ID D5BN92_PUNMI Unreviewed; 477 AA.
AC D5BN92;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ADE40285.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ADE40285.1};
GN OrderedLocusNames=SAR116_2042 {ECO:0000313|EMBL:ADE40285.1};
OS Puniceispirillum marinum (strain IMCC1322).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC Puniceispirillum.
OX NCBI_TaxID=488538 {ECO:0000313|EMBL:ADE40285.1, ECO:0000313|Proteomes:UP000007460};
RN [1] {ECO:0000313|EMBL:ADE40285.1, ECO:0000313|Proteomes:UP000007460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC1322 {ECO:0000313|EMBL:ADE40285.1,
RC ECO:0000313|Proteomes:UP000007460};
RX PubMed=20382761; DOI=10.1128/JB.00347-10;
RA Oh H.M., Kwon K.K., Kang I., Kang S.G., Lee J.H., Kim S.J., Cho J.C.;
RT "Complete genome sequence of "Candidatus Puniceispirillum marinum"
RT IMCC1322, a representative of the SAR116 clade in the
RT Alphaproteobacteria.";
RL J. Bacteriol. 192:3240-3241(2010).
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; CP001751; ADE40285.1; -; Genomic_DNA.
DR RefSeq; WP_013046912.1; NC_014010.1.
DR AlphaFoldDB; D5BN92; -.
DR STRING; 488538.SAR116_2042; -.
DR KEGG; apb:SAR116_2042; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_5; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000007460; 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:ADE40285.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007460}.
FT DOMAIN 4..129
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 223
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 235..239
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 272
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 372..374
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 306
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 359
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 382
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 477 AA; 53669 MW; D318C1635F29E0BB CRC64;
MASSIIIHWF RQDLRLADNP SLVAAAQAGD VLPLFILDDD NAGDHKTGAA GRSWLHHALN
ALNMSLDGKL CVMRGDPVDI IPKLVAKVGA SGVFWNRCYE PWRIARDKML KTNLTNNNIQ
VESFNGSLLW EPWTVLKGDG TPYRVFTPFY RRGCLNAAPP RLPLARPDAM QLVADPESSM
SIDALNLLPD HDWGAKMASH WQIGEAAAMT RLHDFVEGGL NGYKDGRNFP ARPHTSRLSA
HLHWGEISPN MAWYAAIEKR DQAGFDNDID VFLSELGWRE FSHSLLYHFP HLPRQNLQPK
FDSFPWQSDD NALRAWQQGK TGYPIIDAGM RELWETGYMH NRVRMIVGSF LVKNLLLHWH
HGEAWFWDCL VDADLANNSA GWQWIAGCGA DAAPYFRVFN PITQGTKFDA DGSYTRRFVP
ELATLPNKYL FSPWEAPALE LQAAGITLGK DYPNPIVDVK RSREAALAAF ATTRVEP
//
