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Database: UniProt
Entry: F7V5G3_CLOSS
LinkDB: F7V5G3_CLOSS
Original site: F7V5G3_CLOSS 
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
//
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