PHR_BUCAI
ID PHR_BUCAI Reviewed; 483 AA.
AC P57386;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BU300;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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; BA000003; BAB13009.1; -; Genomic_DNA.
DR RefSeq; NP_240123.1; NC_002528.1.
DR RefSeq; WP_010896056.1; NC_002528.1.
DR AlphaFoldDB; P57386; -.
DR SMR; P57386; -.
DR STRING; 107806.10038974; -.
DR PRIDE; P57386; -.
DR EnsemblBacteria; BAB13009; BAB13009; BAB13009.
DR KEGG; buc:BU300; -.
DR PATRIC; fig|107806.10.peg.311; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_0_6; -.
DR OMA; WQWSASS; -.
DR Proteomes; UP000001806; 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..483
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085106"
FT DOMAIN 2..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 278..285
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 345..346
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT BINDING 109
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 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 225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 237..241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 376..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 310
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 363
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 386
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
SQ SEQUENCE 483 AA; 57530 MW; 9701CE076EBC5020 CRC64;
MQKNLIWFRN DLRVYDNTAL HQACQNDTDK VISLFISTPK QWHNQSVSKK KISFMYYHLI
SLQKELLKLN IILYYHESTD FLNSIEYLIF FCKKHKVNNL FYNYEYAINE RYRDYLVKKK
LSQKGFLVKG FHDNLLFSNR QIRNQKNETY KVFTFFKKKV IQNLHNNIPQ CFPVPSKRKS
DRDIFLTSIS LKNVNLNFNK NFFPVGEKEA INRLKNFCIY KFNDYFLKRD YPFLDATSML
SPYLSAGIIS SRYCLKVLLK TKNSLPLNVL LTSPWFDQIL WREFYYHLLI GFPKISRSES
LVTWEKEIHW INNIKHFNAW KEGNTGFPII DAGMRQLNEL GWMHNRLRMI TSSFLVKNLL
INWREGEEHF ISNLIDGDLA LNNGGWQWSA SVGCDSVPYI RIFNPLHQSK TFDESGNFIK
KFIPELKNVP NHHIHQPHEW SKQKNFKIDY PNPIINYSES RKTSLSLFKQ ARLKLHKNGL
KNS
