ID   NUOF_RHOCA              Reviewed;         431 AA.
AC   O07948;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F;
DE            EC=7.1.1.-;
DE   AltName: Full=NADH dehydrogenase I subunit F;
DE   AltName: Full=NDH-1 subunit F;
GN   Name=nuoF;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=9108316; DOI=10.1016/s0014-5793(97)00212-3;
RA   Duborjal H., Dupuis A., Chapel A., Kieffer S., Lunardi J., Issartel J.P.;
RT   "Immuno-purification of a dimeric subcomplex of the respiratory NADH-CoQ
RT   reductase of Rhodobacter capsulatus equivalent to the FP fraction of the
RT   mitochondrial complex I.";
RL   FEBS Lett. 405:345-350(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Herter S.M., Schiltz E., Drews G.;
RT   "The NADH-binding fragment of the NADH:ubiquinone oxidoreductase from
RT   Rhodobacter capsulatus: proteins and gene structure.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC       Note=Binds 1 FMN. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; Y10142; CAA71232.1; -; Genomic_DNA.
DR   EMBL; Y09884; CAA71013.1; -; Genomic_DNA.
DR   EMBL; AF029365; AAC24991.1; -; Genomic_DNA.
DR   RefSeq; WP_013067247.1; NZ_VIBE01000008.1.
DR   AlphaFoldDB; O07948; -.
DR   SMR; O07948; -.
DR   GeneID; 31490403; -.
DR   OMA; CDDVIMD; -.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1440.230; -; 1.
DR   Gene3D; 3.40.50.11540; -; 1.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR   InterPro; IPR011538; Nuo51_FMN-bd.
DR   InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR   InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR   InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   SUPFAM; SSF140490; SSF140490; 1.
DR   SUPFAM; SSF142019; SSF142019; 1.
DR   TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Flavoprotein; FMN; Iron; Iron-sulfur; Metal-binding; NAD; Quinone;
KW   Translocase; Ubiquinone.
FT   CHAIN           1..431
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000118578"
FT   BINDING         54..63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..214
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         346
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         349
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         352
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         392
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  47133 MW;  08AFA168C18BF8B4 CRC64;
     MLNDHDRIFT NIYGMHDRSL KGAMARGHWD GTAAILGNGR DWIIEQVKAS GLRGRGGAGF
     PTGLKWSFMP KQSDGRPSFL VINADESEPG TCKDREIMRH DPHTLIEGAL IAGFAMGARA
     AYIYIRGEYV REKEALQAAI DECYEAGLIG KNACRSDYDF DVYLHHGAGA YICGEETALL
     ESLEGKKGMP RMKPPFPAGS GLYGCPTTVN NVESIAVVPT ILRRGGAWFA GIGRPNNTGV
     KLFAMSGHVN TPCVVEEAMS ISMKELIEKH GGGVRGGWKN LKAVIPGGAS CPVIPAHLCE
     DAIMDYDGMR EKQSSFGTAC LIVMDQQTDI IKAIARLSKF FKHESCGQCT PCREGTSWMW
     RVMERLVTGE AEVEEIDMLF SVTKQVEGHT ICALGDAAAW PIQGLIRHYR EEIEDRIKAR
     KTGRMGAMAA E