Identification
Name:Deoxyribodipyrimidine photo-lyase
Synonyms:
  • DNA photolyase
  • Photoreactivating enzyme
Gene Name:phrB
Enzyme Class:
Biological Properties
General Function:Involved in DNA photolyase activity
Specific Function:Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Metabolites:
ECMDB IDNameView
GO Classification:
Function
carbon-carbon lyase activity
catalytic activity
DNA photolyase activity
lyase activity
Process
cellular macromolecule metabolic process
DNA metabolic process
DNA repair
macromolecule metabolic process
metabolic process
Gene Properties
Blattner:b0708
Gene OrientationClockwise
Centisome Percentage:15.92
Left Sequence End738730
Right Sequence End740148
Gene Sequence:
>1419 bp
ATGAGCCAGTCACTGTTTAGCCAACCATTGAACGTTATTAACGTCGGCATCGCCATGTTT
AGCGATGACCTGAAAAAGCAGCATGTAGAAGTGACTCAACTCGACTGGACGCCGCCGGGG
CAGGGCAATATGCAGGTGGTGCAGGCGCTGGATAACATTGCCGATTCGCCGCTGGCGGAC
AAAATCGCCGCCGCTAACCAGCAGGCGCTGGAGCGTATTATCCAGTCGCATCCGGTGCTG
ATTGGTTTTGATCAGGCGATTAACGTGGTGCCGGGCATGACGGCGAAAACCATTCTTCAC
GCCGGGCCGCCGATCACCTGGGAAAAAATGTGCGGCGCGATGAAAGGCGCGGTCACCGGA
GCGCTGGTGTTCGAAGGACTGGCGAAAGATCTCGACGAGGCGGCTGAACTGGCGGCTTCC
GGGGAGATCACCTTCTCGCCGTGTCACGAGCACGACTGCGTGGGATCGATGGCGGGTGTT
ACCTCGGCCTCGATGTTTATGCACATCGTAAAAAACAAAACCTACGGCAACATCGCTTAT
ACCAACATGAGCGAGCAGATGGCGAAGATTTTGCGTATGGGCGCTAACGACCAGAGCGTG
ATTGACCGCCTGAACTGGATGCGTGATGTGCAGGGACCAATACTGCGCGACGCGATGAAA
ATTATCGGCGAAATCGATCTGCGCTTAATGCTGGCGCAGGCGCTGCATATGGGCGATGAG
TGCCATAACCGCAATAACGCCGGGACGACACTGCTGATTCAGGCGCTGACGCCGGGGATT
ATTCAGGCGGGTTATTCCGTCGAGCAACAGCGCGAAGTGTTTGAGTTTGTCGCCAGCAGC
GACTACTTCTCCGGCCCGACGTGGATGGCGATGTGTAAAGCGGCGATGGATGCGGCGCAT
GGCATCGAATACAGCACCGTGGTCACCACCATGGCGCGTAACGGCGTCGAGTTCGGCCTG
CGGGTCAGCGGCCTGCCGGGGCAATGGTTTACCGGCCCGGCGCAGCAGGTGATCGGCCCG
ATGTTTGCCGGTTATAAGCCGGAAGATTCGGGGCTGGATATCGGCGACAGCGCCATCACC
GAAACCTACGGTATTGGCGGATTTGCTATGGCGACCGCGCCCGCTATCGTCGCGCTGGTG
GGCGGCACGGTGGAAGAAGCTATTGATTTCTCCCGTCAGATGCGCGAAATCACCCTCGGT
GAAAACCCCAACGTCACCATTCCGCTGCTCGGTTTTATGGGCGTGCCGTCGGCAATCGAC
ATCACCCGCGTGGGTAGCAGCGGCATTCTGCCGGTGATCAACACCGCCATCGCCCATAAA
GATGCGGGCGTCGGCATGATTGGCGCGGGCATTGTGCATCCACCTTTTGCCTGCTTCGAG
AAAGCCATTCTTGGCTGGTGCGAACGTTACGGCGTCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:472
Protein Molecular Weight:53667
Protein Theoretical pI:7
PDB File:1DNP
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Deoxyribodipyrimidine photo-lyase
MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLN
GLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERA
LRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGS
IEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSA
SLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIA
WTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDW
REGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWL
PELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK
References
External Links:
ResourceLink
Uniprot ID:P00914
Uniprot Name:PHR_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674464
PDB ID:1DNP
Ecogene ID:EG10736
Ecocyc:EG10736
ColiBase:b0708
Kegg Gene:b0708
EchoBASE ID:EB0729
CCDB:PHR_ECOLI
BacMap:16128683
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
  • Byrdin, M., Eker, A. P., Vos, M. H., Brettel, K. (2003). "Dissection of the triple tryptophan electron transfer chain in Escherichia coli DNA photolyase: Trp382 is the primary donor in photoactivation." Proc Natl Acad Sci U S A 100:8676-8681. Pubmed: 12835419
  • 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
  • Li, Y. F., Sancar, A. (1990). "Active site of Escherichia coli DNA photolyase: mutations at Trp277 alter the selectivity of the enzyme without affecting the quantum yield of photorepair." Biochemistry 29:5698-5706. Pubmed: 2200511
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Park, H. W., Kim, S. T., Sancar, A., Deisenhofer, J. (1995). "Crystal structure of DNA photolyase from Escherichia coli." Science 268:1866-1872. Pubmed: 7604260
  • Sancar, G. B., Smith, F. W., Lorence, M. C., Rupert, C. S., Sancar, A. (1984). "Sequences of the Escherichia coli photolyase gene and protein." J Biol Chem 259:6033-6038. Pubmed: 6325460
  • Weber, S. (2005). "Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase." Biochim Biophys Acta 1707:1-23. Pubmed: 15721603