PHR_SALTY
ID PHR_SALTY Reviewed; 473 AA.
AC P25078;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE EC=4.1.99.3;
DE AltName: Full=DNA photolyase;
DE AltName: Full=Photoreactivating enzyme;
GN Name=phrB; Synonyms=phr; OrderedLocusNames=STM0709;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1840665; DOI=10.1093/nar/19.18.4885;
RA Li Y.F., Sancar Z.;
RT "Cloning, sequencing, expression and characterization of DNA photolyase
RT from Salmonella typhimurium.";
RL Nucleic Acids Res. 19:4885-4890(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP REVIEW.
RX PubMed=15721603; DOI=10.1016/j.bbabio.2004.02.010;
RA Weber S.;
RT "Light-driven enzymatic catalysis of DNA repair: a review of recent
RT biophysical studies on photolyase.";
RL Biochim. Biophys. Acta 1707:1-23(2005).
CC -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl
CC pyrimidine dimers (in cis-syn configuration), which are formed between
CC adjacent bases on the same DNA strand upon exposure to ultraviolet
CC radiation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC DNA).; EC=4.1.99.3;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000250|UniProtKB:P00914};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC subunit. {ECO:0000250|UniProtKB:P00914};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Absorption:
CC Abs(max)=384 nm;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43069.1; Type=Miscellaneous discrepancy; Note=Submitted sequence seems to have every 20th amino acid deleted.; Evidence={ECO:0000305};
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DR EMBL; X60662; CAA43069.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE006468; AAL19653.1; -; Genomic_DNA.
DR PIR; S22321; S22321.
DR RefSeq; NP_459694.1; NC_003197.2.
DR RefSeq; WP_001142016.1; NC_003197.2.
DR AlphaFoldDB; P25078; -.
DR SMR; P25078; -.
DR STRING; 99287.STM0709; -.
DR PaxDb; P25078; -.
DR PRIDE; P25078; -.
DR EnsemblBacteria; AAL19653; AAL19653; STM0709.
DR GeneID; 1252229; -.
DR KEGG; stm:STM0709; -.
DR PATRIC; fig|99287.12.peg.741; -.
DR HOGENOM; CLU_010348_2_2_6; -.
DR OMA; WQWSASS; -.
DR PhylomeDB; P25078; -.
DR BioCyc; SENT99287:STM0709-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR Gene3D; 3.40.50.620; -; 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; PTHR11455; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; SSF48173; 1.
DR SUPFAM; SSF52425; SSF52425; 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 1: Evidence at protein level;
KW Chromophore; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..473
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085110"
FT DOMAIN 2..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 276..283
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 343..344
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P00914"
FT BINDING 110
FT /ligand="(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:15636"
FT /evidence="ECO:0000250|UniProtKB:P00914"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 236..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 374..376
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 406
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 308
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 361
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 384
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT CONFLICT 115
FT /note="A -> R (in Ref. 1; CAA43069)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="A -> E (in Ref. 1; CAA43069)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53675 MW; C54CBC13BF05D394 CRC64;
MPTHLVWFRR DLRLQDNLAL AAACRDASAR VLALYISTPA QWQAHDMAPR QAAFISAQLN
ALQTALAEKG IPLLFHEVAD FNASIETVKN VCRQHDVSHL FYNYQYEFNE RQRDAAVEKT
LPSVICEGFD DSVILAPGAV MTGNHEMYKV FTPFKNAWLK RLKEDIPPCV PAPKIRVSGA
LSTPLTPVSL NYPQQAFDAA LFPVEENAVI AQLRQFCAQG ADEYALRRDF PAVDGTSRLS
ASLATGGLSP RQCLHRLLAE QPQALDGGPG SVWLNELIWR EFYRHLMTWY PALCKHQPFI
RWTKRVAWQE NPHYFQAWQK GETGYPIVDA AMRQLNATGW MHNRLRMITA SFLVKDLLID
WRLGERYFMS QLIDGDLAAN NGGWQWAAST GTDAAPYFRI FNPTTQGERF DRDGEFIRQW
LPALRDIPGK AIHEPWRWAE KAGVVLDYPR PIVEHKQARI ATLSAYEAAR KGA
