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Jann_1194 Jann_1194 cycA cycA puhA puhA pufC pufC pufM pufM pufL pufL pufA pufA pufB pufB Jann_0302 Jann_0302 Jann_0325 Jann_0325 Jann_0326 Jann_0326 Jann_0327 Jann_0327 Jann_0484 Jann_0484 Jann_0545 Jann_0545 Jann_0546 Jann_0546 Jann_0632 Jann_0632 Jann_0673 Jann_0673 Jann_0736 Jann_0736 Jann_0737 Jann_0737 azoR1 azoR1 Jann_0804 Jann_0804 Jann_0809 Jann_0809 Jann_0811 Jann_0811 Jann_0852 Jann_0852 Jann_1044 Jann_1044 nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD Jann_1179 Jann_1179 Jann_1183 Jann_1183 Jann_1190 Jann_1190 nuoK nuoK Jann_1195 Jann_1195 nuoN nuoN Jann_1249 Jann_1249 Jann_1250 Jann_1250 Jann_1259 Jann_1259 Jann_1332 Jann_1332 Jann_1333 Jann_1333 Jann_1441 Jann_1441 Jann_1443 Jann_1443 pucB pucB pucA pucA Jann_1848 Jann_1848 azoR2 azoR2 Jann_2176 Jann_2176 Jann_2211 Jann_2211 Jann_2228 Jann_2228 Jann_2229 Jann_2229 Jann_2558 Jann_2558 Jann_2559 Jann_2559 Jann_2560 Jann_2560 Jann_2611 Jann_2611 Jann_2671 Jann_2671 Jann_3045 Jann_3045 Jann_3123 Jann_3123 Jann_3151 Jann_3151 Jann_3155 Jann_3155 Jann_3168 Jann_3168 Jann_3309 Jann_3309 Jann_3559 Jann_3559 Jann_3562 Jann_3562 Jann_3600 Jann_3600 Jann_3635 Jann_3635 Jann_3670 Jann_3670 Jann_3672 Jann_3672 Jann_3692 Jann_3692 Jann_3717 Jann_3717 Jann_3749 Jann_3749 Jann_3768 Jann_3768 ccoP ccoP ccoO ccoO ccoN ccoN Jann_3864 Jann_3864 Jann_3966 Jann_3966 Jann_3968 Jann_3968 msrQ msrQ
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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
Jann_1194NADH dehydrogenase subunit L. (711 aa)
cycACytochrome c2. (148 aa)
puhAReaction center protein H chain. (260 aa)
pufCPhotosynthetic reaction center cytochrome c subunit; The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. (414 aa)
pufMReaction center protein M chain; The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. (332 aa)
pufLReaction center protein L chain; Belongs to the reaction center PufL/M/PsbA/D family. (302 aa)
pufALight-harvesting protein B-870 alpha chain; Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. (55 aa)
pufBLight-harvesting protein B-800-850 beta chain B; Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. (60 aa)
Jann_0302Cytochrome B561. (181 aa)
Jann_0325Ubiquinol-cytochrome c reductase iron-sulfur subunit; 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. (191 aa)
Jann_0326Cytochrome b/b6-like protein; 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. (451 aa)
Jann_0327Cytochrome c1. (269 aa)
Jann_0484Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (548 aa)
Jann_0545Electron transfer flavoprotein alpha subunit. (308 aa)
Jann_0546Electron transfer flavoprotein beta-subunit. (253 aa)
Jann_0632Hypothetical protein. (215 aa)
Jann_0673Flavodoxin/nitric oxide synthase. (152 aa)
Jann_0736Cytochrome bd quinol oxidase subunit 1 apoprotein. (478 aa)
Jann_0737Cytochrome bd quinol oxidase subunit 2 apoprotein. (337 aa)
azoR1(Acyl-carrier protein) phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (191 aa)
Jann_0804Succinate dehydrogenase subunit B; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (264 aa)
Jann_0809Succinate dehydrogenase subunit A; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (606 aa)
Jann_0811Succinate dehydrogenase subunit C. (127 aa)
Jann_0852Protoporphyrinogen oxidase. (173 aa)
Jann_1044Tryptophan repressor binding protein. (178 aa)
nuoANADH dehydrogenase subunit 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. (121 aa)
nuoBNADH dehydrogenase 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). (177 aa)
nuoCNADH dehydrogenase subunit 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. (207 aa)
