STRINGSTRING
scyA scyA petA petA petB petB petC petC SO_0714 SO_0714 sorA sorA sorB sorB SO_0717 SO_0717 SO_0718 SO_0718 SO_0801 SO_0801 SO_0882 SO_0882 nuoN nuoN nuoM nuoM nuoL nuoL nuoK nuoK nuoJ nuoJ nuoI nuoI nuoH nuoH nuoG nuoG nuoF nuoF nuoE nuoE nuoCD nuoCD nuoB nuoB nuoA nuoA SO_1251 SO_1251 rseP rseP SO_1748 SO_1748 ccpA ccpA uspE uspE fnr fnr SO_2357 SO_2357 ccoS ccoS ccoI ccoI ccoH ccoH ccoP ccoP ccoQ ccoQ ccoO ccoO ccoN ccoN SO_2365 SO_2365 SO_2930 SO_2930 SO_2931 SO_2931 SO_3056 SO_3056 ybgT ybgT cydB cydB cydA cydA SO_3560 SO_3560 SO_3750 SO_3750 cydC cydC cydD cydD SO_3848 SO_3848 SO_3907 SO_3907 SO_4022 SO_4022 SO_4047 SO_4047 SO_4048 SO_4048 SO_4142 SO_4142 SO_4538 SO_4538 coxB coxB coxA coxA ctaG ctaG coxC coxC SO_4611 SO_4611 SO_4612 SO_4612 ctaA ctaA ctaB ctaB senC senC cytcB cytcB ccoG ccoG SO_4811 SO_4811
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.
Node Color
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
Your Input:
scyAPeriplasmic monoheme cytochrome c5 ScyA. (99 aa)
petAUbiquinol-cytochrome c reductase FeS subunit PetA; 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. (196 aa)
petBUbiquinol-cytochrome c reductase cytochrome b subunit PetB; 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. (404 aa)
petCUbiquinol-cytochrome c reductase cytochrome c1 subunit PetC. (231 aa)
SO_0714Periplasmic monoheme cytochrome c4. (100 aa)
sorASulfite dehydrogenase molybdopterin-binding subunit SorA. (408 aa)
sorBSulfite dehydrogenase cytochrome c subunit SorB. (127 aa)
SO_0717Periplasmic monoheme cytochrome c4. (111 aa)
SO_0718Predicted secreted protein. (159 aa)
SO_0801Esterase/lipase/thioesterase domain protein. (304 aa)
SO_0882Oxidoreductase GMC family. (533 aa)
nuoNNADH-ubiquinone oxidoreductase subunit N NuoN; 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. (487 aa)
nuoMNADH-ubiquinone oxidoreductase subunit M NuoM. (514 aa)
nuoLNADH-ubiquinone oxidoreductase subunit L NuoL. (615 aa)
nuoKNADH-ubiquinone oxidoreductase subunit K NuoK; 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-ubiquinone oxidoreductase subunit J NuoJ; 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. (183 aa)
nuoINADH-ubiquinone oxidoreductase subunit I NuoI; 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. (180 aa)
nuoHNADH-ubiquinone oxidoreductase subunit H NuoH; 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. (322 aa)
nuoGNADH-ubiquinone oxidoreductase subunit G NuoG; 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 (By similarity). (909 aa)
nuoFNADH-ubiquinone oxidoreductase subunit F NuoF; 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. (461 aa)
nuoENADH-ubiquinone oxidoreductase subunit E NuoE. (180 aa)
nuoCDNADH-ubiquinone oxidoreductase subunit CD NuoCD; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family. (601 aa)
nuoBNADH-ubiquinone oxidoreductase subunit B NuoB; 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. (224 aa)
nuoANADH-ubiquinone oxidoreductase subunit A NuoA; 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. (134 aa)
SO_1251Ferredoxin 4Fe-4S. (83 aa)
rsePRseA degrading zinc metalloprotease RseP. (456 aa)
SO_1748Monoheme cytochrome c. (509 aa)
