ID   NAOX_ENTFA              Reviewed;         446 AA.
AC   P37061;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=NADH oxidase;
DE            Short=NOXase;
DE            EC=1.6.3.4 {ECO:0000250|UniProtKB:A2RIB7};
GN   Name=nox; OrderedLocusNames=EF_1586;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX   PubMed=1404382; DOI=10.1016/0022-2836(92)90215-6;
RA   Ross R.P., Claiborne A.;
RT   "Molecular cloning and analysis of the gene encoding the NADH oxidase from
RT   Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the
RT   flavoprotein disulfide reductases.";
RL   J. Mol. Biol. 227:658-671(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 3-17; 34-52 AND 226-250.
RC   STRAIN=ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1;
RX   PubMed=2511195; DOI=10.1016/s0021-9258(19)47189-5;
RA   Ahmed S.A., Claiborne A.;
RT   "The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH
RT   oxidase and NADH peroxidase cysteinyl redox centers.";
RL   J. Biol. Chem. 264:19856-19863(1989).
RN   [4]
RP   REVIEW, ACTIVE SITE, AND OXIDATION AT CYS-42.
RX   PubMed=8262333; DOI=10.1096/fasebj.7.15.8262333;
RA   Claiborne A., Miller H., Parsonage D., Ross R.P.;
RT   "Protein-sulfenic acid stabilization and function in enzyme catalysis and
RT   gene regulation.";
RL   FASEB J. 7:1483-1490(1993).
CC   -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC       water.
CC   -!- CATALYTIC ACTIVITY: [NADH oxidase]:
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:0000250|UniProtKB:A2RIB7};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC       Note=Binds 1 FAD per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Homodimer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; X68847; CAA48728.1; -; Genomic_DNA.
DR   EMBL; AE016830; AAO81372.1; -; Genomic_DNA.
DR   PIR; S26965; S26965.
DR   RefSeq; NP_815302.1; NC_004668.1.
DR   RefSeq; WP_002361833.1; NZ_KE136528.1.
DR   AlphaFoldDB; P37061; -.
DR   SMR; P37061; -.
DR   STRING; 226185.EF_1586; -.
DR   PeroxiBase; 5456; EfNadOxd01.
DR   EnsemblBacteria; AAO81372; AAO81372; EF_1586.
DR   KEGG; efa:EF1586; -.
DR   PATRIC; fig|226185.45.peg.1919; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_1_0_9; -.
DR   SABIO-RK; P37061; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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   1: Evidence at protein level;
KW   Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation;
KW   Oxidoreductase; Redox-active center; Reference proteome.
FT   CHAIN           1..446
FT                   /note="NADH oxidase"
FT                   /id="PRO_0000184701"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P37062"
FT   ACT_SITE        42
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000269|PubMed:8262333"
FT   BINDING         7..11
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         42
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         79
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         110..113
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         150..165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         177
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P37062"
FT   BINDING         186
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P37062"
FT   BINDING         243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P37062"
FT   BINDING         271..281
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         300
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   BINDING         328
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P37062"
FT   BINDING         424
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
FT   MOD_RES         42
FT                   /note="Cysteine sulfinic acid (-SO2H)"
FT                   /evidence="ECO:0000250|UniProtKB:Q5XC60"
SQ   SEQUENCE   446 AA;  48915 MW;  D0762A47FC3DC071 CRC64;
     MKVVVVGCTH AGTSAVKSIL ANHPEAEVTV YERNDNISFL SCGIALYVGG VVKNAADLFY
     SNPEELASLG ATVKMEHNVE EINVDDKTVT AKNLQTGATE TVSYDKLVMT TGSWPIIPPI
     PGIDAENILL CKNYSQANVI IEKAKDAKRV VVVGGGYIGI ELVEAFVESG KQVTLVDGLD
     RILNKYLDKP FTDVLEKELV DRGVNLALGE NVQQFVADEQ GKVAKVITPS QEFEADMVIM
     CVGFRPNTEL LKDKVDMLPN GAIEVNEYMQ TSNPDIFAAG DSAVVHYNPS QTKNYIPLAT
     NAVRQGMLVG RNLTEQKLAY RGTQGTSGLY LFGWKIGSTG VTKESAKLNG LDVEATVFED
     NYRPEFMPTT EKVLMELVYE KGTQRIVGGQ LMSKYDITQS ANTLSLAVQN KMTVEDLAIS
     DFFFQPHFDR PWNYLNLLAQ AALENM
//