ID H5V327_ATLHE Unreviewed; 487 AA.
AC H5V327;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:GAB52259.1};
GN Name=phrB {ECO:0000313|EMBL:GAB52259.1};
GN ORFNames=EH105704_06_00290 {ECO:0000313|EMBL:GAB52259.1};
OS Atlantibacter hermannii NBRC 105704.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB52259.1, ECO:0000313|Proteomes:UP000010297};
RN [1] {ECO:0000313|EMBL:GAB52259.1, ECO:0000313|Proteomes:UP000010297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB52259.1,
RC ECO:0000313|Proteomes:UP000010297};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL Submitted (FEB-2012) 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}.
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:GAB52259.1}.
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DR EMBL; BAFF01000006; GAB52259.1; -; Genomic_DNA.
DR RefSeq; WP_002436000.1; NZ_BAFF01000006.1.
DR AlphaFoldDB; H5V327; -.
DR eggNOG; COG0415; Bacteria.
DR Proteomes; UP000010297; 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; 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:GAB52259.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010297}.
FT DOMAIN 2..135
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 237..241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 277..284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 309
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 362
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 385
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 487 AA; 55763 MW; 50FFE3E03ABEFF11 CRC64;
MTTHLVWFRA DLRVNDNLAL AAACRDPQAR VIGLFIATPL QWREHHLAPR QAAWMQAHLH
DLQRSLAEKG IPLTVLQVDD FAASVDALAA FCGQQRVDAL FYNYQYELNE RQRDAAVEKR
LADGVVCQGF DDYVMLAPGS VTTGNHEMYK VFTPFSRAFL KRLQAHLPEC VSAPAVRASG
PLDDPEPFAP FHYPQRELDA TLFPVGEKAA LSRLRHFCRQ SVADYERDRD YPAVDGTSRL
SPWLAIGVLS PRQCLHRLLC EHPDALTGGQ GAKWLNELLW REFYLHILAY WPALCRYKAF
IPWTERVQWN QNDAQFAAWC EGKTGYPIVD AAMRQMNTTG WMHNRLRMIT GSFLVKDLLI
DWRRGERYFM SQLVDGMLAA NNGGWQWVAS TGHDAAPWFR IFNPTTQGER FDPQGDFVRQ
WLPELRHIPG KDVHQPWLWA QKQRVTLDYP QPIVEHKQAR VATLAAYEAA RAVTGSHDEK
HRTGKPD
//
