ID   Q46DW0_METBF            Unreviewed;       506 AA.
AC   Q46DW0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:AAZ69932.1};
GN   OrderedLocusNames=Mbar_A0960 {ECO:0000313|EMBL:AAZ69932.1};
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69932.1};
RN   [1] {ECO:0000313|EMBL:AAZ69932.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Fusaro {ECO:0000313|EMBL:AAZ69932.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Anderson I., Richardson P.;
RT   "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR   EMBL; CP000099; AAZ69932.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46DW0; -.
DR   STRING; 269797.Mbar_A0960; -.
DR   PaxDb; 269797-Mbar_A0960; -.
DR   KEGG; mba:Mbar_A0960; -.
DR   eggNOG; arCOG01069; Archaea.
DR   HOGENOM; CLU_003291_1_3_2; -.
DR   OrthoDB; 27922at2157; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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   PANTHER; PTHR43429:SF3; NADH OXIDASE-RELATED; 1.
DR   PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
FT   DOMAIN          40..326
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          373..468
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   506 AA;  55203 MW;  928F8C2CE332D95C CRC64;
     MGSDSGTESA VDEIQKAAKS DEKFQEAVSA QNLEKKDPIK VIIIGGGACG MAVATKIRRQ
     SDFEITVISR DSHTAYSHCG IPFVLGREIK SFEKLIVKPK DFFKRNRIDV RLNECVSSID
     LDLKVVRTGE RTYPFDKLVI ATGSLPFIPL TGSTNVLPYG VFTLRNLDDG VLFEKALKTV
     ERVCIIGAGT IGIECAVALS RRGVKAILIN RSKNLLSRQL DPDISEIIRE HLESLGIEVI
     SGELAVYPEN FWKEKILYVG ERQLPADLVL LASGVKPEVS LALEAGIEIG KAGGIIVNEI
     LQVKAGDKAR EEFLPYVYAG GECVEVTDLI TGEAKLSQLG TTARHMADII GNNITGKSTP
     LGPLANPWVA VAGDLQFGGV GITSKEAESH GIKINTGFSL SRTRASYYPG RKDLYIKLLF
     KDDILVGAQL AGGEGIKERI DALSLAIRKK TTIRDLLDLE TCYTPPVSML VDPLRLAVKA
     TIRNIKEKKG KQIQEKEMEG KQIQEK
//