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Database: UniProt
Entry: A0A1I5XGL0_9RHOB
LinkDB: A0A1I5XGL0_9RHOB
Original site: A0A1I5XGL0_9RHOB 
ID   A0A1I5XGL0_9RHOB        Unreviewed;       473 AA.
AC   A0A1I5XGL0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SFQ31090.1};
GN   ORFNames=SAMN05421853_103390 {ECO:0000313|EMBL:SFQ31090.1};
OS   Roseivivax halotolerans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseivivax.
OX   NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ31090.1, ECO:0000313|Proteomes:UP000243106};
RN   [1] {ECO:0000313|Proteomes:UP000243106}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-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; FOXV01000003; SFQ31090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5XGL0; -.
DR   STRING; 93684.SAMN05421853_103390; -.
DR   Proteomes; UP000243106; 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:SFQ31090.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243106}.
FT   DOMAIN          5..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         236..240
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         271
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         373..375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            305
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            360
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            383
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   473 AA;  53572 MW;  DEB9C4454A5F3A67 CRC64;
     MADTRPTILW HRRDLRLSDH PALDAAARRG GPVIPVFIRD NLVDKLGTAP VWRLGLGLGV
     LGESYAEKGS RLILRAGPPL EVLRKLVEET GAGAVYWMRA YDADSVERDE RVKSGLKDDG
     LEAKSFAGHL MFEPWSVETK QGEFYKVYTP FWRAVKDREV PEPIATPGKI PAPADWPASD
     ALDEWSLGAG MDRGADVVRP YVQLGESAAQ ARLGAFVSSK IGAYKANRDI PAVDGTSNLS
     ENLALGEITP HQCWAAGMRA LNDGKDDAQT FLQELVWREF AYHLLWHTPQ LETGNWREEW
     DAFPWNEDER KSEVIAWKRA RTGMAFVDAA LREMYVTGRM HNRGRMIVAS YLCKHLMCHW
     KIGKEWFEDC LIDWDPASNA MGWQWSAGSG PDATPYFRVF NPETQVDRFD KDRTFINRWI
     AEGQNNPPET ALSYFEAIPR SWKISPDDDY PEPIVGAKEG RQRALDAYEN RDF
//
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