ID F7V5G3_CLOSS Unreviewed; 673 AA.
AC F7V5G3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=NADH:flavin oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=CXIVA_20250 {ECO:0000313|EMBL:BAK47992.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK47992.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
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; AP012212; BAK47992.1; -; Genomic_DNA.
DR RefSeq; WP_013977949.1; NC_015737.1.
DR AlphaFoldDB; F7V5G3; -.
DR STRING; 1042156.CXIVA_20250; -.
DR KEGG; cls:CXIVA_20250; -.
DR eggNOG; COG0446; Bacteria.
DR eggNOG; COG1902; Bacteria.
DR HOGENOM; CLU_012153_1_2_9; -.
DR OrthoDB; 9772736at2; -.
DR Proteomes; UP000008937; 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.
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:UP000008937}.
FT DOMAIN 11..355
FT /note="NADH:flavin oxidoreductase/NADH oxidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00724"
FT DOMAIN 416..635
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 673 AA; 73912 MW; F349ADF8A231DB53 CRC64;
MPETNPYFPH LFSPLKVGSK VIKNRIEAAP ALFAFLHYIE GTAFHYAPGT PKRAFMMLES
KAAGGAGTVT FGELSPNHTY DKRFPFEPEI DFTSRDDEIF QITKKTAEMI KSYGALAMGE
LISTGEIKGN LGDGINPKGP SAKVLPDGTQ VEAFTKEEIH GLYQDYITAC RWFRDAGWDG
IMIHCGHGWL PAQFLSPMYN KRTDEYGGSF ENRARFTVEL LSAVREAMGP DFVIEVRVSS
SEHLKGGLEL EDCIRYVKQF EPYIDLLHVS CGHYLSSSRS LEFTTAYAPH GVNIDSAAEI
KKHVSVPVAV VGGINSPEQA EAAIASGKVD MISLGREFFA DPEFPVKAET GRADEIRRCL
RCGRCYPGPS GEHETERPSI KFPPLDSCTI NPYTVWPASH HKILPEDMPK PKASRRVLVI
GGGCGGLQGA VTACDRGHQV ILCERSDALG GILRFTDHTE HKIDIRHFKD LLIREVRKRP
IDIRLNCEVT PEMIREIQPD AVILATGSDD LILPIKGIAH AVTAMDAYAS DFSALGKSTI
VLGGGLVGCE AAADYIDRGI ETTIVEMQEC LMPECVGLYR TAVHDFLDQH GCHYEVNAKV
TEVGKDYVIA EQNGTAITLR ADSVVNAMGR RPHPSDDLRA AIHVPVWEIG DCIGARQIGD
AVREAWTAAM EIV
//