Beta-galactosidase (P00722)

Identification
Name:Beta-galactosidase
Synonyms:
  • Beta-gal
  • Lactase
Gene Name:lacZ
Enzyme Class:
Biological Properties
General Function:Involved in beta-galactosidase activity
Specific Function:Hydrolysis of terminal non-reducing beta-D- galactose residues in beta-D-galactosides
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Galactan + 1.0Water ↔ 1.0D-Galactose + 1.0Galactan
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0alpha-Lactose + 1.0Water ↔ 1.0alpha-D-Glucose + 1.0D-Galactose
ReactionCard
1.0beta-D-Galactosyl-1,4-beta-D-glucosylceramide+1.0Thumb ↔ 1.0Glucosylceramide+1.0Thumb
1.0beta-D-Galactosyl-1,4-beta-D-glucosylceramide + 1.0Water ↔ 1.0Glucosylceramide + 1.0D-Galactose
ReactionCard
1.03-Ketolactose+1.0Thumb ↔ 1.03-Keto-beta-D-galactose+1.0Thumb
1.03-Ketolactose + 1.0Water ↔ 1.03-Keto-beta-D-galactose + 1.0b-D-Glucose
ReactionCard
1.0Lactose+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Lactose + 1.0Water ↔ 1.0D-Glucose + 1.0D-Galactose
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Beta-D-Glucose+1.0Thumb
1.0alpha-Lactose + 1.0Water → 1.0beta-D-Galactose + 1.0Beta-D-Glucose + 1.0b-D-Glucose
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0alpha-Lactose → 1.0D-Galactose + 1.0D-Glucose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB03345alpha-D-GlucoseMetaboCard
ECMDB00186alpha-LactoseMetaboCard
ECMDB00516b-D-GlucoseMetaboCard
ECMDB04025beta-D-GalactoseMetaboCard
ECMDB00143D-GalactoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB21653GalactanMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
beta-galactosidase complex
macromolecular complex
protein complex
Function
beta-galactosidase activity
binding
carbohydrate binding
catalytic activity
cation binding
galactosidase activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
ion binding
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b0344
Gene OrientationCounterclockwise
Centisome Percentage:7.81
Left Sequence End362455
Right Sequence End365529
Gene Sequence:
>3075 bp
ATGACCATGATTACGGATTCACTGGCCGTCGTTTTACAACGTCGTGACTGGGAAAACCCT
GGCGTTACCCAACTTAATCGCCTTGCAGCACATCCCCCTTTCGCCAGCTGGCGTAATAGC
GAAGAGGCCCGCACCGATCGCCCTTCCCAACAGTTGCGCAGCCTGAATGGCGAATGGCGC
TTTGCCTGGTTTCCGGCACCAGAAGCGGTGCCGGAAAGCTGGCTGGAGTGCGATCTTCCT
GAGGCCGATACTGTCGTCGTCCCCTCAAACTGGCAGATGCACGGTTACGATGCGCCCATC
TACACCAACGTGACCTATCCCATTACGGTCAATCCGCCGTTTGTTCCCACGGAGAATCCG
ACGGGTTGTTACTCGCTCACATTTAATGTTGATGAAAGCTGGCTACAGGAAGGCCAGACG
CGAATTATTTTTGATGGCGTTAACTCGGCGTTTCATCTGTGGTGCAACGGGCGCTGGGTC
GGTTACGGCCAGGACAGTCGTTTGCCGTCTGAATTTGACCTGAGCGCATTTTTACGCGCC
GGAGAAAACCGCCTCGCGGTGATGGTGCTGCGCTGGAGTGACGGCAGTTATCTGGAAGAT
CAGGATATGTGGCGGATGAGCGGCATTTTCCGTGACGTCTCGTTGCTGCATAAACCGACT
ACACAAATCAGCGATTTCCATGTTGCCACTCGCTTTAATGATGATTTCAGCCGCGCTGTA
CTGGAGGCTGAAGTTCAGATGTGCGGCGAGTTGCGTGACTACCTACGGGTAACAGTTTCT
TTATGGCAGGGTGAAACGCAGGTCGCCAGCGGCACCGCGCCTTTCGGCGGTGAAATTATC
GATGAGCGTGGTGGTTATGCCGATCGCGTCACACTACGTCTGAACGTCGAAAACCCGAAA
CTGTGGAGCGCCGAAATCCCGAATCTCTATCGTGCGGTGGTTGAACTGCACACCGCCGAC
GGCACGCTGATTGAAGCAGAAGCCTGCGATGTCGGTTTCCGCGAGGTGCGGATTGAAAAT
GGTCTGCTGCTGCTGAACGGCAAGCCGTTGCTGATTCGAGGCGTTAACCGTCACGAGCAT
CATCCTCTGCATGGTCAGGTCATGGATGAGCAGACGATGGTGCAGGATATCCTGCTGATG
AAGCAGAACAACTTTAACGCCGTGCGCTGTTCGCATTATCCGAACCATCCGCTGTGGTAC
