nuoI:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.

Standard name

NuoI

Synonyms

NADH:ubiquinone oxidoreductase, chain I[1], B2281[2][1], NuoI[2][1] , ECK2275, JW2276, b2281

Product description

NuoI[2][3];

Component of connecting fragment of NADH dehydrogenase I[3]; NADH dehydrogenase I[2][3]

NADH:ubiquinone oxidoreductase subunit I, complex I; NADH dehydrogenase I[4]

EC number (for enzymes)

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Notes

Function

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<protect> Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status

NOT

GO:0005737

cytoplasm

PMID:7607227[5]

IMP: Inferred from Mutant Phenotype

C

Seeded from Riley et al 2006 [1].

See Discussion page for explanation of 'NOT' qualifier.

complete

GO:0005886

plasma membrane

PMID:7607227[5]

IDA: Inferred from Direct Assay

C

The NADH dehydrogenase I complex fractionates with cytoplasmic membranes.

complete

GO:0005506

iron ion binding

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01351

F

Seeded from EcoCyc (v14.0)

complete

GO:0005506

iron ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0408

F

Seeded from EcoCyc (v14.0)

complete

Contributes to

GO:0003954

NADH dehydrogenase activity

PMID:3122832[6]

IDA: Inferred from Direct Assay

F

Purified NADH dehydrogenase I in membrane vesicles can oxidize NADH.

complete

GO:0051539

4 iron, 4 sulfur cluster binding

PMID:7690854[7]

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:P29921

F

E. coli NuoI is 31% identical to the NQO9 subunit of NADH dehydrogenase I from Paracoccus denitrificans. EPR spectra from purified, recombinant, reconstituted NQO9 protein is consistent with the presence of two [4Fe-4S] clusters.[8]

complete

GO:0009055

electron carrier activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001450

F

Seeded from EcoCyc (v14.0)

complete

GO:0030964

NADH dehydrogenase complex

PMID:7607227[5]

IDA: Inferred from Direct Assay

C

The E. coli NADH dehydrogenase complex was purified and the subunits separated by SDS-PAGE. The N-termini of these 6 polypeptides were sequenced after deblocking with methanolic HCl.

complete

GO:0009055

electron carrier activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR017900

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009051

F

Seeded from EcoCyc (v14.0)

complete

GO:0016491

oxidoreductase activity

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

F

Seeded from EcoCyc (v14.0)

complete

GO:0016651

oxidoreductase activity, acting on NADH or NADPH

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010226

F

Seeded from EcoCyc (v14.0)

complete

GO:0019684

photosynthesis, light reaction

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01351

P

Seeded from EcoCyc (v14.0)

complete

GO:0019898

extrinsic to membrane

GO_REF:0000023

IEA: Inferred from Electronic Annotation

SP_SL:SL-9903

C

Seeded from EcoCyc (v14.0)

complete

GO:0046872

metal ion binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0479

F

Seeded from EcoCyc (v14.0)

complete

GO:0048038

quinone binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0874

F

Seeded from EcoCyc (v14.0)

complete

GO:0050136

NADH dehydrogenase (quinone) activity

GOA:spec
GO_REF:0000003

IEA: Inferred from Electronic Annotation

EC:1.6.99.5

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR001450

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009051

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR017900

F

Seeded from EcoCyc (v14.0)

complete

GO:0051536

iron-sulfur cluster binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0411

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010226

F

Seeded from EcoCyc (v14.0)

complete

GO:0051539

4 iron, 4 sulfur cluster binding

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0004

F

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:hamap
GO_REF:0000020

IEA: Inferred from Electronic Annotation

HAMAP:MF_01351

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR009051

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:interpro
GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010226

P

Seeded from EcoCyc (v14.0)

complete

GO:0055114

oxidation reduction

GOA:spkw
SP_KW:GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0560

P

Seeded from EcoCyc (v14.0)

complete

Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Partner Type Partner Notes References Evidence

Protein

Subunits of connecting fragment of NADH dehydrogenase I

could be indirect

Protein

rimJ

PMID:16606699[9]

Experiment(s):EBI-1142422

Protein

gpmB

PMID:16606699[9]

Experiment(s):EBI-1142422

Protein

Subunits of NADH dehydrogenase I

could be indirect


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Notes

Localization

See Help:Product_localization for how to add or edit information in this section of EcoliWiki.

