Skip Header

Contribute Send feedback
Read comments (?) or add your own

P05327 (PHR_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Deoxyribodipyrimidine photo-lyase
EC=4.1.99.3
Alternative name(s):
DNA photolyase
Photoreactivating enzyme
Gene names
Name:phr
Synonyms:phrA
Ordered Locus Names:syc1392_c
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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.

Binds 1 coenzyme F420 (8-HDF / 7,8-didemethyl-8-hydroxy-5-deazaflavin) non-covalently per subunit.

Subunit structure

Monomer. Ref.6

Sequence similarities

Belongs to the DNA photolyase class-1 family.

Contains 1 photolyase/cryptochrome alpha/beta domain.

Biophysicochemical properties

Absorption:

Abs(max)=440 nm

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 484483Deoxyribodipyrimidine photo-lyase
PRO_0000085112

Regions

Domain3 – 132130Photolyase/cryptochrome alpha/beta
Nucleotide binding240 – 2478FAD
Nucleotide binding346 – 3527FAD
Nucleotide binding380 – 3823FAD
Region36 – 383F420 binding
Region101 – 1099F420 binding
Region141 – 1488DNA binding
Region283 – 2908Interaction with DNA
Region349 – 3502Interaction with DNA

Sites

Binding site511F420
Binding site2281FAD
Binding site2321DNA
Binding site2481F420
Binding site3861FAD
Binding site4111DNA
Binding site4721DNA
Site3141Electron transfer via tryptophanyl radical By similarity
Site3671Electron transfer via tryptophanyl radical By similarity
Site3901Electron transfer via tryptophanyl radical By similarity

Experimental info

Sequence conflict2591R → Q in CAA30190. Ref.1
Sequence conflict3521W → R in CAA30190. Ref.1
Sequence conflict4461G → E in CAA30190. Ref.1

Secondary structure

1 .......................................................................... 484
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05327 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 2DAC6D9CFD515E3D

FASTA48454,462
        10         20         30         40         50         60 
MAAPILFWHR RDLRLSDNIG LAAARAQSAQ LIGLFCLDPQ ILQSADMAPA RVAYLQGCLQ 

        70         80         90        100        110        120 
ELQQRYQQAG SRLLLLQGDP QHLIPQLAQQ LQAEAVYWNQ DIEPYGRDRD GQVAAALKTA 

       130        140        150        160        170        180 
GIRAVQLWDQ LLHSPDQILS GSGNPYSVYG PFWKNWQAQP KPTPVATPTE LVDLSPEQLT 

       190        200        210        220        230        240 
AIAPLLLSEL PTLKQLGFDW DGGFPVEPGE TAAIARLQEF CDRAIADYDP QRNFPAEAGT 

       250        260        270        280        290        300 
SGLSPALKFG AIGIRQAWRA ASAAHALSRS DEARNSIRVW QQELAWREFY QHALYHFPSL 

       310        320        330        340        350        360 
ADGPYRSLWQ QFPWENREAL FTAWTQAQTG YPIVDAAMRQ LTETGWMHNR CWMIVASFLT 

       370        380        390        400        410        420 
KDLIIDWRRG EQFFMQHLVD GDLAANNGGW QWSASSGMDP KPLRIFNPAS QAKKFDATAT 

       430        440        450        460        470        480 
YIKRWLPELR HVHPKDLISG EITPIGRRGY PAPIVNHNLR QKQFKALYNQ LKAAIAEPEA 


EPDS

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a photolyase gene from the cyanobacterium Anacystis nidulans."
Yasui A., Takao M., Oikawa A., Kiener A., Walsh C.T., Eker A.P.M.
Nucleic Acids Res. 16:4447-4463(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[3]"DNA photoreactivating enzyme from the cyanobacterium Anacystis nidulans."
Eker A.P.M., Kooiman P., Hessels J.K.C., Yasui A.
J. Biol. Chem. 265:8009-8015(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-26.
[4]"Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase."
Weber S.
Biochim. Biophys. Acta 1707:1-23(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[5]"Crystal structure of DNA photolyase from Anacystis nidulans."
Tamada T., Kitadokoro K., Higuchi Y., Inaka K., Yasui A., de Ruiter P.E., Eker A.P., Miki K.
Nat. Struct. Biol. 4:887-891(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD AND 8-HDF.
[6]"DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction."
Kort R., Komori H., Adachi S., Miki K., Eker A.
Acta Crystallogr. D 60:1205-1213(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH FAD, SUBUNIT.
[7]"Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair."
Mees A., Klar T., Gnau P., Hennecke U., Eker A.P.M., Carell T., Essen L.-O.
Science 306:1789-1793(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-475 IN COMPLEX WITH FAD; 8-HDF AND DAMAGED DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X07230 Genomic DNA. Translation: CAA30190.1.
AP008231 Genomic DNA. Translation: BAD79582.1.
RefSeqYP_172102.1. NC_006576.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1OWLX-ray1.80A1-484[»]
1OWMX-ray2.30A1-484[»]
1OWNX-ray2.30A1-484[»]
1OWOX-ray2.30A1-484[»]
1OWPX-ray2.30A1-484[»]
1QNFX-ray1.80A1-484[»]
1TEZX-ray1.80A/B/C/D2-475[»]
ProteinModelPortalP05327.
SMRP05327. Positions 1-475.
ModBaseSearch...

Protein-protein interaction databases

STRING269084.syc1392_c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79582; BAD79582; syc1392_c.
GeneID3199486.
KEGGsyc:syc1392_c.
PATRIC32488703. VBISynElo117686_1605.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0415.
HOGENOMHOG000245621.
KOK01669.
OMADHDTAND.
ProtClustDBCLSK836654.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR002081. Cryptochrome/DNA_photolyase_1.
IPR018394. DNA_photolyase_1_CS_C.
IPR006050. DNA_photolyase_N.
IPR019947. Photolyase_8HDF.
IPR005101. Photolyase_FAD-bd/Cryptochr_C.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
PRINTSPR00147. DNAPHOTLYASE.
SUPFAMSSF52425. DNA_photolyase_N. 1 hit.
SSF48173. Photolyase_FAD-bd/Cryptochr_C. 1 hit.
TIGRFAMsTIGR03556. photolyase_8HDF. 1 hit.
PROSITEPS00394. DNA_PHOTOLYASES_1_1. 1 hit.
PS00691. DNA_PHOTOLYASES_1_2. False negative.
PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05327.

Entry information

Entry namePHR_SYNP6
AccessionPrimary (citable) accession number: P05327
Secondary accession number(s): Q5N288
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 111 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents