ID F5W0J3_9STRE Unreviewed; 459 AA.
AC F5W0J3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
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:EGL86471.1};
GN ORFNames=HMPREF9967_1297 {ECO:0000313|EMBL:EGL86471.1};
OS Streptococcus infantis SK1076.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1005705 {ECO:0000313|EMBL:EGL86471.1, ECO:0000313|Proteomes:UP000010138};
RN [1] {ECO:0000313|EMBL:EGL86471.1, ECO:0000313|Proteomes:UP000010138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK1076 {ECO:0000313|EMBL:EGL86471.1,
RC ECO:0000313|Proteomes:UP000010138};
RA Durkin A.S., Radune D., Hostetler J., Torralba M., Gillis M., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (APR-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:EGL86471.1}.
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DR EMBL; AFNN01000015; EGL86471.1; -; Genomic_DNA.
DR RefSeq; WP_006150632.1; NZ_AFNN01000015.1.
DR AlphaFoldDB; F5W0J3; -.
DR eggNOG; COG0446; Bacteria.
DR OrthoDB; 9802028at2; -.
DR Proteomes; UP000010138; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Oxidoreductase {ECO:0000313|EMBL:EGL86471.1}.
FT DOMAIN 3..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 349..444
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 459 AA; 50233 MW; 0D509A20E6A8EBE3 CRC64;
MSKIVVVGAN HAGTACINTM LDNFGNENEI VVFDQNSNIS FLGCGMALWI GEQIDGAEGL
FYSDKEKLEA KGAKVYMNSP VLSIDYDNKV VTAEVEGKEH KESYDKLIFA TGSTPILPPI
EGVEIVKGNR EFKTTLENVQ FVKLYQNAEE VINKLADKSK HLERIAVVGG GYIGVELAEA
FERLGKEVVL VDIVDTVLNG YYDKDFTQMM AKNLEDHNIR LALGQTVKAI EGNGKVERLV
TDKETFDVDM VVLAVGFRPN TALADGKIEL FRNGAFLVDK KQETSIPGVY AVGDCATVYD
NARKDTSYIA LASNAVRTGI VGAYNACGHE LEGIGVQGSN GISIYGLHMV STGLTLEKAK
AAGYNATETG FNDLQKPEFM KHDNHEVAIK IVFDKDSREI LGAQMVSRDS SIGMAIHMFS
LAIQEHVTID KLALTDLFFL PHFNKPYNYI TMAALSAEK
//
