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Database: UniProt
Entry: A0A0K1K3X3_9BURK
LinkDB: A0A0K1K3X3_9BURK
Original site: A0A0K1K3X3_9BURK 
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
//
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