PHR_THET2
ID PHR_THET2 Reviewed; 420 AA.
AC P61496; P37250;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE EC=4.1.99.3;
DE AltName: Full=DNA photolyase;
DE AltName: Full=Photoreactivating enzyme;
GN Name=phr; OrderedLocusNames=TT_P0058;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RX PubMed=9335302; DOI=10.1128/jb.179.20.6499-6503.1997;
RA Kato R., Hasegawa K., Hidaka Y., Kuramitsu S., Hoshino T.;
RT "Characterization of a thermostable DNA photolyase from an extremely
RT thermophilic bacterium, Thermus thermophilus HB27.";
RL J. Bacteriol. 179:6499-6503(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27; PLASMID=pTT27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-194.
RX PubMed=8215386; DOI=10.1128/aem.59.9.3150-3153.1993;
RA Hoshino T., Fujii R., Nakahara T.;
RT "Molecular cloning and sequence analysis of the crtB gene of Thermus
RT thermophilus HB27, an extreme thermophile producing carotenoid pigments.";
RL Appl. Environ. Microbiol. 59:3150-3153(1993).
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 -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; AB001637; BAA22943.1; -; Genomic_DNA.
DR EMBL; AE017222; AAS82388.1; -; Genomic_DNA.
DR RefSeq; WP_011174501.1; NC_005838.1.
DR AlphaFoldDB; P61496; -.
DR SMR; P61496; -.
DR STRING; 262724.TT_P0058; -.
DR EnsemblBacteria; AAS82388; AAS82388; TT_P0058.
DR KEGG; tth:TT_P0058; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_0; -.
DR OMA; WQWSASS; -.
DR OrthoDB; 184000at2; -.
DR Proteomes; UP000000592; Plasmid pTT27.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding; Plasmid.
FT CHAIN 1..420
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085114"
FT DOMAIN 2..124
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 152..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..251
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 310..311
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 209..213
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 341..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT SITE 275
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 328
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT SITE 351
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000250"
FT CONFLICT 196
FT /note="R -> A (in Ref. 1; BAA22943)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 47909 MW; 788F208F40F512B4 CRC64;
MGPLLVWHRG DLRLHDHPAL LEALARGPVV GLVVLDPNNL KTTPRRRAWF LENVRALREA
YRARGGALWV LEGLPWEKVP EAARRLKAKA VYALTSYTPY GRYRDAKVQE ALPVPLHLLP
APHLLPPDLP RAYRVYTPFA RRFLGVEAPL PAPEALPKGP EEGEIPREDP GLPLPEPGEE
AALAGLRAFL EAKLPRYAEE RDRLDGEGGS RLSPYFALGV LSPRLAAWEA ERRGGEGARK
WVAELLWRDF SYHLLYHFPW MAERPLDPRF QALPWQEDEA LFRAWYEGRT GVPLVDAAMR
ELHATGFLSN RARMNAAQFA VKHLLLPWKR CEEAFRHLLL DGDRAVNLQG WQWAGGLGVD
AAPYFRVFNP VLQGERHDPE GRWLKRWAPE YPSYAPKDPV VDLEEARRRY LRLARDLARG
