ID A0A0Q8LUN7_9MICO Unreviewed; 451 AA.
AC A0A0Q8LUN7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KRB36663.1};
GN ORFNames=ASD93_11485 {ECO:0000313|EMBL:KRB36663.1};
OS Microbacterium sp. Root180.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736483 {ECO:0000313|EMBL:KRB36663.1, ECO:0000313|Proteomes:UP000050802};
RN [1] {ECO:0000313|EMBL:KRB36663.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36663.1,
RC ECO:0000313|Proteomes:UP000050802};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB36663.1, ECO:0000313|Proteomes:UP000050802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root180 {ECO:0000313|EMBL:KRB36663.1,
RC ECO:0000313|Proteomes:UP000050802};
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=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:KRB36663.1}.
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DR EMBL; LMHS01000003; KRB36663.1; -; Genomic_DNA.
DR RefSeq; WP_056122483.1; NZ_LMHS01000003.1.
DR AlphaFoldDB; A0A0Q8LUN7; -.
DR STRING; 1736483.ASD93_11485; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000050802; 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; 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:KRB36663.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050802}.
FT DOMAIN 3..132
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
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 268
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 369..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 302
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 356
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 379
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 451 AA; 50660 MW; 29DC712BA952A7BC CRC64;
MPSPSIVWLR DDLRLADNPA LRAAVDRGEP VVVLYVLDEE SPGVRALGGA ARWWLHHSLA
SLGERLAERG ARLVLRRGPA ERVVREAVTD AAAGAVFWNR RYGGPEREVD AALKAGLRAD
GVEVASFAGS LLFEPWTVTT GAGTHFSVFT PFWRACLALP APRQPLPEPR EVAGARHPIA
SDELEDWGLL PTGPDWADGL RETWEPGEPA GRRRLREFLT HDLDAYDRAR DEPSAGATSL
LSPRLRWGEV SPFTVWHEAV EHGHGGRFLS ELGWREFAWH TLFHSPDLAT ANLRREFDAF
PWPRLKPTHL EAWQRGRTGV ALVDAGMREL WETGYMHNRV RMVTASFLVK NLLIDWRRGE
EWFWDTLVDA DAANNPFNWQ WVAGSGADAA PYFRVFNPEL QAKKFDADGH YVRRWAPEHL
SDDPPEPIVD LGETRKAALA AYDVVKRALR G
//
