NUOF_ECOLI
ID NUOF_ECOLI Reviewed; 445 AA.
AC P31979; P78239;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 164.
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;
DE AltName: Full=NUO6;
GN Name=nuoF; OrderedLocusNames=b2284, JW2279;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / AN387;
RX PubMed=7690854; DOI=10.1006/jmbi.1993.1488;
RA Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.;
RT "The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase
RT in Escherichia coli. Organization of the 14 genes and relationship between
RT the derived proteins and subunits of mitochondrial complex I.";
RL J. Mol. Biol. 233:109-122(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8157582; DOI=10.1128/jb.176.8.2143-2150.1994;
RA Pruss B.M., Nelms J.M., Park C., Wolfe A.J.;
RT "Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect
RT growth on mixed amino acids.";
RL J. Bacteriol. 176:2143-2150(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-114.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8366049; DOI=10.1128/jb.175.17.5642-5647.1993;
RA Zambrano M.M., Kolter R.G.;
RT "Escherichia coli mutants lacking NADH dehydrogenase I have a competitive
RT disadvantage in stationary phase.";
RL J. Bacteriol. 175:5642-5647(1993).
RN [7]
RP PROTEIN SEQUENCE OF 1-9.
RX PubMed=7607227; DOI=10.1111/j.1432-1033.1995.tb20594.x;
RA Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.;
RT "Isolation and characterization of the proton-translocating NADH:
RT ubiquinone oxidoreductase from Escherichia coli.";
RL Eur. J. Biochem. 230:538-548(1995).
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X68301; CAA48365.1; -; Genomic_DNA.
DR EMBL; L25055; AAA03537.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC75344.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16113.1; -; Genomic_DNA.
DR EMBL; L19569; AAA53584.1; -; Genomic_DNA.
DR PIR; B65000; B65000.
DR RefSeq; NP_416787.1; NC_000913.3.
DR RefSeq; WP_000789500.1; NZ_LN832404.1.
DR PDB; 7NYR; EM; 3.30 A; F=1-445.
DR PDB; 7NYU; EM; 3.80 A; F=1-445.
DR PDB; 7NYV; EM; 3.70 A; F=1-445.
DR PDB; 7NZ1; EM; 2.10 A; F=1-445.
DR PDBsum; 7NYR; -.
DR PDBsum; 7NYU; -.
DR PDBsum; 7NYV; -.
DR PDBsum; 7NZ1; -.
DR AlphaFoldDB; P31979; -.
DR SMR; P31979; -.
DR BioGRID; 4260513; 64.
DR ComplexPortal; CPX-243; Respiratory chain complex I.
DR DIP; DIP-10382N; -.
DR IntAct; P31979; 7.
DR STRING; 511145.b2284; -.
DR TCDB; 3.D.1.1.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR jPOST; P31979; -.
DR PaxDb; P31979; -.
DR PRIDE; P31979; -.
DR EnsemblBacteria; AAC75344; AAC75344; b2284.
DR EnsemblBacteria; BAA16113; BAA16113; BAA16113.
DR GeneID; 946753; -.
DR KEGG; ecj:JW2279; -.
DR KEGG; eco:b2284; -.
DR PATRIC; fig|1411691.4.peg.4452; -.
DR EchoBASE; EB1723; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_0_1_6; -.
DR InParanoid; P31979; -.
DR OMA; CDDVIMD; -.
DR PhylomeDB; P31979; -.
DR BioCyc; EcoCyc:NUOF-MON; -.
DR BioCyc; MetaCyc:NUOF-MON; -.
DR PRO; PR:P31979; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0030964; C:NADH dehydrogenase complex; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0045272; C:plasma membrane respiratory chain complex I; IDA:EcoCyc.
DR GO; GO:0045271; C:respiratory chain complex I; IC:ComplexPortal.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IMP:EcoCyc.
DR GO; GO:0010181; F:FMN binding; ISS:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IMP:EcoCyc.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IMP:EcoCyc.
DR GO; GO:0045333; P:cellular respiration; IBA:GO_Central.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Direct protein sequencing; Flavoprotein; FMN; Iron;
KW Iron-sulfur; Metal-binding; NAD; Quinone; Reference proteome; Translocase;
KW Ubiquinone.
FT CHAIN 1..445
FT /note="NADH-quinone oxidoreductase subunit F"
FT /id="PRO_0000118568"
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"
FT CONFLICT 3..11
FT /note="NIIRTPETH -> KHYPYSRND (in Ref. 6; AAA53584)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="L -> R (in Ref. 1; CAA48365)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="A -> R (in Ref. 6; AAA53584)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="A -> R (in Ref. 1; CAA48365)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> I (in Ref. 6; AAA53584)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="A -> R (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 12..16
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 26..31
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 100..107
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 178..181
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 183..190
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 246..258
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 260..265
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 335..348
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 380..390
FT /evidence="ECO:0007829|PDB:7NZ1"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:7NZ1"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 400..414
FT /evidence="ECO:0007829|PDB:7NZ1"
FT HELIX 416..421
FT /evidence="ECO:0007829|PDB:7NZ1"
SQ SEQUENCE 445 AA; 49292 MW; 7F39A7DBE50C2075 CRC64;
MKNIIRTPET HPLTWRLRDD KQPVWLDEYR SKNGYEGARK ALTGLSPDEI VNQVKDAGLK
GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQLPH LLVEGMLISA
FALKAYRGYI FLRGEYIEAA VNLRRAIAEA TEAGLLGKNI MGTGFDFELF VHTGAGRYIC
GEETALINSL EGRRANPRSK PPFPATSGAW GKPTCVNNVE TLCNVPAILA NGVEWYQNIS
KSKDAGTKLM GFSGRVKNPG LWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL
TEAHLDLPME FESIGKAGSR LGTALAMAVD HEINMVSLVR NLEEFFARES CGWCTPCRDG
LPWSVKILRA LERGEGQPGD IETLEQLCRF LGPGKTFCAH APGAVEPLQS AIKYFREEFE
AGIKQPFSNT HLINGIQPNL LKERW
