ID   NAOX_LACLM              Reviewed;         446 AA.
AC   A2RIB7; P81759; Q8KR34;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=NADH oxidase;
DE            Short=NOXase;
DE            EC=1.6.99.3;
GN   Name=noxE; OrderedLocusNames=llmg_0408;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Lactobacillales; Streptococcaceae; Lactococcus.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21930283; PubMed=11932446;
RA   Hoefnagel M.H.N., Starrenburg M.J.C., Martens D.E., Hugenholtz J.,
RA   Kleerebezem M., Van Swam I.I., Bongers R., Westerhoff H.V.,
RA   Snoep J.L.;
RT   "Metabolic engineering of lactic acid bacteria, the combined approach:
RT   kinetic modelling, metabolic control and experimental analysis.";
RL   Microbiology 148:1003-1013(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17307855; DOI=10.1128/JB.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   AGRICOLA=IND23261759; DOI=10.1016/S0958-6946(01)00031-0;
RA   Lopez de Felipe F., Hugenholtz J.;
RT   "Purification and characterisation of the water forming NADH-oxidase
RT   from Lactococcus lactis.";
RL   Int. Dairy J. 11:37-44(2001).
CC   -!- FUNCTION: Catalyzes the four-electron reduction of molecular
CC       oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-
CC       NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the
CC       electron acceptor. Under anaerobic conditions, DCIP and MB can
CC       replace oxygen as the electron acceptor.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- ENZYME REGULATION: Inhibited by hydrogen peroxide, sulfhydryl
CC       reagents and quinine, but not by EDTA.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.1 uM for beta-NADH (in the presence of oxygen);
CC         Vmax=83 umol/min/mg enzyme toward beta-NADH (in the presence of
CC         oxygen);
CC       pH dependence:
CC         Optimum pH is 6.0-9.0. Below pH 6.0 the enzyme is reversibly
CC         inactivated, above pH 10.0 the enzyme is irreversibly
CC         inactivated;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; AY046926; AAL02357.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97012.1; -; Genomic_DNA.
DR   RefSeq; YP_001031758.1; -.
DR   GeneID; 4796799; -.
DR   GenomeReviews; AM406671_GR; llmg_0408.
DR   KEGG; llm:llmg_0408; -.
DR   OMA; A2RIB7; YLGCGTA.
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; 2.
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   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_0000292941.
FT   NP_BIND       7     11       FAD (By similarity).
FT   NP_BIND     109    112       FAD (By similarity).
FT   ACT_SITE     10     10       Proton acceptor (By similarity).
FT   ACT_SITE     42     42       Redox-active (By similarity).
FT   BINDING      42     42       FAD (By similarity).
FT   BINDING     159    159       NAD; via amide nitrogen (By similarity).
FT   BINDING     178    178       NAD (By similarity).
FT   BINDING     187    187       NAD (By similarity).
FT   BINDING     244    244       NAD; via amide nitrogen (By similarity).
FT   BINDING     282    282       FAD (By similarity).
FT   BINDING     298    298       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     300    300       FAD; via amide nitrogen (By similarity).
FT   BINDING     329    329       NAD; via carbonyl oxygen (By similarity).
FT   MOD_RES      42     42       Cysteine sulfenic acid (-SOH) (By
FT                                similarity).
FT   CONFLICT     11     11       A -> AA (in Ref. 3; AA sequence).
SQ   SEQUENCE   446 AA;  48872 MW;  1B1FA2FE313D6C03 CRC64;
     MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR QIEKPDELFY
     AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII EAYDKLVLAT GSRPIIPNLP
     GKDLKGIHFL KLFQEGQAID AEFAKEKVKR IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE
     NTSLASYYDE EFAKGMDENL AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI
     NCIGFTANSA LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA
     SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL GLEVSFSDFE
     DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII AGNINMFSLA IQEKKTIDEL
     ALLDLFFLPH FNSPYNYMTV AALNAK
//