ID A9BJX3_PETMO Unreviewed; 462 AA.
AC A9BJX3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ABX31716.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ABX31716.1};
GN OrderedLocusNames=Pmob_0994 {ECO:0000313|EMBL:ABX31716.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX31716.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX31716.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000879; ABX31716.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BJX3; -.
DR STRING; 403833.Pmob_0994; -.
DR KEGG; pmo:Pmob_0994; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_0; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
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:ABX31716.1}.
FT DOMAIN 16..146
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 230
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 242..246
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 276..283
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 462 AA; 54390 MW; AC16EEC2AAE1CFDE CRC64;
MLKALEVIKI SNYKYKIGLH IFRRDLRLED NTSLIEALQS CERVIPAFIF DDRQIKDNDY
KSDNAVQFMI ACLKELNDQL HQLNARLYFF EGLTAKVVES LIKTLGIEAV FVNKDYTPFS
KKRDNEIKAI CERERVDFKE HFDVLLHEPT EVLKDNGMPY IKFTDFLKKS KKIDVREPQK
NKFKNYFTEE ISSSIALQVD KFPQNENLIL KGGRKEGLSY IERIVKLKNY SETRNTPSID
GTTKLSPHLK FGTVSVREVY GKVNENFGNE HEIITQLHWR DFFTHILYHF PHVLGNSFKE
KYNQIQWEND VDKFKAWCTG RTGYPIVDAG MRQLNLTGWM HNRVRMITGS FLVKDLHIDW
RWGEKYFAQR LVDYDPAINN GNWQWVASTG CDAQPFFRIF NPILQQQKFD PECNYIKTWL
PELTNLNLEQ IHTLNIPKDI DYPTPIVDHK VASEKAKKLY KI
//
