ID A0A0S8I481_9DELT Unreviewed; 623 AA.
AC A0A0S8I481;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=NADH:flavin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMJ94_05870 {ECO:0000313|EMBL:KPK92121.1};
OS Deltaproteobacteria bacterium SM23_61.
OC Bacteria; Deltaproteobacteria.
OX NCBI_TaxID=1703399 {ECO:0000313|EMBL:KPK92121.1, ECO:0000313|Proteomes:UP000051218};
RN [1] {ECO:0000313|EMBL:KPK92121.1, ECO:0000313|Proteomes:UP000051218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_61 {ECO:0000313|EMBL:KPK92121.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK92121.1}.
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DR EMBL; LJUR01000038; KPK92121.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8I481; -.
DR STRING; 1703399.AMJ94_05870; -.
DR PATRIC; fig|1703399.3.peg.4234; -.
DR Proteomes; UP000051218; Unassembled WGS sequence.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 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; 2.
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.
PE 4: Predicted;
FT DOMAIN 7..108
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 117..319
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 365..585
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 623 AA; 68416 MW; 1F096A7CD5032B9F CRC64;
MKNENWKLFT PFKIKDLQVK NRIALLPMGN KLQSAGGEVT PRLIDFYVEV ARGGAGLVIV
QAAYVTEEFG GTRLLNSSDD QVSGLNILAE SIKTWGAQAA IQISHRGYRG SSARSVTTLS
VSEIEDLIEA FGSAGERAKR AGFDLVEIHG AHGYLIPQFL SGKTNLREDE YGGDLEKRMT
FALRVFQAVR NAVGKEFPIS FRLSGDEFLP GGICLEDTKK ISRALEQEGV DLISLSAGKG
PETREWTIQP MAFPRGCLAH LSEELKPSLR VPILIAGRIN DPLLAESILQ EEKADLIGLG
RALIADPHFP RKALEGRAEE IRKCIACNYC NGKRLIMELP LKCTVNPEAG IRKTMAITPA
TRKKRVLVAG GGPAGMECAH TLRQRGHEVL LFEKNSFLGG KLRVAAIPPH KQEINEFTDF
LVRRTRREKI PIFLNCEVQA HTLRDVQPDI LVLATGGKAF CPSIPGLAKE LCATAEEALT
REWSVRRILV LGGGMVGCEV AEFLAMQGKD IVIVEKLAEL GLELEPITRK LLLTRLMQTK
PAVYTKSEVV RVEGTRAFVR NSKGEQSQID FDTLIFAAGF IAEDPFPASE MPDGLDTYRI
GDCLGSRRIL DAIHEGYHAG LAI
//