ccpADiheme cytochrome c5 peroxidase CcpA. (333 aa)
uspEUniversal stress protein UspE. (310 aa)
fnrOxygen-responsive transcriptional regulator of anaerobiosis response Fnr; Regulates anaerobic growth on fumarate, nitrite, Fe(3+), TMAO, DMSO, thiosulfate and sulfite, but not on nitrate nor Mn(4+). (250 aa)
SO_2357Cbb3-type cytochrome oxidase assembly protein disulfide bond oxidoreductase DsbD family. (234 aa)
ccoSCbb3-type cytochrome oxidase assembly protein CcoS. (67 aa)
ccoICbb3-type cytochrome oxidase-associated copper translocating P-ATPase CcoI. (799 aa)
ccoHCbb3-type cytochrome oxidase assembly protein CcoH. (159 aa)
ccoPCbb3-type cytochrome c oxidase subunit III CcoP; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (322 aa)
ccoQCbb3-type cytochrome c oxidase subunit IV CcoQ. (58 aa)
ccoOCbb3-type cytochrome c oxidase subunit II CcoO. (208 aa)
ccoNCbb3-type cytochrome c oxidase subunit I CcoN; Belongs to the heme-copper respiratory oxidase family. (478 aa)
SO_2365Predicted lipoprotein. (161 aa)
SO_2930Bifunctional pectinolytic enzyme/cytochrome c. (907 aa)
SO_2931Cytochrome c lipoprotein. (390 aa)
SO_3056Flavocytochrome c heme submit. (127 aa)
ybgTProtein YbgT. (38 aa)
cydBCytochrome d ubiquinol oxidase subunit II CydB. (379 aa)
cydACytochrome d ubiquinol oxidase subunit I CydA. (518 aa)
SO_3560Predicted non-catalytic member of peptidase subfamily M16B. (949 aa)
SO_3750Predicted non-catalytic member of peptidase subfamily M16B. (471 aa)
cydCABC-type cysteine/glutathione export system bifunctional ATPase and permease component CydC. (583 aa)
cydDABC-type cysteine/glutathione export system bifunctional ATPase and permease components CydD. (646 aa)
SO_3848Cytoplasmic protein of unknown function. (166 aa)
SO_3907Cytochrome oxidase copper metallochaperone. (160 aa)
SO_4022Periplasmic peptidase family M16B. (943 aa)
SO_4047SoxA-like diheme cytochrome c. (351 aa)
SO_4048Diheme cytochrome c4. (208 aa)
SO_4142Periplasmic monoheme cytochrome c. (109 aa)
SO_4538Predicted non-catalytic member of peptidase subfamily M16B. (492 aa)
coxBAa3-type cytochrome c oxidase subunit II CoxB; 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). (513 aa)
coxAAa3 type cytochrome c oxidase subunit I CoxA; 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. (530 aa)
ctaGAa3 type cytochrome c oxidase assembly protein CtaG. (193 aa)
coxCAa3 type cytochrome c oxidase subunit III CoxC. (291 aa)
SO_4611Aa3 type cytochrome c oxidase biogenesis protein Surf1-like protein. (281 aa)
SO_4612Uncharacterized protein. (181 aa)
ctaAHeme A synthase CtaA. (330 aa)
ctaBProtoheme IX farnesyltransferase (heme O synthase) CtaB; 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. (300 aa)
senCCytochrome c oxidase biogenesis protein SenC. (213 aa)
cytcBDiheme cytochrome c4 CytcB. (207 aa)
ccoGCbb3-type cytochrome oxidase assembly protein CcoG. (475 aa)
SO_4811Periplasmic peptidase family M16B. (443 aa)
Your Current Organism:
Shewanella oneidensis
NCBI taxonomy Id: 211586
Other names: S. oneidensis MR-1, Shewanella oneidensis ATCC 700550, Shewanella oneidensis MR-1, Shewanella oneidensis str. MR-1, Shewanella oneidensis strain MR-1, Shewanella sp. MR-1
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