A/B/C/D=1-1024.
DR PDB; 7BTK; X-ray; 2.70 A; A/B/C/D=1-1024.
DR PDBsum; 1DP0; -.
DR PDBsum; 1F4A; -.
DR PDBsum; 1F4H; -.
DR PDBsum; 1HN1; -.
DR PDBsum; 1JYN; -.
DR PDBsum; 1JYV; -.
DR PDBsum; 1JYW; -.
DR PDBsum; 1JYX; -.
DR PDBsum; 1JZ2; -.
DR PDBsum; 1JZ3; -.
DR PDBsum; 1JZ4; -.
DR PDBsum; 1JZ5; -.
DR PDBsum; 1JZ6; -.
DR PDBsum; 1JZ7; -.
DR PDBsum; 1JZ8; -.
DR PDBsum; 1PX3; -.
DR PDBsum; 1PX4; -.
DR PDBsum; 3CZJ; -.
DR PDBsum; 3DYM; -.
DR PDBsum; 3DYO; -.
DR PDBsum; 3DYP; -.
DR PDBsum; 3E1F; -.
DR PDBsum; 3I3B; -.
DR PDBsum; 3I3D; -.
DR PDBsum; 3I3E; -.
DR PDBsum; 3IAP; -.
DR PDBsum; 3IAQ; -.
DR PDBsum; 3J7H; -.
DR PDBsum; 3MUY; -.
DR PDBsum; 3MUZ; -.
DR PDBsum; 3MV0; -.
DR PDBsum; 3MV1; -.
DR PDBsum; 3SEP; -.
DR PDBsum; 3T08; -.
DR PDBsum; 3T09; -.
DR PDBsum; 3T0A; -.
DR PDBsum; 3T0B; -.
DR PDBsum; 3T0D; -.
DR PDBsum; 3T2O; -.
DR PDBsum; 3T2P; -.
DR PDBsum; 3T2Q; -.
DR PDBsum; 3VD3; -.
DR PDBsum; 3VD4; -.
DR PDBsum; 3VD5; -.
DR PDBsum; 3VD7; -.
DR PDBsum; 3VD9; -.
DR PDBsum; 3VDA; -.
DR PDBsum; 3VDB; -.
DR PDBsum; 3VDC; -.
DR PDBsum; 4CKD; -.
DR PDBsum; 4DUV; -.
DR PDBsum; 4DUW; -.
DR PDBsum; 4DUX; -.
DR PDBsum; 4TTG; -.
DR PDBsum; 4V40; -.
DR PDBsum; 4V41; -.
DR PDBsum; 4V44; -.
DR PDBsum; 4V45; -.
DR PDBsum; 5A1A; -.
DR PDBsum; 6CVM; -.
DR PDBsum; 6DRV; -.
DR PDBsum; 6KUZ; -.
DR PDBsum; 6TSH; -.
DR PDBsum; 6TSK; -.
DR PDBsum; 6TTE; -.
DR PDBsum; 6X1Q; -.
DR PDBsum; 7BRS; -.
DR PDBsum; 7BTK; -.
DR AlphaFoldDB; P00722; -.
DR PCDDB; P00722; -.
DR SMR; P00722; -.
DR DIP; DIP-10081N; -.
DR IntAct; P00722; 76.
DR STRING; 511145.b0344; -.
DR BindingDB; P00722; -.
DR ChEMBL; CHEMBL4603; -.
DR DrugBank; DB02294; (5R,6S,7S,8S)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-A]piperidine.
DR DrugBank; DB01920; 1-O-[O-Nitrophenyl]-Beta-D-Galactopyranose.
DR DrugBank; DB02228; 2-deoxy-2-fluoro-Beta-D-galactose.
DR DrugBank; DB04382; 2-Deoxy-alpha-D-galactopyranose.
DR DrugBank; DB04155; 2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-Glucopyranose.
DR DrugBank; DB02632; 4-nitrophenyl-beta-D-galactoside.
DR DrugBank; DB04116; Allolactose.
DR DrugBank; DB01885; D-Galctopyranosyl-1-On.
DR DrugBank; DB01862; Isopropyl beta-D-thiogalactopyranoside.
DR DrugBank; DB04465; Lactose.
DR DrugBank; DB04530; S,S-(2-Hydroxyethyl)Thiocysteine.
DR DrugBank; DB13503; Tyrothricin.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR PaxDb; P00722; -.
DR PRIDE; P00722; -.
DR ABCD; P00722; 6 sequenced antibodies.
DR EnsemblBacteria; AAC73447; AAC73447; b0344.
DR EnsemblBacteria; BAE76126; BAE76126; BAE76126.
DR GeneID; 945006; -.
DR KEGG; ecj:JW0335; -.
DR KEGG; eco:b0344; -.
DR EchoBASE; EB0522; -.
DR eggNOG; COG3250; Bacteria.
DR HOGENOM; CLU_002346_0_2_6; -.
DR InParanoid; P00722; -.
DR OMA; SNWQLQG; -.
DR PhylomeDB; P00722; -.
DR BioCyc; EcoCyc:BETAGALACTOSID-MON; -.
DR BioCyc; MetaCyc:BETAGALACTOSID-MON; -.
DR BRENDA; 3.2.1.23; 2026.
DR SABIO-RK; P00722; -.
DR EvolutionaryTrace; P00722; -.
DR PHI-base; PHI:6268; -.
DR PRO; PR:P00722; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009341; C:beta-galactosidase complex; IDA:EcoCyc.
