ID W2UI47_9GAMM Unreviewed; 445 AA.
AC W2UI47;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ETN93693.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:ETN93693.1};
GN Name=phrA {ECO:0000313|EMBL:ETN93693.1};
GN ORFNames=U062_01583 {ECO:0000313|EMBL:ETN93693.1};
OS Gammaproteobacteria bacterium MOLA455.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Porticoccaceae.
OX NCBI_TaxID=1411685 {ECO:0000313|EMBL:ETN93693.1, ECO:0000313|Proteomes:UP000018839};
RN [1] {ECO:0000313|EMBL:ETN93693.1, ECO:0000313|Proteomes:UP000018839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOLA455 {ECO:0000313|EMBL:ETN93693.1,
RC ECO:0000313|Proteomes:UP000018839};
RX PubMed=24482511;
RA Courties A., Riedel T., Jarek M., Papadatou M., Intertaglia L., Lebaron P.,
RA Suzuki M.T.;
RT "Draft Genome Sequence of the Gammaproteobacterial Strain MOLA455, a
RT Representative of a Ubiquitous Proteorhodopsin-Producing Group in the
RT Ocean.";
RL Genome Announc. 2:e01203-e01213(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETN93693.1}.
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DR EMBL; AZIN01000001; ETN93693.1; -; Genomic_DNA.
DR AlphaFoldDB; W2UI47; -.
DR STRING; 1411685.U062_01583; -.
DR PATRIC; fig|1411685.3.peg.1568; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000018839; Unassembled WGS sequence.
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:ETN93693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018839}.
FT DOMAIN 1..96
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 189
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 238
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 339..341
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 272
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 326
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 349
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 445 AA; 50698 MW; 7FECDA033ABB7513 CRC64;
MFIFDESGEQ DWTLGGASRW WLHHALQSLD KSLGGKLTIY SGDALTILSD LSTAMSAKAV
YWNRCYEPRS IERDAKIKSS LKEAGLEVQS FNGSLLWEPW QVLKKDGTPY KVFTPYYRRG
CLQKVAPRQP LPVPVTMNLV KAENSLAVED LSLLPTIGWD KKLHGDWDIS EDGARDRLDD
FVFSGIQDYR EGRNFPSKKN VSRLSPYFHF GQMSVNTAWY AANDAAALID NESNLDTFLS
ELGWREFSYY LLYHFPKLPT DNLQQRFDVF PWAANTDAEL KAWQKGKTGY PLVDAGMREL
WNTGYMHNRV RMVVGSFMVK NLLIHWHSGE RWFWDCLVDA DLAANSASWQ WIAGCGADAA
PFFRIFNPIT QSEKFDKQGD YIRRHVPELA EMPAKYIHAP WLAPAEVLAA AGVKIGTDYP
APIVDIKESR ERALAAFKMT KNDLL
//
