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 27-MAR-2024, entry version 220. 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; Pseudomonadota; 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8BK7; EM; 3.30 A; A/B/C/D=1-1024. DR PDB; 8BK8; EM; 2.90 A; A/B/C/D=1-1024. DR PDB; 8BKG; EM; 3.20 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 PDBsum; 8BK7; -. DR PDBsum; 8BK8; -. DR PDBsum; 8BKG; -. DR AlphaFoldDB; P00722; -. DR EMDB; EMD-10563; -. DR EMDB; EMD-10564; -. DR EMDB; EMD-10574; -. DR EMDB; EMD-16091; -. DR EMDB; EMD-16092; -. DR EMDB; EMD-16097; -. DR EMDB; EMD-21995; -. DR EMDB; EMD-2548; -. DR EMDB; EMD-2824; -. DR EMDB; EMD-2984; -. DR EMDB; EMD-5995; -. DR EMDB; EMD-7770; -. DR EMDB; EMD-8908; -. DR PCDDB; P00722; -. DR SMR; P00722; -. DR BioGRID; 849400; 1. 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; 511145-b0344; -. DR ABCD; P00722; 6 sequenced antibodies. DR EnsemblBacteria; AAC73447; AAC73447; b0344. 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; EITDFCH; -. DR OrthoDB; 9758603at2; -. DR PhylomeDB; P00722; -. DR BioCyc; EcoCyc:BETAGALACTOSID-MONOMER; -. DR BioCyc; MetaCyc:BETAGALACTOSID-MONOMER; -. DR BRENDA; 3.2.1.23; 2026. DR SABIO-RK; P00722; -. DR EvolutionaryTrace; P00722; -. DR PHI-base; PHI:6268; -. DR PHI-base; PHI:9897; -. 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:CACAO. DR Gene3D; 2.70.98.10; -; 1. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. 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 PANTHER; PTHR46323; BETA-GALACTOSIDASE; 1. DR PANTHER; PTHR46323:SF2; BETA-GALACTOSIDASE; 1. DR Pfam; PF02929; Bgal_small_N; 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 Pfam; PF16353; LacZ_4; 1. DR PRINTS; PR00132; GLHYDRLASE2. DR SMART; SM01038; Bgal_small_N; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 2. DR SUPFAM; SSF74650; Galactose mutarotase-like; 1. DR SUPFAM; SSF49785; Galactose-binding domain-like; 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:8BK8" 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 STRAND 605..608 FT /evidence="ECO:0007829|PDB:8BKG" 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 //