ID   NADO_THEBR              Reviewed;         651 AA.
AC   P32382;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=NADH oxidase;
DE            EC=1.-.-.-;
OS   Thermoanaerobacter brockii (Thermoanaerobium brockii).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=29323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=RT8.G4;
RX   PubMed=8357835; DOI=10.1016/0167-4781(93)90113-r;
RA   Liu X.-L., Scopes R.K.;
RT   "Cloning, sequencing and expression of the gene encoding NADH oxidase from
RT   the extreme anaerobic thermophile Thermoanaerobium brockii.";
RL   Biochim. Biophys. Acta 1174:187-190(1993).
CC   -!- FUNCTION: Reduces a range of alternative electron acceptors.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + H(+) + NADH = AH2 + NAD(+); Xref=Rhea:RHEA:11356,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P42593};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P42593};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:P42593};
CC   -!- SUBUNIT: Homohexamer.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the NADH:flavin
CC       oxidoreductase/NADH oxidase family. {ECO:0000305}.
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DR   EMBL; X67220; CAA47660.1; -; Genomic_DNA.
DR   PIR; S35706; S35706.
DR   AlphaFoldDB; P32382; -.
DR   SMR; P32382; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003954; F:NADH dehydrogenase activity; IEA:RHEA.
DR   Gene3D; 3.20.20.70; -; 1.
DR   Gene3D; 3.50.50.60; -; 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   Pfam; PF00724; Oxidored_FMN; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; FAD; Flavoprotein; FMN; Iron;
KW   Iron-sulfur; Metal-binding; NAD; Oxidoreductase.
FT   CHAIN           1..651
FT                   /note="NADH oxidase"
FT                   /id="PRO_0000194480"
FT   ACT_SITE        175
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         104
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         223
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         320..321
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         344
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         347
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         351
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         364
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         396
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         415
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         423
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         433
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
FT   BINDING         460
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:P42593"
SQ   SEQUENCE   651 AA;  71306 MW;  F2282A24DA817439 CRC64;
     MTHFPNLFSE GRIGNLVIRN RIVMPPMATN LANEDGSVSQ RLIDYYVARA RGGVGLIILE
     NVQVDYPQGK NVACQLRLDD DKYMAGFFEL AEAVHSYGAK IFMQIHHAGR QTTPGITEGL
     QPVAPSPVPC SFLGTQPREL TINEIEEIIQ KFVDAAVRAK GAMFDGIELH GAHGYLIGQF
     MSPRTNRRVD KYGGSFERRM RFPLEIIRRI KEAVGEDYPI SFRFSADEFV EGGNTLEEGK
     QIAKMLEEAG VHVLHVSAGI YESMPTLLEP SRFEQGWRVY LAEEIKKVVN IPVITVGVIR
     EPEFAEKIIA EGRADFVAVG RGLIADPEWP KKAKEGRQNE IRKCISCNIG CIGGRVFQNL
     RLRCTVNPVA GREGVYSEIK QAPVKKKVVV VGGGPAGMQA AITAAKRGHQ VILYEKKQHL
     GGQLEIASAS PGKAKIKWFR DWLEAELSRA GVEVRSGVTA DAETIAALSP DYVILATGSE
     PVTPRIKGAE KENTFVFQAW DVLAGKVSFD KDEEVVVIGG GLVGCETAHY LAEKGAKVTI
     VEMLSDIAID MEPISRFDMM QQFTKLGISA RTGKVVTEIL PRGVAAVGKE GKQDFIRAHK
     VVLAIGQSPV GNELKKTLED KGIDVRVIGD AYNVGKIIDA VSSGFQVAWQ I