PHR_ALKPO
ID PHR_ALKPO Reviewed; 479 AA.
AC Q04449; D3FU53;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE EC=4.1.99.3;
DE AltName: Full=DNA photolyase;
DE AltName: Full=Photoreactivating enzyme;
GN Name=phr; OrderedLocusNames=BpOF4_00935;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 141-479.
RX PubMed=7678007; DOI=10.1016/s0021-9258(18)54205-8;
RA Quirk P.G., Hicks D.B., Krulwich T.A.;
RT "Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and
RT characterization of the pH-regulated cytochrome caa3 oxidase it encodes.";
RL J. Biol. Chem. 268:678-685(1993).
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).
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; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; CP001878; ADC48255.1; -; Genomic_DNA.
DR EMBL; M94110; AAA22361.1; -; Genomic_DNA.
DR AlphaFoldDB; Q04449; -.
DR SMR; Q04449; -.
DR STRING; 398511.BpOF4_00935; -.
DR EnsemblBacteria; ADC48255; ADC48255; BpOF4_00935.
DR KEGG; bpf:BpOF4_00935; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_9; -.
DR OMA; YQKFLGI; -.
DR Proteomes; UP000001544; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW Reference proteome.
FT CHAIN 1..479
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085105"
FT DOMAIN 6..137
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 278..285
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 344..345
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 241..245
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 278..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 375..377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 407
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 309
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 362
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 385
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
SQ SEQUENCE 479 AA; 56018 MW; A4CA3EEBEFB548E8 CRC64;
MGNSDSLKAV WFRRDFRLHD HTALKHAIEA IEKHGGKWLA FFYLDPKTAS VEPVHHDYFF
QTVMQFKQML KTNGGDLYII TGTIEGALSK LLQAFPEIDA VYANDDRVGD GRLRDEAAEH
FLAKQSIPFY TFEDAYLTEP DQVLKKDGTP YKVFTPYYKA WAKERKRTPA VIKRDVLLGS
VHKGTAPDRE AETLFNNLIK KCSYDWSAIG EEHAIKRLQM FTKKRLSGYK ANRDFPSITG
TSRLSPYIKT GAVSSRSIYY HILNAEADSY SAETFLKELA WRDFYRMVHF YEPDCKDREI
MEGYRELNWS HDQDDLTSWK RGETGFPIVD AGMRQLLNEG WMHNRLRMIT ASFLTKDLLI
DWRLGERYFE RMLIDYDPSS NIGGWQWAAS VGTDAVPYFR IFNPVTQSKR FDENGTYIRT
YIPELNHVPD HYIHEPWKMS EEEQVKYKCR LDEDYPLPIV DHSKQRKKAL SFFKGDDEE
