ID A0A0U5L1S8_9GAMM Unreviewed; 475 AA.
AC A0A0U5L1S8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:CUU23336.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:CUU23336.1};
GN Name=phrB {ECO:0000313|EMBL:CUU23336.1};
GN ORFNames=EM595_1100 {ECO:0000313|EMBL:CUU23336.1};
OS Duffyella gerundensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Duffyella.
OX NCBI_TaxID=1619313 {ECO:0000313|EMBL:CUU23336.1, ECO:0000313|Proteomes:UP000059419};
RN [1] {ECO:0000313|Proteomes:UP000059419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Blom J.;
RL Submitted (NOV-2015) 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; LN907827; CUU23336.1; -; Genomic_DNA.
DR RefSeq; WP_067428720.1; NZ_LN907827.1.
DR AlphaFoldDB; A0A0U5L1S8; -.
DR STRING; 1619313.EM595_1100; -.
DR KEGG; ege:EM595_1100; -.
DR PATRIC; fig|1619313.3.peg.1142; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000059419; Chromosome 1.
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; 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:CUU23336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000059419}.
FT DOMAIN 2..136
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 433..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 238..242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 275
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 278..285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 376..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 310
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 363
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 386
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 475 AA; 54704 MW; 40A643087101BDA9 CRC64;
MATHLVWLRN DLRINDNYAL HAACRDNKAT VIALYVATPG QWQDHDMAPK QAAFIAKSLH
LLQQSLAERG IALHYQQCDR YDDAVETVKT FCQQQKVDAF FYNYQYAINE RERDAAVERA
LNALNITCQG FDDGLLLPPG SVQSGSNGMY KVFTPFSKAF VRRLHQELPE CVPAPAARDG
APLTTLHRLT PFDYPQEAFD ETLFPPGEQG GLARLREFCQ QPVVQYQDRR NFPVLDGTSR
LSVHLATGTL SPRQCLHRLL KHHPDALDDG KSFIWLNELI WREFYTHLMV AWPMLCKHQP
FIGWTRKVQW QENNALLTAW QQGQTGYPIV DAAMRQMNAL GWMHNRLRMI TASFLVKDLL
IDWRTGERYF MRQLIDGDYA ANNGGWQWAA STGTDSAPYF RIFNPTTQGE RFDKDGEFIR
RWLPELKDVP DSDIHSPQQW AEKNHKKLDY PQPIVEHKDA RKKTLDAFEA ARNAS
//
