ID   NAOX_METJA              Reviewed;         448 AA.
AC   Q58065;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative NADH oxidase;
DE            Short=NOXase;
DE            EC=7.1.1.2;
GN   OrderedLocusNames=MJ0649;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes the four-electron reduction of molecular oxygen to
CC       water. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB98641.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB98641.1; ALT_INIT; Genomic_DNA.
DR   PIR; A64381; A64381.
DR   RefSeq; WP_064496570.1; NC_000909.1.
DR   AlphaFoldDB; Q58065; -.
DR   SMR; Q58065; -.
DR   STRING; 243232.MJ_0649; -.
DR   EnsemblBacteria; AAB98641; AAB98641; MJ_0649.
DR   GeneID; 1451515; -.
DR   KEGG; mja:MJ_0649; -.
DR   eggNOG; arCOG01069; Archaea.
DR   HOGENOM; CLU_003291_1_3_2; -.
DR   InParanoid; Q58065; -.
DR   OMA; ACGIPYW; -.
DR   OrthoDB; 40511at2157; -.
DR   PhylomeDB; Q58065; -.
DR   BRENDA; 1.6.3.3; 3260.
DR   Proteomes; UP000000805; 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; 3.50.50.60; -; 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   3: Inferred from homology;
KW   FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; Redox-active center;
KW   Reference proteome; Translocase.
FT   CHAIN           1..448
FT                   /note="Putative NADH oxidase"
FT                   /id="PRO_0000184704"
FT   ACT_SITE        42
FT                   /note="Redox-active"
FT   BINDING         7..11
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         132
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..167
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   MOD_RES         42
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   448 AA;  48876 MW;  8790664DF98D9DCD CRC64;
     MRAIIIGSGA AGLTTASTIR KYNKDMEIVV ITKEKEIAYS PCAIPYVIEG AIKSFDDIIM
     HTPEDYKRER NIDILTETTV IDVDSKNNKI KCVDKDGNEF EMNYDYLVLA TGAEPFIPPI
     EGKDLDGVFK VRTIEDGRAI LKYIEENGCK KVAVVGAGAI GLEMAYGLKC RGLDVLVVEM
     APQVLPRFLD PDMAEIVQKY LEKEGIKVML SKPLEKIVGK EKVEAVYVDG KLYDVDMVIM
     ATGVRPNIEL AKKAGCKIGK FAIEVNEKMQ TSIPNIYAVG DCVEVIDFIT GEKTLSPFGT
     AAVRQGKVAG KNIAGVEAKF YPVLNSAVSK IGDLEIGGTG LTAFSANLKR IPIVIGRAKA
     LTRARYYPGG KEIEIKMIFN EDGKVVGCQI VGGERVAERI DAMSIAIFKK VSAEELANME
     FCYAPPVSMV HEPLSLAAED ALKKLSNK