ID Q24QW4_DESHY Unreviewed; 657 AA.
AC Q24QW4;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=NADH oxidase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=DSY3789 {ECO:0000313|EMBL:BAE85578.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE85578.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE85578.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE85578.1,
RC ECO:0000313|Proteomes:UP000001946};
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85578.1; -; Genomic_DNA.
DR AlphaFoldDB; Q24QW4; -.
DR STRING; 138119.DSY3789; -.
DR KEGG; dsy:DSY3789; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR Proteomes; UP000001946; 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 SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 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:UP000001946}.
FT DOMAIN 9..333
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 379..615
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 657 AA; 71462 MW; 4CAA4BE412C03AD2 CRC64;
MTMSDFKYLF SPLKIGSMEI PNRIMMSPHG VTGLKPGSDE QLAYFEARAK GGAGFVGIAG
CAVHTMHVYQ GLFMTSRDPA NIPKIKRLVD VIHKYGGKAF IHGPWMNGAP DMPQTSKVVP
ATLWGDNQSR EMSIDEIKQL VLDHAISAAN MREAGADGME FPIGGGAGLQ YFVSPLYNKR
SDEYGGDLDN RIRIILEIAA EIKKMAGRDF NIGFKVNPDE SLLGGPDLET GIEICRRLAA
SGDVDWIRIA ARGQKPQMTH FHYPPSYMPQ GTNNYASAAV REVVDNIPII GGGRMTTAEF
MEQSIAEGQC DAVFAARAFI VDPEWPNKAK RGETEEIRHC IGDVEGCFLR SCFGMPVGCT
YNVEIGHEGQ TLAPAEKKKK VAIIGGGPAG LQAALTAAQR GHDIILVEKE DHLGGHVWLE
GQLPGLTDRQ ALPTWYEHQL RKLANVDIRL ETEADADYVL SLGADAVIVA TGAEFSPTGI
SYMQMNAAEG YATEGYVYTP EDVILKGVEL GDRVLIFDGI GYVTGPGVAE MLADQGKEVV
YVNVDPMIGR SVQLLGQHQV MALRLKDKVE FIPNNAPLAV KDHTVTLKNI LTYDLTEIED
IDSVVMVASR PSRDELYHAL VGKIDELHII ADAADSHWNS FGTDDATKAG HKVALAL
//
