ID A0A1L8PAB6_9LACT Unreviewed; 483 AA.
AC A0A1L8PAB6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Deoxyribodipyrimidine photolyase {ECO:0000313|EMBL:OJF92188.1};
GN ORFNames=AX762_03015 {ECO:0000313|EMBL:OJF92188.1};
OS Alkalibacterium sp. 20.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Alkalibacterium.
OX NCBI_TaxID=1798803 {ECO:0000313|EMBL:OJF92188.1, ECO:0000313|Proteomes:UP000182750};
RN [1] {ECO:0000313|EMBL:OJF92188.1, ECO:0000313|Proteomes:UP000182750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=20 {ECO:0000313|EMBL:OJF92188.1,
RC ECO:0000313|Proteomes:UP000182750};
RA Wang D., Kot W., Qin Y., Naqvi K., Hansen L., Rensing C.;
RT "Genome sequencing of a beta-galactosidase producing bacteria
RT Alkalibacterium sp. 20.";
RL Submitted (FEB-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 -!- 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:OJF92188.1}.
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DR EMBL; LSRN01000045; OJF92188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8PAB6; -.
DR STRING; 1798803.AX762_03015; -.
DR Proteomes; UP000182750; Unassembled WGS sequence.
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:OJF92188.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000182750}.
FT DOMAIN 6..134
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 236..240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 269
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 272..279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 369..371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 303
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 356
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 379
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 483 AA; 56317 MW; 030C1A713B2AE90C CRC64;
MRRGRLVAVM WFRRDLRLED NVALKHAIEE SDELFLLFHV NPEQFLGEGS INQSAFFKSV
VILQEELKEK GATLHILYGD LKDCFTRLKK ELPNWSDVYI NRDEKGYGLE RDKVAGGLFK
ELGIKAHGYH DHHLHSAQEI KTNSGTYYKV FTPYFNKWKE LQKPHVVDVN FDAEKTVKQP
VFIEDENQFD QLLDRQVHID NHQSGTQEAH KRLNDFVENH LSDYKEARDY PLKDATSHLS
KHLRAGEISI RTVFDRVNRA ENSLGKHTFI QELAWRDFYN AIYATHPDQK EVSINPSFRQ
VEWDNNEQNF KKWKEGQTGF PIVDAAMRQL NETGWMHNRL RMVTASFLTK DLLTDWRWGE
KYFQEMLSDY DAASNIGGWQ WASSTGADGV PYFRVFNPTT QSEKFDKDGS FIKKYVPELK
HIDNKKIHEP SKLTAEEQET FGVVIGEDYP GPIVSHKRSR ELAIQAFENS KKKTENMKAA
DPK
//
