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Database: UniProt
Entry: A0A1P8UG73_9GAMM
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ID   A0A1P8UG73_9GAMM        Unreviewed;       487 AA.
AC   A0A1P8UG73;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:APZ42853.1};
GN   ORFNames=BW247_06885 {ECO:0000313|EMBL:APZ42853.1};
OS   Acidihalobacter ferrooxydans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Acidihalobacter.
OX   NCBI_TaxID=1765967 {ECO:0000313|EMBL:APZ42853.1, ECO:0000313|Proteomes:UP000243807};
RN   [1] {ECO:0000313|EMBL:APZ42853.1, ECO:0000313|Proteomes:UP000243807}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V8 {ECO:0000313|EMBL:APZ42853.1,
RC   ECO:0000313|Proteomes:UP000243807};
RA   Khaleque H.N., Ramsay J.P., Murphy R.J.T., Kaksonen A.H., Boxall N.J.,
RA   Watkin E.L.J.;
RT   "Draft sequence of Acidihalobacter ferrooxidans strain DSM 14175 (strain
RT   V8).";
RL   Submitted (JAN-2017) 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}.
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DR   EMBL; CP019434; APZ42853.1; -; Genomic_DNA.
DR   RefSeq; WP_076836501.1; NZ_CP019434.1.
DR   AlphaFoldDB; A0A1P8UG73; -.
DR   STRING; 1765967.BW247_06885; -.
DR   OrthoDB; 9772484at2; -.
DR   Proteomes; UP000243807; Chromosome.
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; PS00691; DNA_PHOTOLYASES_1_2; 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:APZ42853.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243807}.
FT   DOMAIN          4..133
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT                   /evidence="ECO:0000259|PROSITE:PS51645"
FT   BINDING         228
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         240..244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   BINDING         381..383
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT   SITE            314
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            368
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT   SITE            391
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ   SEQUENCE   487 AA;  55075 MW;  95BB7A0F6FDBC4AA CRC64;
     MTAHPAIVWF RRDLRLADNP ALAAALNNHR RIVPVYIHAP DEEAPWAPGA ASRWWLQHSL
     TALDARLREH GSGLVIRHGR TLETLRQLIA ETGANAVHWN RLYEPATIAR DTEVKEALRA
     EGTAAHSHNA ALLFEPWSLT TQSGGPYRVF TPFWKACLRQ GLPEQGEALS EIPPETLLPS
     AAHSAALDTL GLLPTIPWDA GFNDHWQPGE AGAWNMLREF LDHAGARYAK DRDRPGQRST
     SRLSPHLHFG EIGPRQIVHA VRARQAADAR PGAHASLDSL LRELGWREFS HHLLYHFPHT
     PATALDERFA RFAWRRDDAD LLAAWQRGRT GIPLVDAGMR ELWHTGWMHN RVRMVVASFL
     TKNLLLPWQD GARWFWDTLV DADLANNTQG WQWTTGCGAD AAPYFRVFNP VLQSRKFDPD
     GVYLRRWLPE LACLPDTALH APWEAPEHVL RSARVRLGSD YPRPIVELRA SRQRALDAYA
     RIRVMPA
//
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