ID   A0A1S9CHY6_9FIRM        Unreviewed;       444 AA.
AC   A0A1S9CHY6;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:OON96470.1};
GN   ORFNames=ATN36_00755 {ECO:0000313|EMBL:OON96470.1};
OS   Epulopiscium sp. Nele67-Bin005.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Candidatus Epulonipiscium.
OX   NCBI_TaxID=1764963 {ECO:0000313|EMBL:OON96470.1, ECO:0000313|Proteomes:UP000190895};
RN   [1] {ECO:0000313|Proteomes:UP000190895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ngugi D.K., Miyake S., Stingl U.;
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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:OON96470.1}.
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DR   EMBL; LNZR01000056; OON96470.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1S9CHY6; -.
DR   STRING; 1764963.ATN36_00755; -.
DR   Proteomes; UP000190895; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000190895}.
FT   DOMAIN          1..305
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          328..429
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   444 AA;  48572 MW;  51089656A87B8C92 CRC64;
     MKVVVIGCTH AGTAAIVNIK GIHENAEITV YERNNNISFL SCGIALNVAQ VVKDAQTLFY
     SSPNHLQELG VNTKMEHEVQ AVDIANKKVT VKDLNSGEIF DDSYDKLIVT LGSWPITPPI
     AGIDLGNIIL SKNYSHSQAI IEKAKDAKNV VVIGAGYIGV ELAEAFEMLG KNTTLIDAEP
     RIMNKYLDQT YTDIAEKAFT DHGVTLALGH KVTSFEGTDG NVTKVKTDKG EFETDLVILC
     IGFRPNTDLL KGQLDMLPNG AIVIDEYMQT SVKDVFAAGD CCMVRFNPAE DNRYIPLATN
     AVRMGTLIAK NLVEPKLKYM GTQGTSGIKI YDHNIASTGL TEQVAKATTS YDVASVTITD
     AHRAEFMPTF EEVTLTLVYD KTTHVILGGQ ITSLAEVTQH MNTLSVAIQN KMTVEELAMT
     DFFFQPHYNK PWGLLNTVAL EVLK
//