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Database: UniProt
Entry: F4CQY1_PSEUX
LinkDB: F4CQY1_PSEUX
Original site: F4CQY1_PSEUX 
ID   F4CQY1_PSEUX            Unreviewed;       410 AA.
AC   F4CQY1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Ferredoxin--NAD(+) reductase {ECO:0000313|EMBL:AEA23680.1};
DE            EC=1.18.1.3 {ECO:0000313|EMBL:AEA23680.1};
GN   OrderedLocusNames=Psed_1441 {ECO:0000313|EMBL:AEA23680.1};
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:AEA23680.1, ECO:0000313|Proteomes:UP000007809};
RN   [1] {ECO:0000313|EMBL:AEA23680.1, 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; AEA23680.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CQY1; -.
DR   STRING; 675635.Psed_1441; -.
DR   KEGG; pdx:Psed_1441; -.
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:AEA23680.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007809}.
FT   DOMAIN          5..299
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          318..402
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   410 AA;  43575 MW;  2319257BAEB0CDE4 CRC64;
     MRRERIVLVG AGRAAAAAAA TLRREGFDGD LVVVGDEPHP PYRRPPLSKA WDGAAPCVDD
     LLVRDAEWYG TNAVELITGT RAVALDCASR QLTLADGARL GYDRLLLATG GRPRRLPGVR
     GDRIHHLRTV ADAAALREQL AGDGPLVVLG GGFLGCEVAA AARASGVEVT IVEMAPTLLS
     RAVSPELGEL FAALHRSRGV TVLTGERVDS VVQAGDQVVV RTCAQVLECA ALLVAIGISR
     STELLSGTPV ACDDGVLVDE FAATSVPGVY AAGDVAAAHH PRYGRRVRVE HDDNAVRQAT
     VAARNMLGAR DVYDDPHWFW SDQFEHNLQM VGSPEGHDRS VVRGSPGEGA FSVFHLRGDR
     LVSVLAFDRG RDVVTGRKLV AAGATVAAEQ LEDDAVDLRR LLRRQGGRPS
//
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