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ppa ppa ppk ppk HEAR1115 HEAR1115 coxN coxN HEAR1117 HEAR1117 coxP coxP HEAR1119 HEAR1119 cydA cydA cydB cydB HEAR1376 HEAR1376 ccoP ccoP HEAR1642 HEAR1642 fixO fixO fixN fixN sdhB sdhB sdhA sdhA sdhD sdhD sdhC sdhC nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA HEAR2035 HEAR2035 ndh ndh cyoD cyoD cyoC cyoC cyoB cyoB cyoA cyoA ctaB ctaB HEAR2911 HEAR2911 HEAR2915 HEAR2915 HEAR2916 HEAR2916 ctaD ctaD ctaC ctaC petC petC petB petB petA petA HEAR3246 HEAR3246 HEAR3327 HEAR3327 HEAR3328 HEAR3328 HEAR3329 HEAR3329 HEAR3333 HEAR3333 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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ppaInorganic pyrophosphatase (Pyrophosphate phospho-hydrolase) (PPase); Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (179 aa)
ppkPolyphosphate kinase (Polyphosphoric acid kinase) (ATP-polyphosphate phosphotransferase); 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. (705 aa)
HEAR1115Putative Cytochrome c oxidase, subunit II (Cytochrome bb3 subunit 2) CoxM; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (400 aa)
coxNCytochrome c oxidase subunit 1; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (586 aa)
HEAR1117Putative cytochrome c oxidase subunit III CoxO; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (216 aa)
coxPCytochrome-c oxidase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (230 aa)
HEAR1119Conserved hypothetical protein; Homologs of previously reported genes of unknown function. (105 aa)
cydACytochrome bd ubiquinol oxidase subunit I; Function of homologous gene experimentally demonstrated in an other organism; carrier. (533 aa)
cydBCytochrome bd ubiquinol oxidase subunit II; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (384 aa)
HEAR1376Conserved hypothetical protein; Homologs of previously reported genes of unknown function. (40 aa)
ccoPCytochrome c oxidase cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (312 aa)
HEAR1642Putative Cytochrome c oxidase cbb3-type, subunit III (CcoQ); Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (57 aa)
fixOCytochrome c oxidase cbb3-type, monoheme subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (204 aa)
fixNCytochrome c oxidase cbb3-type, subunit 1; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the heme-copper respiratory oxidase family. (483 aa)
sdhBSuccinate dehydrogenase (ubiquinone), Fe-S protein; Function of homologous gene experimentally demonstrated in an other organism; carrier; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (236 aa)
sdhASuccinate dehydrogenase, flavoprotein subunit; Function of homologous gene experimentally demonstrated in an other organism; carrier; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (592 aa)
sdhDSuccinate dehydrogenase hydrophobic membrane anchor subunit; Function of strongly homologous gene; membrane component. (121 aa)
sdhCSuccinate dehydrogenase cytochrome b556 subunit (Cytochrome b-556); Function of strongly homologous gene; membrane component. (136 aa)
nuoNNADH-ubiquinone oxidoreductase, chain N; 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; Belongs to the complex I subunit 2 family. (494 aa)
nuoMNADH-quinone oxidoreductase subunit M; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (496 aa)
nuoLNADH-quinone oxidoreductase subunit L (NADH dehydrogenase I subunit L) (NDH-1 subunit L); Function of homologous gene experimentally demonstrated in an other organism; enzyme. (687 aa)
nuoKNADH-quinone oxidoreductase subunit K (NADH dehydrogenase I subunit K) (NDH-1 subunit K); 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; Belongs to the complex I subunit 4L family. (102 aa)
nuoJNADH-quinone oxidoreductase subunit J (NADH dehydrogenase I subunit J) (NDH-1 subunit J); 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. (213 aa)
nuoINADH-quinone oxidoreductase subunit I (NADH dehydrogenase I subunit I) (NDH-1 subunit I); 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. (162 aa)
nuoHNADH-quinone oxidoreductase subunit H (NADH dehydrogenase I subunit H) (NDH-1 subunit H); 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. (357 aa)
nuoGNADH-quinone oxidoreductase subunit G (NADH dehydrogenase I subunit G) (NDH-1 subunit G); 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 75 kDa subunit family. (777 aa)
nuoFNADH-quinone oxidoreductase subunit F (NADH dehydrogenase I subunit F) (NDH-1 subunit F); NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family. (431 aa)
