ndhM

Nicotinate dehydrogenase medium molybdopterin subunit

330 amino acids

Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.

Belongs to the xanthine dehydrogenase family.

34.476 kDa

MKKRGKGVGSMWYGIGNTGLPNPAAAFVEIHGDGSANVMFGAADIGQGSGTAMAQIAAEELGLDYEKIHVTWGDTMVTPDGGATSASRQTLITGNAVILACRQAKETLAKTAAEKLDCAPEELSFRDNTVFITADPERSMTYGELMAAMKAAGRMAVGAGSYNPNTTGLAPENMSGIPFEVYSYATTIAEVEVDTETGEVDVLKVVSAHDVGTPINRSMVEGQIEGGVTMGQGFVLMEEIEVNTKNGAIKNPSMSKYIIPSNRDVPEIHSILVESEGGPGPFGAKGVGEPALIPMIPAVVAAIEDALGTRFTHTPIMPKDIVAAVKAQEK

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

220 amino acids

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.

Belongs to the NDH complex subunit M family.

25.665 kDa

MATTASPFLSPAKLSLERRLPRATWTARRSVRFPPVRAQDQQQQVKEEEEEAAVENLPPPPQEEEQRRERKTRRQGPAQPLPVQPLAESKNMSREYGGQWLSCTTRHIRIYAAYINPETNAFDQTQMDKLTLLLDPTDEFVWTDETCQKVYDEFQDLVDHYEGAELSEYTLRLIGSDLEHFIRKLLYDGEIKYNMMSRVLNFSMGKPRIKFNSSQIPDVK

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

220 amino acids

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.

Belongs to the NDH complex subunit M family.

25.665 kDa

MATTASPFLSPAKLSLERRLPRATWTARRSVRFPPVRAQDQQQQVKEEEEEAAVENLPPPPQEEEQRRERKTRRQGPAQPLPVQPLAESKNMSREYGGQWLSCTTRHIRIYAAYINPETNAFDQTQMDKLTLLLDPTDEFVWTDETCQKVYDEFQDLVDHYEGAELSEYTLRLIGSDLEHFIRKLLYDGEIKYNMMSRVLNFSMGKPRIKFNSSQIPDVK

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

217 amino acids

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.

Belongs to the NDH complex subunit M family.

24.795 kDa

MVAAFSYTACTKLSLLHPSMVAQIRPRTTQKAFVVTNPEQDSTLEVQETETLKEEQSTEKMKKQPTPLRPVEKQLNVKSKGMGDFGGQWLSSVTRHVRIYAAYIDPETCEFDQSQMDKLTLILDPTEEFVWDDESCNKVYSYFQELVDHYEGAPLTEYTLRLIGSDVEHYIRKMLFDGEIQYNMDARVLNFSMGKPRVQFNTSNIEGGGDGQPQEDA

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

208 amino acids

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.

Belongs to the NDH complex subunit M family.

24.167 kDa

MAATSSYTACTKFSMLGWIGGKRELRKRRAFFISAQQQAEVEESQQVNAQEEEQEKMKQQGKQKLPRPVEPQVNVKSKNMSREYGGQWLSSVTRHVRIYAAYIDPVTCEFDQTQMDKLTLILDPTNEFVWTSETCNKVYAYFQELVDHYEGAPLTEYTLRLIGSDIEHYIRKLLYDGEIKYNMNARVLNFSMGKPRILFNDGLPQNVQ

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

204 amino acids

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.

Belongs to the NDH complex subunit M family.

23.13 kDa

MASTSMSLTRACKVHAVLACSIPSVSSAFLTTNVTFLGQPVEMPSQRWSQRRCSRPGPVTVRAEEVKEVTQAKGLSRESGGQWLSCTTRHVRIYAGYVDPETQVMDQSQLDKLTLMLDPDNEFEWPEEMVEKVYDKYRELVETYAGADLTEYTLRLIGSDLEHYIRKLLLAGELKYNLDCRVLNFSMGKPRIDPADLDDVEVEE

ndhM

NAD(P)H-quinone oxidoreductase subunit M, chloroplastic

203 amino acids

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.

Belongs to the NDH complex subunit M family.

