ID A0A0Q5H439_9BURK Unreviewed; 490 AA.
AC A0A0Q5H439;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KQQ87468.1};
GN ORFNames=ASF77_18095 {ECO:0000313|EMBL:KQQ87468.1};
OS Massilia sp. Leaf139.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ87468.1, ECO:0000313|Proteomes:UP000051760};
RN [1] {ECO:0000313|EMBL:KQQ87468.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87468.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ87468.1, ECO:0000313|Proteomes:UP000051760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ87468.1,
RC ECO:0000313|Proteomes:UP000051760};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
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 family.
CC {ECO:0000256|RuleBase:RU004182}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQQ87468.1}.
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DR EMBL; LMOJ01000025; KQQ87468.1; -; Genomic_DNA.
DR RefSeq; WP_056343764.1; NZ_LMOJ01000025.1.
DR AlphaFoldDB; A0A0Q5H439; -.
DR STRING; 1736272.ASF77_18095; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000051760; Unassembled WGS sequence.
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:KQQ87468.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051760}.
FT DOMAIN 5..138
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 229
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 241..245
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 381..383
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 312
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 368
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 391
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 490 AA; 54407 MW; 3584067359D2F0C4 CRC64;
MIPKSKSLVW FRRDLRVFDH AALHHALRDA MQAGGVVHCV FVFDTEILAG LPRDDRRVRF
IHASLQELDA ELRALGGGLI VRHGPASLEI PRLAAELDAH AVYLNEDYEP DAIGRDASVA
EALANEGRAL LRFKDQVIFE KNEVLTMAGG IYGVFTPYKN AWLKRLNAQP EAAAPWMIEP
YAAALAPAPA TPLPSLAQLG FDDGPLPAPA GMTGANRLFE DFLPRLADYG TARDFPTQDT
TSRLSIHLRF GTTSVRHLVR TLRQMMANGA GGAGAPVWLS ELIWREFYAM ILFHHPHIAG
ASFKPAFDAV AWEAGEDAQT LFAAWCEGRT GYPLVDAAMA QLNTTGFMHN RLRMVTASFL
VKDLGIDWRW GERYFARHLN DYDLASNVGG WQWAASTGCD AQPWFRIFNP TTQSQRFDKQ
GAFIRQYLPQ LAGLDARDIH APWLVPEAEL AACGIVLGRD YPRPVVDHAQ ARQRTLERFA
MVKAAQPDSD
//
