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EKF03728.1 EKF03728.1 ndhD ndhD ndhD-2 ndhD-2 ndhC ndhC ndhK ndhK ndhJ ndhJ EKF05885.1 EKF05885.1 ndhI ndhI EKE99675.1 EKE99675.1 ndhB ndhB EKF00357.1 EKF00357.1 EKF00356.1 EKF00356.1 ndhD-3 ndhD-3 EKF00710.1 EKF00710.1 EKE97463.1 EKE97463.1 EKF05888.1 EKF05888.1
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query proteins and first shell of interactors
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second shell of interactors
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a 3D structure is known or predicted
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Your Input:
EKF03728.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R6185 0. proton-translocating NADH-quinone oxidoreductase, chain L K05577; Psort location: CytoplasmicMembrane, score: 10.00. (699 aa)
ndhDProton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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; Belongs to the complex I subunit 4 family. (524 aa)
ndhD-2Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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; Belongs to the complex I subunit 4 family. (562 aa)
ndhCNADH dehydrogenase subunit A; 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. (120 aa)
ndhKNADH dehydrogenase subunit B; 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 20 kDa subunit family. (245 aa)
ndhJNADH dehydrogenase, subunit C; 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. (174 aa)
EKF05885.1NAD(P)H-quinone oxidoreductase subunit M; KEGG: npu:Npun_F3688 1.8e-230 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
ndhINADH-plastoquinone oxidoreductase, I subunit; 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; Belongs to the complex I 23 kDa subunit family. (194 aa)
EKE99675.1NADH-ubiquinone/plastoquinone oxidoreductase chain 6; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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. Belongs to the complex I subunit 6 family. (216 aa)
ndhBProton-translocating NADH-quinone oxidoreductase, chain; 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. (520 aa)
EKF00357.1NAD(P)H-quinone oxidoreductase subunit D4; KEGG: npu:Npun_R4289 6.0e-225 proton-translocating NADH-quinone oxidoreductase, chain M K05575; Psort location: CytoplasmicMembrane, score: 10.00. (499 aa)
EKF00356.1NAD(P)H-quinone oxidoreductase subunit F; KEGG: npu:Npun_R4290 2.9e-287 NdhF3 family NAD(P)H dehydrogenase K05577; Psort location: CytoplasmicMembrane, score: 10.00. (618 aa)
ndhD-3Proton-translocating NADH-quinone oxidoreductase, chain M; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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; Belongs to the complex I subunit 4 family. (537 aa)
EKF00710.1Hypothetical protein; KEGG: ava:Ava_2796 1.5e-61 NAD(P)H-quinone oxidoreductase subunit 4 K05575. (146 aa)
EKE97463.1Protein HymB; KEGG: ava:Ava_4654 4.7e-232 respiratory-chain NADH dehydrogenase domain-containing protein K05587; Psort location: Cytoplasmic, score: 9.12. (548 aa)
EKF05888.1KEGG: ava:Ava_0749 4.7e-296 NAD(P)H-quinone oxidoreductase subunit F K05577; Psort location: CytoplasmicMembrane, score: 10.00. (619 aa)
Your Current Organism:
Tolypothrix sp. PCC7601
NCBI taxonomy Id: 1188
Other names: Calothrix sp. PCC 7601, Fremyella diplosiphon ACMM 396, Fremyella diplosiphon IAM M-100, Fremyella diplosiphon UTEX B 481, Microchaete diplosiphon UTEX B 481, T. sp. PCC 7601, Tolypothrix (Calothrix) sp. PCC 7601, Tolypothrix sp. PCC 7601, Tolypothrix sp. PCC 7601 = UTEX B 481
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