DR GO; GO:0031420; F:alkali metal ion binding; IDA:EcoCyc.
DR GO; GO:0004565; F:beta-galactosidase activity; IDA:EcoCyc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0005990; P:lactose catabolic process; IMP:EcoCyc.
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 3D-structure; Direct protein sequencing; Glycosidase; Hydrolase; Magnesium;
KW Manganese; Metal-binding; Reference proteome; Sodium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:97298"
FT CHAIN 2..1024
FT /note="Beta-galactosidase"
FT /id="PRO_0000057650"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:6420154"
FT ACT_SITE 538
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:1350782"
FT BINDING 103
FT /ligand="substrate"
FT BINDING 202
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 202
FT /ligand="substrate"
FT BINDING 417
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11045615"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11045615"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11045615"
FT BINDING 462
FT /ligand="substrate"
FT BINDING 538..541
FT /ligand="substrate"
FT BINDING 598
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11045615"
FT BINDING 602
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 605
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT BINDING 605
FT /ligand="substrate"
FT BINDING 1000
FT /ligand="substrate"
FT SITE 358
FT /note="Transition state stabilizer"
FT SITE 392
FT /note="Transition state stabilizer"
FT SITE 1000
FT /note="Important for ensuring that an appropriate
FT proportion of lactose is converted to allolactose"
FT MUTAGEN 202
FT /note="D->E,N: Causes a significant decrease in binding
FT affinity in the absence of monovalent cations or in the
FT presence of potassium ions, but only a moderate decrease in
FT the presence of sodium ions."
FT /evidence="ECO:0000269|PubMed:15060622"
FT MUTAGEN 202
FT /note="D->F: Obliterates all binding and catalysis."
FT /evidence="ECO:0000269|PubMed:15060622"
FT MUTAGEN 358
FT /note="H->D,F,L,N: Less stable to heat than wild-type.
FT Causes significant destabilizations of the first transition
FT state."
FT /evidence="ECO:0000269|PubMed:9665715"
FT MUTAGEN 392
FT /note="H->E,F,K: Essentially inactive unless very rapid
FT purification. Causes very large destabilizations of the
FT transition state."
FT /evidence="ECO:0000269|PubMed:11310566"
FT MUTAGEN 462
FT /note="E->H: Slowly inactivates galactosidase activity by
FT reducing the binding of magnesium. It increases binding
FT specificity."
FT /evidence="ECO:0000269|PubMed:7577931"
FT MUTAGEN 538
FT /note="E->Q: 10000-fold decrease in the beta-galactosidase
FT activity."
FT /evidence="ECO:0000269|PubMed:11732897"
FT MUTAGEN 541
FT /note="H->E,F,N: Poorly reactive with galactosyl
FT substrates. Less stable to heat than wild-type."
FT /evidence="ECO:0000269|PubMed:8662937"
FT MUTAGEN 602
FT /note="F->A: Decreases the stability of the loop 794-804."
FT /evidence="ECO:0000269|PubMed:11732897"
FT MUTAGEN 795
FT /note="G->A: It forces the apoenzyme to adopt the closed
FT rather than the open conformation. Reduces the binding
FT affinity."
FT /evidence="ECO:0000269|PubMed:14621996"
FT MUTAGEN 798
FT /note="E->A,L: The catalytic efficiency is not increased,
FT when the sodium concentration increases."
FT /evidence="ECO:0000269|PubMed:17126292"
FT MUTAGEN 798
FT /note="E->D,Q: Small increase of the catalytic efficiency,
FT when the sodium concentration increases."
FT /evidence="ECO:0000269|PubMed:17126292"
FT MUTAGEN 1000
FT /note="W->F,G,L,T: Decreases affinity for substrate."
FT /evidence="ECO:0000269|PubMed:12578395"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:6X1Q"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3T09"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:3J7H"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 220..232
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 236..249
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 266..275
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3MUZ"
FT STRAND 289..298
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 310..318
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:3IAQ"
FT STRAND 323..331
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 397..406
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 424..429
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 434..448
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 454..458
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 461..463
FT /evidence="ECO:0007829|PDB:1JYW"
FT HELIX 467..479
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:5A1A"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:1JZ6"
FT HELIX 550..559
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 563..569
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:7BRS"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:6CVM"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 590..593
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 617..624
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 627..633
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 636..641
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 652..659
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 662..670
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 691..703
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 708..710
FT /evidence="ECO:0007829|PDB:1JZ8"
FT STRAND 714..726
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 740..743
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 745..752
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 755..760
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 761..763
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 765..771
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 777..784
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 791..794
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:1PX4"
FT STRAND 804..806
FT /evidence="ECO:0007829|PDB:3J7H"
FT HELIX 807..814
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 815..818
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 820..830
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 832..845
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 848..860
FT /evidence="ECO:0007829|PDB:1JZ7"
FT TURN 861..863
FT /evidence="ECO:0007829|PDB:1F4H"
FT STRAND 865..873
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:5A1A"
FT STRAND 881..890
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 894..904
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 915..922
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 923..926
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 939..947
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 950..963
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 965..970
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 974..976
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 981..991
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 999..1001
FT /evidence="ECO:0007829|PDB:1JZ7"
FT HELIX 1006..1008
FT /evidence="ECO:0007829|PDB:1JZ7"
FT STRAND 1013..1022
FT /evidence="ECO:0007829|PDB:1JZ7"
SQ 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
