Annotation rule MF_01351
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General rule information [?]

Accession MF_01351
Dates 23-JUN-2006 (Created)
29-JUL-2013 (Last updated, Version 34)
Name NDH1_NuoI
Scope Bacteria
Plastid
Templates Q56224 (NQO9_THET8); P0AFD6 (NUOI_ECOLI): [Recover all]

Propagated annotation [?]


Identifier, protein and gene names [?]

case <OG:Chloroplast>
Identifier
NDHI
Protein name
RecName: Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic;
EC=1.6.5.-;
AltName: Full=NAD(P)H dehydrogenase subunit I;
Short=NDH subunit I;
AltName: Full=NADH-plastoquinone oxidoreductase subunit I;
Gene name
ndhI
else case <OC:Cyanobacteria>
Identifier
NDHI
Protein name
RecName: Full=NAD(P)H-quinone oxidoreductase subunit I;
EC=1.6.5.-;
AltName: Full=NAD(P)H dehydrogenase I subunit I;
AltName: Full=NDH-1 subunit I;
Short=NDH-I;
Gene name
ndhI
else
Identifier
NUOI
Protein name
RecName: Full=NADH-quinone oxidoreductase subunit I;
EC=1.6.99.5;
AltName: Full=NADH dehydrogenase I subunit I;
AltName: Full=NDH-1 subunit I;
Gene name
nuoI
end case

Comments [?]

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 (By similarity).
else case <OC:Mycobacterium> or <OC:Rhodothermus>
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 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
Cofactor Binds 2 4Fe-4S clusters per subunit (By similarity).
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 is composed of at least 11 different subunits (By similarity).
else case <OC:Enterobacteriaceae> or <OC:Shewanellaceae> or <OC:Pseudomonadaceae>
Subunit 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).
else case <OC:Deinococci>
Subunit NDH-1 is composed of 15 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).
else
Subunit NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex (By similarity).
end case
case <OG:Chloroplast>
Subcellular location Plastid, chloroplast thylakoid membrane; Peripheral membrane protein (By similarity).
else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
Subcellular location Cellular thylakoid membrane; Peripheral membrane protein (By similarity).
else case <OC:Gloeobacter>
Subcellular location Cell inner membrane; Peripheral membrane protein (Potential).
else case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location Cell membrane; Peripheral membrane protein (Potential).
else case <Property:Membrane=2>
Subcellular location Cell inner membrane; Peripheral membrane protein (Potential).
end case
Similarity Belongs to the complex I 23 kDa subunit family.

Keywords [?]

case <OG:Chloroplast> or <OC:Cyanobacteria> and not <OC:Gloeobacter>
else case <OC:Gloeobacter>
else case not defined <Property:Membrane> or <Property:Membrane=1>
else case <Property:Membrane=2>
end case
case <OG:Chloroplast> or <OC:Cyanobacteria>
else case not <OC:Mycobacterium> and not <OC:Rhodothermus> and not <OC:Archaea>
end case

Gene Ontology [?]

GO:0005506; Molecular function: iron ion binding.
GO:0055114; Biological process: oxidation-reduction process.
case <OG:Chloroplast> or <OC:Cyanobacteria>
GO:0016655; Molecular function: oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor.
GO:0019684; Biological process: photosynthesis, light reaction.
else
GO:0050136; Molecular function: NADH dehydrogenase (quinone) activity.
end case
case <OC:Cyanobacteria> and not <OC:Gloeobacter>
GO:0042651; Cellular component: thylakoid membrane.
else case <OG:Chloroplast>
GO:0009535; Cellular component: chloroplast thylakoid membrane.
else
GO:0005886; Cellular component: plasma membrane.
end case

Cross-references [?]

Pfam PF00037; Fer4; 2;
PRINTS PR00353; 4FE4SFRDOXIN; 1;
PROSITE PS00198; 4FE4S_FER_1; 2;
PS51379; 4FE4S_FER_2; 2; trigger=PRU00711;

Features [?]

From: NQO9_THET8 (Q56224)
Key     From     To       Description   Tag   Condition   FTGroup
METAL     53     53       Iron-sulfur 1 (4Fe-4S) (By similarity)     C   1
METAL     56     56       Iron-sulfur 1 (4Fe-4S) (By similarity)     C   1
METAL     59     59       Iron-sulfur 1 (4Fe-4S) (By similarity)     C   1
METAL     63     63       Iron-sulfur 2 (4Fe-4S) (By similarity)     C   2
METAL     98     98       Iron-sulfur 2 (4Fe-4S) (By similarity)     C   2
METAL     101     101       Iron-sulfur 2 (4Fe-4S) (By similarity)     C   2
METAL     104     104       Iron-sulfur 2 (4Fe-4S) (By similarity)     C   2
METAL     108     108       Iron-sulfur 1 (4Fe-4S) (By similarity)     C   1

Additional information [?]

Size range 131-264 amino acids
Related rules None
Fusion Nter: MF_01350 (nuoH); Cter: None
Comments In NOCFA is N-terminally fused with nuoH, another subunit of the same complex. See also comments on subunit composition in family MF_01350 (nuoH/ndhA). THET8 and PARDE are annotated with another nomenclature.