Beta-galactosidase

Details

Name
Beta-galactosidase
Kind
protein
Synonyms
  • 3.2.1.23
  • Beta-gal
  • Lactase
Gene Name
lacZ
UniProtKB Entry
P00722Swiss-Prot
Organism
Escherichia coli (strain K12)
NCBI Taxonomy ID
83333
Amino acid sequence
>lcl|BSEQ0019112|Beta-galactosidase
MTMITDSLAVVLQRRDWENPGVTQLNRLAAHPPFASWRNSEEARTDRPSQQLRSLNGEWR
FAWFPAPEAVPESWLECDLPEADTVVVPSNWQMHGYDAPIYTNVTYPITVNPPFVPTENP
TGCYSLTFNVDESWLQEGQTRIIFDGVNSAFHLWCNGRWVGYGQDSRLPSEFDLSAFLRA
GENRLAVMVLRWSDGSYLEDQDMWRMSGIFRDVSLLHKPTTQISDFHVATRFNDDFSRAV
LEAEVQMCGELRDYLRVTVSLWQGETQVASGTAPFGGEIIDERGGYADRVTLRLNVENPK
LWSAEIPNLYRAVVELHTADGTLIEAEACDVGFREVRIENGLLLLNGKPLLIRGVNRHEH
HPLHGQVMDEQTMVQDILLMKQNNFNAVRCSHYPNHPLWYTLCDRYGLYVVDEANIETHG
MVPMNRLTDDPRWLPAMSERVTRMVQRDRNHPSVIIWSLGNESGHGANHDALYRWIKSVD
PSRPVQYEGGGADTTATDIICPMYARVDEDQPFPAVPKWSIKKWLSLPGETRPLILCEYA
HAMGNSLGGFAKYWQAFRQYPRLQGGFVWDWVDQSLIKYDENGNPWSAYGGDFGDTPNDR
QFCMNGLVFADRTPHPALTEAKHQQQFFQFRLSGQTIEVTSEYLFRHSDNELLHWMVALD
GKPLASGEVPLDVAPQGKQLIELPELPQPESAGQLWLTVRVVQPNATAWSEAGHISAWQQ
WRLAENLSVTLPAASHAIPHLTTSEMDFCIELGNKRWQFNRQSGFLSQMWIGDKKQLLTP
LRDQFTRAPLDNDIGVSEATRIDPNAWVERWKAAGHYQAEAALLQCTADTLADAVLITTA
HAWQHQGKTLFISRKTYRIDGSGQMAITVDVEVASDTPHPARIGLNCQLAQVAERVNWLG
LGPQENYPDRLTAACFDRWDLPLSDMYTPYVFPSENGLRCGTRELNYGPHQWRGDFQFNI
SRYSQQQLMETSHRHLLHAEEGTWLNIDGFHMGIGGDDSWSPSVSAEFQLSAGRYHYQLV
WCQK
Number of residues
1024
Molecular Weight
116482.045
Theoretical pI
5.2
GO Classification
Functions
alkali metal ion binding / beta-galactosidase activity / carbohydrate binding / magnesium ion binding
Processes
lactose catabolic process
Components
beta-galactosidase complex
General Function
Not Available
Specific Function
alkali metal ion binding
Pfam Domain Function
Signal Regions
Not Available
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0019113|Beta-galactosidase (lacZ)
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
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00722
UniProtKB Entry NameBGAL_ECOLI
GenBank Protein ID146577
GenBank Gene IDJ01636
PDB ID(s)1DP0, 1F4A, 1F4H, 1HN1, 1JYN, 1JYV, 1JYW, 1JYX, 1JZ2, 1JZ3, 1JZ4, 1JZ5, 1JZ6, 1JZ7, 1JZ8, 1PX3, 1PX4, 3CZJ, 3DYM, 3DYO, 3DYP, 3E1F, 3I3B, 3I3D, 3I3E, 3IAP, 3IAQ, 3J7H, 3MUY, 3MUZ, 3MV0, 3MV1, 3SEP, 3T08, 3T09, 3T0A, 3T0B, 3T0D, 3T2O, 3T2P, 3T2Q, 3VD3, 3VD4, 3VD5, 3VD7, 3VD9, 3VDA, 3VDB, 3VDC, 4CKD, 4DUV, 4DUW, 4DUX, 4TTG, 4V40, 4V41, 4V44, 4V45, 5A1A
KEGG IDecj:JW0335
NCBI Gene ID945006
General References
  1. Kalnins A, Otto K, Ruther U, Muller-Hill B: Sequence of the lacZ gene of Escherichia coli. EMBO J. 1983;2(4):593-7. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Fowler AV, Zabin I: Amino acid sequence of beta-galactosidase. XI. Peptide ordering procedures and the complete sequence. J Biol Chem. 1978 Aug 10;253(15):5521-5. [Article]
  5. Calos MP, Miller JH: Molecular consequences of deletion formation mediated by the transposon Tn9. Nature. 1980 May 1;285(5759):38-41. [Article]
  6. Buchel DE, Gronenborn B, Muller-Hill B: Sequence of the lactose permease gene. Nature. 1980 Feb 7;283(5747):541-5. [Article]
  7. Jobe A, Bourgeois S: lac Repressor-operator interaction. VI. The natural inducer of the lac operon. J Mol Biol. 1972 Aug 28;69(3):397-408. [Article]
  8. Huber RE, Parfett C, Woulfe-Flanagan H, Thompson DJ: Interaction of divalent cations with beta-galactosidase (Escherichia coli). Biochemistry. 1979 Sep 18;18(19):4090-5. [Article]
  9. Fowler AV, Smith PJ: The active site regions of lacZ and ebg beta-galactosidases are homologous. J Biol Chem. 1983 Sep 10;258(17):10204-7. [Article]
