ID A0A0K1K3X3_9BURK Unreviewed; 487 AA.
AC A0A0K1K3X3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AKU23913.1};
GN ORFNames=ACZ75_23100 {ECO:0000313|EMBL:AKU23913.1};
OS Massilia sp. NR 4-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1678028 {ECO:0000313|EMBL:AKU23913.1, ECO:0000313|Proteomes:UP000056897};
RN [1] {ECO:0000313|EMBL:AKU23913.1, ECO:0000313|Proteomes:UP000056897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NR 4-1 {ECO:0000313|EMBL:AKU23913.1,
RC ECO:0000313|Proteomes:UP000056897};
RA Sul W.J.;
RT "Massilia sp. NR 4-1 isolated from rhizosphere of Torreya nucifera in
RT national heritage Bijarim forest, volcanic Jeju Island, Korea.";
RL Submitted (JUN-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}.
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DR EMBL; CP012201; AKU23913.1; -; Genomic_DNA.
DR RefSeq; WP_050411577.1; NZ_CP012201.1.
DR AlphaFoldDB; A0A0K1K3X3; -.
DR STRING; 1678028.ACZ75_23100; -.
DR KEGG; mnr:ACZ75_23100; -.
DR PATRIC; fig|1678028.3.peg.4686; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000056897; 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:AKU23913.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000056897}.
FT DOMAIN 4..133
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 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 378..380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 309
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 365
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 388
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 487 AA; 54267 MW; D24459E7A342CBCC CRC64;
MAFDTTLVWF RRDLRSFDHA ALHHALRRSR RVFCVFVFDK TILDGLPRRD RRVDFIHASV
AQLGADLQQL GGHLLVRHAD AATAIPALAA ELGAQAVFAN HDYEPQAMVR DAAVAAALEA
QGRSFHSFKD QVIFEKDEVL SQAGTPFSVF TPYKNAWLKK MQADPSCLAP WQVEPYAASL
APGAGTLPTL AELGFEPSNL DQLAIPTGMA GGAALFENFQ SRVADYGFAR DYPALKGPSY
LSLHLRFGTV SIRHLVRTVA ELSARGQAGE GGAVWLSELI WREFYMMILY QHPHVVHSSF
KPAYDAIEWE TGPAADAAFA AWCEGRTGYP LVDAAMAQIN QTGYMHNRLR MVAACFLIKD
LGIDWRRGEA YFALHLNDFD LAANNGGWQW ASSSGCDAQP YFRIFNPVTQ SEKFDAEGRF
IRRYLPQLAK LADKEVHAPW LVPRMLLQQR GIELGRNYPE PIVQHDAARK RTLERYAVVK
APGQPPA
//