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Database: UniProt
Entry: X7FF73_9RHOB
LinkDB: X7FF73_9RHOB
Original site: X7FF73_9RHOB 
ID   X7FF73_9RHOB            Unreviewed;       472 AA.
AC   X7FF73;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ETX30726.1};
GN   ORFNames=RISW2_07930 {ECO:0000313|EMBL:ETX30726.1};
OS   Roseivivax isoporae LMG 25204.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=1449351 {ECO:0000313|EMBL:ETX30726.1, ECO:0000313|Proteomes:UP000023430};
RN   [1] {ECO:0000313|EMBL:ETX30726.1, ECO:0000313|Proteomes:UP000023430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 25204 {ECO:0000313|EMBL:ETX30726.1,
RC   ECO:0000313|Proteomes:UP000023430};
RA   Lai Q., Li G., Shao Z.;
RT   "Roseivivax isoporae LMG 25204 Genome Sequencing.";
RL   Submitted (JAN-2014) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETX30726.1}.
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DR   EMBL; JAME01000002; ETX30726.1; -; Genomic_DNA.
DR   RefSeq; WP_043765771.1; NZ_JAME01000002.1.
DR   AlphaFoldDB; X7FF73; -.
DR   STRING; 1449351.RISW2_07930; -.
DR   PATRIC; fig|1449351.3.peg.389; -.
DR   eggNOG; COG0415; Bacteria.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000023430; Unassembled WGS sequence.
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:ETX30726.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023430}.
FT   DOMAIN          4..130
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         235..239
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         270
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         372..374
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            304
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            359
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            382
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   472 AA;  53227 MW;  402738EA6F72E6FF CRC64;
     MPDAPTLLWM RRDLRLSDHP ALAAALDRGG PVIPVFIRDG LVDALGTAPA WRLGLGIGHL
     DGALRDKGSR LTLRSGNAAE VLLELVEETG ARAVHWMRAY DPDSVDRDTR VKEALKARGI
     AAESFAGHLM FEPWTVETGQ GGYYKVYTPF WRAVKERDVA APLAAPSDLA APDSWPGSET
     LGDWGLGRFM DRGAEVVRPY VRLGEDAAQG RLGAFMASKV AAYDTARDIP SEDGTSGLSE
     NLSLGEITPR QCWHAGLRAR EEGKTGAETF LQELVWREFA YHLMWHTPRL LTGNWREEWD
     GFPWNEDRRR AEVRAWERGR TGVAFVDAAM REMYVTGRMH NRGRMIVASY LTKHLMTHWR
     IGCDWFEDCL IDWDPASNAL GWQWSAGSGP DATPYFRVFN PETQLDRFDK GRTYVRRWIA
     EGQKSPPKEA LSYFDAIPRS WKMSAQDDYP APVVGPKEGR KRALEAYENR DF
//
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