23.538 kDa

MAASSSYMACAKFSMLGWLGGRRELKMRRVISVSPQEQAEVQESQEVNAQEEEKVKQPVQPRPVEPQVNVKSKNMGREYGGQWLSSVTRHVRIYAAYIDPETCEFDQTQTDKLTLILDPTDEFVWTDETCYKVYSYFQELVDHYEGAPLTEYTLRLIGSDIEHYIRKLLYDGEIKYNMNARVLNFSMGKPRILFNNDGQLQDV

ndhM

NAD(P)H-quinone oxidoreductase subunit M

121 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.762 kDa

MDNPMLLKSTTRHVRIFAGEIDRDGDLVPSQQVLTLDIDPDNEFNWNEDALQKVYRKFDELVEASSGADLTDYNLRRVGSDLEHYLRSLLQLGEISYNLSARVTNYSMGVPQVAIDDKQVS

ndhM

NAD(P)H-quinone oxidoreductase subunit M

121 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.994 kDa

MLKCTTRHVHIFAGEVTADNHFVPRDDLLTLDVDPDNELVWNDAALQKVYARFEELVEEYRGRDLTEYNLRRIGSDLEHFIRSLLKQGEIAYNLQGRTPNYSMGFPQIPAEEIVGQYIPKG

ndhM

NAD(P)H-quinone oxidoreductase subunit M

121 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.946 kDa

MLKCTTRHVHIFAGEVTADNNFVPRDDLFTLDVDPDNELVWTDAALQKVYARFEELVEEYRGRDLTEYNIRRIGSDLEHFIRSLLKQGEIAYNLQGRAPNFSMGFPQIPAEEIVGQYIPKG

ndhM

NAD(P)H-quinone oxidoreductase subunit M

121 amino acids

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).

Belongs to the complex I NdhM subunit family.

14.078 kDa

MLVKSTTRHVRIFSAEVQGNELIPSNNVLTMDVDPDNEFVWNEDALQQVYRRFDELVESYSGEDLTDYNLRRIGSDLEHFIRDLLQAGKVSYNLDCRVLNYSMGLPKVENQETAGKYWLDN

ndhM

NAD(P)H-quinone oxidoreductase subunit M

119 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.759 kDa

MFVKSTTRHIRIYAAEVHNSELVESDNMLTLDVDPDNEFNWDEDALQKVYRKFDELVEAASGEELSDYNLRRIGSDLEHFVRNLLQNGEISYNLKSRVLNYSMGLPKVESPETEGAYNL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

119 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.984 kDa

MLLKSTTRHIRIYTAEIQNNELVESDNVLTLDVDPDNEFLWDEDSLQKVYRKFDDLVESYSGEDLTEYNLRRIGSDLELFIRSLLQQGEISYNLDSRVLNYSMGLPRVESPETEGKYRL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

