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Reviewed, UniProtKB/Swiss-Prot P31979 (NUOF_ECOLI)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADH-quinone oxidoreductase subunit F
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit F
    NDH-1 subunit F
    NUO6
Gene names
Name: nuoF
Ordered Locus Names: b2284, JW2279
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.

Catalytic activity

NADH + quinone = NAD+ + quinol.

Cofactor

Binds 1 FMN Potential.

Binds 1 4Fe-4S cluster Potential.

Subunit structure

Composed of 13 different subunits. Subunits nuoCD, E, F, and G constitute the peripheral sector of the complex.

Sequence similarities

Belongs to the complex I 51 kDa subunit family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445NADH-quinone oxidoreductase subunit F
PRO_0000118568

Regions

Nucleotide binding61 – 7010NAD By similarity
Nucleotide binding174 – 22148FMN By similarity

Sites

Metal binding3511Iron-sulfur (4Fe-4S) Potential
Metal binding3541Iron-sulfur (4Fe-4S) Potential
Metal binding3571Iron-sulfur (4Fe-4S) Potential
Metal binding3981Iron-sulfur (4Fe-4S) Potential

Experimental info

Sequence conflict3 – 119NIIRTPETH → KHYPYSRND in AAA53584. Ref.6
Sequence conflict261L → R in CAA48365. Ref.1
Sequence conflict381A → R in AAA53584. Ref.6
Sequence conflict411A → R in CAA48365. Ref.1
Sequence conflict511V → I in AAA53584. Ref.6
Sequence conflict3701A → R Ref.1
Sequence conflict3701A → R Ref.2

Sequences

Sequence LengthMass (Da)Tools
P31979-1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 7F39A7DBE50C2075

FASTA44549,292
        10         20         30         40         50         60 
MKNIIRTPET HPLTWRLRDD KQPVWLDEYR SKNGYEGARK ALTGLSPDEI VNQVKDAGLK 

        70         80         90        100        110        120 
GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQLPH LLVEGMLISA 

       130        140        150        160        170        180 
FALKAYRGYI FLRGEYIEAA VNLRRAIAEA TEAGLLGKNI MGTGFDFELF VHTGAGRYIC 

       190        200        210        220        230        240 
GEETALINSL EGRRANPRSK PPFPATSGAW GKPTCVNNVE TLCNVPAILA NGVEWYQNIS 

       250        260        270        280        290        300 
KSKDAGTKLM GFSGRVKNPG LWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL 

       310        320        330        340        350        360 
TEAHLDLPME FESIGKAGSR LGTALAMAVD HEINMVSLVR NLEEFFARES CGWCTPCRDG 

       370        380        390        400        410        420 
LPWSVKILRA LERGEGQPGD IETLEQLCRF LGPGKTFCAH APGAVEPLQS AIKYFREEFE 

       430        440 
AGIKQPFSNT HLINGIQPNL LKERW 

« Hide

References

« Hide 'large scale' references
[1]"The gene locus of the proton-translocating NADH: ubiquinone oxidoreductase in Escherichia coli. Organization of the 14 genes and relationship between the derived proteins and subunits of mitochondrial complex I."
Weidner U., Geier S., Ptock A., Friedrich T., Leif H., Weiss H.
J. Mol. Biol. 233:109-122(1993) [PubMed: 7690854] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / AN387.
[2]"Mutations in NADH:ubiquinone oxidoreductase of Escherichia coli affect growth on mixed amino acids."
Pruss B.M., Nelms J.M., Park C., Wolfe A.J.
J. Bacteriol. 176:2143-2150(1994) [PubMed: 8157582] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Escherichia coli mutants lacking NADH dehydrogenase I have a competitive disadvantage in stationary phase."
Zambrano M.M., Kolter R.G.
J. Bacteriol. 175:5642-5647(1993) [PubMed: 8366049] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-114.
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli."
Leif H., Sled V.D., Ohnishi T., Weiss H., Friedrich T.
Eur. J. Biochem. 230:538-548(1995) [PubMed: 7607227] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-9.

Cross-references

Sequence databases

X68301 Genomic DNA. Translation: CAA48365.1.
L25055 Unassigned DNA. Translation: AAA03537.1.
U00096 Genomic DNA. Translation: AAC75344.1.
AP009048 Genomic DNA. Translation: BAA16113.1.
L19569 Genomic DNA. Translation: AAA53584.1.
PIRB65000.
RefSeqAP_002882.1.
NP_416787.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

TCDB3.D.1.1.1. proton-translocating NADH dehydrogenase (NDH) family.

Genome annotation databases

GeneID946753.
GenomeReviewsGene locus JW2279 in contig AP009048_GR.
Gene locus b2284 in contig U00096_GR.
KEGGecj:JW2279.
eco:b2284.

Organism-specific databases

EchoBASEEB1723.
EcoGeneEG11774. nuoF.
CMRSearch...

Phylogenomic databases

HOGENOMP31979.
OMAP31979. LPHLLIE.

Enzyme and pathway databases

BioCycEcoCyc:NUOF-MON.
MetaCyc:NUOF-MON.

Family and domain databases

InterProIPR001949. NADH-UbQ_OxRdtase_51KDa_CS.
IPR019575. NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
IPR011537. NADH-UbQ_OxRdtase_suF.
IPR011538. NADH_UbQ_OxRdtase_51KDa_su.
IPR019554. Soluble_ligand_bd.
[Graphical view]
PfamPF01512. Complex1_51K. 1 hit.
PF10589. NADH_4Fe-4S. 1 hit.
PF10531. SLBB. 1 hit.
[Graphical view]
TIGRFAMsTIGR01959. nuoF_fam. 1 hit.
PROSITEPS00644. COMPLEX1_51K_1. 1 hit.
PS00645. COMPLEX1_51K_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOF_ECOLI
AccessionPrimary (citable) accession number: P31979
Secondary accession number(s): P78239
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1997
Last modified: June 16, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents