Search for
You are here: ExPASy CH  > Databases  > Around UniProtKB  > HAMAP

HAMAP annotation rule: MF_01357

Send feedback new


Accession MF_01357
Dates 18-NOV-2008 (Created)
30-NOV-2009 (Last updated, Version 5)
Data class Protein
Names NDH1_NuoC




case <OG:Chloroplast>
Identifier NDHJ
Protein name
RecName: Full=NAD(P)H-quinone oxidoreductase subunit J, chloroplastic;
EC=1.6.5.-;
AltName: Full=NAD(P)H dehydrogenase, subunit J;
AltName: Full=NADH-plastoquinone oxidoreductase subunit J;
Gene name ndhJ

else case <OC:Cyanobacteria>
Identifier NDHJ
Protein name
RecName: Full=NAD(P)H-quinone oxidoreductase subunit J;
EC=1.6.5.-;
AltName: Full=NAD(P)H dehydrogenase, subunit J;
AltName: Full=NADH-plastoquinone oxidoreductase subunit J;
AltName: Full=NDH-1 subunit J;
Short=NDH-J;
Gene name ndhJ

else
Identifier NUOC
Protein name
RecName: Full=NADH-quinone oxidoreductase subunit C;
EC=1.6.99.5;
AltName: Full=NADH dehydrogenase I subunit C;
AltName: Full=NDH-1 subunit C;
Gene name nuoC
end case


case <OG:Chloroplast>
FUNCTION: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (By similarity).

else case <OC:Cyanobacteria>
FUNCTION: NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration (By similarity).

else case <OC:Actinobacteria> or <OC:Bacteroidetes> or <OC:Chlorobi> or <OC:Deinococcus-Thermus> or <OC:Firmicutes>
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 a menaquinone. 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 (By similarity).

else
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 (By similarity).
end case


case <OG:Chloroplast> or <OC:Cyanobacteria>
CATALYTIC ACTIVITY: NAD(P)H + plastoquinone = NAD(P)(+) + plastoquinol.

else
CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
end case


case <OG:Chloroplast>
SUBUNIT: NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus (By similarity).

else case <OC:Cyanobacteria>
SUBUNIT: NDH-1 can be composed of about 15 different subunits; different subcomplexes with different compositions have been identified which probably have different functions (By similarity).

else case <OC:Deinococci>
SUBUNIT: NDH-1 is composed of 15 different subunits. Subunits nuoB, C, D, E, F, and G constitute the peripheral sector of the complex (By similarity).

else
SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits nuoB, C, D, E, F, and G constitute the peripheral sector of the complex (By similarity).
end case


case <OG:Chloroplast>
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side (By similarity).

else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).

else case <OC:Gloeobacter> or <Property:Membrane=2>
SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).

else case <Property:Membrane=1>
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side (By similarity).
end case

SIMILARITY: Belongs to the complex I 30 kDa subunit family.
PROSITE PS00542; COMPLEX1_30K; 1;
Pfam PF00329; Complex1_30kDa; 1;
TIGRFAMs TIGR01961; NuoC_fam; 1;
NAD.

case <OG:Chloroplast> or <OC:Cyanobacteria>

else case not <OC:Actinobacteria> and not <OC:Bacteroidetes> and not <OC:Chlorobi> and not <OC:Deinococcus-Thermus> and not <OC:Firmicutes>
end case


case <OG:Chloroplast> or <Property:Thylakoid>

else case not <Property:Thylakoid> and <Property:Membrane=2>

else case <Property:Membrane=1>
end case

GO:0055114; Biological process: oxidation reduction.
GO:0019684; Biological process: photosynthesis, light reaction.

case <OG:Chloroplast> or <OC:Cyanobacteria>
GO:0016655; Molecular function: oxidoreductase activity, acting on NADH or NADPH, quinone or similar compound as acceptor.

else
GO:0050136; Molecular function: NADH dehydrogenase (quinone) activity.
end case


case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.

else case <Property:Thylakoid>
GO:0042651; Cellular component: thylakoid membrane.

else case <Property:Membrane=1>
GO:0005886; Cellular component: plasma membrane.

else case <Property:Membrane=2>
GO:0005886; Cellular component: plasma membrane.
end case




Size range: 148-309 amino acids
Related UniRules: MF_01359 (NUOCD (supersedes the current rule)); MF_01397 (NUOCD (supersedes the current rule))
Template: P33599 (NUOCD_ECOLI); P19125 (NDHJ_SYNY3): [Recover all]
Scope: Bacteria
Plastid
Fusion: Nter: None; Cter: None
Duplicate: in RHIE6, RHIME
Plasmid encoded: in RHIME
Comments: 14 proteins form the NDH-1 complex in most bacteria, there are at least 15 subunits in cyanobacteria and chloroplasts. PARDE and THET8 are annotated with another nomenclature. In some bacteria this protein is fused with nuoD, see families MF_01359 and MF_01397. In many bacteria there are both the individual and fused versions.

View rule in raw text format (no links)