ACGCTGTGCGACCGCTACGGCCTGTATGTGGTGGATGAAGCCAATATTGAAACCCACGGC
ATGGTGCCAATGAATCGTCTGACCGATGATCCGCGCTGGCTACCGGCGATGAGCGAACGC
GTAACGCGAATGGTGCAGCGCGATCGTAATCACCCGAGTGTGATCATCTGGTCGCTGGGG
AATGAATCAGGCCACGGCGCTAATCACGACGCGCTGTATCGCTGGATCAAATCTGTCGAT
CCTTCCCGCCCGGTGCAGTATGAAGGCGGCGGAGCCGACACCACGGCCACCGATATTATT
TGCCCGATGTACGCGCGCGTGGATGAAGACCAGCCCTTCCCGGCTGTGCCGAAATGGTCC
ATCAAAAAATGGCTTTCGCTACCTGGAGAGACGCGCCCGCTGATCCTTTGCGAATACGCC
CACGCGATGGGTAACAGTCTTGGCGGTTTCGCTAAATACTGGCAGGCGTTTCGTCAGTAT
CCCCGTTTACAGGGCGGCTTCGTCTGGGACTGGGTGGATCAGTCGCTGATTAAATATGAT
GAAAACGGCAACCCGTGGTCGGCTTACGGCGGTGATTTTGGCGATACGCCGAACGATCGC
CAGTTCTGTATGAACGGTCTGGTCTTTGCCGACCGCACGCCGCATCCAGCGCTGACGGAA
GCAAAACACCAGCAGCAGTTTTTCCAGTTCCGTTTATCCGGGCAAACCATCGAAGTGACC
AGCGAATACCTGTTCCGTCATAGCGATAACGAGCTCCTGCACTGGATGGTGGCGCTGGAT
GGTAAGCCGCTGGCAAGCGGTGAAGTGCCTCTGGATGTCGCTCCACAAGGTAAACAGTTG
ATTGAACTGCCTGAACTACCGCAGCCGGAGAGCGCCGGGCAACTCTGGCTCACAGTACGC
GTAGTGCAACCGAACGCGACCGCATGGTCAGAAGCCGGGCACATCAGCGCCTGGCAGCAG
TGGCGTCTGGCGGAAAACCTCAGTGTGACGCTCCCCGCCGCGTCCCACGCCATCCCGCAT
CTGACCACCAGCGAAATGGATTTTTGCATCGAGCTGGGTAATAAGCGTTGGCAATTTAAC
CGCCAGTCAGGCTTTCTTTCACAGATGTGGATTGGCGATAAAAAACAACTGCTGACGCCG
CTGCGCGATCAGTTCACCCGTGCACCGCTGGATAACGACATTGGCGTAAGTGAAGCGACC
CGCATTGACCCTAACGCCTGGGTCGAACGCTGGAAGGCGGCGGGCCATTACCAGGCCGAA
GCAGCGTTGTTGCAGTGCACGGCAGATACACTTGCTGATGCGGTGCTGATTACGACCGCT
CACGCGTGGCAGCATCAGGGGAAAACCTTATTTATCAGCCGGAAAACCTACCGGATTGAT
GGTAGTGGTCAAATGGCGATTACCGTTGATGTTGAAGTGGCGAGCGATACACCGCATCCG
GCGCGGATTGGCCTGAACTGCCAGCTGGCGCAGGTAGCAGAGCGGGTAAACTGGCTCGGA
TTAGGGCCGCAAGAAAACTATCCCGACCGCCTTACTGCCGCCTGTTTTGACCGCTGGGAT
CTGCCATTGTCAGACATGTATACCCCGTACGTCTTCCCGAGCGAAAACGGTCTGCGCTGC
GGGACGCGCGAATTGAATTATGGCCCACACCAGTGGCGCGGCGACTTCCAGTTCAACATC
AGCCGCTACAGTCAACAGCAACTGATGGAAACCAGCCATCGCCATCTGCTGCACGCGGAA
GAAGGCACATGGCTGAATATCGACGGTTTCCATATGGGGATTGGTGGCGACGACTCCTGG
AGCCCGTCAGTATCGGCGGAATTCCAGCTGAGCGCCGGTCGCTACCATTACCAGTTGGTC
TGGTGTCAAAAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:1024
Protein Molecular Weight:116482
Protein Theoretical pI:5
PDB File:1JZ2
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Beta-galactosidase
MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP
TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA
GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV
LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK
LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG
MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD
PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA
HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR
QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ
WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP
LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA
HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG
LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV
WCQK
References
External Links:
ResourceLink
Uniprot ID:P00722
Uniprot Name:BGAL_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674486
PDB ID:1JZ2
Ecogene ID:EG10527
Ecocyc:EG10527
ColiBase:b0344
Kegg Gene:b0344
EchoBASE ID:EB0522
CCDB:BGAL_ECOLI
BacMap:16128329
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Buchel, D. E., Gronenborn, B., Muller-Hill, B. (1980). "Sequence of the lactose permease gene." Nature 283:541-545. Pubmed: 6444453
