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Reviewed, UniProtKB/Swiss-Prot P0AFD6 (NUOI_ECOLI)

Last modified November 3, 2009. Version 43. 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 I
    EC=1.6.99.5
Alternative name(s):
    NADH dehydrogenase I subunit I
    NDH-1 subunit I
    NUO9
Gene names
Name: nuoI
Ordered Locus Names: b2281, JW2276
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length180 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. HAMAP MF_01351

Catalytic activity

NADH + quinone = NAD+ + quinol. HAMAP MF_01351

Cofactor

Binds 2 4Fe-4S clusters per subunit By similarity.

Subunit structure

NDH-1 is composed of 13 different subunits. Subunits nuoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity.

Subcellular location

Cell inner membrane; Peripheral membrane protein Potential.

Sequence similarities

Belongs to the complex I 23 kDa subunit family.

Contains 2 4Fe-4S ferredoxin-type domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 180180NADH-quinone oxidoreductase subunit I HAMAP MF_01351
PRO_0000118722

Regions

Domain50 – 80314Fe-4S ferredoxin-type 1
Domain90 – 119304Fe-4S ferredoxin-type 2

Sites

Metal binding601Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding631Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding661Iron-sulfur 1 (4Fe-4S) By similarity
Metal binding701Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding991Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1021Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1051Iron-sulfur 2 (4Fe-4S) By similarity
Metal binding1091Iron-sulfur 1 (4Fe-4S) By similarity

Experimental info

Sequence conflict24 – 296AFAKRE → GSPNQ in CAA48368. Ref.1
Sequence conflict165 – 17511EAENEAKPIDV → DRRTKPSLSTF in CAA48368. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P0AFD6-1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: B31860402432C171

FASTA18020,538
        10         20         30         40         50         60 
MTLKELLVGF GTQVRSIWMI GLHAFAKRET RMYPEEPVYL PPRYRGRIVL TRDPDGEERC 

        70         80         90        100        110        120 
VACNLCAVAC PVGCISLQKA ETKDGRWYPE FFRINFSRCI FCGLCEEACP TTAIQLTPDF 

       130        140        150        160        170        180 
EMGEYKRQDL VYEKEDLLIS GPGKYPEYNF YRMAGMAIDG KDKGEAENEA KPIDVKSLLP 

« 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]"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.
[3]"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.
[4]"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.
[5]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[6]"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 1-4.
Strain: K12 / MG1655 / ATCC 47076.

Cross-references

Sequence databases

X68301 Genomic DNA. Translation: CAA48368.1.
U00096 Genomic DNA. Translation: AAC75341.1.
AP009048 Genomic DNA. Translation: BAA16109.2.
PIRG64999.
RefSeqAP_002879.1.
NP_416784.1.

3D structure databases

HSSPHSSP built from PDB template 1CLF based on UniProtKB P00195.
ModBaseSearch...

Protein-protein interaction databases

STRINGP0AFD6.

Protein family/group databases

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

Genome annotation databases

GeneID946757.
GenomeReviewsGene locus JW2276 in contig AP009048_GR.
Gene locus b2281 in contig U00096_GR.
KEGGecj:JW2276.
eco:b2281.

Organism-specific databases

EchoBASEEB2013.
EcoGeneEG12089. nuoI.
CMRSearch...

Phylogenomic databases

HOGENOMP0AFD6.
OMADFFRINF.

Enzyme and pathway databases

BioCycEcoCyc:NUOI-MON.
MetaCyc:NUOI-MON.

Gene expression databases

GenevestigatorP0AFD6.

Family and domain databases

HAMAPMF_01351.
[Tree]
InterProIPR017896. 4Fe4S_Fe-S-bd.
IPR001450. 4Fe4S_Fe_S_bd_subgr.
IPR017900. 4Fe4S_Fe_S_CS.
IPR010226. NADH_quinone_OxRdtase_chainI.
[Graphical view]
PfamPF00037. Fer4. 2 hits.
[Graphical view]
TIGRFAMsTIGR01971. NuoI. 1 hit.
PROSITEPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNUOI_ECOLI
AccessionPrimary (citable) accession number: P0AFD6
Secondary accession number(s): P33604, P76488, P78183
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 3, 2009
This is version 43 of the entry and version 1 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