ID A0A1D7Y237_9FLAO Unreviewed; 435 AA.
AC A0A1D7Y237;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:AOR29469.1};
GN ORFNames=FORMB_24520 {ECO:0000313|EMBL:AOR29469.1};
OS Formosa sp. Hel1_33_131.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Formosa.
OX NCBI_TaxID=1336794 {ECO:0000313|EMBL:AOR29469.1, ECO:0000313|Proteomes:UP000094750};
RN [1] {ECO:0000313|EMBL:AOR29469.1, ECO:0000313|Proteomes:UP000094750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_33_131 {ECO:0000313|EMBL:AOR29469.1,
RC ECO:0000313|Proteomes:UP000094750};
RA Unfried F., Harder J., Teeling H., Hahnke R.L., Markert S., Kappelmann L.,
RA Chafee M.;
RT "Glycan utilization in Formosa spp.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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 family.
CC {ECO:0000256|RuleBase:RU004182}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017260; AOR29469.1; -; Genomic_DNA.
DR RefSeq; WP_069677629.1; NZ_CP017260.1.
DR AlphaFoldDB; A0A1D7Y237; -.
DR STRING; 1336794.FORMB_24520; -.
DR KEGG; for:FORMB_24520; -.
DR PATRIC; fig|1336794.4.peg.2398; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000094750; 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; 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:AOR29469.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094750}.
FT DOMAIN 4..133
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 214
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 258..265
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 289
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 342
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 365
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 435 AA; 50643 MW; F9A6DC7FB0134E28 CRC64;
MKTTVSLFWF RRDLRLHDNH GLFEALKHNE AVLPIFIFDT SILDSLPKND ARVEFIHEQL
QAINTNLQAH GSGLSVYHGT PEAVIEQLTT EYDVSSVYYN RDYEPYALSR DQSISDLLES
KSIAFNSFKD HVIFEQNEIT KDDGLPYKVY TPFSKKWLAA FNTDRCSAFH SEELLSNTYQ
SSSFPWVDLK SMGFEPNPVK VAPYKVESGI IENYEATRNF PAVDGTSKLG PHLRFGTVSV
REIVSKAIQH TNNTFLKELI WREFFMQILW HFPHTVTQSF KPQYEAIKWR NDPEEYKQWC
DGNTGYPLVD AGMRELNQTG FMHNRVRMLV GSFLCKHLLI DWRLGEAYFA EKLHDFELSS
NVSNWQWVAG CGVDAAPYFR IFNPTTQVTN FDKEHKYIKK WVPEYQELTY PTPMVDHKFA
RERCLSTYKE ALGKN
//
