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Annotation rule MF_01351 |
General rule information
[?]
Accession |
MF_01351 |
Dates |
23-JUN-2006 (Created) 19-NOV-2019 (Last updated, Version 42) |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
case <OG:Chloroplast>
Protein name |
RecName:
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Full=NAD(P)H-quinone oxidoreductase subunit I, chloroplastic;
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EC 7.1.1.-;
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AltName:
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Full=NAD(P)H dehydrogenase subunit I;
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Short=NDH subunit I;
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AltName:
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Full=NADH-plastoquinone oxidoreductase subunit I;
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else case <OC:Cyanobacteria>
Protein name |
RecName:
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Full=NAD(P)H-quinone oxidoreductase subunit I;
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EC 7.1.1.-;
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AltName:
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Full=NAD(P)H dehydrogenase I subunit I;
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AltName:
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Full=NDH-1 subunit I;
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Short=NDH-I;
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else
Protein name |
RecName:
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Full=NADH-quinone oxidoreductase subunit I;
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EC 7.1.1.-;
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AltName:
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Full=NADH dehydrogenase I subunit I;
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AltName:
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Full=NDH-1 subunit I;
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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. |
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. |
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. |
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. |
end case
case <OG:Chloroplast> or <OC:Cyanobacteria>
Catalytic activity |
RHEA:42608: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
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RHEA:42612: a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+)
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else
Catalytic activity |
RHEA:57888: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
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end case
case <OG:Chloroplast>
Subunit |
NDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus. |
else case <OC:Cyanobacteria>
Subunit |
NDH-1 is composed of at least 11 different subunits. |
else case <OC:Enterobacterales> 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. |
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. |
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. |
end case
case <OG:Chloroplast>
Subcellular location |
Plastid, chloroplast thylakoid membrane; Peripheral membrane protein. |
else case <OC:Cyanobacteria> and not <OC:Gloeobacter>
Subcellular location |
Cellular thylakoid membrane; Peripheral membrane protein. |
else case <OC:Gloeobacter>
Subcellular location |
Cell inner membrane; Peripheral membrane protein. |
else case not defined <Property:Membrane> or <Property:Membrane=1>
Subcellular location |
Cell membrane; Peripheral membrane protein. |
else case <Property:Membrane=2>
Subcellular location |
Cell inner membrane; Peripheral membrane protein. |
end case
Similarity |
Belongs to the complex I 23 kDa subunit family. |
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
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
end case
From: NQO9_THET8 (Q56224) |
Key
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From
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To
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Description
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Tag
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|
Condition
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FTGroup
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METAL
|
|
53
|
|
53
|
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Iron-sulfur 1 (4Fe-4S)
|
|
|
|
C
|
|
1
|
METAL
|
|
56
|
|
56
|
|
Iron-sulfur 1 (4Fe-4S)
|
|
|
|
C
|
|
1
|
METAL
|
|
59
|
|
59
|
|
Iron-sulfur 1 (4Fe-4S)
|
|
|
|
C
|
|
1
|
METAL
|
|
63
|
|
63
|
|
Iron-sulfur 2 (4Fe-4S)
|
|
|
|
C
|
|
2
|
METAL
|
|
98
|
|
98
|
|
Iron-sulfur 2 (4Fe-4S)
|
|
|
|
C
|
|
2
|
METAL
|
|
101
|
|
101
|
|
Iron-sulfur 2 (4Fe-4S)
|
|
|
|
C
|
|
2
|
METAL
|
|
104
|
|
104
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Iron-sulfur 2 (4Fe-4S)
|
|
|
|
C
|
|
2
|
METAL
|
|
108
|
|
108
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Iron-sulfur 1 (4Fe-4S)
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|
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C
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1
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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. |