NAOX_ENTFA
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 03-AUG-2022, entry version 140.
DE RecName: Full=NADH oxidase;
DE Short=NOXase;
DE EC=7.1.1.2;
GN Name=nox; OrderedLocusNames=EF_1586;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; 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 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:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
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 -!- MISCELLANEOUS: The active site is the redox-active Cys-42 oxidized to
CC Cys-SOH. The oxidized form is stabilized by a hydrogen bond formation
CC with His-10.
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 OMA; ACGIPYW; -.
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 GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 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 Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; NAD; Oxidation;
KW Oxidoreductase; Redox-active center; Reference proteome; Translocase.
FT CHAIN 1..446
FT /note="NADH oxidase"
FT /id="PRO_0000184701"
FT ACT_SITE 10
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
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"
FT BINDING 42
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 110..113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 150..165
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 243
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="Cysteine sulfenic acid (-SOH)"
FT /evidence="ECO:0000269|PubMed:8262333"
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