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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
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. 14, 2020.
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