Deoxyribodipyrimidine photo-lyase

Details

Name
Deoxyribodipyrimidine photo-lyase
Synonyms
  • 4.1.99.3
  • DNA photolyase
  • Photoreactivating enzyme
  • phr
Gene Name
phrB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0012084|Deoxyribodipyrimidine photo-lyase
MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLN
GLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERA
LRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGS
IEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSA
SLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIA
WTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDW
REGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWL
PELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK
Number of residues
472
Molecular Weight
53666.505
Theoretical pI
7.22
GO Classification
Functions
deoxyribodipyrimidine photo-lyase activity / DNA binding / nucleotide binding
Processes
DNA repair / protein-chromophore linkage
General Function
Nucleotide binding
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0012085|Deoxyribodipyrimidine photo-lyase (phrB)
ATGACTACCCATCTGGTCTGGTTTCGCCAGGATTTACGTCTGCACGATAATCTCGCACTG
GCTGCCGCCTGCCGCAATTCGTCTGCACGCGTGCTGGCGTTGTATATCGCTACACCACGC
CAGTGGGCGACGCATAACATGTCGCCGCGTCAGGCTGAACTTATCAATGCTCAACTGAAT
GGGCTACAAATAGCGCTTGCGGAAAAAGGTATTCCTTTATTGTTCCGTGAAGTGGATGAC
TTTGTCGCCAGTGTCGAAATAGTTAAACAGGTGTGCGCGGAAAACAGCGTTACCCACCTG
TTTTATAACTATCAGTATGAAGTGAATGAGCGGGCGCGGGATGTGGAAGTTGAAAGAGCG
CTGCGTAACGTGGTGTGTGAAGGATTTGATGACAGCGTGATCCTGCCGCCTGGCGCGGTG
ATGACCGGTAATCACGAGATGTACAAAGTCTTTACGCCTTTTAAGAATGCCTGGCTGAAA
CGGCTGCGGGAAGGGATGCCGGAGTGCGTCGCTGCGCCAAAAGTTCGTAGTAGCGGATCG
ATAGAGCCCTCGCCATCCATTACGCTGAATTATCCTCGTCAGTCTTTCGATACTGCGCAT
TTTCCGGTGGAAGAAAAAGCGGCGATTGCGCAATTACGCCAGTTTTGCCAGAACGGTGCC
GGAGAATATGAGCAACAACGAGATTTTCCGGCAGTGGAAGGCACCAGCCGTTTGTCGGCC
AGCCTGGCAACGGGCGGGTTATCGCCTCGCCAGTGCTTGCATCGCTTGTTGGCTGAACAG
CCGCAGGCGCTGGACGGTGGGGCCGGTAGTGTCTGGCTTAATGAGCTGATCTGGCGCGAG
TTTTACCGTCACCTGATAACGTATCACCCCTCGTTGTGTAAACATCGTCCATTTATTGCC
TGGACGGATCGTGTACAGTGGCAGAGCAATCCCGCACATTTACAGGCCTGGCAGGAAGGC
AAAACGGGATACCCGATTGTTGATGCCGCTATGCGTCAGCTTAACAGCACTGGCTGGATG
CATAACAGGCTACGGATGATTACAGCCAGTTTTCTGGTGAAAGATTTATTGATCGACTGG
CGCGAAGGCGAGCGATATTTCATGTCGCAGCTGATTGATGGTGATTTGGCAGCCAATAAC
GGTGGCTGGCAGTGGGCCGCTTCAACCGGAACCGATGCAGCGCCGTATTTTCGTATTTTC
AACCCGACAACCCAGGGCGAGAAATTTGATCATGAGGGCGAGTTTATCCGCCAGTGGCTA
CCGGAACTGCGCGATGTGCCAGGGAAAGTGGTGCATGAGCCGTGGAAGTGGGCGCAGAAA
GCAGGTGTGACGCTGGATTATCCGCAACCGATAGTCGAGCACAAAGAAGCGAGAGTACAA
ACGTTGGCAGCGTATGAGGCGGCGCGGAAGGGGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP00914
UniProtKB Entry NamePHR_ECOLI
GenBank Gene IDK01299
General References
  1. Sancar GB, Smith FW, Lorence MC, Rupert CS, Sancar A: Sequences of the Escherichia coli photolyase gene and protein. J Biol Chem. 1984 May 10;259(9):6033-8. [Article]
  2. 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
  3. 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]
  4. 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]
  5. Li YF, Sancar A: Active site of Escherichia coli DNA photolyase: mutations at Trp277 alter the selectivity of the enzyme without affecting the quantum yield of photorepair. Biochemistry. 1990 Jun 19;29(24):5698-706. [Article]
  6. Byrdin M, Eker AP, Vos MH, Brettel K: 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. 2003 Jul 22;100(15):8676-81. Epub 2003 Jun 30. [Article]
  7. Weber S: Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase. Biochim Biophys Acta. 2005 Feb 25;1707(1):1-23. [Article]
  8. Park HW, Kim ST, Sancar A, Deisenhofer J: Crystal structure of DNA photolyase from Escherichia coli. Science. 1995 Jun 30;268(5219):1866-72. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails