ID H0A1P4_9PROT Unreviewed; 484 AA.
AC H0A1P4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Putative deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:EHM00129.1};
GN ORFNames=HMPREF9946_02736 {ECO:0000313|EMBL:EHM00129.1};
OS Acetobacteraceae bacterium AT-5844.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM00129.1, ECO:0000313|Proteomes:UP000003292};
RN [1] {ECO:0000313|EMBL:EHM00129.1, ECO:0000313|Proteomes:UP000003292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2011) 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 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:EHM00129.1}.
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DR EMBL; AGEZ01000086; EHM00129.1; -; Genomic_DNA.
DR AlphaFoldDB; H0A1P4; -.
DR STRING; 1054213.HMPREF9946_02736; -.
DR PATRIC; fig|1054213.3.peg.2519; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_010348_2_2_5; -.
DR OrthoDB; 9772484at2; -.
DR BioCyc; ABAC1054213:G1H32-2529-MONOMER; -.
DR Proteomes; UP000003292; 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:EHM00129.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003292}.
FT DOMAIN 10..137
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT BINDING 232
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 244..248
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 278
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 378..380
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 484 AA; 53728 MW; 006283CEA188FA37 CRC64;
MSASPSSSAS PAILWFRNDL RLEDNAALHA ASEGKTLPVY VLDDEAAGRW AVGAAGRWWL
HHSLKALAEA LRRLGSGLLL LRGRAETLIP QLAREIGAAA VHAATLAAPW ARQRDAAIAK
ALQAGGRRLE LHDSSLVRPD VVVTGQGKPY SVYTPFARAV MKLGDPPPPI PAPRRLDGVK
APTGGISLDD LALLPRRPEP DWAAGFSSLW QPGEAGARDQ LQRFLNDALA EYPDGRNRPG
EDGSSRLSPH LHWGEISARQ VWHAVRESEA PASAADTFLK EIIWREFSHN ILWHHPGLPE
APLRPEYTQF PYNRNIEAQR AWQRGRTGYP IVDAGMRQLW RLGWMHNRVR MIVASLFVKH
LLQPWQDGEA WFWDTLVDAD LGNNSFNWQW VAGSGADASP FFRIFNPVLQ GEKFDPKGEY
VRTFVPELAQ LPDRWLHRPW EAPAEVLREA GVTLGETYPE PIVDHATGRA RALEALAAMK
ARAG
//
