ID E1IFR8_9CHLR Unreviewed; 450 AA.
AC E1IFR8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=AD-dependent pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFO79959.1};
GN ORFNames=OSCT_2169 {ECO:0000313|EMBL:EFO79959.1};
OS Oscillochloris trichoides DG-6.
OC Bacteria; Chloroflexota; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Oscillochloridaceae; Oscillochloris.
OX NCBI_TaxID=765420 {ECO:0000313|EMBL:EFO79959.1, ECO:0000313|Proteomes:UP000054010};
RN [1] {ECO:0000313|EMBL:EFO79959.1, ECO:0000313|Proteomes:UP000054010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG-6 {ECO:0000313|EMBL:EFO79959.1,
RC ECO:0000313|Proteomes:UP000054010};
RX PubMed=21037015; DOI=10.1128/JB.00931-10;
RA Kuznetsov B.B., Ivanovsky R.N., Keppen O.I., Sukhacheva M.V.,
RA Bumazhkin B.K., Patutina E.O., Beletsky A.V., Mardanov A.V., Baslerov R.V.,
RA Panteleeva A.N., Kolganova T.V., Ravin N.V., Skryabin K.G.;
RT "Draft genome sequence of the anoxygenic filamentous phototrophic bacterium
RT Oscillochloris trichoides subsp. DG-6.";
RL J. Bacteriol. 193:321-322(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:EFO79959.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADVR01000094; EFO79959.1; -; Genomic_DNA.
DR RefSeq; WP_006562731.1; NZ_GL501404.1.
DR AlphaFoldDB; E1IFR8; -.
DR STRING; 765420.OSCT_2169; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_0; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000054010; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054010}.
FT DOMAIN 8..295
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 335..437
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 450 AA; 47034 MW; 50C9799D5E78CD2C CRC64;
MSNQQHERVI IIGGGAAGMS AAAKARRSNP NLELVAYERS GYVSYGACGL PYAIKGEIAR
IEDVVVRTPA QFAKQGITAL VRHEVLALDT VAQTLEVRNL ETGVTFTDHY DKLLIAAGGS
PSRPPIPGAN LPGVFALRNV EDALAIQAWI HQHRPSQGVI IGGGYIGLEM AEALAVHDIE
LTIVEQLPQL LPSLDAEMAA HVHAELERQG VAIQTGQGVS AINGDDRVRE VIAGATSFPA
EIVIMAVGVR PNVNLARQAG ITIGPTGAIA VDDQQRTNLP NVWSAGDVTE AINLVTGKPT
WVPLGTTANK QGKVAGENLA GGAARFGGIV GTSVVKIFET TAASTGLTEA RAKAEGLAVK
TASATANSRA HYMPGHADIH VRLVYEAGSG RMLGGQLVGH EGVSKRIDII AAALHAGWSV
EQLGELDLAY APPFSPVWDP ILVAANLAKK
//