  • Calos, M. P., Miller, J. H. (1980). "Molecular consequences of deletion formation mediated by the transposon Tn9." Nature 285:38-41. Pubmed: 6246435
  • Fowler, A. V., Smith, P. J. (1983). "The active site regions of lacZ and ebg beta-galactosidases are homologous." J Biol Chem 258:10204-10207. Pubmed: 6411710
  • Fowler, A. V., Zabin, I. (1978). "Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures and the complete sequence." J Biol Chem 253:5521-5525. Pubmed: 97298
  • Gebler, J. C., Aebersold, R., Withers, S. G. (1992). "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. Pubmed: 1350782
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Herrchen, M., Legler, G. (1984). "Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli." Eur J Biochem 138:527-531. Pubmed: 6420154
  • Huber, R. E., Hakda, S., Cheng, C., Cupples, C. G., Edwards, R. A. (2003). "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. Pubmed: 12578395
  • Huber, R. E., Hlede, I. Y., Roth, N. J., McKenzie, K. C., Ghumman, K. K. (2001). "His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state." Biochem Cell Biol 79:183-193. Pubmed: 11310566
  • Huber, R. E., Parfett, C., Woulfe-Flanagan, H., Thompson, D. J. (1979). "Interaction of divalent cations with beta-galactosidase (Escherichia coli)." Biochemistry 18:4090-4095. Pubmed: 114210
  • Jacobson, R. H., Zhang, X. J., DuBose, R. F., Matthews, B. W. (1994). "Three-dimensional structure of beta-galactosidase from E. coli." Nature 369:761-766. Pubmed: 8008071
  • Jobe, A., Bourgeois, S. (1972). "lac Repressor-operator interaction. VI. The natural inducer of the lac operon." J Mol Biol 69:397-408. Pubmed: 4562709
  • Juers, D. H., Hakda, S., Matthews, B. W., Huber, R. E. (2003). "Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase." Biochemistry 42:13505-13511. Pubmed: 14621996
  • Juers, D. H., Heightman, T. D., Vasella, A., McCarter, J. D., Mackenzie, L., Withers, S. G., Matthews, B. W. (2001). "A structural view of the action of Escherichia coli (lacZ) beta-galactosidase." Biochemistry 40:14781-14794. Pubmed: 11732897
  • Juers, D. H., Jacobson, R. H., Wigley, D., Zhang, X. J., Huber, R. E., Tronrud, D. E., Matthews, B. W. (2000). "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. Pubmed: 11045615
  • Kalnins, A., Otto, K., Ruther, U., Muller-Hill, B. (1983). "Sequence of the lacZ gene of Escherichia coli." EMBO J 2:593-597. Pubmed: 6313347
  • Martinez-Bilbao, M., Gaunt, M. T., Huber, R. E. (1995). "E461H-beta-galactosidase (Escherichia coli): altered divalent metal specificity and slow but reversible metal inactivation." Biochemistry 34:13437-13442. Pubmed: 7577931
  • Matthews, B. W. (2005). "The structure of E. coli beta-galactosidase." C R Biol 328:549-556. Pubmed: 15950161
  • Roth, N. J., Huber, R. E. (1996). "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. Pubmed: 8662937
  • Roth, N. J., Rob, B., Huber, R. E. (1998). "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. Pubmed: 9665715
  • Sutendra, G., Wong, S., Fraser, M. E., Huber, R. E. (2007). "Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site." Biochem Biophys Res Commun 352:566-570. Pubmed: 17126292
  • Xu, J., McRae, M. A., Harron, S., Rob, B., Huber, R. E. (2004). "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. Pubmed: 15060622