ID   NUOF_RICBR              Reviewed;         417 AA.
AC   Q1RHA0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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; OrderedLocusNames=RBE_1183;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC       reaction to proton translocation (for every two electrons transferred,
CC       four hydrogen ions are translocated across the cytoplasmic membrane),
CC       and thus conserves the redox energy in a proton gradient (By
CC       similarity). {ECO:0000250}.
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; CP000087; ABE05264.1; -; Genomic_DNA.
DR   RefSeq; WP_011477842.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHA0; -.
DR   SMR; Q1RHA0; -.
DR   STRING; 336407.RBE_1183; -.
DR   EnsemblBacteria; ABE05264; ABE05264; RBE_1183.
DR   KEGG; rbe:RBE_1183; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_0_1_5; -.
DR   OMA; CREGTDW; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000001951; Chromosome.
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.
FT   CHAIN           1..417
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000274787"
FT   BINDING         54..63
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..213
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         345
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         348
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         351
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         391
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   417 AA;  45632 MW;  AD1855FFF50107C9 CRC64;
     MLKKEDRIFT NLHGEQSHDL KSSKKLGDWD NTKALLNKGK EWIIEEVKKS GLRGRGGAGF
     STGTKWSFMP KESKKPSYLV VNADESEPGT CKDRDILRYE PHKLIEGCLL ASFAIGANSC
     YIYIRGEFYN EASNIQRALD EAYKDGLIGK NACGSGFNCD IYLHRGAGAY ICGEETALLE
     SLEGKKGMPR LKPPFPAGFG LYGCPTTINN VESIAVVPTI LRRGASWFAS IGKPNNTGTK
     IFCISGHVNK PCNVEEAMGI PLKEIIEKHA GGVRGGWDNL KAIIPGGSSV PLLPKSLCET
     ADMDFDSLKA AGSSLGTGGI IVMDKSTDII YAIARLSKFY MHESCGQCTP CREGTGWMWR
     VMMRLVKGDA KKSEIDQLLE VTKEIEGHTI CALGDAAAWP IQGLIKHFRN EIESRIQ