ID   NUOF_BUCBP              Reviewed;         444 AA.
AC   Q89AU2;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=bbp_147;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC   -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC       constitute the peripheral sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AE016826; AAO26881.1; -; Genomic_DNA.
DR   RefSeq; WP_011091282.1; NC_004545.1.
DR   AlphaFoldDB; Q89AU2; -.
DR   SMR; Q89AU2; -.
DR   STRING; 224915.bbp_147; -.
DR   PRIDE; Q89AU2; -.
DR   EnsemblBacteria; AAO26881; AAO26881; bbp_147.
DR   GeneID; 56470691; -.
DR   KEGG; bab:bbp_147; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_0_1_6; -.
DR   OMA; CDDVIMD; -.
DR   OrthoDB; 688908at2; -.
DR   Proteomes; UP000000601; 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   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 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   Reference proteome; Translocase.
FT   CHAIN           1..444
FT                   /note="NADH-quinone oxidoreductase subunit F"
FT                   /id="PRO_0000118573"
FT   BINDING         62..71
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         177..224
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         357
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         360
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
FT   BINDING         401
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   444 AA;  49916 MW;  C3AD7DF2D8583EA9 CRC64;
     MKKLLSRTSE THPLTWRLNA QQDTVWIKEY KRKNGYRAFE KVVNHMTSED VIDLIKQSGL
     KGRGGAGFLT GLKWSLMPPL NDEYGYTRYL LCNADEMEPG TYKDRFLMEK VPHQLLEGIL
     ISAFALSVTK SYIFLRGEYV NTERILKQSI IEATNYGYLG KNVCGSNLTF EIFIHTGAGR
     YICGEETALI NSLEGRRANP RFKPPFPAYV GLWGKPTCVN NVETLSNVPA IFLNGVKWYK
     GLSKSLDTGT KMMGFSGSVK FPGIWELPFG ITAREIFERY AGGMKNNKKL KVWQPGGAST
     SFLIDKHLDV PMDFVNIKKV GSRLGTALAM AVDDSVSIVS LVRNIEEFFS RESCGFCTPC
     RDGLPWIVKI LKVLEQKIGV PEDIEILEQL CEQLGPGRTF CAHAPGAIEP LKSALKYFRL
     EFELCVNSNS TIKCKYIHSS ISEY