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ndhN

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N, chloroplastic
Organism
Arabidopsis thaliana
Length
209 amino acids
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.
Similarity
Belongs to the NDH complex subunit N family.
Mass
23.398 kDa
Sequence
MGSRAICIQRVAPPCFEASQVKKIKTVGSFLVNTRSKRRRSTGVKCSSIADYIGGDLVKPDIGQWLQDVEEHKAIAIYAPHEGGYEGRYLNRLKMQGYYFLDISARGLGDPETTLLKNYPVCPAHLGKQPIARWYYPPEVDYRLAALPPSAKGLVVWVLEAKVLSKSELQFLALLPSLRPNVRVIAECGNWRKFVWKPLAEIANLAAQE

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
162 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.637 kDa
Sequence
MALITTGNGLIRDLEKFGSVGVYVPLEGGFEGRYRRRLRAAGYTTLQFTARGLGDVAAYLTGVHGVRPPHLGKKSSGNGAAVGNVYYLPPIVGSQLEHLPPKSKGLVLWIIEGHILSDQEVEFLTSLPSLEPRVKVVVERGGDRTFRWKALKDTFSASYQAV

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
162 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.706 kDa
Sequence
MALITTGNGLIRDLEKFGSVGVYVPLEGGFEGRYRRRLRAAGYTTLQFTARGLGDVAAYLTGVHGVRPPHLGKKSSGNGAAVGNVYYLPPIVGSQLEHLPPKSKGLVLWIIEGHILSDQEVEFLTDLPKLEPRVKVVVERGGDRTFRWKALKDTFSASYQAV

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
161 amino acids
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).
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.63 kDa
Sequence
MLPLPLIANGKGFIRALENDGALAVYAPLEGGYEGRYQRRLRANGYASISLSARGLGDVEAYLMQVHGVRPAHLGKKNIAQEGAVGPIYFAQPIAGYQLENLPAQSKGLVLWILEGYILSQTEIQDLISLTKRVPKLKVVLEMGGDRVFRWQPLLDCLQAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
159 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.562 kDa
Sequence
MPLLNLVLDNGSRFVADVEKHSSIALWAPPEGGIEGNYQRRLRGIGYRTQIITAKGLGDISRFLLESHGVRPAHLGKKDKRVFTLPPELAIYMDTLPASAKGFVLWIIEGKVLSLFELESLVGLPAAVPKLKVIVEVGSDYNIRWMPLEQAVSKMAEGR

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.145 kDa
Sequence
MALITTGSKFLRALEQEGALAVYAPLEGGYEGRYLRRLRSKGYSALTYSARGLGDPAQFLMDIHGVRPPHLGKQTIGNEAAVGRVEYVLPLVGYPLQNLPANAKGLVLWLLEGHVLSPQELSYFVTLPQAEPRLKVVIEMGGDRGFSWQPLAAVAEAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Trichodesmium erythraeum (strain IMS101)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.452 kDa
Sequence
MALITTGRGMIRDLEKSGSLAVYPPLEGGFEGRYQRRLRASGYVSESITARGLGDLAMYLTGVHGVRPPHLGKKTVGNGPAVGYVYYVPPIVNYKLEHLPPKAKGLVLWIMEGQILSSQEIEYLTVLPKSEPRVKVIVEMGGDRFFRWTPLQNTLVPA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Microcystis aeruginosa (strain NIES-843)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.699 kDa
Sequence
MALLTTGKPFIRDLEQYGALGVYAPLEGGYEGRYQRRLRATGYNVLHITARGLGDLSAYLTGIHGVRPPHLGKKNIGREAAVGPVYFIPPIATYQLENLPPKSKGLVIWIIESFVLSSEEKQYLINLSQQEPRLKFVLELGGERYFRWQPLSKSLIAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.372 kDa
Sequence
MALITTGNGLIRDLEKFGALGVYVPLEGGYEGRYQRRLRAAGYTTLHITAKGLGDVAAYLTRIHGVRPPHLGKKSTGSGAAVGQVYYLPPILDSHLEQLPPKSKGLVLWIIEGHILSNEELEYLTNLPQLEPRVKVVIERGGDRAFRWTSLEKTLLAS

