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0  structures 89  species 0  interactions 98  sequences 1  architecture

Family: NdhN (PF11909)

Summary: NADH-quinone oxidoreductase cyanobacterial subunit N

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NADH-quinone oxidoreductase cyanobacterial subunit N Provide feedback

The proton-pumping NADH:ubiquinone oxidoreductase catalyzes the electron transfer from NADH to ubiquinone linked with proton translocation across the membrane. It is the largest, most complex and least understood of the respiratory chain enzymes and is referred to as Complex I. The subunit composition of the enzyme varies between groups of organisms. Complex I originating from mammalian mitochondria contains 45 different proteins, whereas in bacteria, the corresponding complex NDH-1 consists of 14 different polypeptides. Homologues of these 14 proteins are found among subunits of the mitochondrial complex I, and therefore bacterial NDH-1 might be considered a model proton-pumping NADH dehydrogenase with a minimal set of subunits. Escherichia coli NDH-1 readily disintegrates into 3 subcomplexes: a water-soluble NADH dehydrogenase fragment (NuoE, -F, and -G),the connecting fragment (NuoB, -C, -D, and -I), and the membrane fragment (NuoA, -H, -J, -K, -L, -M, -N). In cyanobacteria and their descendants, the chloroplasts of green plants, the subunit composition of NDH-1 remains obscure. The genes for eleven subunits NdhA-NdhK, homologous to the NuoA-NuoD and NuoH-NuoN of the E. coli complex, have been found in the genome of Synechocystis sp. PCC 6803 which has a family of 6 ndhD genes and a family of 3 ndhF genes. Two reported multisubunit complexes, NDH-1L and NDH-1M, represent distinct NDH-1 complexes in the thylakoid membrane of Synechocystis 6803 -cyanobacterium. NDH-1L was shown to be essential for photoheterotrophic cell growth, whereas expression of NDH-1M was a prerequisite for CO2 uptake and played an important role in growth of cells at low CO2. Here we report the subunit composition of these two complexes. Fifteen proteins were discovered in NDH-1L including NdhL, a new component of the membrane fragment, and Ssl1690 (designated as NdhO), a novel peripheral subunit [1]. The cyanobacterial NDH-1 complex contains additional subunits, NdhM and NdhN, compared with the minimal set of the bacterial enzyme and these seem to be specific for thylakoid-located NDH-1 of photosynthetic organisms [2].

Literature references

  1. Mathiesen C, Hagerhall C;, Biochim Biophys Acta. 2002;1556:121-132.: Transmembrane topology of the NuoL, M and N subunits of NADH:quinone oxidoreductase and their homologues among membrane-bound hydrogenases and bona fide antiporters. PUBMED:12460669 EPMC:12460669

  2. Battchikova N, Zhang P, Rudd S, Ogawa T, Aro EM; , J Biol Chem. 2005;280:2587-2595.: Identification of NdhL and Ssl1690 (NdhO) in NDH-1L and NDH-1M complexes of Synechocystis sp. PCC 6803. PUBMED:15548534 EPMC:15548534


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR020874

NAD(P)H-quinone oxidoreductase (NDH-1) shuttles electrons from an unknown electron donor, via FMN and iron-sulphur (Fe-S) centres, 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. It 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. NDH-1 can be composed of about 15 different subunits, although different subcomplexes with different compositions have been identified which probably have different functions.

This entry represents subunit N.

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  Seed
(20)
Full
(98)
Representative proteomes NCBI
(90)
Meta
(139)
RP15
(8)
RP35
(29)
RP55
(40)
RP75
(45)
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  Seed
(20)
Full
(98)
Representative proteomes NCBI
(90)
Meta
(139)
RP15
(8)
RP35
(29)
RP55
(40)
RP75
(45)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

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Seed source: Lonsdale D
Previous IDs: none
Type: Family
Author: Coggill P
Number in seed: 20
Number in full: 98
Average length of the domain: 149.60 aa
Average identity of full alignment: 50 %
Average coverage of the sequence by the domain: 87.57 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 60.1 59.9
Noise cut-off 21.1 16.7
Model length: 154
Family (HMM) version: 3
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