ID A0A011QSI6_9LACT Unreviewed; 474 AA.
AC A0A011QSI6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:EXJ22674.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:EXJ22674.1};
GN ORFNames=ADIAL_1928 {ECO:0000313|EMBL:EXJ22674.1};
OS Alkalibacterium sp. AK22.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1229520 {ECO:0000313|EMBL:EXJ22674.1, ECO:0000313|Proteomes:UP000020164};
RN [1] {ECO:0000313|EMBL:EXJ22674.1, ECO:0000313|Proteomes:UP000020164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK22 {ECO:0000313|Proteomes:UP000020164};
RA Singh A., Pinnaka A.K.;
RL Submitted (JAN-2014) 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 -!- 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:EXJ22674.1}.
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DR EMBL; JANL01000041; EXJ22674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A011QSI6; -.
DR STRING; 1229520.ADIAL_1928; -.
DR PATRIC; fig|1229520.3.peg.1870; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000020164; 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; 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:EXJ22674.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000020164}.
FT DOMAIN 1..129
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 219
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 231..235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 264
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 267..274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 364..366
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 298
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 351
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 374
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 474 AA; 55768 MW; 07C09AB864BDF72B CRC64;
MTSVMWFRRD LRLEDNMALK HAFEEADRLY MVFHVNPEQF LEEGSTNQAS FFSSVQTLRE
EIEEKGGKLH ILKGDLKACF EKLYDELADW TDVYINRDEK GYGLERDKMI AAFFKEKNIK
AHGYFDHHMH ASGEIKTNSG TPYQKFTPYF RKWKELQKPE PVEVSFDADK VMQRPVFTED
RDSFEAFLSQ QKELKELKQG TQAAHDSLDN FIDEYLKDYK EARDFPLKDA TSHMSHHLRS
GEISVRTVYH KVMQAPQSEG RETYIQELAW RDFYNMVFAG NPDQKDTEID ENFRKVQWDN
NEDNFKKWTE GQTGYPIVDA AMRQLNQTGW MHNRLRMITA SFLIKDLLID WKWGERYFQE
KLVDYDVSSN VGGWQWAAST GTDGVPYFRV FNPNTQSEKY DKDGDFIRQY VPELKNITSK
KIHDPSKLSD EEQETFGVHL GEDYPRPIVD HKQSRELAIQ AYEDSKKKVQ GSKS
//
