ID A0A0C5W3E3_9GAMM Unreviewed; 476 AA.
AC A0A0C5W3E3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AJR05946.1};
GN ORFNames=H744_1c0921 {ECO:0000313|EMBL:AJR05946.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR05946.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR05946.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR05946.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP005973; AJR05946.1; -; Genomic_DNA.
DR RefSeq; WP_044621159.1; NZ_CP005973.1.
DR AlphaFoldDB; A0A0C5W3E3; -.
DR STRING; 658445.H744_1c0921; -.
DR KEGG; pgb:H744_1c0921; -.
DR PATRIC; fig|658445.3.peg.997; -.
DR HOGENOM; CLU_010348_2_2_6; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000032303; Chromosome 1.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; PS00691; DNA_PHOTOLYASES_1_2; 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:AJR05946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT DOMAIN 6..139
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 239..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 281..288
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 379..381
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 313
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 366
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 389
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 476 AA; 54909 MW; 9694F9EEF8C1F3AF CRC64;
MSQHKHIGLV WFRADLRVVD NTALFIAAEQ CDQLIALYVS TPMQWHEHHV APIQVDLLRR
RLPILQQQLE ALGIPLIFKE VADFEQIPQT LLEVSSKHGV SHVFCNKQYE WNELQRDDKT
GHRLAQEQVK FSVFDDSCVI APGKVQTQKG EAFKVFTPFR REWLKQFRAL SPTPLPIPEP
VENPVVVDEP GQITVTYPSS DSMAWPVEEE TIRQRLVTFC YEKVEDYHQQ RDIPAIDGTS
CLSPYLALGM LSPRQCIAVL MAVSPMCLDA PESGAFSWLN EIIWREFYRH LLVAYPDLCR
GQPFQSWTQN VQWQQSSELL SAWQHGLTGF PIVDAAMRQL NQTGWMHNRL RMITASFLTK
DLLIHWQAGE QWFMSKLIDG DFASNNGGWQ WAASTGTDAQ PYFRVFNPTT QGERFDPKGE
FIRTWLHELK DVPDKYIHQP HLWPGSEQIH YPKPIVDHKQ ARLLAISSFK IAKEAQ
//
