ID B0K0E3_THEPX Unreviewed; 612 AA.
AC B0K0E3;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=NADH:flavin oxidoreductase/NADH oxidase {ECO:0000313|EMBL:ABY92668.1};
GN OrderedLocusNames=Teth514_1378 {ECO:0000313|EMBL:ABY92668.1};
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter.
OX NCBI_TaxID=399726 {ECO:0000313|EMBL:ABY92668.1, ECO:0000313|Proteomes:UP000002155};
RN [1] {ECO:0000313|EMBL:ABY92668.1, ECO:0000313|Proteomes:UP000002155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514 {ECO:0000313|EMBL:ABY92668.1,
RC ECO:0000313|Proteomes:UP000002155};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000923; ABY92668.1; -; Genomic_DNA.
DR AlphaFoldDB; B0K0E3; -.
DR KEGG; tex:Teth514_1378; -.
DR HOGENOM; CLU_012153_1_2_9; -.
DR Proteomes; UP000002155; 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; 2.
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}.
FT DOMAIN 13..105
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 107..312
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 358..580
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 612 AA; 68109 MW; ABE09A2C5E12DAD8 CRC64;
MKEVINMLLK EGKIGKIKLK NRLIMLPTVT NLSNEGFVSE REVEYYKRRS KGVSLVIVGA
SYVNKLGKFF INQIGIDDDD KIEGLKRLSE VIRQNGAKAG IQLAMHNPKY KPSDFTKEQL
QDFVQNFVEA AIRAEKSGFD AVELHFAHGW FVNQFLSPDT NKRTDEYGGN FEGRTKFALD
ILREVKKTIP EMTVICRING SDFTDRGFTI EESVRFAKLL EYHGADALDI SSGVSSTSEY
HISPMGIGDK PLIGIVKRIK ENVTIPVIAI DKLGSVYDWE KVLEDGIADF IGIARGFIGD
PDLAEKLIKG HEEDIRYCIH CNQACIAYIQ KGLSVSCMIN PEVGREKEFE VKTDKPLNIA
VIGGGPAGMS AAKYLAKKGH NVTLFEKENK LGGQLNVAKV PPHKQEIGKV IEYLENDLKK
YNVKVHLNKK ISLQEIKEMP YDKIVIATGS KPAKINLDAD INPYMAIEVL EGNIPKGRDI
AIIGGGLTGL ETAEYLAEKG KKVTVLEMKE EVGEGIYPMV KKLILNRLKE LKVDIITNAL
IKEISGGKLM YTSKDTYKVV KVEDVVLAVG NLPDTEFEEL KNENRYYFIG DCKTVASAVE
AIRDGAELSL II
//
