ID   PHR_VIBCH               Reviewed;         469 AA.
AC   Q9KNA8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=VcPhr; OrderedLocusNames=VC_A0057;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   CHARACTERIZATION, COFACTOR, AND PHOTOLYASE ACTIVITY.
RX   PubMed=12878596; DOI=10.1074/jbc.m305792200;
RA   Worthington E.N., Kavakli I.H., Berrocal-Tito G., Bondo B.E., Sancar A.;
RT   "Purification and characterization of three members of the
RT   photolyase/cryptochrome family blue-light photoreceptors from Vibrio
RT   cholerae.";
RL   J. Biol. Chem. 278:39143-39154(2003).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl
CC       pyrimidine dimers (in cis-syn configuration), which are formed between
CC       adjacent bases on the same DNA strand upon exposure to ultraviolet
CC       radiation.
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:12878596};
CC       Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:12878596};
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000269|PubMed:12878596};
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC       subunit. The occupancy is 0.2. Usually had equal molar flavin and
CC       folate. {ECO:0000269|PubMed:12878596};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; AE003853; AAF95971.1; -; Genomic_DNA.
DR   PIR; G82505; G82505.
DR   RefSeq; NP_232458.1; NC_002506.1.
DR   RefSeq; WP_001241766.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KNA8; -.
DR   SMR; Q9KNA8; -.
DR   STRING; 243277.VC_A0057; -.
DR   DNASU; 2612142; -.
DR   EnsemblBacteria; AAF95971; AAF95971; VC_A0057.
DR   GeneID; 57741527; -.
DR   KEGG; vch:VC_A0057; -.
DR   PATRIC; fig|243277.26.peg.2702; -.
DR   eggNOG; COG0415; Bacteria.
DR   HOGENOM; CLU_010348_2_0_6; -.
DR   OMA; WQWSASS; -.
DR   BioCyc; VCHO:VCA0057-MON; -.
DR   BRENDA; 4.1.99.3; 15862.
DR   Proteomes; UP000000584; Chromosome 2.
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; 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   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   Reference proteome.
FT   CHAIN           1..469
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000235307"
FT   DOMAIN          1..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   BINDING         107
FT                   /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:15636"
FT                   /evidence="ECO:0000250|UniProtKB:P00914"
SQ   SEQUENCE   469 AA;  54360 MW;  BF161ABEEEA83D5C CRC64;
     MRLVWFRRDL RSFDNTALTA ALNSGDPVAA MYIATPEQWH QHHLAPIQAD LIWRRLAELQ
     QELAALNVPL FYQQVADFQA AAVAVSQLAK TLNATQVLAN RDYELDEQQR DQLAQQLLSE
     QGIIWSAFDD KCVLPPGSVR TKQGEFFKVF TPFKRAWLTL FQPPVIGKNR PVALWNVPSA
     LAELVWHPEQ AFDYPRIDST PWAADFETVR AQLRDFCRER VQDYHQARDF PAREGTSSLS
     PYLAIGVLSA RQCVARLYHE SSMGELSEGA QVWLSELIWR EFYQHLVAIE PNLSKSRDFV
     EWGARLEWWN DNEKFQLWCE GKTGYPIVDA AMRQLNQTGW MHNRLRMIVA SFLTKDLHID
     WRWGERYFMS RLIDGDYAAN NGGWQWCAST GCDGQPYFRI FNPVSQGEKF DPNGDFIRRW
     VPELRSVSSA YIHQPWTYPA VNSVLYPARL VDHKQEREVT LRLYKTAKG