ID I0K5M0_9BACT Unreviewed; 452 AA.
AC I0K5M0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:CCG99423.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:CCG99423.1};
GN ORFNames=FAES_1413 {ECO:0000313|EMBL:CCG99423.1};
OS Fibrella aestuarina BUZ 2.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrella.
OX NCBI_TaxID=1166018 {ECO:0000313|EMBL:CCG99423.1, ECO:0000313|Proteomes:UP000011058};
RN [1] {ECO:0000313|EMBL:CCG99423.1, ECO:0000313|Proteomes:UP000011058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 2T {ECO:0000313|Proteomes:UP000011058};
RX PubMed=22689241; DOI=10.1128/JB.00550-12;
RA Filippini M., Qi W., Blom J., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of Fibrella aestuarina BUZ 2T, a Filamentous Marine
RT Bacterium.";
RL J. Bacteriol. 194:3555-3555(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HE796683; CCG99423.1; -; Genomic_DNA.
DR RefSeq; WP_015330522.1; NC_020054.1.
DR AlphaFoldDB; I0K5M0; -.
DR STRING; 1166018.FAES_1413; -.
DR KEGG; fae:FAES_1413; -.
DR PATRIC; fig|1166018.3.peg.3144; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_10; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000011058; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
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; IPR018394; DNA_photolyase_1_CS_C.
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; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|ARBA:ARBA00022991, 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:CCG99423.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011058}.
FT DOMAIN 6..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 230..234
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 261..268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 358..360
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 292
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 345
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 368
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 452 AA; 52700 MW; C4BFEBDE6D7068C2 CRC64;
MKPETPIAIM WHRRDLRLHD NAALYYALKA GRPVLPLFIF DKDILDHLND KRDRRVEFIY
EEVLAMQQAL HKQGSTLLVR YGRPLDVFKE LASEYTLANV FTNYDYETYA KGRDAEVATY
LKSVNAGFHS YKDQTLFDRD EVLTGSGKPY TVFGPYSRNW LSKLDDPFYL KSYPTEKYAD
RFLKTAPTPM VTLEQMGFEP LNEKFPKSTV SDKLLTTYDK TRDFPAQRGT SELSIHLRFG
TISIRELARQ AQANNLTYLK ELCWRDFYFQ VLDHFPHVEH ESFRREYDQV PWLNRPEDIE
RWKAGQTGYP LVDAGMRQLN EIGWMHNRVR MVTASFCVKH LLIDWRIGEA YFAEKLRDYD
LSANNGGWQW AAGSGTDAAP YFRVFNPTEQ ARKFDPKGEY IRRWVPEYNN PAGASVTYPA
PIVDHAFARQ RAITTYKTAL NAEKNGEPVK LR
//
