ID A0A242DAT6_9ENTE Unreviewed; 447 AA.
AC A0A242DAT6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=NADH oxidase {ECO:0000313|EMBL:OTO19617.1};
GN ORFNames=A5875_000951 {ECO:0000313|EMBL:OTO19617.1};
OS Enterococcus sp. 3H8_DIV0648.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834178 {ECO:0000313|EMBL:OTO19617.1, ECO:0000313|Proteomes:UP000194623};
RN [1] {ECO:0000313|EMBL:OTO19617.1, ECO:0000313|Proteomes:UP000194623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3H8_DIV0648 {ECO:0000313|EMBL:OTO19617.1,
RC ECO:0000313|Proteomes:UP000194623};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 3H8_DIV0648.";
RL Submitted (MAY-2017) 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:OTO19617.1}.
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DR EMBL; NGLG01000001; OTO19617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242DAT6; -.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000194623; 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 Oxidation {ECO:0000256|ARBA:ARBA00023097}.
FT DOMAIN 1..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 330..429
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 447 AA; 48659 MW; 3E6340EE9D021FA2 CRC64;
MKVVVVGCTH AGTAAVKNIL ANHPDAEVTV FERNDNISFL SCGIALYVGG VVKDPAGLFY
SNPEELTSLG ATVNMEHDVT NIDTDAKKVT AKDLKTNEEK IVDYDKLVVT TGSWPIIPPI
KGIESKNVLL CKNYNQANVI IEQAKDAKKV VVVGGGYIGI ELVEAFAESG KQVTLIDGLS
RILNKYLDEP FTNLLEKELV DRGVTLALGE NVNEFVADES GAVTKVVTAS QEFDADMVIL
CVGFRPNTDL LRGKVDMLPS GAIKVNEYMQ SSNPDIFSAG DSTVVHYNPT GKDQYIPLAT
NAVRQGMLVG QNLVEQKVKY RGTQGTSGLY LFGWTIGSTG LTKESAALND IDVNVTVIED
NYRPEFMPTT ENVLMEIVSE KGTNKILGAQ FLSKYDITQS ANTLSVAIQN GMTLEDLALQ
DFFFQPHFDR PWNYLNILAQ AALAEAE
//
