ID C6YWG5_9GAMM Unreviewed; 464 AA.
AC C6YWG5;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE SubName: Full=FAD binding domain of DNA photolyase family protein {ECO:0000313|EMBL:AJI74680.1};
GN ORFNames=BZ13_112 {ECO:0000313|EMBL:AJI74680.1};
OS Francisella philomiragia subsp. philomiragia ATCC 25015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=539329 {ECO:0000313|EMBL:AJI74680.1, ECO:0000313|Proteomes:UP000031897};
RN [1] {ECO:0000313|EMBL:AJI74680.1, ECO:0000313|Proteomes:UP000031897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O#319L {ECO:0000313|EMBL:AJI74680.1,
RC ECO:0000313|Proteomes:UP000031897};
RX PubMed=25931589;
RA Johnson S.L., Daligault H.E., Davenport K.W., Coyne S.R., Frey K.G.,
RA Koroleva G.I., Broomall S.M., Bishop-Lilly K.A., Bruce D.C., Chertkov O.,
RA Freitas T., Jaissle J., Ladner J.T., Rosenzweig C.N., Gibbons H.S.,
RA Palacios G.F., Redden C.L., Xu Y., Minogue T.D., Chain P.S.;
RT "Genome sequencing of 18 francisella strains to aid in assay development
RT and testing.";
RL Genome Announc. 3:0-0(2015).
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; CP010019; AJI74680.1; -; Genomic_DNA.
DR RefSeq; WP_004287886.1; NZ_DS999316.1.
DR AlphaFoldDB; C6YWG5; -.
DR KEGG; fpt:BZ13_112; -.
DR PATRIC; fig|539329.6.peg.113; -.
DR HOGENOM; CLU_010348_2_2_6; -.
DR Proteomes; UP000031897; Chromosome.
DR GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
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:SF9; (6-4)-PHOTOLYASE, ISOFORM A; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 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:AJI74680.1}.
FT DOMAIN 4..125
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 229..233
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 263
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 363..365
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 297
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 350
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 373
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 464 AA; 54623 MW; 0063BA83AA8F3235 CRC64;
MPKKIAIHWF RQDLRLADNP ALHQASQADE TITIFILDEN QEIGGASKLW LHHSLSSLSK
SLNNKLNFFS GNPLEIIKKL VKENNITDFY WNRCYDKYSI DRDTQIKQFL QEQDINVSSF
NGSLLIEPWQ CKKDDGTHYK VYTPFYKELI KIRKYRSNIV KPSFNSLKKL ETADELDSLK
LLEPKLSWQN IIDQWQIGED ASHQILEEFL DGKVKEYKIA RDFMSTDSTS KLSPYLHFGE
ISPNQIFNAV QSLDYIGNNE EHFIKELVWR DFSYYQIYYY PELHNKNINQ KFDSFEWDND
ATLLKRWQTG QTGIPIVDAG MRELWQTGYM HNRVRMIVAS FLIKNCLIHW KYGEKWFFDT
LFDADFASNN ANWQWVAGCG LDAAPYFRIF NPVLQAEKFE AYEYIRKYVP ELKFLPNKLI
AKPWEASELV LQEAGVKLGD NYPTPVIDLK KSRDKALELH KKLN
//