ID   PHR_SYNY3               Reviewed;         488 AA.
AC   Q55081;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE            EC=4.1.99.3;
DE   AltName: Full=DNA photolyase;
DE   AltName: Full=Photoreactivating enzyme;
GN   Name=phrA; Synonyms=phr; OrderedLocusNames=slr0854;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=11254140; DOI=10.1007/s004380000383;
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].
RC   STRAIN=PCC 6803 / Kazusa;
RX   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., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [3]
RP   EXPRESSION IN SYNECHOCYSTIS, CHARACTERIZATION, COFACTOR, AND SUBUNIT.
RX   PubMed=10896222; DOI=10.1007/s002030000164;
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-dimer-
RT   specific DNA photolyase.";
RL   Arch. Microbiol. 173:412-417(2000).
RN   [4]
RP   EXPRESSION IN E.COLI, AND FAD COFACTOR.
RX   PubMed=10871367; DOI=10.1093/nar/28.12.2353;
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 photolyase-
RT   like genes of Synechocystis sp. PCC6803.";
RL   Nucleic Acids Res. 28:2353-2362(2000).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Exhibits specific, light-dependent repair activity for a cyclobutyl
CC       pyrimidine dimer by catalyzing the light-dependent monomerization (300-
CC       600 nm) of the dimers (in cis-syn configuration), which are formed
CC       between adjacent bases on the same DNA strand upon exposure to
CC       ultraviolet radiation. It has been shown that photorepair is more
CC       important than excision repair for UV-induced DNA lesions in
CC       Synechocystis. Its disruption does not affect circadian rhythm.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:10896222};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10896222};
CC   -!- COFACTOR:
CC       Name=coenzyme F420-(gamma-Glu)n; Xref=ChEBI:CHEBI:133980;
CC         Evidence={ECO:0000269|PubMed:10896222};
CC       Note=Binds 1 coenzyme F420 non-covalently per subunit.
CC       {ECO:0000269|PubMed:10896222};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10896222}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; U51943; AAB81109.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA17790.1; -; Genomic_DNA.
DR   PIR; S74829; S74829.
DR   AlphaFoldDB; Q55081; -.
DR   SMR; Q55081; -.
DR   IntAct; Q55081; 3.
DR   STRING; 1148.1652872; -.
DR   PaxDb; Q55081; -.
DR   EnsemblBacteria; BAA17790; BAA17790; BAA17790.
DR   KEGG; syn:slr0854; -.
DR   eggNOG; COG0415; Bacteria.
DR   InParanoid; Q55081; -.
DR   OMA; WQWSASS; -.
DR   PhylomeDB; Q55081; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR   InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR   InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR   InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR   InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR019947; Photolyase_8HDF.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   TIGRFAMs; TIGR03556; photolyase_8HDF; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..488
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085113"
FT   DOMAIN          17..146
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          297..304
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          363..364
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         242
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         254..258
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         394..396
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         425
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   SITE            328
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            381
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            404
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   488 AA;  56026 MW;  BEEE64ABA0919332 CRC64;
     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