ID B8KKQ3_9GAMM Unreviewed; 488 AA.
AC B8KKQ3;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EED31670.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:EED31670.1};
GN Name=phrB {ECO:0000313|EMBL:EED31670.1};
GN ORFNames=NOR53_3707 {ECO:0000313|EMBL:EED31670.1};
OS gamma proteobacterium NOR5-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=566466 {ECO:0000313|EMBL:EED31670.1};
RN [1] {ECO:0000313|EMBL:EED31670.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NOR5-3 {ECO:0000313|EMBL:EED31670.1};
RA Amann R., Fuchs B., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (SEP-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 class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
CC -!- SIMILARITY: Belongs to the DNA photolyase family.
CC {ECO:0000256|RuleBase:RU004182}.
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DR EMBL; DS999406; EED31670.1; -; Genomic_DNA.
DR AlphaFoldDB; B8KKQ3; -.
DR STRING; 566466.NOR53_3707; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_7_1_6; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000003977; Unassembled WGS sequence.
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:EED31670.1}.
FT DOMAIN 1..131
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 488 AA; 56204 MW; E6BD2D66F3A02EB2 CRC64;
MNTLVWLKRD LRLQDHAPLR AAIAAGSSTL LLYCFEPELL SDPHYSDRHW RFVWQSLEDM
RRSLGPQASA LHVCLGDPRE IFARLLQDGQ LQRVYSYEET GLAKTFARDR DVAAMLQSHG
IPWEEFPSNG VQRGRCNRKG WNRDWGRQMN TPCDTTNPQE IYSNAAAGST LKAFHLTDPP
QSWTASHKDF QTGGESTARR TLRDFLERRV SGYARNISKP LASRESCSRL SPYLAWGNLS
IRQVYQALGE AQNRGGPSRA LQAFESRLHW HCHFIQKFEM ECRMEHEDIN RGYLAHPRAF
CEDRVRAWAQ GNTGYPLIDA SMRCLAATGY INFRSRAMLV SFLTHHLWQD WRVGAAHLAG
LFLDFEPGIH FAQLQMQAGV TGINTIRIYN PVKQSEEHDP DGVFIRQWVP ELAEVPAPMI
HRPWDLSPME QIIYGLDTKA YSPPIVDVSE TYRSARDRLW ALKDDSVVRR ERKRILSRHI
EKRYQSAT
//