Compartment Description Evidence Reference/Source Notes

Cytoplasm

PMID:9298646[10], PMID:11416161[11]

EchoLocation:nuoI


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Notes

Structure and Physical Properties

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<protect> Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

Name
Sequence

at EcoCyc

MTLKELLVGF GTQVRSIWMI GLHAFAKRET RMYPEEPVYL PPRYRGRIVL TRDPDGEERC
VACNLCAVAC PVGCISLQKA ETKDGRWYPE FFRINFSRCI FCGLCEEACP TTAIQLTPDF
EMGEYKRQDL VYEKEDLLIS GPGKYPEYNF YRMAGMAIDG KDKGEAENEA KPIDVKSLLP
Length

180

Mol. Wt

20.537 kDa

pI

5.3 (calculated)

Extinction coefficient

24,410 - 25,535 (calc based on 9 Y, 2 W, and 9 C residues)


Domains/Motifs/Modification Sites

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.

Type Residues Description Notes References

Domain

92..115

PF00037 4Fe-4S binding domain

PMID:19920124[12]

<motif_map/>

Structure
See Help:Product_structure for help entering or editing information in this section of EcoliWiki.

Structures

<beststructure> gene=nuoI taxon=562,83333 </beststructure>

Models

View models at:

</protect>

Structure figures

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</protect>

Notes

Gene Product Resources

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See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.

Resource type Source Notes/Reference

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Notes

Accessions in Other Databases

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See Help:Gene_accessions for help with entering information into the Gene Accessions table.

Database Accession Notes

NCBI (Protein) (EcoliWiki Page)

GI:16130216

Escherichia coli str. K-12 substr. MG1655

NCBI (Protein) (EcoliWiki Page)

GeneID:946757

Escherichia coli str. K-12 substr. MG1655

ASAP

ASAP:ABE-0007539

Escherichia coli str. K-12 substr. MG1655

UniProt (EcoliWiki Page)

UniProtKB/Swiss-Prot:P0AFD6

Escherichia coli str. K-12 substr. MG1655

EcoCyc

EcoCyc:EG12089

Escherichia coli str. K-12 substr. MG1655

EcoGene

EcoGene:EG12089

Escherichia coli str. K-12 substr. MG1655

NCBI (Gene) (EcoliWiki Page)

GeneID:946757

Escherichia coli str. K-12 substr. MG1655

RegulonDB

RegulonDB:ECK120001994

Escherichia coli str. K-12 substr. MG1655

EchoBASE

EchoBASE:EB2013

Escherichia coli str. K-12 substr. MG1655

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Notes

Links

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References

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See Help:References for how to manage references in EcoliWiki.

  1. 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
  5. 5.0 5.1 5.2 Leif, H et al. (1995) Isolation and characterization of the proton-translocating NADH: ubiquinone oxidoreductase from Escherichia coli. Eur. J. Biochem. 230 538-48 PubMed
  6. Matsushita, K et al. (1987) NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry 26 7732-7 PubMed
  7. Weidner, U et al. (1993) 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. J. Mol. Biol. 233 109-22 PubMed
  8. Yano, T et al. (1999) Characterization of the putative 2x[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Expression, reconstitution, and EPR characterization. J. Biol. Chem. 274 28598-605 PubMed
  9. 9.0 9.1 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
  10. Link, AJ et al. (1997) Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis 18 1259-313 PubMed
  11. Moreno-Bruna, B et al. (2001) Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 98 8128-32 PubMed
  12. Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed

Categories

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