ID A0A1A8T9T1_9GAMM Unreviewed; 467 AA.
AC A0A1A8T9T1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:SBS28394.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:SBS28394.1};
GN Name=phrB {ECO:0000313|EMBL:SBS28394.1};
GN ORFNames=MSP8886_01156 {ECO:0000313|EMBL:SBS28394.1};
OS Marinomonas spartinae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1792290 {ECO:0000313|EMBL:SBS28394.1, ECO:0000313|Proteomes:UP000092544};
RN [1] {ECO:0000313|EMBL:SBS28394.1, ECO:0000313|Proteomes:UP000092544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8886 {ECO:0000313|EMBL:SBS28394.1,
RC ECO:0000313|Proteomes:UP000092544};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FLOB01000002; SBS28394.1; -; Genomic_DNA.
DR RefSeq; WP_067013642.1; NZ_FLOE01000003.1.
DR AlphaFoldDB; A0A1A8T9T1; -.
DR STRING; 1792290.MSP8886_01156; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000092544; 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:SBS28394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092544}.
FT DOMAIN 3..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 232..236
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 272..279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 304
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 357
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 380
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 467 AA; 54615 MW; E980FF91146FE403 CRC64;
MAIEQLVWIR NDLRWQDNPA LYFASLKGPI RVIVIATPKQ WQEHHESGSK IGLRAGLIRC
LFSKLVSLGI PADLIEVDRF KHIPDILCQY CQDNGIKHLW YNQDFPIHER QRDQAVKQAL
QAIHIEVHPQ EPDLIVSRPV LSQQGTPFKV FTPFYKRWLT MLNEQSIEPL PIPKKQADAL
SEQPLTMIWQ QPFRDDLWKP DQDKANQTLW QFCHRKEDLY DKQRDFPMTP GTSTLSPYLA
LGALGPRECV YAIAYVCNEQ GRSWQDSIWL KELAWRDFYR QLMLHFPTLS KHKPFKPETD
RIVWRDNKAE RLAWQKGQTG FPIVDAAMRQ LNQTGWMHNR LRMITASFFS KLLFADWHHG
EQYFMSKLID GEFAANNGGW QWSASTGCDA APYFRVFNPT RQSERYDAKG EFIRRFVPEL
KSLDNKSIHN PSTDQRDALG YPNPIVDYKT ARKAAIEAFD RLKNHHS
//
