ID   J4TLB4_9FIRM            Unreviewed;       444 AA.
AC   J4TLB4;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:EJP25449.1};
DE            EC=1.6.99.3 {ECO:0000313|EMBL:EJP25449.1};
GN   Name=noxE {ECO:0000313|EMBL:EJP25449.1};
GN   ORFNames=HMPREF1142_0463 {ECO:0000313|EMBL:EJP25449.1};
OS   Peptostreptococcaceae bacterium AS15.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae.
OX   NCBI_TaxID=936556 {ECO:0000313|EMBL:EJP25449.1, ECO:0000313|Proteomes:UP000006605};
RN   [1] {ECO:0000313|EMBL:EJP25449.1, ECO:0000313|Proteomes:UP000006605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AS15 {ECO:0000313|EMBL:EJP25449.1,
RC   ECO:0000313|Proteomes:UP000006605};
RA   Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (JUL-2012) 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:EJP25449.1}.
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DR   EMBL; ALJM01000006; EJP25449.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4TLB4; -.
DR   PATRIC; fig|936556.4.peg.485; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000006605; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   Oxidoreductase {ECO:0000313|EMBL:EJP25449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006605}.
FT   DOMAIN          3..306
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          331..430
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   444 AA;  48689 MW;  6C1DAA2CEDDD969E CRC64;
     MSKIVVVGAN HAGTCAINTI TGFNEGDEVV VFDQNSNISF LGCGMALWIG GQISKPDGLF
     YSNKQKLESQ GAKVNMNSKV DKIYFDRKVV SATLENGQRI EESYDKLILA TGSLPIVPPI
     PGRDLENVQM VKLFQNAQEV IDKLKNPDIK TIAVVGAGYI GVELAEAFER HHKKVILVDV
     AKTSLSNYYD AEFSSLMDKN LSDNGVQLAF GETVKEIKGN CKVESIVTDK NEYQCDMVIL
     AIGFRPNNEL GKDYLETMPN GAYIVDETQE TSMKDVYAIG DCATVQFNAT GEKSYIALAT
     NAVRSGIIAA YNACGKRLET VGVQGSNAIA IYDLKMVSTG VSEQKAKQLG MDVLSTSFDD
     LQKASFLETT NPNVKLKIVY DRNTRVIVGA QMASTYDMSM GIHMFSLAIQ EKVTIDKLKL
     LDIFFLPHFN QPYNYITMAA LSAK
//