nuoENADH-quinone oxidoreductase subunit E (NADH dehydrogenase I subunit E) (NDH-1 subunit E); Function of strongly homologous gene; enzyme. (159 aa)
nuoDNADH-ubiquinone oxidoreductase D subunit (NADH dehydrogenase subunit D); 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; Belongs to the complex I 49 kDa subunit family. (417 aa)
nuoCNADH-quinone oxidoreductase chain C (NADH dehydrogenase I, chain C) (NDH-1, chain C); 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; Belongs to the complex I 30 kDa subunit family. (198 aa)
nuoBNADH-quinone oxidoreductase subunit B (NADH dehydrogenase I subunit B) (NDH-1 subunit B); 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 (By similarity). (158 aa)
nuoANADH-quinone oxidoreductase chain A (NADH dehydrogenase I, chain A) (NDH-1, chain A); 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; Belongs to the complex I subunit 3 family. (119 aa)
HEAR2035NADH dehydrogenase; Function of strongly homologous gene; enzyme. (435 aa)
ndhNADH dehydrogenase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (460 aa)
cyoDCytochrome o ubiquinol oxidase protein CyoD (Ubiquinol oxidase chain D); Function of homologous gene experimentally demonstrated in an other organism; carrier. (136 aa)
cyoCCytochrome o ubiquinol oxidase subunit 3 (Cytochrome o ubiquinol oxidase subunit III); Function of homologous gene experimentally demonstrated in an other organism; carrier. (214 aa)
cyoBCytochrome o ubiquinol oxidase subunit I; Function of homologous gene experimentally demonstrated in an other organism; carrier; Belongs to the heme-copper respiratory oxidase family. (667 aa)
cyoAUbiquinol oxidase subunit 2; Function of homologous gene experimentally demonstrated in an other organism; carrier. (355 aa)
ctaBPutative protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. (294 aa)
HEAR2911Putative cytochrome oxidase assembly; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (379 aa)
HEAR2915Cytochrome c oxidase polypeptide III; Function of strongly homologous gene; carrier. (288 aa)
HEAR2916Cytochrome c oxidase assembly protein CtaG; Function of strongly homologous gene; carrier. (192 aa)
ctaDCytochrome c oxidase subunit 1 (Cytochrome c oxidase polypeptide I) (Cytochrome aa3 subunit 1); Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. (533 aa)
ctaCCytochrome c oxidase, subunit II (Cytochrome aa3 subunit 2); Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). (386 aa)
petCCytochrome c1 precursor; Function of strongly homologous gene; carrier. (254 aa)
petBCytochrome b; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (467 aa)
petAUbiquinol-cytochrome c reductase iron-sulfur subunit (Rieske iron-sulfur protein) (RISP); Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis. (202 aa)
HEAR3246Putative cytochrome c; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative carrier. (125 aa)
HEAR3327Succinate dehydrogenase/fumarate reductase Fe-S protein subunit; Function of strongly homologous gene; enzyme. (238 aa)
HEAR3328Putative fumarate reductase respiratory complex transmembrane subunit; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (115 aa)
HEAR3329Putative fumarate reductase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (118 aa)
HEAR3333Putative succinate dehydrogenase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (580 aa)
atpCATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit); Produces ATP from ADP in the presence of a proton gradient across the membrane. (140 aa)
atpDATP synthase subunit beta (ATPase subunit beta) (ATP synthase F1 sector subunit beta); 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. (466 aa)
atpGATP synthase gamma chain (ATP synthase F1 sector 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. (289 aa)
atpAATP synthase subunit alpha (ATPase subunit alpha) (ATP synthase F1 sector subunit alpha); 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. (511 aa)
atpHATP synthase delta chain AtpH; 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. (177 aa)
atpFATP synthase F0, B chain; 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. (156 aa)
atpEATP synthase F0, C chain (Lipid-binding protein); 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. (81 aa)
atpBATP synthase F0, A chain; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (281 aa)
Your Current Organism:
Herminiimonas arsenicoxydans
NCBI taxonomy Id: 204773
Other names: CCM 7303, DSM 17148, H. arsenicoxydans, Herminiimonas arsenicoxydans Muller et al. 2006, LMG 22961, LMG:22961, strain ULPAs1
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