119 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.555 kDa

MLKSTTRHVHIFAADIRNDNFIASDTKLTLDVDPDNEFIWNDPALQKVYSEFDRLVAAYTGLALTEYNLRRIGSDLENFIRGLLQQGEIAYNLDSRVLNFSMGRPQVRGPGQIENRPGQ

ndhM

NAD(P)H-quinone oxidoreductase subunit M

119 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.839 kDa

MLLKSTTRHVRIYTAEIQKNELIPSETVLTLDVDPDNEFVWPEESLQKVYRQFDALVESNSGEDLTEYNLRRIGSDLEAFIRDLLQKGELRYNLDSRVMNFSMGLPQMDHPDSQGAYLQ

ndhM

NAD(P)H-quinone oxidoreductase subunit M

118 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.473 kDa

MENATLLKSTTRHIRIFAAEIDRDGELVPSNQVLTLDIDPDNEFNWNEDALQKIYRKFDELVEASSGADLTDYNLRRIGSDLEHYLRSLLQKGEISYNLSARVTNYSLGLPQVAVEDK

ndhM

NAD(P)H-quinone oxidoreductase subunit M

118 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.748 kDa

MLLKSTTRHIRLYTAEIKNSELVPSDNVLTLDVDPDNEFNWGEDSLQKVYRKFDELVESYSGQDLTDYNLRRIGSDLEHFIRSLLQKGDISYNLQSRVLNYSMGLPKVESPETEGKYR

ndhM

NAD(P)H-quinone oxidoreductase subunit M

118 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.473 kDa

MENATLLKSTTRHIRIFAAEIDRDGELVPSNQVLTLDIDPDNEFNWNEDALQKIYRKFDELVEASSGADLTDYNLRRIGSDLEHYLRSLLQKGEISYNLSARVTNYSLGLPQVAVEDK

ndhM

NAD(P)H-quinone oxidoreductase subunit M

116 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.057 kDa

MSDTPLKCTTRHVRIFTATVEDNGELKASSDKLTLDLDPDNEFEWDQPVLAKVQQRFAELVDAAAGTELSDYNLRRIGTDLEGFIRQLLQAGELRYNLGARVLNYSMGLPRTPETL

ndhM

NAD(P)H-quinone oxidoreductase subunit M, organellar chromatophore

115 amino acids

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).

Belongs to the complex I NdhM subunit family.

13.093 kDa

MANTILKSTTRHIRIFTARVENNDLIADTSQLTLDIDPDNEFLWEQSTIEKIQSRFKELVECHTGADLTDYTLRRIGTELEGTLFSLLQAGELSYNPNARVLNYSMGLPRTTELS

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.42 kDa

MEKMLLKSTTRHVRIFTAEVVDEELKFHPNKLTLDLDPDNEFIWNEDSLNKINEKFNGLIKERAGKDLDDYELRKIGSEIEGLIKFLLQNGQLSYNPDCRVMNYSMGLPMTNEVL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.382 kDa

MSDTILKCTTRHVRIFTAVVENNDLILDNGHLTLDIDPDNEFSWSDQSIKKVQDYFRELVELQADNELSDYTLRKIGSLLEDFIRKLLKDGELSYNPNSRVMNYSMGLPRTQELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.531 kDa

MEKMLLKSTTRHVRIFTAEVVDKELQFHPNKLTLDLDPDNEFIWNEDSLKKINQKFKELINERAGRDLDDYELRKIGSEVEGLIKFLLQNGELSYNPDCRVMNYSMGLPKTNELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.115 kDa

MNETLLKCTTRHVRIFTARVENNDLVPDPDQLTLDLDPDNEFLWTESVIKEIQQRFAELVASHAGGELSDYNLRKIGSELEGTIRKLLQAGKLSYNPECRVLNYSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.303 kDa

MTDSILKCTTRHIRIFTARCENNDLVQDSEHLTLDLDPDNEFIWEELVIGKVHKRFSELVDSYSGKDLSDYNLRKIGSDLEGTIRQLLQAGELKYNPDCRVLNYSMGLPRTKDLL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.48 kDa

MEKMLLKSTTRHVRIFTAEVVNNDLKYHPNKLTLDLDPDNEFIWNEESLKKVNQKFTELVEERAGKSLDDYELRKIGSEVEGLIKYLLQNSLLSYNPECRVMNYSMGLPKTKEVL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.44 kDa

MEKMLLKSTTRHVRIFTAEVVDNELQFHPNKLTLDLDPDNEFIWNEDSLNEINKKFNELIKERAGKDLDDYELRKIGSEIEGLIKILLQNGQLSYNPDCRVMNYSMGLPKTNEVL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.318 kDa

MTDPLLKCTTRHIRIFTAITQNNNLIEDSDHLTMDLDPDNEFLWENQAIEKVQNRFSELVESQVGQELSDYVLRKIGSDLESYIRQMLQAGEVSYNPDSRVLNYSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.13 kDa

MNETLLKCTTRHVRIFTARVENNDLVPDPNQLTLDLDPDNEFLWTESVTKEIQQRFAELVASHAGGELSDYNLRRIGSELEGTIRKLLQAGKLSYNPECRVLNYSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.431 kDa

MEKMLLKSTTRHVRIFTADVINNDLVFHPNKLTLDLDPDNEFIWNEDSLKKVNQRFTELVQERAGKSLDDYELRKIGSEIEGLIKYLLQNGLLSYNPECRVMNYSMGLPKTKEVL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.489 kDa

MEKMLLKSTTRHVRIFTAEVVDEELKFHPNKLTLDLDPDNEFIWNEDSLNKINEKFNELIKERAGKDLDDYELRKIGSEIEGLIKFLLQNGQLSYNPDCRVMNYSMGLPKTNEVL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.421 kDa

