ID B2A0W4_NATTJ Unreviewed; 646 AA.
AC B2A0W4;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:ACB85994.1};
GN OrderedLocusNames=Nther_2429 {ECO:0000313|EMBL:ACB85994.1};
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Bacillota; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570 {ECO:0000313|EMBL:ACB85994.1, ECO:0000313|Proteomes:UP000001683};
RN [1] {ECO:0000313|EMBL:ACB85994.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACB85994.1, ECO:0000313|Proteomes:UP000001683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF
RC {ECO:0000313|Proteomes:UP000001683};
RX PubMed=21642468; DOI=10.1128/JB.05157-11;
RA Zhao B., Mesbah N.M., Dalin E., Goodwin L., Nolan M., Pitluck S.,
RA Chertkov O., Brettin T.S., Han J., Larimer F.W., Land M.L., Hauser L.,
RA Kyrpides N., Wiegel J.;
RT "Complete genome sequence of the anaerobic, halophilic alkalithermophile
RT Natranaerobius thermophilus JW/NM-WN-LF.";
RL J. Bacteriol. 193:4023-4024(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC oxidoreductase/NADH oxidase family. {ECO:0000256|ARBA:ARBA00011048}.
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DR EMBL; CP001034; ACB85994.1; -; Genomic_DNA.
DR RefSeq; WP_012448840.1; NC_010718.1.
DR AlphaFoldDB; B2A0W4; -.
DR STRING; 457570.Nther_2429; -.
DR KEGG; nth:Nther_2429; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_1_9; -.
DR InParanoid; B2A0W4; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000001683; Chromosome.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02803; OYE_like_FMN_family; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR001155; OxRdtase_FMN_N.
DR PANTHER; PTHR42917; 2,4-DIENOYL-COA REDUCTASE; 1.
DR PANTHER; PTHR42917:SF2; 2,4-DIENOYL-COA REDUCTASE [(2E)-ENOYL-COA-PRODUCING]; 1.
DR Pfam; PF00724; Oxidored_FMN; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023014};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000001683}.
FT DOMAIN 6..336
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 384..612
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 646 AA; 71297 MW; CE017C767CFD2E4D CRC64;
MVYNELFQRG RIGKLTIKNR TVMPAMGTSL AEPTGEPSEE MIKYYEERAK NGCGLIITEI
TRVDEDYGVG TANQLSATSP QHIPGLEKLA RRVQIHDSKL FVQLHHPGRQ GHARLIGDKQ
IIAPSELECQ VTKEKPRAMT TEEAEGLVKK FVKGAVISQK AGVDGVEIHG AHGYLINQFL
SPYTNRRTDK YGGNFENRMR FLTEIIVGIK YMCGNDFPIS VRLSADEFNP KGIDLQEGTK
IAKYLESIGV DAINVSCGSY ETGTTIIEPN AFQQGWKKHL AAKIRLKLNI PVIAVNNIKE
PQIAEQMLSD QVCDFVGLGR SQLADPQWIY KAYQGKDEMI RPCISCLYCI EQLMGGRKFK
CSVNPYLGRE QEFSQLTVDG QGDTVAIIGG GPAGMVAAET LALRGFTPVI FEKEQELGGT
LLTADKTPHK EQITRYVKYM EKRLTELNVK LNLGQEATVD TIKALSPKAV FVAAGANPIV
PKDISGIDKD HVYTVFDVLK GEVELTNQHV AVIGSGLTGL ETAELLGQQG NKISVVEMAK
EIGPSVYRNI LADITGRLKH YDVNYMPLQQ LKKVTDNSII TLDRQKSTLA ELEVDAVVLA
LGVTPNTKLA EEFYQSFENC YYIGDIVEAA RIPEAVRDGL EKGSIL
//
