ID   NAOX_MYCPN              Reviewed;         479 AA.
AC   P75389;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Probable NADH oxidase;
DE            Short=NOXase;
DE            EC=1.6.99.3;
GN   Name=nox; OrderedLocusNames=MPN_394; ORFNames=MP444;
OS   Mycoplasma pneumoniae.
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=2104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   MEDLINE=97105885; PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
RA   Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: Catalyzes the four-electron reduction of molecular
CC       oxygen to water (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; U00089; AAB96092.1; -; Genomic_DNA.
DR   PIR; S73770; S73770.
DR   RefSeq; NP_110082.1; -.
DR   HSSP; P37062; 1NHP.
DR   GeneID; 877135; -.
DR   GenomeReviews; U00089_GR; MPN_394.
DR   KEGG; mpn:MPN394; -.
DR   HOGENOM; P75389; -.
DR   OMA; P75389; DFFFQPH.
DR   BioCyc; MPNE272634:MPN394-MON; -.
DR   BRENDA; 1.6.99.3; 39500.
DR   GO; GO:0005737; C:cytoplasm; 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; IPR013027; FAD_pyr_nucl-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; PR00368; FADPNR.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    479       Probable NADH oxidase.
FT                                /FTId=PRO_0000184703.
FT   NP_BIND       8     12       FAD (By similarity).
FT   NP_BIND     111    114       FAD (By similarity).
FT   NP_BIND     170    185       NAD (By similarity).
FT   NP_BIND     295    305       FAD (By similarity).
FT   ACT_SITE     11     11       Proton acceptor (By similarity).
FT   ACT_SITE     43     43       Redox-active.
FT   BINDING      43     43       FAD (By similarity).
FT   BINDING     197    197       NAD (By similarity).
FT   BINDING     264    264       NAD; via amide nitrogen (By similarity).
FT   BINDING     323    323       FAD; via amide nitrogen (By similarity).
FT   MOD_RES      43     43       Cysteine sulfenic acid (-SOH) (By
FT                                similarity).
SQ   SEQUENCE   479 AA;  52875 MW;  66B86EA3BA8E53F1 CRC64;
     MKKVIVIGVN HAGTSFIRTL LSKSKDFQVN AYDRNTNISF LGCGIALAVS GVVKNTEDLF
     YSTPEELKAM GANVFMAHDV VGLDLDKKQV IVKDLATGKE TVDHYDQLVV ASGAWPICMN
     VENEVTHTQL QFNHTDKYCG NIKNLISCKL YQHALTLIDS FRHDKSIKSV AIVGSGYIGL
     ELAEAAWQCG KQVTVIDMLD KPAGNNFDEE FTNELEKAMK KAGINLMMGS AVKGFIVDAD
     KNVVKGVETD KGRVDADLVI QSIGFRPNTQ FVPKDRQFEF NRNGSIKVNE YLQALNHENV
     YVIGGAAAIY DAASEQYENI DLATNAVKSG LVAAMHMIGS KAVKLESIVG TNALHVFGLN
     LAATGLTEKR AKMNGFDVGV SIVDDNDRPE FMGTFDKVRF KLIYDKKTLR LLGAQLLSWN
     TNHSEIIFYI ALAVQKKMLI SELGLVDVYF LPHYNKPFNF VLAAVLQALG FSYYTPKNK
//