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N, organellar chromatophore
Organism
Paulinella chromatophora
Length
158 amino acids
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).
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.483 kDa
Sequence
MPLLLTGQEFRRDLERDGALALFVPLEGGAETRLMRRLRAVGYKAYLTSAKGLGDPEAYLLKLHEQHVPHLGRRMSTEGKPEGKSVGHVPKVMPMLGPLLEGKSPILLWLLEGQVLSSSELSAISNLPKREPRLKIVVEMGGARALRWESLGKLVESR

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9301)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.817 kDa
Sequence
MPLLLTGKKFHNDLKTNKCLAIFAPLEGGYETRLLRRMRAKGFKTFITSARGLGDPEVFLLKLHGVRPPHLGHQSVGRNGALGEVQQVIPQASELFNENDKNKLLWLLEGQVLSQSELESLIEICTKDNKLTIVVEMGGSRKLEWKSLSNYILDEFEN

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9215)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.786 kDa
Sequence
MPLLLTGKKFHNDLKTNKCLAIFAPLEGGYETRLLRRMRAKGFKTFITSARGLGDPEVFLLKLHGVRPPHLGHQSVGRNGALGEVQQVIPQASELFNENDKNKLLWLLEGQVLSQSELESLIEICTNDNKLTIVVEMGGSRKLEWKPLSNYILDEFES

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9312)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.772 kDa
Sequence
MPLLLTGKQFHNDLKTNKCLAIFAPLEGGYETRLLRRMRAKGFKTFITSARGLGDPEVFLLKLHGVRPPHLGHQSVGRNGALGEVQQVIPQASELFNENDKNKLLWLLEGQVLSQSELESLIEICTNDNKLSIVVEMGGSRKLEWKPLSNYILDEFES

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain AS9601)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.772 kDa
Sequence
MPLLLSGKKFHNDLKTNKCLAIFAPLEGGYETRLLRRMRAKGFKTFITSARGLGDPEVFLLKLHGVRPPHLGHQSVGRNGALGEVQQVIPQASELFNENDKNKLLWLLEGQVLSQSELESLIEICTNDNKLTIVVEMGGSRKLEWKPLSNYILDEFES

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus elongatus (strain PCC 7942)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.145 kDa
Sequence
MALITTGSKFLRALEQEGALAVYAPLEGGYEGRYLRRLRSKGYSALTYSARGLGDPAQFLMDIHGVRPPHLGKQTIGNEAAVGRVEYVLPLVGYPLQNLPANAKGLVLWLLEGHVLSPQELSYFVTLPQAEPRLKVVIEMGGDRGFSWQPLAAVAEAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Cyanothece sp. (strain ATCC 51142)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.242 kDa
Sequence
MALLTTGKGFVRALEKSGALGVYAPLEGGFEGRYQRRLRTNGYDSLSLTARGLGDVSAYLMGVHGVRPPHLGKKNIGQGAAVGPIYFVPPIAAYQLESLSPQSKGLVLWILEGYILSKAELEYLVSLPQQEPRIKVVVELGGERYFRWEPLENLIAVA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.582 kDa
Sequence
MALFTTGRQFIQDLEKSGALGIYVPSEGGFEGRYQRRLRAAGYSTLHISAPGLGDLPSYLTQVHGVRPPHLGKSTQGNTDWGVKTFFLPPLVNYHLENLPPKARGLVLWMIDGKRLSRQELAYLSILPAQEPKVKIVIELGGDRQFRWQPLKEMAAAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Cyanothece sp. (strain PCC 7424)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.617 kDa
Sequence
MPLLTTGKSFIRALEKSGALGVYVPLEGGFEGRYQRRLRANGYTPYNLTARGLGDLSSYLTGIHGVRPPHLGKKNIGQDAAVGPVYFVPPIATYQLETLPPKSKGLVLWIIEGMILSRAEIEYLTYLPQQEPRLKIVVEMGGERYFRWQPLEQSIQAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Cyanothece sp. (strain PCC 8801)
Length
158 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.392 kDa
Sequence
MALLTNGKGFIRALEKSGSLAVYAPLEGGFEGRYQRRLRTNGYHTFSLTARGLGDVSAYLMGVHGVRPPHLGKKNIGQEAAVGPVYFVPPIAAYQLETLPPKSKGLVLWILEGFILSQTELEYLANLPTLEPRLKVVIELGGERYFSWKPLPEVIKVA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Length
157 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.191 kDa
Sequence
MALLTTGKSFIRTVEKSGAVAVYAPLEGGFEGRYVRRLRCSGYSVVNLTARGLGDVAAYLTQYHGIRPPHLGKKDIAGSGAAVGLRYYVPGIASYQLENLPQKSKGIILWIIEGFVLSRQEQEYLVSLTQDNPQIKVVVEMGGDRQFSFKPLADLLV

