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Database: UniProt
Entry: A0A1L6I2Q9_9BURK
LinkDB: A0A1L6I2Q9_9BURK
Original site: A0A1L6I2Q9_9BURK 
ID   A0A1L6I2Q9_9BURK        Unreviewed;       505 AA.
AC   A0A1L6I2Q9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:APR37906.1};
GN   ORFNames=BTO02_20310 {ECO:0000313|EMBL:APR37906.1};
OS   Paraburkholderia sp. SOS3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR37906.1, ECO:0000313|Proteomes:UP000184708};
RN   [1] {ECO:0000313|EMBL:APR37906.1, ECO:0000313|Proteomes:UP000184708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SOS3 {ECO:0000313|EMBL:APR37906.1,
RC   ECO:0000313|Proteomes:UP000184708};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|ARBA:ARBA00001932};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC   -!- SIMILARITY: Belongs to the DNA photolyase family.
CC       {ECO:0000256|RuleBase:RU004182}.
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DR   EMBL; CP018812; APR37906.1; -; Genomic_DNA.
DR   RefSeq; WP_075159078.1; NZ_CP018812.1.
DR   AlphaFoldDB; A0A1L6I2Q9; -.
DR   STRING; 1926494.BTO02_20310; -.
DR   KEGG; para:BTO02_20310; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000184708; Chromosome 2.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.40.80; -; 1.
DR   Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR   PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR   SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore {ECO:0000256|RuleBase:RU004182};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW   1}; Lyase {ECO:0000313|EMBL:APR37906.1}.
FT   DOMAIN          12..152
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         247
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         295
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         298..305
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         399..401
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            330
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            386
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            409
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   505 AA;  57944 MW;  E877A6400520A533 CRC64;
     MTEPRQLDAS FDHGLVWFRR DLRTGDNAAL YYALKHCRHV WCVFVFDSTI LQPLIDRARE
     RDPKQMPRDR RVDFIVASVA ELDRSLRDGH GGLMVSHGDP RDVIPKLAER LKIDAVFANH
     DYEPSAIERD ETVADRLRDA QRELITFKDQ AIFERDEVLN GQNKPFSVFT PYRNAWLRKL
     TPFDLKPYPV ERYAKSLAKP PAEFDHGIPS LSQLGFERSN LADLKLPPGM SGAQQLLEDF
     LTRIDSYADR RNFPAAAGPS YLSVHQRFGT VSIRTLARLA NDLSLQPDGG GASAWLTELI
     WRDFYFMILT HHPQVADGAP FKPEFDSVRW ERGHEADAAF AAWREARTGY PLVDAAMLQI
     NTTGYMHNRL RMVTASFLVK DLGLDWHLGE QYFAEMLNDF DLSANNGNWQ WAASTGCDAQ
     PWFRIFNPVT QSERFDPQGR FIKRYLPQLE KVPPKWIHAP WLASAEQLAE WGVVLGENYP
     PPMVDHAQAR QLTLERFGRV RPRKG
//
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