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atpH atpH atpF atpF atpE atpE atpB-2 atpB-2 ndh ndh ndhC ndhC ndhH ndhH ndhJ ndhJ ndhK ndhK ndhA ndhA ndhI ndhI ndhG ndhG ndhE ndhE ndhF ndhF ndhD ndhD ndhB ndhB ppa ppa ppk-1 ppk-1 atpB-1 atpB-1 atpC-1 atpC-1 atpD-1 atpD-1 ppk-2 ppk-2 cydA cydA cydB cydB atpG atpG atpA atpA CT2040 CT2040 CT2041 CT2041 CT2042 CT2042 atpD-2 atpD-2 atpC-2 atpC-2 sdhB sdhB sdhA sdhA CT2268 CT2268
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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atpHATP synthase F1, delta subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Belongs to the ATPase delta chain family. (181 aa)
atpFATP synthase F0, B subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (175 aa)
atpEATP synthase F0, C subunit; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. (73 aa)
atpB-2ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (276 aa)
ndhNADH dehydrogenase; Identified by similarity to GP:2708705; match to protein family HMM PF00070; match to protein family HMM PF07992. (430 aa)
ndhCNADH dehydrogenase I, subunit 3; NDH-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 a 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; Belongs to the complex I subunit 3 family. (143 aa)
ndhHNADH dehydrogenase I, 20 kdA subunit; NDH-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 a 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. (189 aa)
ndhJNADH dehydrogenase I, 30 kDa subunit; NDH-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 a 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; Belongs to the complex I 30 kDa subunit family. (173 aa)
ndhKNADH dehydrogenase I, 49 kDa subunit; NDH-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 a 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; Belongs to the complex I 49 kDa subunit family. (368 aa)
ndhANADH dehydrogenase I, subunit 1; NDH-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. (359 aa)
ndhINADH dehydrogenase I, 23 kDA subunit; Identified by similarity to EGAD:12904; similarity to EGAD:162929; match to protein family HMM PF00037. (216 aa)
ndhGNADH dehydrogenase I, subunit 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. (173 aa)
ndhENADH dehydrogenase I, subunit 4L; NDH-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 a 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; Belongs to the complex I subunit 4L family. (107 aa)
ndhFNADH dehydrogenase I, subunit 5; Identified by similarity to SP:P50939; match to protein family HMM PF00361; match to protein family HMM PF00662; match to protein family HMM TIGR01974. (755 aa)
ndhDNADH dehydrogenase I, subunit 4; Identified by similarity to EGAD:42981; match to protein family HMM PF00361; match to protein family HMM TIGR01972. (545 aa)
ndhBNADH dehydrogenase I, subunit 2; NDH-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 a 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; Belongs to the complex I subunit 2 family. (511 aa)
ppaSoluble inorganic pyrophosphatase; Identified by similarity to EGAD:101738; match to protein family HMM PF00719. (137 aa)
ppk-1Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP); Belongs to the polyphosphate kinase 1 (PPK1) family. (698 aa)
atpB-1ATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (221 aa)
atpC-1ATP synthase F1, epsilon subunit; Identified by similarity to GP:1929514; match to protein family HMM PF02823. (129 aa)
atpD-1ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (480 aa)
ppk-2Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP); Belongs to the polyphosphate kinase 1 (PPK1) family. (714 aa)
cydACytochrome d ubiquinol oxidase, subunit I; Identified by similarity to EGAD:15777; match to protein family HMM PF01654; Belongs to the cytochrome ubiquinol oxidase subunit 1 family. (451 aa)
cydBCytochrome d ubiquinol oxidase, subunit II; Identified by similarity to EGAD:15418; match to protein family HMM PF02322; match to protein family HMM TIGR00203. (340 aa)
atpGATP synthase F1, gamma subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. (292 aa)
atpAATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (526 aa)
CT2040Succinate/fumarate oxidoreductase, putative; Identified by similarity to GP:3378542; match to protein family HMM PF02754. (283 aa)
CT2041Succinate/fumarate oxidoreductase, iron-sulfur protein, putative; Identified by match to protein family HMM PF00111; match to protein family HMM TIGR00384. (345 aa)
CT2042Succinate/fumarate oxidoreductase, flavoprotein subunit; Identified by match to protein family HMM PF00890; match to protein family HMM PF02910; match to protein family HMM PF07992; match to protein family HMM TIGR01812. (567 aa)
atpD-2ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (462 aa)
atpC-2ATP synthase F1, epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (88 aa)
sdhBSuccinate dehydrogenase, iron-sulfur protein; Identified by match to protein family HMM PF00037. (257 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Identified by similarity to EGAD:21386; match to protein family HMM PF00890; match to protein family HMM PF02910; match to protein family HMM PF07992; match to protein family HMM TIGR01811. (646 aa)
CT2268Succinate dehydrogenase, cytochrome subunit, putative; Identified by similarity to GP:6580638; match to protein family HMM TIGR02046. (240 aa)
Your Current Organism:
Chlorobaculum tepidum
NCBI taxonomy Id: 194439
Other names: C. tepidum TLS, Chlorobaculum tepidum TLS, Chlorobium tepidum TLS
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