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Description:
Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase)(Photoreactivating enzyme).
Molecular weight: 53667
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
07-MAR-2006, entry version 70.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Escherichia.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein PHR_ECOLI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | K01299 | AAA24388.1 | - |
| EMBL | X57399 | CAB56782.1 | - |
| EMBL | U00096 | AAC73802.1 | - |
| EMBL | D90709 | BAA35367.1 | - |
| EMBL | D90710 | BAA35372.1 | - |
| PIR | A01137 | WZECD. | |
| PDB | 1DNP | X-ray | A/B=2-472. |
| GenomeReviews | U00096_GR | b0708.1 | |
| EchoBASE | EB0729 | -.1 | |
| EcoGene | EG10736 | phrB. | |
| BioCyc | EcoCyc:EG10736-MONOMER | -.1 | |
| LinkHub | P00914 | -.1 | |
| GO | GO:0005515 | F:protein binding | IPI. |
| InterPro | IPR002081 | DNA_photolyase_1. | |
| InterPro | IPR006050 | DNA_photolyase_N. | |
| InterPro | IPR006051 | FAD_bd_N. | |
| InterPro | IPR005101 | Photolyse_FAD_bd. | |
| Pfam | PF00875 | DNA_photolyase | 1. |
| Pfam | PF03441 | FAD_binding_7 | 1. |
| PRINTS | PR00147 | DNAPHOTLYASE. | |
| ProDom | PD004390 | FAD_binding_N | 1. |
| PROSITE | PS00394 | DNA_PHOTOLYASES_1_1 | 1. |
| PROSITE | PS00691 | DNA_PHOTOLYASES_1_2 | 1. |
Keywords:
3D-structure; Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=84185763; PubMed=6325460;
RA Sancar G.B., Smith F.W., Lorence M.C., Rupert C.S., Sancar A.;
RT "Sequences of the Escherichia coli photolyase gene and protein.";
RL J. Biol. Chem. 259:6033-6038(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110;
RA Begley T.P.;
RL Submitted (JAN-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655;
RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110;
RX MEDLINE=97061202; PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [5]
RP REVIEW.
RA Sancar G.B., Sancar A.;
RT "Structure and function of DNA photolyases.";
RL Trends Biochem. Sci. 12:259-261(1987).
RN [6]
RP MUTAGENESIS OF TRP-278.
RX MEDLINE=90344791; PubMed=2200511;
RA Li Y.F., Sancar A.;
RT "Active site of Escherichia coli DNA photolyase: mutations at Trp277
RT alter the selectivity of the enzyme without affecting the quantum
RT yield of photorepair.";
RL Biochemistry 29:5698-5706(1990).
RN [7]
RP MUTAGENESIS OF TRP-383, AND ELECTRON TRANSFER CHAIN.
RX PubMed=12835419; DOI=10.1073/pnas.1531645100;
RA Byrdin M., Eker A.P., Vos M.H., Brettel K.;
RT "Dissection of the triple tryptophan electron transfer chain in
RT Escherichia coli DNA photolyase: Trp382 is the primary donor in
RT photoactivation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8676-8681(2003).
RN [8]
RP REVIEW.
RX PubMed=15721603; DOI=10.1016/j.bbabio.2004.02.010;
RA Weber S.;
RT "Light-driven enzymatic catalysis of DNA repair: a review of recent
RT biophysical studies on photolyase.";
RL Biochim. Biophys. Acta 1707:1-23(2005).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FAD AND MTF, AND
RP SUBUNIT.
RX MEDLINE=95327928; PubMed=7604260;
RA Park H.-W., Kim S.-T., Sancar A., Deisenhofer J.;
RT "Crystal structure of DNA photolyase from Escherichia coli.";
RL Science 268:1866-1872(1995).
Feature:
CHAIN 1 472 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000085108.
NP_BIND 235 239 FAD.
NP_BIND 275 282 FAD.
NP_BIND 373 375 FAD.
REGION 109 110 MTF binding.
REGION 275 282 Interaction with DNA (By similarity).
REGION 342 343 Interaction with DNA (By similarity).
BINDING 223 223 FAD.
BINDING 227 227 DNA (By similarity).
BINDING 272 272 FAD.
BINDING 405 405 DNA (By similarity).
SITE 307 307 Electron transfer via tryptophanyl
radical.
SITE 360 360 Electron transfer via tryptophanyl
radical.
SITE 383 383 Electron transfer via tryptophanyl
radical.
MUTAGEN 278 278 W->X: Reduces DNA-binding affinity.
MUTAGEN 383 383 W->F: Abolishes photolyase activity.
STRAND 3 7
STRAND 9 10
STRAND 14 14
TURN 15 16
HELIX 18 23
STRAND 24 25
STRAND 30 37
HELIX 39 44
TURN 45 46
HELIX 50 68
TURN 69 70
STRAND 73 77
STRAND 79 80
TURN 81 83
HELIX 86 95
STRAND 97 103
STRAND 107 107
HELIX 108 120
TURN 122 123
STRAND 124 129
STRAND 135 135
TURN 137 138
STRAND 139 140
TURN 143 144
STRAND 145 145
STRAND 149 150
HELIX 151 163
TURN 164 164
STRAND 191 191
TURN 198 200
STRAND 201 201
STRAND 204 204
HELIX 205 217
TURN 218 218
HELIX 219 226
TURN 227 228
TURN 230 231
STRAND 232 232
STRAND 244 246
HELIX 250 259
HELIX 261 265
TURN 266 266
STRAND 267 267
TURN 268 269
HELIX 272 288
TURN 293 294
STRAND 295 295
STRAND 298 299
HELIX 300 304
STRAND 305 305
HELIX 311 319
TURN 320 320
STRAND 322 323
HELIX 325 335
HELIX 342 349
TURN 352 355
STRAND 356 356
HELIX 360 368
TURN 372 373
HELIX 376 386
TURN 387 387
TURN 391 392
TURN 396 397
HELIX 402 409
TURN 410 412
HELIX 414 419
HELIX 421 423
TURN 424 425
STRAND 426 426
TURN 428 429
HELIX 430 432
STRAND 433 433
HELIX 434 439
TURN 440 442
STRAND 446 447
STRAND 451 452
HELIX 454 468
TURN 469 469
Comments:
-!- 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 noncovalently per
subunit.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=384 nm;
-!- SUBUNIT: Monomer.
-!- 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.
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Sequence length: 472
MTTHLVWFRQ DLRLHDNLAL AAACRNSSAR VLALYIATPR QWATHNMSPR QAELINAQLN
GLQIALAEKG IPLLFREVDD FVASVEIVKQ VCAENSVTHL FYNYQYEVNE RARDVEVERA
LRNVVCEGFD DSVILPPGAV MTGNHEMYKV FTPFKNAWLK RLREGMPECV AAPKVRSSGS
IEPSPSITLN YPRQSFDTAH FPVEEKAAIA QLRQFCQNGA GEYEQQRDFP AVEGTSRLSA
SLATGGLSPR QCLHRLLAEQ PQALDGGAGS VWLNELIWRE FYRHLITYHP SLCKHRPFIA
WTDRVQWQSN PAHLQAWQEG KTGYPIVDAA MRQLNSTGWM HNRLRMITAS FLVKDLLIDW
REGERYFMSQ LIDGDLAANN GGWQWAASTG TDAAPYFRIF NPTTQGEKFD HEGEFIRQWL
PELRDVPGKV VHEPWKWAQK AGVTLDYPQP IVEHKEARVQ TLAAYEAARK GK