|
|
|
|
|
|
|
Description:
Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase)(Photoreactivating enzyme).
Molecular weight: 56026
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:
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-MAR-2006, entry version 40.
Phylogenetic order:
Bacteria Cyanobacteria Chroococcales Synechocystis.
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_SYNY3:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | U51943 | AAB81109.1 | - |
| EMBL | BA000022 | BAA17790.1 | - |
| PIR | S74829 | S74829. | |
| HSSP | P05327 | 1QNF | |
| GenomeReviews | BA000022_GR | slr0854.1 | |
| BioCyc | SSP1148:SLR0854-MONOMER | -.1 | |
| 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:
Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RA Ng W.-O., Pakrasi H.B.;
RT "DNA photolyase homologs are the major UV resistance factors in the
RT cyanobacterium Synechocystis sp. PCC 6803.";
RL Mol. Gen. Genet. 264:924-930(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=97061201; PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
RA Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
RA Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
RA Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the
RT entire genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP EXPRESSION IN SYNECHOCYSTIS, CHARACTERIZATION, COFACTORS, AND SUBUNIT.
RA Ng W.-O., Zentella R., Wang Y., Taylor J.-S.A., Pakrasi H.B.;
RT "PhrA, the major photoreactivating factor in the cyanobacterium
RT Synechocystis sp. strain PCC 6803 codes for a cyclobutane-pyrimidine-
RT dimer-specific DNA photolyase.";
RL Arch. Microbiol. 173:412-417(2000).
RN [4]
RP EXPRESSION IN E.COLI, AND FAD COFACTOR.
RA Hitomi K., Okamoto K., Daiyasu H., Miyashita H., Iwai S., Toh H.,
RA Ishiura M., Todo T.;
RT "Bacterial cryptochrome and photolyase: characterization of two
RT photolyase-like genes of Synechocystis sp. PCC6803.";
RL Nucleic Acids Res. 28:2353-2362(2000).
Feature:
CHAIN 1 488 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000085113.
NP_BIND 254 258 FAD (By similarity).
NP_BIND 394 396 FAD (By similarity).
REGION 297 304 Interaction with DNA (By similarity).
REGION 363 364 Interaction with DNA (By similarity).
BINDING 242 242 FAD (By similarity).
BINDING 246 246 DNA (By similarity).
BINDING 425 425 DNA (By similarity).
SITE 328 328 Electron transfer via tryptophanyl
radical (By similarity).
SITE 381 381 Electron transfer via tryptophanyl
radical (By similarity).
SITE 404 404 Electron transfer via tryptophanyl
radical (By similarity).
Comments:
-!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
Exhibits specific, light-dependent repair activity for a
cyclobutyl pyrimidine dimer by catalyzing the light-dependent
monomerization (300-600 nm) of the dimers (in cis-syn
configuration), which are formed between adjacent bases on the
same DNA strand upon exposure to ultraviolet radiation. It has
been shown that photorepair is more important than excision repair
for UV-induced DNA lesions in Synechocystis. Its disruption does
not affect circadian rhythm.
-!- CATALYTIC ACTIVITY: Cyclobutadipyrimidine (in DNA) = 2 pyrimidine
residues (in DNA).
-!- COFACTOR: Binds 1 FAD per subunit.
-!- COFACTOR: Binds 1 8-hydroxy-5-deazaflavin (F420) noncovalently per
subunit.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
Sequence length: 488
MGRQLILFPM SDQSDHPLIL LWHRRDLRLN DHLALAKARQ KTAKIVGVFC LDNKILQAED
MAPARVAYLL GCLQSLQDHY QRLGSELLVF QADPVQLLPK LANTLGAHGV TWTLDTEPYA
QKRDLAVAQA LRERGLAIAT EWDQLMHHPG EVLTQAGSPY TVYTPFWKNW SQLPKTSPVP
TPKDLQGLTP AEKEKLAPLE PLAIPQLADL GFIWDQPLPL TPGEEAAEQR LDWFVAHGLE
EYQQNRNFPA LDGTSQLSAA LKFGVISPRT LWQTTLEAWE QSRSEEARAS IETWQQELAW
REFYQHCLYS FPALAQGPYR SPFQEFPWEE NQDHFQAWCE GRTGYPIIDA AMAQLNQTGW
MHNRCRMIVA SFLIKDLILN WQWGELYFMQ TLYDGDLAAN NGGWQWSASS GMDPKPLRIF
NPHTQAQKFD PEGEYIRTWL PQLARFDTGD LLTGKLTPGS RRSVNYPEPI VDHNQQQREF
KRRYQLVK