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Database: UniProt
Entry: A0A2C5UQK6_RAOPL
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ID   A0A2C5UQK6_RAOPL        Unreviewed;       480 AA.
AC   A0A2C5UQK6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:VFS64178.1};
DE            EC=4.1.99.3 {ECO:0000313|EMBL:VFS64178.1};
GN   Name=phrB {ECO:0000313|EMBL:VFS64178.1};
GN   ORFNames=NCTC12998_02476 {ECO:0000313|EMBL:VFS64178.1};
OS   Raoultella planticola (Klebsiella planticola).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Raoultella.
OX   NCBI_TaxID=575 {ECO:0000313|EMBL:VFS64178.1, ECO:0000313|Proteomes:UP000345637};
RN   [1] {ECO:0000313|EMBL:VFS64178.1, ECO:0000313|Proteomes:UP000345637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12998 {ECO:0000313|EMBL:VFS64178.1,
RC   ECO:0000313|Proteomes:UP000345637};
RG   Pathogen Informatics;
RL   Submitted (MAR-2019) 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; CAADJE010000022; VFS64178.1; -; Genomic_DNA.
DR   RefSeq; WP_032688812.1; NZ_VKNI01000025.1.
DR   AlphaFoldDB; A0A2C5UQK6; -.
DR   KEGG; rpln:B1209_19115; -.
DR   Proteomes; UP000345637; Unassembled WGS sequence.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:1901363; F:heterocyclic compound binding; IEA:UniProt.
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; 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:VFS64178.1}.
FT   BINDING         223
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         235..239
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         272
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         275..282
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         373..375
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            307
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            360
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            383
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   480 AA;  54210 MW;  1AC1D0E83798BA55 CRC64;
     MATHLVWFRA DLRIHDNQAL AAACRDPHAR VLALFIATPG QWHQHGMAPR QAAFIVRHLR
     SLQSALAERG IALQVAEAED FSASVQLLAD YCAQQQVSHL FYNYQYEINE RQRDAAVEKR
     LSGVVCHGFD DALLLSPGSV LTGNHEMYKV FTPFKNAFLR RLREALPECV AAPTVRGHGP
     LTPAPLPEIG YPQEAFDPHL FAEDEKTAIA RLRRFCQQQA ADYDLQRDFP ATEGTSRLSP
     CLAVGVLSPR QCLHRLLAEQ PAALDGEAGS VWLNELIWRE FYRHLMVFYP DLCKGRPFIA
     WTDNVTWRDD VQGLEAWQAG KTGFPIVDAA MRQLNATGWM HNRLRMIAAS FLVKDLRIDW
     RAGERYFINR LIDGDLAANN GGWQWAASTG TDAAPYFRIF NPTTQGEKFD KGGAFIRQWL
     PELADVPDKA LHQPWIWADK QRVSLNYPRP LVDHKQARLE TLAAWEAASK SLTPRPGRGS
//
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