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Phr

Protein FULL name:

CPD photolyase, DNA photolyase


Phr (Escherichia coli strain K-12 substr. MG1655) is product of expression of phr gene.


Phr is involved in:

DDS in Escherichia coli strain K-12 substr. MG1655
     
DRR in Escherichia coli strain K-12 substr. MG1655
     


Keywords:



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.

CATALYTIC ACTIVITY: Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).

COFACTOR: Binds 1 FAD per subunit.

COFACTOR: Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit.

BIOPHYSICOCHEMICAL PROPERTIES: Absorption: Abs(max)=384 nm;

SUBUNIT: Monomer.

INTERACTION: P68739:nfi; NbExp=1; IntAct=EBI-555781, EBI-551698;

MISCELLANEOUS: There are only 10-20 molecules of photolyase per E.coli cell.

MISCELLANEOUS: Upon absorption of visible light electrons are transferred from Trp-307 through Trp-360 to Trp 383, and from there to FADH, giving rise to the fully reduced catalytic FADH(-).

SIMILARITY: Belongs to the DNA photolyase class-1 family.

SIMILARITY: Contains 1 DNA photolyase domain.


NCBI GenPept GI number(s): 6006450
Species: Escherichia coli

Links to other databases:

Database ID Link
Uniprot P00914 P00914
PFAM: - P00914 (Link - using uniprot id)
InterPro: IPR002081
IPR005101
IPR006050
IPR006051
IPR002081
IPR005101
IPR006050
IPR006051
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPR
QAELINAQLNGLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHL
FYNYQYEVNERARDVEVERALRNVVCEGFDDSVILPPGAVMTGNHEMYKV
FTPFKNAWLKRLREGMPECVAAPKVRSSGSIEPSPSITLNYPRQSFDTAH
FPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSASLATGGLSPR
QCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIA
WTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITAS
FLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIF
NPTTQGEKFDHEGEFIRQWLPELRDVPGKVVHEPWKWAQKAGVTLDYPQP
IVEHKEARVQTLAAYEAARKGK

Phr (Escherichia coli strain K-12 substr. MG1655) is able to recognize following damages:
References:

Title Authors Journal
Sequences of the Escherichia coli photolyase gene and protein. Sancar GB, Smith FW, Lorence MC, Rupert CS, Sancar A J Biol Chem May 10, 1984
Active site of Escherichia coli DNA photolyase: mutations at Trp277 alter the selectivity of the enzyme without affecting the quantum yield of photorepair. Li YF, Sancar A Biochemistry June 19, 1990
Crystal structure of DNA photolyase from Escherichia coli. Park HW, Kim ST, Sancar A, Deisenhofer J Science June 1, 1995
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. 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. DNA Res June 1, 1996
The complete genome sequence of Escherichia coli K-12. 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 Science Sept. 5, 1997
Dissection of the triple tryptophan electron transfer chain in Escherichia coli DNA photolyase: Trp382 is the primary donor in photoactivation. Byrdin M, Eker AP, Vos MH, Brettel K Proc Natl Acad Sci U S A July 22, 2003
Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase. Weber S Biochim Biophys Acta Jan. 25, 2005
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T Mol Syst Biol Jan. 1, 2006


Last modification of this entry: Nov. 11, 2010.

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