ID F9HEQ1_9STRE Unreviewed; 315 AA.
AC F9HEQ1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=NADH oxidase {ECO:0000256|ARBA:ARBA00039201};
DE EC=1.6.3.4 {ECO:0000256|ARBA:ARBA00039092};
GN Name=noxE {ECO:0000313|EMBL:EGP65728.1};
GN ORFNames=HMPREF9182_0079 {ECO:0000313|EMBL:EGP65728.1};
OS Streptococcus sp. oral taxon 056 str. F0418.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=904294 {ECO:0000313|EMBL:EGP65728.1, ECO:0000313|Proteomes:UP000004514};
RN [1] {ECO:0000313|Proteomes:UP000004514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0418 {ECO:0000313|Proteomes:UP000004514};
RA Durkin A.S., Kim M., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete sequence of Bifidobacterium breves ACS-071-V-Sch8b.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 NADH + O2 = 2 H2O + 2 NAD(+); Xref=Rhea:RHEA:37799,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036014};
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:EGP65728.1}.
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DR EMBL; AFQU01000001; EGP65728.1; -; Genomic_DNA.
DR AlphaFoldDB; F9HEQ1; -.
DR eggNOG; COG0446; Bacteria.
DR Proteomes; UP000004514; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000004514}.
FT DOMAIN 10..176
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 205..301
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 315 AA; 34578 MW; F67548980880F851 CRC64;
MYQNAEEVIE KLQDKSKHIE RVAVVGGGYI GVELAEAFER LGKEVVLVDI VDTVLNGYYD
KDFTEMMAKN LEEHNIRLAL EQTVQAVEGD GKVERLVTDK ETFDVDMVVL AVGFRPNTSL
GAGKIELFRN GAFLVDKKQE TSIPGVFAVG DCATIYDNAR QDTSYIALAS NAVRSGIVGA
HNACGHELEG IGVQGSNGIS IYGLHMVSTG LTLEKAKQAG YNAVETGFND LQKPEFIKHD
NQEVAIKIVF DKDTRVILGA QMVSRDISIS MGIHMFSLAI QEHVTIDKLA LTDLFFLPHF
NKPYNYITMA ALSAE
//
