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HAMAP rule MF_01350

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General rule information [?]

Accession MF_01350
Dates 24-MAY-2006 (Created)
14-JUL-2023 (Last updated, Version 44)
Name NDH1_NuoH
Scope(s) Bacteria
Archaea
Methanosarcinales
Plastid
Template(s) P26522 (NU1C_SYNY3); P29920 (NQO8_PARDE); Q60019 (NQO8_THET8); P0AFD4 (NUOH_ECOLI); P42032 (NUOH_RHOCA); [ Recover all ]
Triggered by HAMAP; MF_01350 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <OG:Chloroplast>
Identifier NU1C
Protein name RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic;
                 EC=7.1.1.-;
AltName: Full=NAD(P)H dehydrogenase subunit 1;
                 Short=NDH subunit 1;
AltName: Full=NADH-plastoquinone oxidoreductase subunit 1;
Gene name Name=ndhA;
else case <OC:Cyanobacteriota>
Identifier NU1C
Protein name RecName: Full=NAD(P)H-quinone oxidoreductase subunit 1;
                 EC=7.1.1.-;
AltName: Full=NAD(P)H dehydrogenase I subunit 1;
AltName: Full=NDH-1 subunit 1;
AltName: Full=NDH-A;
Gene name Name=ndhA;
else case <OC:Methanomicrobia>
Identifier FPOH
Protein name RecName: Full=F(420)H(2) dehydrogenase subunit H;
                 EC=1.5.98.3;
AltName: Full=F(420)H(2)-dependent phenazine dehydrogenase subunit H;
AltName: Full=F(420)H(2)-dependent phenazine oxidoreductase subunit H;
                 Short=FPO subunit H;
Gene name Name=fpoH;
else
Identifier NUOH
Protein name RecName: Full=NADH-quinone oxidoreductase subunit H;
                 EC=7.1.1.-;
AltName: Full=NADH dehydrogenase I subunit H;
AltName: Full=NDH-1 subunit H;
Gene name Name=nuoH;
end case

Comments [?]

case <OG:Chloroplast>
FUNCTIONNDH 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:Cyanobacteriota>
FUNCTIONNDH-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:Methanomicrobia>
FUNCTIONComponent of the F(420)H(2) dehydrogenase (FPO complex) which is part of the energy-conserving F(420)H(2):heterodisulfide oxidoreductase system. The membrane-bound electron transfer system of the complex plays an important role in the metabolism of methylotrophic methanogens when the organisms grow on methanol or methylamines. Catalyzes the oxidation of methanophenazine to dihydromethanophenazine. It shuttles electrons from F(420)H(2), via FAD and iron-sulfur (Fe-S) centers, to methanophenazine (an electron carrier in the membrane). It couples the redox reaction to proton translocation (for every two electrons transferred, two hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
else case <OC:Mycobacterium> or <OC:Rhodothermus>
FUNCTIONNDH-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
FUNCTIONNDH-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. This subunit may bind ubiquinone.
end case
case <OG:Chloroplast> or <OC:Cyanobacteriota>
CATALYTIC ACTIVITY Reaction=a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+); Xref=Rhea:RHEA:42608, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:62192;
CATALYTIC ACTIVITY Reaction=a plastoquinone + (n+1) H(+)(in) + NADPH = a plastoquinol + n H(+)(out) + NADP(+); Xref=Rhea:RHEA:42612, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15378, ChEBI:CHEBI:17757, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62192;
else case <OC:Bacteria> and not <OC:Cyanobacteriota>
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;
else case <OC:Methanomicrobia>
CATALYTIC ACTIVITY Reaction=methanophenazine + reduced coenzyme F420-(gamma-L-Glu)(n) = dihydromethanophenazine + H(+) + oxidized coenzyme F420-(gamma-L- Glu)(n); Xref=Rhea:RHEA:54752, Rhea:RHEA-COMP:12939, Rhea:RHEA- COMP:14378, ChEBI:CHEBI:15378, ChEBI:CHEBI:29118, ChEBI:CHEBI:50375, ChEBI:CHEBI:133980, ChEBI:CHEBI:139511; EC=1.5.98.3;
end case
case <OG:Chloroplast>
SUBUNITNDH is composed of at least 16 different subunits, 5 of which are encoded in the nucleus.
else case <OC:Cyanobacteriota>
SUBUNITNDH-1 is composed of at least 11 different subunits.
else case <OC:Enterobacterales> or <OC:Shewanellaceae> or <OC:Pseudomonadaceae>
SUBUNITNDH-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>
SUBUNITNDH-1 is composed of 15 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex.
else case <OC:Methanomicrobia>
SUBUNITThe FPO complex is composed of at least 13 different subunits. FpoA, FpoH, FpoJ, FpoK, FpoL, FpoM and FpoN proteins constitute the membrane sector of the complex.
else
SUBUNITNDH-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 LOCATIONPlastid, chloroplast thylakoid membrane; Multi- pass membrane protein.
else case <OC:Cyanobacteriota> and not <OC:Gloeobacter>
SUBCELLULAR LOCATIONCellular thylakoid membrane; Multi-pass membrane protein.
else case <OC:Gloeobacter>
SUBCELLULAR LOCATIONCell inner membrane; Multi-pass membrane protein.
else case not defined <Property:Membrane> or <Property:Membrane=1> or <OC:Archaea>
SUBCELLULAR LOCATIONCell membrane; Multi-pass membrane protein.
else case <Property:Membrane=2>
SUBCELLULAR LOCATIONCell inner membrane; Multi-pass membrane protein.
end case
SIMILARITYBelongs to the complex I subunit 1 family.

