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
//