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
//