MSNTILKCTTRHVRIFTAVVENNDLIFDNGHLTLDIDPDNEFSWSDQSIKKVQDYFRELVDFQADNELSDYSLRKIGSLLEDFIRKLLKDGELSYNPNSRVMNYSMGLPRTQELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.13 kDa

MAETLLKSTTRHIRLFTARVENGDLVPDPEQLTLDLDPDNEFLWTEGTVTTIQTRFRDLVESYAGQPLNDYNLRRIGTELEGSIRELLQAGSLTYNPDCRVMNYSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

12.897 kDa

MADTLLKCTTRHVRLFTARVDNQDLVPSADELTLDLDPDNEFLWSDAVVSKVQQRFQQLVEAGAGGELSDYSLRRIGTDLEGYIRQLLQAGELSYNPDGRVQNFSMGLPRTPDLL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.179 kDa

MADTLLKSTTRHVRLFTARVNEGRLVPDPNQLTLDLDPDNEFLWNDSCIQTVQQRFRELVEAHAGQPLNDYNLRRIGSELEGSIRQLLQAGQLSYNPDCRVLNYSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.057 kDa

MADTLLKCTTRHVRLFTARVDNDDLVPSANELTLDLDPDNEFIWSESCISQVQQRFKQLVDAAAGGELSDYTLRRIGTDLEGFIRQLLQRGELSYNPEARVQNFSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

12.81 kDa

MADTLLKCTTRHVRLFTAALQEEDLVPSDDQLTLDLDPDNEFLWDAASLAKVQGRFKELVDAAAGGELSDYTLRRIGTDLEGFIRQLLQAGELSYNPDGRVQNFSMGLPRTPELL

ndhM

NAD(P)H-quinone oxidoreductase subunit M

115 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.056 kDa

MLLKSTTRHIRIFAGTVENNELVPDDQALTLDIDPDNELNWNDTAVEQVYRKFDELVESYSGSDLTEYNLRCMGSDLEHFVRSLLQSGEISYNLGSRVNNYSLGLPRVDVDAEAK

ndhM

NAD(P)H-quinone oxidoreductase subunit M

114 amino acids

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.

Belongs to the complex I NdhM subunit family.

13.048 kDa

MLLKSTTRHIHIYTAEVENNELIPSESVLTLDVDPDNELVWSEDALQRVYAKFDELVETYSGEDLTDYNLRRIGSDLEHYVRSLLQKGIVGYNLSSRVRNFSMGLPQVIASESK

ndhM

NAD(P)H-quinone oxidoreductase subunit M

111 amino acids

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).

Belongs to the complex I NdhM subunit family.

12.567 kDa

MLLKSTTRHVHIYAGHVVDGEVHPDTETLTLNVDPDNELEWNEAALAKVEAKFRELVANAAGEDLTEYNLRRIGSDLEHFIRSLLMQGEIGYNLNSRVRNYSLGIPRVNHS

ndhM

NAD(P)H-quinone oxidoreductase subunit M

110 amino acids

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.

Belongs to the complex I NdhM subunit family.

12.697 kDa

MLLKSTTRHIRIFTAEIEGNELQPSDTVLTLDVDPDNEFNWNEEALQKVYRQFDDLVESYAGQELSEYNLRRIGSELEVLLRQMLQAGEISYNLNCRVLNYSMGVPQAVV

ndhM

NAD(P)H-quinone oxidoreductase subunit M

110 amino acids

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.

Belongs to the complex I NdhM subunit family.

12.697 kDa

MLLKSTTRHIRIFTAEIEGNELQPSDTVLTLDVDPDNEFNWNEEALQKVYRQFDDLVESYAGQELSEYNLRRIGSELEVLLRQMLQAGEISYNLNCRVLNYSMGVPQAVV

ndhM

NAD(P)H-quinone oxidoreductase subunit M

109 amino acids

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.

Belongs to the complex I NdhM subunit family.

12.697 kDa

MLLKSTTRHIRIYTAEVKNNQLIESNNVLTLDVDPDNEFNWEEVALNKVYSKFDELVESYNGEELSEYNLRRIGSDLEHFIRSLLQKGEISYNLNARVQNYSMGLPKLG