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 25-NOV-2008, entry version 69. DE RecName: Full=NADH oxidase; DE Short=NOXase; DE EC=1.6.99.3; GN Name=nox; OrderedLocusNames=EF_1586; OS Enterococcus faecalis (Streptococcus faecalis). OC Bacteria; Firmicutes; Lactobacillales; Enterococcaceae; Enterococcus. OX NCBI_TaxID=1351; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661; RX MEDLINE=93021109; 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 RT from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and RT the flavoprotein disulfide reductases."; RL J. Mol. Biol. 227:658-671(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=V583 / ATCC 700802; RX MEDLINE=22550857; 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., RA Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., RA Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., RA Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., RA Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., RA Fraser C.M.; RT "Role of mobile DNA in the evolution of vancomycin-resistant RT Enterococcus faecalis."; RL Science 299:2071-2074(2003). RN [3] RP PROTEIN SEQUENCE OF 3-17; 34-52 AND 226-250. RC STRAIN=ATCC 11700 / 10C1 / DSM 20409 / NCIB 8661; RX MEDLINE=90062089; PubMed=2511195; 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. RX MEDLINE=94085723; PubMed=8262333; RA Claiborne A., Miller H., Parsonage D., Ross R.P.; RT "Protein-sulfenic acid stabilization and function in enzyme catalysis RT and gene regulation."; RL FASEB J. 7:1483-1490(1993). CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular CC oxygen to water. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: Binds 1 FAD per subunit (By similarity). CC -!- SUBUNIT: Homodimer. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-42 oxidized CC to Cys-SOH. The oxidized form is stabilized by an hydrogen bond CC formation with His-10. CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide CC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X68847; CAA48728.1; -; Genomic_DNA. DR EMBL; AE016830; AAO81372.1; -; Genomic_DNA. DR PIR; S26965; S26965. DR RefSeq; NP_815302.1; -. DR HSSP; P37062; 1NHP. DR PeroxiBase; 5456; EfNadOxd01. DR GeneID; 1200486; -. DR GenomeReviews; AE016830_GR; EF_1586. DR KEGG; efa:EF1586; -. DR NMPDR; fig|226185.1.peg.1487; -. DR TIGR; EF_1586; -. DR HOGENOM; P37061; -. DR BioCyc; EFAE226185:EF_1586-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000759; Adrndx_reductase. DR InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase. DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR InterPro; IPR001327; Pyr_OxRdtase_NAD_bd. DR Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1. DR Pfam; PF00070; Pyr_redox; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR PRINTS; PR00419; ADXRDTASE. DR PRINTS; PR00368; FADPNR. DR PRINTS; PR00411; PNDRDTASEI. DR ProDom; PD000139; FAD_pyr_redox; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; FAD; Flavoprotein; NAD; KW Oxidation; Oxidoreductase; Redox-active center. FT CHAIN 1 446 NADH oxidase. FT /FTId=PRO_0000184701. FT NP_BIND 7 11 FAD (By similarity). FT NP_BIND 110 113 FAD (By similarity). FT NP_BIND 150 165 NAD (By similarity). FT NP_BIND 271 281 FAD (By similarity). FT ACT_SITE 10 10 Proton acceptor (By similarity). FT ACT_SITE 42 42 Redox-active. FT BINDING 32 32 FAD (By similarity). FT BINDING 42 42 FAD (By similarity). FT BINDING 177 177 NAD (By similarity). FT BINDING 186 186 NAD (By similarity). FT BINDING 243 243 NAD; via amide nitrogen (By similarity). FT BINDING 299 299 FAD; via amide nitrogen (By similarity). FT BINDING 328 328 NAD; via carbonyl oxygen (By similarity). FT MOD_RES 42 42 Cysteine sulfenic acid (-SOH). 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 //