NUOF_SALTY
ID NUOF_SALTY Reviewed; 445 AA.
AC P33901;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 136.
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=STM2324;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8234329; DOI=10.1073/pnas.90.21.9877;
RA Archer C.D., Wang X., Elliott T.;
RT "Mutants defective in the energy-conserving NADH dehydrogenase of
RT Salmonella typhimurium identified by a decrease in energy-dependent
RT proteolysis after carbon starvation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:9877-9881(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 (By 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 -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16062.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L22504; AAA16062.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; AE006468; AAL21225.1; -; Genomic_DNA.
DR RefSeq; NP_461266.1; NC_003197.2.
DR RefSeq; WP_000800048.1; NC_003197.2.
DR AlphaFoldDB; P33901; -.
DR SMR; P33901; -.
DR STRING; 99287.STM2324; -.
DR PaxDb; P33901; -.
DR PRIDE; P33901; -.
DR EnsemblBacteria; AAL21225; AAL21225; STM2324.
DR GeneID; 1253846; -.
DR KEGG; stm:STM2324; -.
DR PATRIC; fig|99287.12.peg.2461; -.
DR HOGENOM; CLU_014881_0_1_6; -.
DR OMA; CDDVIMD; -.
DR PhylomeDB; P33901; -.
DR BioCyc; SENT99287:STM2324-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IBA:GO_Central.
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 GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
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; Ubiquinone.
FT CHAIN 1..445
FT /note="NADH-quinone oxidoreductase subunit F"
FT /id="PRO_0000118569"
FT BINDING 61..70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 174..221
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
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 398
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
SQ SEQUENCE 445 AA; 49245 MW; E020825E359F382C CRC64;
MKNVIRTPET HPLTWRLRDD KQPVWLDEYR SKNGYEGARK ALTGLSPDEI VSQVKDAGLK
GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQLPH LLVEGMLISA
FALKAYRGYI FLRGEYIEAA VHLRRAIAEA TEAGLLGKNI MGTGFDFELF VHTGAGRYIC
GEETALINSL EGRRANPRSK PPFPATSGVW GKPTCVNNVE TLCNVPAILA NGVEWYQNIS
KSKDAGTKLM GFSGRVKNPG LWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL
TEAHLDLPME FESIGKAGSR LGTALAMAVD HEIGMVSLVR NLEEFFARES CGWCTPCRDG
LPWSVKILRA LERGEGQPGD IETLEQLCRF LGPGKTFCAH APGAVEPLQS AIKYFREEFE
AGIKQPFSNT HLINGIQPNL LKERW
