ID G0HDK1_CORVD Unreviewed; 492 AA.
AC G0HDK1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:AEK36010.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:AEK36010.1};
GN Name=phr {ECO:0000313|EMBL:AEK36010.1};
GN OrderedLocusNames=CVAR_0657 {ECO:0000313|EMBL:AEK36010.1};
OS Corynebacterium variabile (strain DSM 44702 / CIP 107183 / JCM 12073 /
OS NCIMB 30131) (Corynebacterium mooreparkense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=858619 {ECO:0000313|EMBL:AEK36010.1, ECO:0000313|Proteomes:UP000006659};
RN [1] {ECO:0000313|EMBL:AEK36010.1, ECO:0000313|Proteomes:UP000006659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44702 / JCM 12073 / NCIMB 30131
RC {ECO:0000313|Proteomes:UP000006659};
RX PubMed=22053731; DOI=10.1186/1471-2164-12-545;
RA Schroeder J., Maus I., Trost E., Tauch A.;
RT "Complete genome sequence of Corynebacterium variabile DSM 44702 isolated
RT from the surface of smear-ripened cheeses and insights into cheese ripening
RT and flavor generation.";
RL BMC Genomics 12:545-545(2011).
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; CP002917; AEK36010.1; -; Genomic_DNA.
DR RefSeq; WP_014009200.1; NC_015859.1.
DR AlphaFoldDB; G0HDK1; -.
DR STRING; 858619.CVAR_0657; -.
DR KEGG; cva:CVAR_0657; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_11; -.
DR Proteomes; UP000006659; 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:AEK36010.1}.
FT DOMAIN 6..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 253..257
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 407..409
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 325
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 394
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 417
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 492 AA; 54426 MW; 89344C160930BCC0 CRC64;
MTDRSAMTLV WFRDDLRLAD NAALEWAAQG GEVIAVVIDE DAAATGVRPR GAAASWWRER
SLSQLAGRLL EHGVPMLHLA GDPVDIMTAL PGLLAVDAVV WNRRYEEPLR FVDSRIKETL
QAGGTEVHSF PGHLLTEPWQ VTTGEGRPYR VFTPYSRAAT PVAEDAVAQL VEAAAQVPAD
LRGPEKDLPE VPFPPVRPVD PAPWAASLAD HWTPGEEAGQ ATLAAFVTGD RRTTATGSPG
YADGRDIPDA DATTGLSPHL RFGEVSPHRV WYAVARAVDA GDVPAADGSA LHSELLWRDF
AWQRLYHRPD LASRCVREQF TQFPWRWDNS LPGDVKHLGD ATALAQDLSA WRSGTTGIPL
VDAGMRELWT TGWMHNRVRM VVGSFLTKNL LADWRHGEQW FWDTLVDADP ASNPFNWQWV
AGCGDDASPY FRIFNPETQR KKFDPELGYV NRWVPEFVGP EAAHAGPYPP PMVDLRESRQ
RALAAYECLN AP
//
