ID N6Z044_9RHOO Unreviewed; 484 AA.
AC N6Z044;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase {ECO:0000313|EMBL:ENO97235.1};
GN ORFNames=C667_09850 {ECO:0000313|EMBL:ENO97235.1};
OS Thauera phenylacetica B4P.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=1234382 {ECO:0000313|EMBL:ENO97235.1, ECO:0000313|Proteomes:UP000013047};
RN [1] {ECO:0000313|EMBL:ENO97235.1, ECO:0000313|Proteomes:UP000013047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4P {ECO:0000313|EMBL:ENO97235.1,
RC ECO:0000313|Proteomes:UP000013047};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-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 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:ENO97235.1}.
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DR EMBL; AMXF01000057; ENO97235.1; -; Genomic_DNA.
DR RefSeq; WP_004361777.1; NZ_AMXF01000057.1.
DR AlphaFoldDB; N6Z044; -.
DR OrthoDB; 9772484at2; -.
DR Proteomes; UP000013047; 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:ENO97235.1}.
FT DOMAIN 2..139
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 276
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 279..286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 376..378
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 310
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 363
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 386
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 484 AA; 54642 MW; 8C1C12172FE95CCC CRC64;
MPSALVWFRR DLRSFDHAAL YHALRFADRV HCAFVFDTAI LDALPSRRDR RVEFIHASLA
ELDAALDAMA RAAGGTGGGL IVRHGRAEDE IPRLAAALGV DKVFANRDYE PDAIVRDSRV
AQALAEAGIG YEDFKDQVIF ERDEVLTQAG KPYSVFTPYK NAWLKKVDDF QVRAYPVERH
AAHLAPKPAG ETLPGLADIG FEPTRLAELN MPVGMSGGRR LFDDFAARIE RYKRARDFPA
VKGVSYLSTH LRFGTVSIRQ LAAHARARGG EGAETWLSEL IWRDFYHQIL WHHPQVVDRA
FRPEYDAVKW DEAPELFAAW CEARTGYPIV DAAMRQLNQT GWMHNRLRMI VASFLTKDLG
VDWRLGERYF AAQLNDYDLA ANNGGWQWAA STGCDAQPWF RIFNPVTQSE KFDPEGRFIR
RYLPELARVP DKFIHAPWTM GGIDQSACRT KIGVDYPGPI VDHASARERT LQRFGVVKND
AQGG
//
