PHR_THET8
ID PHR_THET8 Reviewed; 420 AA.
AC P61497; P37250; Q53W60;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=TTHB102;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OG Plasmid pTT27.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tsujiuchi H., Masui R., Inoue Y., Shibata T., Yokoyama S., Kuramitsu S.;
RT "Characterization of photolyase from Thermus thermophilus HB8.";
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8; PLASMID=pTT27;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP STRUCTURE BY NMR OF INTERACTION WITH DNA, AND MUTAGENESIS OF ARG-311;
RP TRP-353 AND ARG-366.
RX PubMed=15169780; DOI=10.1074/jbc.m404536200;
RA Torizawa T., Ueda T., Kuramitsu S., Hitomi K., Todo T., Iwai S.,
RA Morikawa K., Shimada I.;
RT "Investigation of the cyclobutane pyrimidine dimer (CPD) photolyase DNA
RT recognition mechanism by NMR analyses.";
RL J. Biol. Chem. 279:32950-32956(2004).
RN [4]
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).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FAD AND THYMINE.
RX PubMed=11707580; DOI=10.1073/pnas.241371398;
RA Komori H., Masui R., Kuramitsu S., Yokoyama S., Shibata T., Inoue Y.,
RA Miki K.;
RT "Crystal structure of thermostable DNA photolyase: pyrimidine-dimer
RT recognition mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13560-13565(2001).
RN [6]
RP ERRATUM OF PUBMED:11707580.
RA Komori H., Masui R., Kuramitsu S., Yokoyama S., Shibata T., Inoue Y.,
RA Miki K.;
RL Proc. Natl. Acad. Sci. U.S.A. 99:1098-1098(2002).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000305}.
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DR EMBL; AB064548; BAB61864.2; -; Genomic_DNA.
DR EMBL; AP008227; BAD71898.1; -; Genomic_DNA.
DR RefSeq; WP_011229192.1; NC_006462.1.
DR RefSeq; YP_145341.1; NC_006462.1.
DR PDB; 1IQR; X-ray; 2.10 A; A=1-420.
DR PDB; 1IQU; X-ray; 2.20 A; A=1-420.
DR PDB; 2J07; X-ray; 1.95 A; A=1-420.
DR PDB; 2J08; X-ray; 2.61 A; A=1-420.
DR PDB; 2J09; X-ray; 2.00 A; A=1-420.
DR PDBsum; 1IQR; -.
DR PDBsum; 1IQU; -.
DR PDBsum; 2J07; -.
DR PDBsum; 2J08; -.
DR PDBsum; 2J09; -.
DR AlphaFoldDB; P61497; -.
DR SMR; P61497; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03462; Thymine.
DR PRIDE; P61497; -.
DR EnsemblBacteria; BAD71898; BAD71898; BAD71898.
DR GeneID; 3169528; -.
DR KEGG; ttj:TTHB102; -.
DR PATRIC; fig|300852.9.peg.2045; -.
DR HOGENOM; CLU_010348_2_2_0; -.
DR OMA; WQWSASS; -.
DR PhylomeDB; P61497; -.
DR BRENDA; 4.1.99.3; 2305.
DR EvolutionaryTrace; P61497; -.
DR Proteomes; UP000000532; 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 3D-structure; Chromophore; DNA damage; DNA repair; DNA-binding; FAD;
KW Flavoprotein; Lyase; Nucleotide-binding; Plasmid; Reference proteome.
FT CHAIN 1..420
FT /note="Deoxyribodipyrimidine photo-lyase"
FT /id="PRO_0000085115"
FT DOMAIN 2..124
FT /note="Photolyase/cryptochrome alpha/beta"
FT REGION 147..176
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:0000269|PubMed:11707580"
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:0000269|PubMed:11707580"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11707580"
FT BINDING 248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11707580"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11707580"
FT BINDING 341..343
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:11707580"
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 MUTAGEN 201
FT /note="R->A: Reduces CPD repair activity by 20%."
FT MUTAGEN 240
FT /note="K->A: Reduces CPD repair activity by 20%."
FT MUTAGEN 247
FT /note="W->A: Reduces CPD repair activity by 20%."
FT MUTAGEN 311
FT /note="R->A: Strongly reduces interaction with DNA."
FT /evidence="ECO:0000269|PubMed:15169780"
FT MUTAGEN 353
FT /note="W->A: Strongly reduces interaction with DNA. Reduces
FT CPD repair activity by 80%."
FT /evidence="ECO:0000269|PubMed:15169780"
FT MUTAGEN 366
FT /note="R->A: Strongly reduces interaction with DNA."
FT /evidence="ECO:0000269|PubMed:15169780"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2J09"
FT HELIX 18..24
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 197..200
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 236..257
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 279..286
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 293..305
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 310..322
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 344..354
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:1IQU"
FT HELIX 382..387
FT /evidence="ECO:0007829|PDB:2J07"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:2J07"
FT HELIX 403..418
FT /evidence="ECO:0007829|PDB:2J07"
SQ SEQUENCE 420 AA; 47901 MW; 773968AC2D300893 CRC64;
MGPLLVWHRG DLRLHDHPAL LEALARGPVV GLVVLDPNNL KTTPRRRAWF LENVRALREA
YRARGGALWV LEGLPWEKVP EAARRLKAKA VYALTSHTPY GRYRDGRVRE ALPVPLHLLP
APHLLPPDLP RAYRVYTPFS RLYRGAAPPL PPPEALPKGP EEGEIPREDP GLPLPEPGEE
AALAGLRAFL EAKLPRYAEE RDRLDGEGGS RLSPYFALGV LSPRLAAWEA ERRGGEGARK
WVAELLWRDF SYHLLYHFPW MAERPLDPRF QAFPWQEDEA LFQAWYEGKT GVPLVDAAMR
ELHATGFLSN RARMNAAQFA VKHLLLPWKR CEEAFRHLLL DGDRAVNLQG WQWAGGLGVD
AAPYFRVFNP VLQGERHDPE GRWLKRWAPE YPSYAPKDPV VDLEEARRRY LRLARDLARG
