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Database: UniProt
Entry: F4CQP8_PSEUX
LinkDB: F4CQP8_PSEUX
Original site: F4CQP8_PSEUX 
ID   F4CQP8_PSEUX            Unreviewed;       413 AA.
AC   F4CQP8;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:AEA23066.1};
DE            EC=1.18.1.3 {ECO:0000313|EMBL:AEA23066.1};
GN   OrderedLocusNames=Psed_0810 {ECO:0000313|EMBL:AEA23066.1};
OS   Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS   CB1190).
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA23066.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA23066.1, ECO:0000313|Proteomes:UP000007809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC   {ECO:0000313|Proteomes:UP000007809};
RX   PubMed=21725009; DOI=10.1128/JB.00415-11;
RA   Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA   Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA   Alvarez-Cohen L.;
RT   "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT   strain CB1190.";
RL   J. Bacteriol. 193:4549-4550(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; CP002593; AEA23066.1; -; Genomic_DNA.
DR   RefSeq; WP_013673007.1; NC_015312.1.
DR   AlphaFoldDB; F4CQP8; -.
DR   STRING; 675635.Psed_0810; -.
DR   KEGG; pdx:Psed_0810; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_11; -.
DR   Proteomes; UP000007809; Chromosome.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
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; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 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   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:AEA23066.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT   DOMAIN          5..300
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          319..402
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   413 AA;  44745 MW;  3C0BBDBCD27DD8FD CRC64;
     MSTRRHVLVG GGVAAAATAT HLRKHGFDGE IVLVGDEPQP PYERPPLSKD FLLGTTEFEE
     FQVRPPAWYD EQSVDLRVGI RVTAIDVPGR SVTLSTGERL GYDGLVLATG VRPRRLPGFD
     GDRVHYLRTA ADSQRLRAQL AESERVVVIG AGFIGCEVAA AAVGLGKQVT IFDPAPTPLA
     RVLGATIGSV MTGIHRSRGV QIRAGEYISE LRHTGDGMLL TSNLGHRVEC DLVVVGIGCE
     PNVELAAEAG LATDGGIVVD EYGRTSAPDI YAAGDVAAQY HPVYGRTIRV EHHDNALRQG
     ANVALNLTGS AEPFAEAHWF WSDQYEHSLQ SVGRPADLED LVIRGSLEDH DFSAFSLVDG
     RIQAVISLNR PRDVLEVRRM LFAPHEVTAE QLRDESVPLK RLIPRSPRAT ARA
//
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