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Database: UniProt
Entry: J1E8Q8_9BURK
LinkDB: J1E8Q8_9BURK
Original site: J1E8Q8_9BURK 
ID   J1E8Q8_9BURK            Unreviewed;       695 AA.
AC   J1E8Q8;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=NADH:flavin oxidoreductase {ECO:0000313|EMBL:EJE48664.1};
GN   ORFNames=PMI14_06930 {ECO:0000313|EMBL:EJE48664.1};
OS   Acidovorax sp. CF316.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE48664.1, ECO:0000313|Proteomes:UP000004811};
RN   [1] {ECO:0000313|EMBL:EJE48664.1, ECO:0000313|Proteomes:UP000004811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF316 {ECO:0000313|EMBL:EJE48664.1,
RC   ECO:0000313|Proteomes:UP000004811};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:EJE48664.1}.
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DR   EMBL; AKJX01000284; EJE48664.1; -; Genomic_DNA.
DR   RefSeq; WP_007861614.1; NZ_AKJX01000284.1.
DR   AlphaFoldDB; J1E8Q8; -.
DR   PATRIC; fig|1144317.3.peg.6307; -.
DR   Proteomes; UP000004811; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd02930; DCR_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR001155; OxRdtase_FMN_N.
DR   PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR   PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT   DOMAIN          18..346
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          395..658
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   695 AA;  73939 MW;  147732FFB8648CDD CRC64;
     MKSIASELPP GHALYPHLLA PLDLGFTQIK NRVLMGSMHT GLEDARDLSR MAAYFRERAE
     GGVGLIVTGG FAPNIAGWTK PFAGTLSTAG AARRHKVVTE AVHGAGGKIA LQILHTGRYA
     YHPLAVAPSR LQSPITPFTP FALSASGVER QIRAFVNCAQ RAREAGYDGV EVMGSEGYLI
     NQFLSAATNR RTDAWGGDYS QRMRLPVEIL ARMREAVGPD FIIIYRLSMI DLVPGGSAWD
     EIVTLGKAVA TGGASIVNTG IGWHEARIPT IATSVPRAAF AWVTQKMKAE FAAAGIATPL
     VTSNRINTPE VAETVLADGC ADMVSMARPL LADPAFVNKA AEGKADRINT CIACNQACLD
     HVFKAKTSSC LVNPRACHET LLVYKPLAPQ QKPKRIAVVG AGPAGLTAAT VAAERGHEVH
     LFDAAEAIGG QLNMAKQVPG KEEFHEMLRY LATRVQDTGV HLHLATPVQA ADLAGYDEVV
     VATGVSPRDP KIPGQEHPKV LSYIDVLRHG KPVGERVAVI GAGGIGFDVA EFLVHGQGHS
     TTLDLPAWQA EWGITDPAEA RGGLAPKGPQ VTPPARQVTL LQRKKGKLGE GLGKTTGWIH
     RTTLKMKQVQ MVGGVNYERI ADEGLLVSHG EQREDPTWIP CDTVVLCAGQ LPLRTLADEL
     LALGRKPHVV GGALEAGELD AKRAIDQAAR LAAAL
//
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