UniProt functional annotation for P0AFE4



	UniProt functional annotation for P0AFE4

UniProt code: P0AFE4.

Organism: Escherichia coli (strain K12).

Taxonomy: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.

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.

Function: There are 2 NADH dehydrogenases in E.coli, however only this complex is able to use dNADH (reduced nicotinamide hypoxanthine dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy-5-methyl-6-decyl- 1,4-benzoquinone) as substrates.

Catalytic activity: Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255|HAMAP-Rule:MF_01456};

Subunit: NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.

Subcellular location: Cell inner membrane; Multi-pass membrane protein.

Similarity: Belongs to the complex I subunit 4L family. {ECO:0000255|HAMAP-Rule:MF_01456}.

Annotations taken from UniProtKB at the EBI.


Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.



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.



Function:		There are 2 NADH dehydrogenases in E.coli, however only this complex is able to use dNADH (reduced nicotinamide hypoxanthine dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy-5-methyl-6-decyl- 1,4-benzoquinone) as substrates.


Catalytic activity:		Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; Evidence={ECO:0000255\|HAMAP-Rule:MF_01456};
Subunit:		NDH-1 is composed of 13 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
Subcellular location:		Cell inner membrane; Multi-pass membrane protein.
Similarity:		Belongs to the complex I subunit 4L family. {ECO:0000255\|HAMAP-Rule:MF_01456}.