ID   NUOF_RICCK              Reviewed;         420 AA.
AC   A8EXI1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=A1E_00580;
OS   Rickettsia canadensis (strain McKiel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=293613;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=McKiel;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia canadensis.";
RL   Submitted (SEP-2007) 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. 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; CP000409; ABV73064.1; -; Genomic_DNA.
DR   RefSeq; WP_012148265.1; NC_009879.1.
DR   AlphaFoldDB; A8EXI1; -.
DR   SMR; A8EXI1; -.
DR   STRING; 293613.A1E_00580; -.
DR   EnsemblBacteria; ABV73064; ABV73064; A1E_00580.
DR   KEGG; rcm:A1E_00580; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_0_1_5; -.
DR   OMA; CREGTDW; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000007056; 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..420
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000316286"
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   420 AA;  46061 MW;  2CE2FF0A1BF4299C CRC64;
     MLKEEDKIFI NLHGQQSHDL KSSKKRGDWD NTKALLDKGR DFIIEEVKQS GLRGRGGAGF
     STGMKWSFMP KNSEKPCYLV VNADESEPGT CKDRDILRFE PHKLIEGCLL ASFAIGANNC
     YIYIRGEFYN EASNIQRALD EAYKDGLIGK NACGSGFDCN IYLHCGAGAY ICGEETALLE
     SLEGKKGMPR LKPPFPASFG LYGCPTTINN VESIAVVPTI LRRGANWFAS IGKPNNTGTK
     VFCISGHVNK PCNVEEVMGI PLKELIEKYA GGVQGGWNNL KAIIPGGSSV PLIPKSICET
     VDMDFDSLRT AGSGLGTGGI IVMNQSTDIV YAIARLSKFY MHESCGQCTP CREGTGWMWR
     VMMRLVKGNA KKSEIDQLLS VTKAIEGHTI CALGDAAAWP IQGLIRHFRD EIEERICHLM