ID H6SJ91_PARPM Unreviewed; 369 AA.
AC H6SJ91;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase type I {ECO:0000313|EMBL:CCG08056.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:CCG08056.1};
GN ORFNames=RSPPHO_01430 {ECO:0000313|EMBL:CCG08056.1};
OS Pararhodospirillum photometricum DSM 122.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Pararhodospirillum.
OX NCBI_TaxID=1150469 {ECO:0000313|EMBL:CCG08056.1, ECO:0000313|Proteomes:UP000033220};
RN [1] {ECO:0000313|EMBL:CCG08056.1, ECO:0000313|Proteomes:UP000033220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM122 {ECO:0000313|Proteomes:UP000033220};
RA Duquesne K., Sturgis J.;
RT "Shotgun genome sequence of Phaeospirillum photometricum DSM 122.";
RL Submitted (FEB-2012) 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; HE663493; CCG08056.1; -; Genomic_DNA.
DR AlphaFoldDB; H6SJ91; -.
DR STRING; 1150469.RSPPHO_01430; -.
DR KEGG; rpm:RSPPHO_01430; -.
DR PATRIC; fig|1150469.3.peg.1611; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_5; -.
DR Proteomes; UP000033220; 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 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 PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF9; CRYPTOCHROME-1; 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; PS00691; DNA_PHOTOLYASES_1_2; 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:CCG08056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033220}.
FT DOMAIN 150..351
FT /note="Cryptochrome/DNA photolyase FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF03441"
FT BINDING 105
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 150
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 253..255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 184
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 240
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 263
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 369 AA; 41081 MW; C246BC14536B1297 CRC64;
MAFQSHAGLL LHDPERLTTR SGTPYGVFTP FWNTLVKTVD PGRPEPAPTR VPAPPTLPAS
ERLEDWALRP SAPDWAAGLR AAWTPGEASA QERLDAFLAA GLEGYADLRD RPDRPATSKL
APSLAWGEIS PRQIWSACQM RPPSPGREGF LRQLGWREFC YHGLHRFPDM AERPLKAPFA
RFPWAGPEES QAALARWRRG LTGYPLVDAG MRALWATGWM HNRVRMVVAS FLVKHLLVDW
RAGLAWFHDT LVDADPANNP AGWQWVAGCG SDAAPYFRIF NPVTQAERFD PEGAYVRRWV
PELARLPAPV IHRPWTASAL DLAAAGVRLG QNYPRPQVDH PQARARALAA LASLDEGRKG
QEKQHGELF
//