Keywords [?]

Membrane
Transmembrane
Transmembrane helix
case <OG:Chloroplast> or <OC:Cyanobacteriota> and not <OC:Gloeobacter>
Thylakoid
else case <OC:Gloeobacter>
Cell membrane
Cell inner membrane
else case not defined <Property:Membrane> or <Property:Membrane=1> or <OC:Archaea>
Cell membrane
else case <Property:Membrane=2>
Cell membrane
Cell inner membrane
end case
case <OG:Chloroplast> or <OC:Cyanobacteriota>
Plastoquinone
NADP
else case not <OC:Mycobacterium> and not <OC:Rhodothermus> and not <OC:Archaea>
Ubiquinone
end case
case not <OC:Methanomicrobia>
NAD
Quinone
<a href="https://www.uniprot.org/keywords/KW-1278">Translocase</a>
end case

Gene Ontology [?]

case <OCellular component:Cyanobacteriota> or <OG:Chloroplast>
GO:0019684; Biological process:photosynthesis, light reaction
end case
case not <OCellular component:Archaea>
GO:0016655; Molecular function:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor
end case
case <OCellular component:Cyanobacteriota> and not <OC:Gloeobacter>
GO:0042651; Cellular component:thylakoid membrane
else case <OG:Chloroplast>
GO:0009535; Cellular component:chloroplast thylakoid membrane
else; https://www.ebi.ac.uk/QuickGO/term/else
GO:0005886; Cellular component:plasma membrane
end case

Cross-references [?]

PROSITE PS00667; COMPLEX1_ND1_1; 1;
PROSITE PS00668; COMPLEX1_ND1_2; 1;
Pfam PF00146; NADHdh; 1;
General Transmembrane; -; 5-9;
General Transmembrane; -; 8-9;

Features [?]


Additional information [?]

Size range 318-467 amino acids
Related rules None
Fusion Nter: None Cter: MF_01351 (nuoI)
Comments 14 proteins form the NDH-1 complex in most bacteria whereas only 11 genes are encoded in cyanobacteria and chloroplast genomes, and 12 in archea. THET8 and PARDE are annotated with an other nomenclature. See: MEDLINE=95317406; PubMed=7796904; DOI=10.1016/0014-5793(95)00548-N; Friedrich T., Steinmuller K., Weiss H.; "The proton-pumping respiratory complex I of bacteria and mitochondria and its homologue in chloroplasts."; FEBS Lett. 367:107-111(1995). See: MEDLINE=98115918; PubMed=9448329; Sazanov L.A., Burrows P.A., Nixon P.J.; "The plastid ndh genes code for an NADH-specific dehydrogenase: isolation of a complex I analogue from pea thylakoid membranes."; Proc. Natl. Acad. Sci. U.S.A. 95:1319-1324(1998). See: MEDLINE=20421945; PubMed=10940377; DOI=10.1016/S0014-5793(00)01867-6; Friedrich T., Scheide D.; "The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases."; FEBS Lett. 479:1-5(2000). In some bacteria (Enterobacteriaceae, Pseudomonadaceae and Shewanellaceae), NDH-1 is made of 13 subunits as there is a fusion of subunits C and D. See: PubMed=16023073; Melo A.M., Lobo S.A., Sousa F.L., Fernandes A.S., Pereira M.M., Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.; "A nhaD Na+/H+ antiporter and a pcd homologues are among the Rhodothermus marinus complex I genes."; Biochim. Biophys. Acta 1709:95-103(2005). In Deinococcota bacteria, NDH-I is composed of 15 subunits See: PubMed=16469879; DOI=10.1126/science.1123809; Sazanov L.A., Hinchliffe P.; "Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus."; Science 311:1430-1436(2006). In NOCFA is C-terminally fused with nuoI, another subunit of the same complex.



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