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Description:
Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase)(Photoreactivating enzyme).
Molecular weight: 53675
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-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2002, sequence version 2.
07-MAR-2006, entry version 52.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Salmonella.
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_SALTY:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X60662 | CAA43069.1 | ALT_SEQ |
| EMBL | AE008728 | AAL19653.1 | - |
| PIR | S22321 | S22321. | |
| HSSP | P00914 | 1DNP | |
| SMR | P25078 | 3-471.1 | |
| GenomeReviews | AE006468_GR | STM0709.1 | |
| StyGene | SG10295 | phrB. | |
| BioCyc | STYP99287:STM0709-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].
RC STRAIN=LT2;
RX MEDLINE=92020120; PubMed=1840665;
RA Li Y.F., Sancar Z.;
RT "Cloning, sequencing, expression and characterization of DNA
RT photolyase from Salmonella typhimurium.";
RL Nucleic Acids Res. 19:4885-4890(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX MEDLINE=21534948; PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA Waterston R., Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT LT2.";
RL Nature 413:852-856(2001).
RN [3]
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).
Feature:
CHAIN 1 473 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000085110.
NP_BIND 236 240 FAD (By similarity).
NP_BIND 374 376 FAD (By similarity).
REGION 109 110 MTF binding (By similarity).
REGION 276 283 Interaction with DNA (By similarity).
REGION 343 344 Interaction with DNA (By similarity).
BINDING 224 224 FAD (By similarity).
BINDING 228 228 DNA (By similarity).
BINDING 406 406 DNA (By similarity).
SITE 308 308 Electron transfer via tryptophanyl
radical (By similarity).
SITE 361 361 Electron transfer via tryptophanyl
radical (By similarity).
SITE 384 384 Electron transfer via tryptophanyl
radical (By similarity).
CONFLICT 115 115 A -> R (in Ref. 1).
CONFLICT 196 196 A -> E (in Ref. 1).
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.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
-!- CAUTION: Ref.1 has submitted a sequence which seems to have every
20th amino acid deleted.
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Sequence length: 473
MPTHLVWFRR DLRLQDNLAL AAACRDASAR VLALYISTPA QWQAHDMAPR QAAFISAQLN
ALQTALAEKG IPLLFHEVAD FNASIETVKN VCRQHDVSHL FYNYQYEFNE RQRDAAVEKT
LPSVICEGFD DSVILAPGAV MTGNHEMYKV FTPFKNAWLK RLKEDIPPCV PAPKIRVSGA
LSTPLTPVSL NYPQQAFDAA LFPVEENAVI AQLRQFCAQG ADEYALRRDF PAVDGTSRLS
ASLATGGLSP RQCLHRLLAE QPQALDGGPG SVWLNELIWR EFYRHLMTWY PALCKHQPFI
RWTKRVAWQE NPHYFQAWQK GETGYPIVDA AMRQLNATGW MHNRLRMITA SFLVKDLLID
WRLGERYFMS QLIDGDLAAN NGGWQWAAST GTDAAPYFRI FNPTTQGERF DRDGEFIRQW
LPALRDIPGK AIHEPWRWAE KAGVVLDYPR PIVEHKQARI ATLSAYEAAR KGA