PHR_BUCBP
ID PHR_BUCBP Reviewed; 478 AA.
AC Q89AJ9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE EC=4.1.99.3;
DE AltName: Full=DNA photolyase;
DE AltName: Full=Photoreactivating enzyme;
GN Name=phrB; OrderedLocusNames=bbp_278;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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 (By similarity). {ECO:0000250}.
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|UniProtKB:P00914};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC subunit. {ECO:0000250|UniProtKB:P00914};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; AE016826; AAO27003.1; -; Genomic_DNA.
DR RefSeq; WP_011091404.1; NC_004545.1.
DR AlphaFoldDB; Q89AJ9; -.
DR SMR; Q89AJ9; -.
DR STRING; 224915.bbp_278; -.
DR EnsemblBacteria; AAO27003; AAO27003; bbp_278.
DR GeneID; 56470819; -.
DR KEGG; bab:bbp_278; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_0_6; -.
DR OMA; YQKFLGI; -.
DR OrthoDB; 184000at2; -.
DR Proteomes; UP000000601; 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:0000166; F:nucleotide 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 Nucleotide-binding; Reference proteome.
FT CHAIN 1..478
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085107"
FT DOMAIN 2..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 279..286
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 346..347
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P00914"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 239..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 377..379
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 409
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 311
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 364
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 387
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
SQ SEQUENCE 478 AA; 57247 MW; 31A25356FB0A1F72 CRC64;
MNVNLMWFRN DLRLSDNSAL HFSCRNNAST VLALFIATPK QWERHCLAPK KKMLIYKNIV
ALKKKITELG IIFYYYESTD YLESTNYIIE FCKIHKVTSI FFNLEYEFYE RQRDKIIKKK
LKKNNIIINC FHDSVLITPG SIKNSYGKMY KKFSYFKYKC IKQLQLNIPS CFPKPQNKNL
HDHYSLDFTI PIFHTYLEKF DANIFPIGED IVYEKLKFFI KYAFNKYNFD QEIFELNSTS
MLSAHLSIGV ISPRQCVTLL FKEYPDIIHK LEECKWINEL LWREFYQHLL YFYPNIGQNQ
SLYHWENRIK WDNNLYYLNL WKQGNTGYPI IDAGMRQLKQ LGWISNRLRM ITASFLVKNL
LIDWRKGEEY FMSQLIDGDF ASNNGNWQWI ASVGTDSMPY FRIFNPMLQS KKFDINAKFI
RKYIPELSNV STYNIHNPCD NNKTNKIHSK YPQPIINYYH SKKKTLLVFK HAKCSNKL