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain CC9902)
Length
157 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.101 kDa
Sequence
MHAPMPLLLTGRGFRRDLEANGCLAVHAPLEGGAETRLLRRLRGAGYRTRMTSARGLGDPEVFLTQKHGIRPPHLGHNCVGRGAAVGEVQQVVPLIGDLLDGDDSVALWILEGQVLSRSELLSLCDLCKREPRLRIIVEMGGARSLRWQPMKALLGA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9515)
Length
156 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.639 kDa
Sequence
MPLLLSGKKFHNDLKKNKCLAMFAPLEGGYETRLLRRMRAKGFKTYITSARGLGDPEVFLLNLHGIRPPHLGHQSIGRNGALGEVQQVIPQASELFNENDKDKLLWLLEGQVLSQSELENLIKLPTADNKLKIVVEMGGSRKLEWKSLNDYVLNEF

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
156 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.662 kDa
Sequence
MPLLLTGKKFHNDLNKNKCLAMFAPLEGGYETRLLRRMRAKGFKTYITSARGLGDPEVFLLKLHGIRPPHLGHQSIGRNGALGEVQQVIPQASELFNENDKDKLLWLLEGQVLSQSELESLIKICTSDNKLKIVVEMGGSRKLEWKSLNDYILNEF

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain NATL1A)
Length
154 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.052 kDa
Sequence
MPLLLSGQKFRTDLESFGCLAILSPLEGGAETRLLRRLRASGYQTQITSARGLGDPVVFLTQLHGIRPPHLGHQNVGRNGALGEVQQVIPQLNELLVEDKPLVLWLLEGQVLSKSELLAISNLCQKEPRIKIVIEMGGARSIKWQPLNEFINKD

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain NATL2A)
Length
154 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.065 kDa
Sequence
MPLLLSGQKFRTDLESFGCLAILSPLEGGAETRLLRRLRASGYQTQVTSARGLGDPVVFLTQLHGIRPPHLGHQNVGRNGALGEVQQVIPQLNELLVEDKPLVLWLLEGQVLSKSELLAINNLCQKEPRIKIVIEMGGARSIKWQPLNEFINKD

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain WH7803)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.804 kDa
Sequence
MPLLLSGRGFRRELESAGCMAVHAPLEGGAETRLLRRLRAAGYRTHLTSARGLGDPEVFLFQKHGVRPPHLGHQSVGRGAAVGEVHDVMPLLGEVFLGDKPVVLWLLEGQVLSRSELLSLCDLCRREPRLKIVVEMGGARSLRWQPMTQLLAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain WH8102)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.758 kDa
Sequence
MPLLLTGRTFRRDLEAHGCLAVHAPLEGGAETRLLRRLRGAGYRTRLWSARGLGDPEVFLTQKHGIRPPHLGHQSVGRGAAVGEVQEVVPQLGDLLDGDAQVALWLLEGQVLSQSELRSLCDLCSREPRLRIIVEMGGARSLRWQPMSGLLAS

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain RCC307)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.551 kDa
Sequence
MPLLLTGRAFRRDLERERALAVYAPLEGGAETRLLRRLRAAGYRTELTSARGLGDPEAFLLGLHGVRPPHLGHHCVGRDAAVGEVQLVMPQLGPALASGAPVVLWMLEGQVLSSAEQASLLALCEREPRLHMVLELGGSRSLRWKPLRAALAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain CC9311)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.767 kDa
Sequence
MPLLLSGRGFRRELESAGCMAVFAPLEGGAETRLLRRLRGAGYRTQLSSARGLGDPEVFLFQKHGIRPPHLGHQSVGRGAAVGEVQEVMPLLGESMLGTKPVVLWLLEGQVLSRSELSALCDLCRREPRLKVVVEMGGARSLRWQPLKELLSN

