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Database: UniProt
Entry: A0A162QU51_9CLOT
LinkDB: A0A162QU51_9CLOT
Original site: A0A162QU51_9CLOT 
ID   A0A162QU51_9CLOT        Unreviewed;       654 AA.
AC   A0A162QU51;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=NADH oxidase {ECO:0000313|EMBL:KZL88971.1};
DE            EC=1.-.-.- {ECO:0000313|EMBL:KZL88971.1};
GN   ORFNames=CLMAG_56690 {ECO:0000313|EMBL:KZL88971.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL88971.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL88971.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL88971.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-2016) 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}.
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:KZL88971.1}.
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DR   EMBL; LWAE01000012; KZL88971.1; -; Genomic_DNA.
DR   RefSeq; WP_066630177.1; NZ_FQXL01000020.1.
DR   AlphaFoldDB; A0A162QU51; -.
DR   STRING; 1121326.CLMAG_56690; -.
DR   PATRIC; fig|1121326.3.peg.5724; -.
DR   OrthoDB; 9772736at2; -.
DR   Proteomes; UP000076603; Unassembled WGS sequence.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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   Oxidoreductase {ECO:0000313|EMBL:KZL88971.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076603}.
FT   DOMAIN          9..347
FT                   /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00724"
FT   DOMAIN          392..614
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   654 AA;  70619 MW;  3AB278DB89389A1D CRC64;
     MSTCKYPHLF TPIILGNTLF RNRIFASPTG YQNLNGDGYL NDGAAAYYER KARGGAASVA
     TFEGIVDGEF GKGGATHICL DTPNIGRGLS RIAYGIKSYG AVASLELQHT GMFANRDLSF
     FGAASKGIAY GPVECEVAGR TIRPMDEKII ERTIQKYATG AALAKRCGFG MVTVHAGHGW
     LLHQFLSPKT NTRTDKWGGA DIENRARLVV AVCNAIRKEV GPGFPIEVRI SGSECYGDGY
     DLDEGIAIAK QLDGHVDLIH VSAGNHEVEE VFAVTHPSMF LGDGCNVKYA AEIKKHVKTP
     VATVGALSDP ELMEEIIASG KADIVEAARA LLADPDFPNK VRSGKEDKAR KCMRCLSCFS
     SELTNGEPYC AINPESGREL EMKYDIPAAA RKKVLVVGGG VGGMKAALTC ADRGHEVILC
     EKSNRLGGVL RCEQDVDFKK KLDYYLNQQA EEIVDSNIEL HLNTKVTAEY AKKINADVII
     AAIGAQSVKP PIPGIDGTNV MSVQDAYTAT DKIGEHVVIL GAGLVGIELG LHLISKDKKV
     KIIEITDHIS DGGNFLHILG LKTEINKRGL EIDFNTKAKE IKENGIVCEY ADGEKTLKAD
     TIIYAVGQKP LREEAIAMNF CAPEFYQIGD CVTPRNITSA TSEAFMIARN IGRL
//
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