  10. Herrchen M, Legler G: Identification of an essential carboxylate group at the active site of lacZ beta-galactosidase from Escherichia coli. Eur J Biochem. 1984 Feb 1;138(3):527-31. [Article]
  11. Gebler JC, Aebersold R, Withers SG: Glu-537, not Glu-461, is the nucleophile in the active site of (lac Z) beta-galactosidase from Escherichia coli. J Biol Chem. 1992 Jun 5;267(16):11126-30. [Article]
  12. Martinez-Bilbao M, Gaunt MT, Huber RE: E461H-beta-galactosidase (Escherichia coli): altered divalent metal specificity and slow but reversible metal inactivation. Biochemistry. 1995 Oct 17;34(41):13437-42. [Article]
  13. Roth NJ, Huber RE: The beta-galactosidase (Escherichia coli) reaction is partly facilitated by interactions of His-540 with the C6 hydroxyl of galactose. J Biol Chem. 1996 Jun 14;271(24):14296-301. [Article]
  14. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  15. Roth NJ, Rob B, Huber RE: His-357 of beta-galactosidase (Escherichia coli) interacts with the C3 hydroxyl in the transition state and helps to mediate catalysis. Biochemistry. 1998 Jul 14;37(28):10099-107. [Article]
  16. Huber RE, Hlede IY, Roth NJ, McKenzie KC, Ghumman KK: His-391 of beta-galactosidase (Escherichia coli) promotes catalyses by strong interactions with the transition state. Biochem Cell Biol. 2001;79(2):183-93. [Article]
  17. Huber RE, Hakda S, Cheng C, Cupples CG, Edwards RA: Trp-999 of beta-galactosidase (Escherichia coli) is a key residue for binding, catalysis, and synthesis of allolactose, the natural lac operon inducer. Biochemistry. 2003 Feb 18;42(6):1796-803. [Article]
  18. Xu J, McRae MA, Harron S, Rob B, Huber RE: 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. 2004 Apr;82(2):275-84. [Article]
  19. Matthews BW: The structure of E. coli beta-galactosidase. C R Biol. 2005 Jun;328(6):549-56. [Article]
  20. Sutendra G, Wong S, Fraser ME, Huber RE: Beta-galactosidase (Escherichia coli) has a second catalytically important Mg2+ site. Biochem Biophys Res Commun. 2007 Jan 12;352(2):566-70. Epub 2006 Nov 20. [Article]
  21. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW: Three-dimensional structure of beta-galactosidase from E. coli. Nature. 1994 Jun 30;369(6483):761-6. [Article]
  22. Juers DH, Jacobson RH, Wigley D, Zhang XJ, Huber RE, Tronrud DE, Matthews BW: 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. 2000 Sep;9(9):1685-99. [Article]
  23. Juers DH, Heightman TD, Vasella A, McCarter JD, Mackenzie L, Withers SG, Matthews BW: A structural view of the action of Escherichia coli (lacZ) beta-galactosidase. Biochemistry. 2001 Dec 11;40(49):14781-94. [Article]
  24. Juers DH, Hakda S, Matthews BW, Huber RE: Structural basis for the altered activity of Gly794 variants of Escherichia coli beta-galactosidase. Biochemistry. 2003 Nov 25;42(46):13505-11. [Article]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
Isopropyl beta-D-thiogalactopyranosideexperimentalunknowntargetDetails
D-Galctopyranosyl-1-OnexperimentalunknowntargetDetails
1-O-[O-Nitrophenyl]-Beta-D-GalactopyranoseexperimentalunknowntargetDetails
2-deoxy-2-fluoro-β-D-galactoseexperimentalunknowntargetDetails
(5R,6S,7S,8S)-5-hydroxymethyl-6,7,8-trihydroxy-tetrazolo[1,5-A]piperidineexperimentalunknowntargetDetails
4-nitrophenyl-beta-D-galactosideexperimentalunknowntargetDetails
AllolactoseexperimentalunknowntargetDetails
2-Fluoro-2-Deoxy-Beta-D-Galactopyranosyl-Beta-D-GlucopyranoseexperimentalunknowntargetDetails
2-Deoxy-alpha-D-galactopyranoseexperimentalunknowntargetDetails
Lactoseapproved, experimental, investigationalunknowntargetDetails
S,S-(2-Hydroxyethyl)ThiocysteineexperimentalunknowntargetDetails
TyrothricinapprovedunknowntargetinhibitorDetails