ID A0A0B3BN61_9PSED Unreviewed; 479 AA.
AC A0A0B3BN61;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:KHO64055.1};
GN ORFNames=PT85_12385 {ECO:0000313|EMBL:KHO64055.1};
OS Pseudomonas flexibilis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO64055.1, ECO:0000313|Proteomes:UP000030980};
RN [1] {ECO:0000313|EMBL:KHO64055.1, ECO:0000313|Proteomes:UP000030980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO64055.1,
RC ECO:0000313|Proteomes:UP000030980};
RA Shin S.-K., Yi H.;
RT "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL Submitted (NOV-2014) 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}.
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:KHO64055.1}.
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DR EMBL; JTAK01000005; KHO64055.1; -; Genomic_DNA.
DR RefSeq; WP_039606812.1; NZ_JTAK01000005.1.
DR AlphaFoldDB; A0A0B3BN61; -.
DR STRING; 706570.PT85_12385; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000030980; 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; 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:KHO64055.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030980}.
FT DOMAIN 1..133
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 237..241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 276
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 279..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 377..379
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 311
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 364
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 387
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 479 AA; 53577 MW; 7E815A459C92990C CRC64;
MRQLIWLRSD LRVHDNRALH AALAAGPTLA VYLITPGQWC AHDDAPCKID FWLRNLTELR
LQLNALNVPL LIRQAERWDA APAVLAELCQ THGIGCVQVN DEYGLNEAAR DQAVADRLAA
QGVGFRRHLD QLLFAPGSLL TRSGGYFKVF SQFRKVAHAR LHDALPDCLP RPQPQAPLAV
EGDSLPDSVA GFARPNETLR QLWLAGEGHA LDRLQRFVDE HLADYDRCRD LPALPGTSQL
SPYLAAGVLS PRQCLHAALR ANQGEFASGQ PGAVAWINEL LWREFYKHVL VGFPRVSRHR
AFRPETEALP WRDAPGELAA WQAGRTGFPL IDAAMRQLAA TGWMHNRLRM LVAMFLSKNL
LIDWRAGERF FMGQLIDGDL AANNGGWQWS ASTGTDAVPY FRLFNPISQS RRFDPYGRFI
RHWLPELAHL DNRAIHEPAA LGGLFGAPNY PRPLVDLSAS RARALAAFRD LPSRETDHE
//
