ID   M0MHY9_9EURY            Unreviewed;       413 AA.
AC   M0MHY9;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:EMA44020.1};
GN   ORFNames=C449_10858 {ECO:0000313|EMBL:EMA44020.1};
OS   Halococcus saccharolyticus DSM 5350.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227455 {ECO:0000313|EMBL:EMA44020.1, ECO:0000313|Proteomes:UP000011669};
RN   [1] {ECO:0000313|EMBL:EMA44020.1, ECO:0000313|Proteomes:UP000011669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5350 {ECO:0000313|EMBL:EMA44020.1,
RC   ECO:0000313|Proteomes:UP000011669};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMA44020.1}.
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DR   EMBL; AOMD01000025; EMA44020.1; -; Genomic_DNA.
DR   RefSeq; WP_006078030.1; NZ_AOMD01000025.1.
DR   AlphaFoldDB; M0MHY9; -.
DR   STRING; 1227455.C449_10858; -.
DR   PATRIC; fig|1227455.4.peg.2227; -.
DR   InParanoid; M0MHY9; -.
DR   OrthoDB; 28009at2157; -.
DR   Proteomes; UP000011669; Unassembled WGS sequence.
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; 3.30.390.30; -; 1.
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   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   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000011669}.
FT   DOMAIN          4..283
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   413 AA;  45231 MW;  2D64862014A18C24 CRC64;
     MAGSYVIIGD GIAGSSAAES LREGAPDADI TVITDEGEAL YNRILIKEFA KGKLPAAPMS
     IHDPEWYDER DIDLQLDTHV TAIDTDEHTL HTHEGTEYTY DKLLVATGGT PVQLPVDNSD
     AEGVHHFWTF DDARAIKEHA EDADTGVVVG AGLLGIDFAA ICGAQEIDAH YLMRGECWWR
     YALSKDGADI IHNALEEKNV TPVFDSGVDH FEVDDSGHIS STVDPNGETY DSEFAGVAIG
     LDFNLEVLQG TDIERDDGVV VDEYMQTSVD DVYAAGDLTR FYDTIIDDYA QNGSWGSAKE
     QGTIAAKNML ADGEEEAFRW VSSYSITHFD FPFLSFGHPT IGDDHAEAKF SDTEWRRLAF
     KDGKIVGGVL IGDLAPQSKY KKLAREERVV ADQKDVLMAE EVDLDDLAPA PEQ
//