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain CC9605)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.699 kDa
Sequence
MPLLLTGQAFRRDLEANGCLAVQAPLEGGAETRLLRRLRGAGYSTRMTSARGLGDPEVFLTQKHGIRPPHLGHQSVGRGAAVGEVQEVAPQLGDLFESDAPVALWLLEGQVLSRSELLSLCDLCKREPRLRIIVEMGGARSLKWEPMTTYLKA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9303)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.863 kDa
Sequence
MPLLLSGRVFRRDLDACGCLAMHVPLEGGSETRLLRRLRAAGYRTQLSSARGLGDPEVFLFQLHGIRPPHLGHQSVGRNGAVGEVQQVMPQLAELFVDNVPVVLWLLEGQVLSRSELLALCDLCKRESRLRVVVEMGGARSLNWQPMSTLLGV

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9211)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
17.188 kDa
Sequence
MPLLLSGKEFRDDLESACCLAIQTPLEGGAETRLLRRLKAAGYRTQITSVRGFGDPEVFLLKLHGIRPPHLGHQNIGRNGALGEVQEVIPQLHELLSEEQPLALWLLEGQVLSRSELLALCDLSEKDPQLKIVVEMGGERKLKWQSMRKFLEQ

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
153 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.852 kDa
Sequence
MPLLLSGRVFRRDLDACGCLAMHVPLEGGSETRLLRRLRAAGYRTQLSSARGLGDPEVFLFELHGIRPPHLGHQSVGRNGAVGEVQQVMPQLAELFVDNAPVVLWLLEGQVLSRSELLALCDLCKRESRLRVVVEMGGARSLNWQPMSTLLGD

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
152 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.766 kDa
Sequence
MPLLLSGRKFRHDLEASGCLAINVPLEGGAETRLLRRLKAAGYKTQITSVRGLGDPEAFLLKLHGIRPPHLGHQNVGRNGALGEVQQVIPQVNELLAGEKSVVLWLLEGQVLSRSEILSLCDLCDKEPRLKIVIEMGGARALRWQSMRSFIQ

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Acaryochloris marina (strain MBIC 11017)
Length
151 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.656 kDa
Sequence
MPLLATGKKFIRTIEQSGAVGIYVPSEGGFEGRYKRRLRATGYLTLFVSAPGMGDLASYFTDVHGVRPPHLGKNQIRTYFLPPFVTYQLENLPPQAKGLALWLYDGKRLAKQELAYLSAITASEPRLKVVVELGGARSFEWQPLSDIVAAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
150 amino acids
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).
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.636 kDa
Sequence
MGLLAGYQFVKDLESAGALALFVPPEGGFEGRYQRRLRSKGYTTLPMSAPGLGDLAAYLTQEHGIRPAHTGKEDIRVYFQPPLVTYHLENLPPNAKGLVLWLIDGKRLSKQEFAYLAQLTQTLPKFKVVVEVGGDRVVRWEPLADWVAAA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain JA-3-3Ab)
Length
147 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.396 kDa
Sequence
MLLVGSGAKFVQQLEQCGALAIFVTPEGGSEGHYLRRLRGAGYEVVTLSSKGIGDLASYLTSSHGVRPATLGKSQRRTYFYPSLIEQYRATLPPKAKGLVFWFYEGHVLSRQELSYLVKLSQEDKGVKFVVELGRERSIRWQPLQSA

Gene
ndhN
Protein
NAD(P)H-quinone oxidoreductase subunit N
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13))
Length
147 amino acids
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.
Similarity
Belongs to the complex I NdhN subunit family.
Mass
16.478 kDa
Sequence
MLLVGSGAKFVQQLEQAGALAIYVTPEGGSEGHYLRRLRGAGYEVVTLSSKGIGDLASYLTRIHGVRPATLGKSERRTYFFPALIEQYRATLPPKAKGLVFWFYEGHVFSQQELSYLVKLSREDKGVKFVVELGRERSIRWQPLQSA