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ECOLI:NUOM

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) nuoM
Protein Name(s) NADH-quinone oxidoreductase subunit M

NADH dehydrogenase I subunit M NDH-1 subunit M NUO13

External Links
UniProt P0AFE8
EMBL X68301
L19568
U00096
AP009048
PIR C64999
RefSeq NP_416780.1
YP_490517.1
ProteinModelPortal P0AFE8
SMR P0AFE8
DIP DIP-59255N
STRING 511145.b2277
TCDB 3.D.1.1.1
DNASU 947731
EnsemblBacteria AAC75337
BAA16105
GeneID 12931893
947731
KEGG ecj:Y75_p2241
eco:b2277
PATRIC 32119921
EchoBASE EB1722
EcoGene EG11773
eggNOG COG1008
HOGENOM HOG000100682
InParanoid P0AFE8
KO K00342
OMA EFAIYVI
OrthoDB EOG647TZ6
PhylomeDB P0AFE8
BioCyc EcoCyc:NUOM-MONOMER
ECOL316407:JW2272-MONOMER
MetaCyc:NUOM-MONOMER
PRO PR:P0AFE8
Proteomes UP000000318
UP000000625
Genevestigator P0AFE8
GO GO:0005887
GO:0030964
GO:0005886
GO:0045272
GO:0008137
GO:0048039
GO:0009060
GO:0042773
GO:0015990
InterPro IPR010227
IPR001750
IPR003918
Pfam PF00361
PRINTS PR01437
TIGRFAMs TIGR01972

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0048039

ubiquinone binding

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11773
PANTHER:PTN000511780

F

Seeded From UniProt

complete

involved_in

GO:0015990

electron transport coupled proton transport

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11773
PANTHER:PTN000511780

P

Seeded From UniProt

complete

involved_in

GO:0009060

aerobic respiration

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11773
PANTHER:PTN000511780

P

Seeded From UniProt

complete

contributes_to

GO:0003954

NADH dehydrogenase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG11773
PANTHER:PTN000511780

F

Seeded From UniProt

complete

part_of

GO:0030964

NADH dehydrogenase complex

PMID:7607227[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:7607227[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

Contributes to

GO:0003954

NADH dehydrogenase activity

PMID:17977822[3]

ECO:0000315

F

Figure 4

I used the Contributes to qualifier because, NuoM KO "...lacked a fully assembled NDH-1" showing NuoM is a subunit that is important in the assembly of NDH-1.(1st paragraph under figure 4 in column 2) Without NuoM, the NADH dehydrogenase activity of the complex is inhibited reinforcing the notion that this subunit contributes that activity of the complex. I did not use the NADH (ubiquinone) dehydrogenase activity GO because this paper does not have experimental evidence supporting that.

complete

enables

GO:0048039

ubiquinone binding

PMID:12730198[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

GO:0015992

proton transport

PMID:17977822[3]

ECO:0000315

P

Figure 6. Proton gradient was measured using ACMA. They looked at membrane vesicles which had the NDH1 complex containing normal NuoM and mutant NuoM subunits. The vesicles that contained unmutated were able to create a proton gradient where as those that had NuoM knocked out were not suggesting that NuoM is a major factor in the proton translocation process. It is IMP because this was determined by comparing mutant phenotypes of NuoM.

complete

part_of

GO:0045272

plasma membrane respiratory chain complex I

PMID:22063474[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

GO:0045838

positive regulation of membrane potential

PMID:17977822[3]

ECO:0000315

P

Figure 5. Membrane vesicles were made containing NDH1 complexs with normal NuoM and mutated NuoM subunits. Membrane potential was measured by changes of oxonol VI. With NuoM, a change in membrane potential was seen but when it was knocked out, there was no change in membrane potential. This suggests NuoM is essential in the complex in order to stimulate membrane potential changes.

complete

part_of

GO:0045272

plasma membrane respiratory chain complex I

PMID:12730198[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0015990

electron transport coupled proton transport

PMID:18590697[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009060

aerobic respiration

PMID:9495756[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:15919996[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:15919996[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008137

NADH dehydrogenase (ubiquinone) activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003918
InterPro:IPR010227

F

Seeded From UniProt

complete

involved_in

GO:0042773

ATP synthesis coupled electron transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003918
InterPro:IPR010227

P

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003918
InterPro:IPR010227

P

Seeded From UniProt

complete

enables

GO:0048038

quinone binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0874

F

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

edit table

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. ↑ 2.0 2.1 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 GONUTS page
  3. ↑ 3.0 3.1 3.2 Torres-Bacete, J et al. (2007) Characterization of the NuoM (ND4) subunit in Escherichia coli NDH-1: conserved charged residues essential for energy-coupled activities. J. Biol. Chem. 282 36914-22 PubMed GONUTS page
  4. ↑ 4.0 4.1 Gong, X et al. (2003) The ubiquinone-binding site in NADH:ubiquinone oxidoreductase from Escherichia coli. J. Biol. Chem. 278 25731-7 PubMed GONUTS page
  5. ↑ Erhardt, H et al. (2012) Disruption of individual nuo-genes leads to the formation of partially assembled NADH:ubiquinone oxidoreductase (complex I) in Escherichia coli. Biochim. Biophys. Acta 1817 863-71 PubMed GONUTS page
  6. ↑ Euro, L et al. (2008) Conserved lysine residues of the membrane subunit NuoM are involved in energy conversion by the proton-pumping NADH:ubiquinone oxidoreductase (Complex I). Biochim. Biophys. Acta 1777 1166-72 PubMed GONUTS page
  7. ↑ Falk-Krzesinski, HJ & Wolfe, AJ (1998) Genetic analysis of the nuo locus, which encodes the proton-translocating NADH dehydrogenase in Escherichia coli. J. Bacteriol. 180 1174-84 PubMed GONUTS page
  8. ↑ 8.0 8.1 Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed GONUTS page
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