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Database: UniProt
Entry: A0A078KVB6_9GAMM
LinkDB: A0A078KVB6_9GAMM
Original site: A0A078KVB6_9GAMM 
ID   A0A078KVB6_9GAMM        Unreviewed;       675 AA.
AC   A0A078KVB6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=2,4-dienoyl-CoA reductase [NADPH] {ECO:0000313|EMBL:CDZ76936.1};
GN   Name=fadH {ECO:0000313|EMBL:CDZ76936.1};
GN   ORFNames=BN59_01215 {ECO:0000313|EMBL:CDZ76936.1};
OS   Legionella massiliensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1034943 {ECO:0000313|EMBL:CDZ76936.1, ECO:0000313|Proteomes:UP000044071};
RN   [1] {ECO:0000313|EMBL:CDZ76936.1, ECO:0000313|Proteomes:UP000044071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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DR   EMBL; CCSB01000001; CDZ76936.1; -; Genomic_DNA.
DR   RefSeq; WP_043873360.1; NZ_CCVW01000001.1.
DR   AlphaFoldDB; A0A078KVB6; -.
DR   STRING; 1034943.BN59_01215; -.
DR   eggNOG; COG0446; Bacteria.
DR   eggNOG; COG1902; Bacteria.
DR   OrthoDB; 8523426at2; -.
DR   Proteomes; UP000044071; 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   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000044071}.
FT   DOMAIN          13..332
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          383..637
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   675 AA;  74713 MW;  F7E492D73F6B4647 CRC64;
     MELRIDNTPF KSIFQPLDLG FTQLKNRILM GSMHTGLEED KEGLNRLAAF YRERAQGGAA
     LIVTGGFAPN RAGRLAPFAA KLTSSKEQQR HEIVTHTVHE AGGKIALQML HAGRYGYHPF
     IVAPSPLKSP ISPFKPWGMS KRRIAKTIGH FARCAHLAKQ AGYDGVEIMG SEGYLINQFI
     VSHTNQRQDE WGGSFANRMR FPVEVVRAVR QVVGTDFIII YRLSMLDLIA EGSSWEEVVL
     LAKAIEQAGA SLINTGIGWH EARIPTIATM VPAAAFTPIT KRLRPEVSIP VITSNRINTP
     ELANQLIEDG IADMVSMARP FLADPQFVEK ARLGESEAIN ICIACNQACL DRVFVNKTAS
     CLVNPRACNE TELVYQSVHH PKQVAVVGAG PAGLAFAAVA AERGHKVTLF ERSAVLGGQF
     NLAKNIPGKE EFQHTINYFT YQLEKYQADI RLNTAADAET LRGFDEVVLA TGIAPRIPEI
     AGLDHEKVMT YIELIQERKK PGNRVAIIGA GGIGFDVGEW LTHQHHTEHT QQFYDEWGID
     IKTEHRGGVK KPEFSASPRE VYLLQRKKEK HGKRLGKTTG WIHRLSLKHK EVKMLSGVSY
     ERIDDEGLHI RIDDEPQVLD VDSVIICAGQ NELRDLYEPL KAAGQSVHLI GGAFKALELD
     ARHAIDQACR LAALI
//
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