NADH-quinone oxidoreductase subunit I - Escherichia coli (strain K12)

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P0AFD6 (NUOI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Protein existence	Evidence 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-Rule MF_01351
Catalytic activity	NADH + quinone = NAD⁺ + quinol. HAMAP-Rule 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 HAMAP-Rule MF_01351.
Sequence similarities	Belongs to the complex I 23 kDa subunit family. Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Quinone
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from mutant phenotype PubMed 9495756. Source: EcoCyc photosynthesis, light reaction Inferred from electronic annotation. Source: HAMAP
Cellular_component	plasma membrane respiratory chain complex I Inferred from direct assay PubMed 11997136. Source: EcoCyc
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay PubMed 22474289. Source: EcoCyc NADH dehydrogenase (quinone) activity Inferred from electronic annotation. Source: HAMAP electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: HAMAP quinone binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 180

180

NADH-quinone oxidoreductase subunit I HAMAP-Rule MF_01351

PRO_0000118722

Regions

Domain

50 – 80

4Fe-4S ferredoxin-type 1

Domain

90 – 119

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 1 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

102

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

105

Iron-sulfur 2 (4Fe-4S) By similarity

Metal binding

109

Iron-sulfur 1 (4Fe-4S) By similarity

Experimental info

Sequence conflict

24 – 29

AFAKRE → GSPNQ in CAA48368. Ref.1

Sequence conflict

165 – 175

EAENEAKPIDV → DRRTKPSLSTF in CAA48368. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P0AFD6 [UniParc].

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

FASTA

180

20,538

        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' referencesShow '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] [Europe PMC] [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. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68301 Genomic DNA. Translation: CAA48368.1. U00096 Genomic DNA. Translation: AAC75341.1. AP009048 Genomic DNA. Translation: BAA16109.2.
PIR	G64999.
RefSeq	NP_416784.1. NC_000913.2. YP_490521.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AFD6.
SMR	P0AFD6. Positions 33-180.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35918N.
IntAct	P0AFD6. 7 interactions.
STRING	511145.b2281.
Protein family/group databases
TCDB	3.D.1.1.1. H+ or Na+-translocating NADH dehydrogenase (NDH) family.
Proteomic databases
PaxDb	P0AFD6.
PRIDE	P0AFD6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75341; AAC75341; b2281. BAA16109; BAA16109; BAA16109.
GeneID	12931516. 946757.
KEGG	ecj:Y75_p2245. eco:b2281.
PATRIC	32119929. VBIEscCol129921_2374.
Organism-specific databases
EchoBASE	EB2013.
EcoGene	EG12089. nuoI.
Phylogenomic databases
eggNOG	COG1143.
HOGENOM	HOG000228291.
KO	K00338.
OMA	DFFRINF.
ProtClustDB	PRK05888.
Enzyme and pathway databases
BioCyc	EcoCyc:NUOI-MONOMER. ECOL316407:JW2276-MONOMER. MetaCyc:NUOI-MONOMER.
Gene expression databases
Genevestigator	P0AFD6.
Family and domain databases
HAMAP	MF_01351. NDH1_NuoI.
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR010226. NADH_quinone_OxRdtase_chainI. [Graphical view]
Pfam	PF00037. Fer4. 2 hits. [Graphical view]
TIGRFAMs	TIGR01971. NuoI. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NUOI_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents