ID B1Y5C9_LEPCP Unreviewed; 493 AA.
AC B1Y5C9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ACB33517.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ACB33517.1};
GN OrderedLocusNames=Lcho_1248 {ECO:0000313|EMBL:ACB33517.1};
OS Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS discophora (strain SP-6)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB33517.1, ECO:0000313|Proteomes:UP000001693};
RN [1] {ECO:0000313|EMBL:ACB33517.1, ECO:0000313|Proteomes:UP000001693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC {ECO:0000313|Proteomes:UP000001693};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT "Complete sequence of Leptothrix cholodnii SP-6.";
RL Submitted (MAR-2008) 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; CP001013; ACB33517.1; -; Genomic_DNA.
DR RefSeq; WP_012346279.1; NC_010524.1.
DR AlphaFoldDB; B1Y5C9; -.
DR STRING; 395495.Lcho_1248; -.
DR KEGG; lch:Lcho_1248; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_7_1_4; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000001693; 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:ACB33517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT DOMAIN 2..131
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 454..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 266
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 493 AA; 55217 MW; CA11C7A63EEC9F27 CRC64;
MSRAVVWFKR DLRVTDHAPL AEAARCDAAL ALFIIEPAWL DSPECHPRHV TWLLKCLAPL
RDALAARGLP LLVRTGEAVE VLAALRREFA CTRLFSHEET GPGWSYARDR AVARWCRAHG
VAWTEWPQTG VIRRLKDRRG WAGRWQQRMD APCVRVPAGW RAAPGFAPST LPADLPTLRE
LGVATAPDTP PAGEAAAQQM LQSFLGGRAL GYRRHLSSPL AAEAGCSRLS EHLAFGTLSL
RMLHQATEAT LRATSDRELA YSLRGFAGRL RWHCHFMQKL EDEPAIEWRN FARSADGLRP
GDGSALQTAD RERLQAWCEG RTGFPMVDAC MRQLRATGWL NFRMRAMLVS FAAYHLWLHW
REPGLFLARQ FLDFEPGIHW SQMQMQSGTT GINTLRIYSP AKQALDHDPQ GEYVRRWVPE
FGSAAYPAPI VDERAAVAAA KQRLYGLRQT PEAHDEAGAI QHKHGSRKSG LPPSGNRPTR
RTRAADDGQG RLF
//
