ID   A0A0F2DVV6_9STRE        Unreviewed;       459 AA.
AC   A0A0F2DVV6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   02-OCT-2024, entry version 27.
DE   RecName: Full=NADH oxidase {ECO:0000256|ARBA:ARBA00039201};
DE            EC=1.6.3.4 {ECO:0000256|ARBA:ARBA00039092};
GN   Name=nox {ECO:0000313|EMBL:KJQ74080.1};
GN   ORFNames=TZ94_01601 {ECO:0000313|EMBL:KJQ74080.1};
OS   Streptococcus infantis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=68892 {ECO:0000313|EMBL:KJQ74080.1, ECO:0000313|Proteomes:UP000033489};
RN   [1] {ECO:0000313|EMBL:KJQ74080.1, ECO:0000313|Proteomes:UP000033489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UC921A {ECO:0000313|EMBL:KJQ74080.1,
RC   ECO:0000313|Proteomes:UP000033489};
RA   Haase E.M.;
RT   "Evolution of amylase-binding proteins of oral streptococcal species.";
RL   Submitted (FEB-2015) 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:KJQ74080.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JYGT01000010; KJQ74080.1; -; Genomic_DNA.
DR   RefSeq; WP_045615831.1; NZ_JYGT01000010.1.
DR   AlphaFoldDB; A0A0F2DVV6; -.
DR   PATRIC; fig|28037.216.peg.1569; -.
DR   OrthoDB; 9802028at2; -.
DR   Proteomes; UP000033489; Unassembled WGS sequence.
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; IPR050260; FAD-dep_Oxidoreductase.
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:KJQ74080.1}.
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;  50286 MW;  A7CEB1A391972CE5 CRC64;
     MSKIVVVGAN HAGTACINTM LDNFGNENEI VVFDQNSNIS FLGCGMALWI GEQIDGAEGL
     FYSDKEKLEA KGAKVYMNSP VLSIDYDNKV VTAEVEGQEH KESYEKLIFA TGSTPILPPI
     EGVEIVKGNR EFKATLENVQ FVKLYQNAEE VINKLADKSK HLERIAVVGG GYIGVELAEA
     FERLGKEVVL VDIVDTVLNG YYDKDFTQMM AKNLEDHNIR LALGQTVKAI EGEGKVERLI
     TDKETFDVDM VVLAVGFRPN TALADGKIEL FRNGAFLVDK KQETSIPGVY AVGDCATVYD
     NARKDTSYIA LASNAVRTGI VGAYNACGHE LEGIGVQGSN GISIYGLHMV STGLTLEKAK
     AAGYNATETG FNDLQKPEFM KHDNYEVAIK IVFDKDSREI LGAQMVSRDS AISMGIHMFS
     LAIQEHVTID KLALTDLFFL PHFNKPYNYI TMAALTAEK
//