nuoDNADH 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. (412 aa)
Jann_1179NADH dehydrogenase 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)
Jann_1183NADH dehydrogenase 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. (672 aa)
Jann_1190NADH dehydrogenase 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. (205 aa)
nuoKNADH dehydrogenase 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)
Jann_1195NADH dehydrogenase subunit M. (514 aa)
nuoNNADH dehydrogenase subunit 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. (483 aa)
Jann_1249Cytochrome c oxidase subunit I. (155 aa)
Jann_1250Cytochrome-c oxidase; Belongs to the heme-copper respiratory oxidase family. (628 aa)
Jann_1259NADH dehydrogenase (quinone). (519 aa)
Jann_1332Thiamine pyrophosphate enzyme-like TPP-binding protein. (730 aa)
Jann_1333Indolepyruvate ferredoxin oxidoreductase beta subunit. (498 aa)
Jann_1441DMSO reductase anchor subunit (DmsC). (291 aa)
Jann_1443Molybdopterin oxidoreductase Fe4S4 protein; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (932 aa)
pucBLight-harvesting protein B-800-850 beta chain B; Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. (51 aa)
pucAPeripheral light harvesting complex subunit; Antenna complexes are light-harvesting systems, which transfer the excitation energy to the reaction centers. (107 aa)
Jann_1848Cytochrome B561. (193 aa)
azoR2(Acyl-carrier protein) phosphodiesterase; Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity; Belongs to the azoreductase type 1 family. (204 aa)
Jann_2176Pyruvate ferredoxin/flavodoxin oxidoreductase. (1132 aa)
Jann_2211Hypothetical protein. (378 aa)
Jann_2228Diheme cytochrome c-type. (299 aa)
Jann_2229Cytochrome c class II. (156 aa)
Jann_2558Formate dehydrogenase alpha subunit. (973 aa)
Jann_2559Formate dehydrogenase beta subunit. (500 aa)
Jann_2560Formate dehydrogenase gamma subunit. (167 aa)
Jann_2611Protein of unknown function DUF989. (413 aa)
Jann_2671Cytochrome B561. (238 aa)
Jann_3045Assimilatory nitrate reductase (NADH) alpha subunit apoprotein; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily. (873 aa)
Jann_3123Rieske (2Fe-2S) protein. (349 aa)
Jann_3151Cytochrome c oxidase subunit III. (270 aa)
Jann_3155Cytochrome c oxidase subunit II; 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). (320 aa)
Jann_3168Ferredoxin. (107 aa)
Jann_33094Fe-4S ferredoxin iron-sulfur binding protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (111 aa)
Jann_3559Hypothetical protein. (287 aa)
Jann_3562Hypothetical protein. (147 aa)
Jann_3600ETC complex I subunit conserved protein. (103 aa)
Jann_3635Hypothetical protein. (126 aa)
Jann_3670Blue (type 1) copper domain. (112 aa)
Jann_3672Di-heme cytochrome c peroxidase. (498 aa)
Jann_3692Multisubunit sodium/proton antiporter, MrpD subunit; TC 2.A.63.1. (500 aa)
Jann_3717Multisubunit potassium/proton antiporter, PhaD subunit; TC 2.A.63.1.1. (539 aa)
Jann_37494Fe-4S ferredoxin iron-sulfur binding protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (116 aa)
Jann_3768Fumarate reductase/succinate dehydrogenase flavoprotein-like protein. (460 aa)
ccoPCytochrome c oxidase cbb3-type subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (292 aa)
ccoOCytochrome c oxidase cbb3-type subunit II. (240 aa)
ccoNCytochrome c oxidase cbb3-type subunit I; Belongs to the heme-copper respiratory oxidase family. (532 aa)
Jann_3864Cytochrome c class I. (170 aa)
Jann_3966Succinate dehydrogenase subunit B. (237 aa)
Jann_3968Succinate dehydrogenase subunit C. (114 aa)
msrQFerric reductase-like transmembrane component-like protein; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reduc [...] (200 aa)
Your Current Organism:
Jannaschia sp. CCS1
NCBI taxonomy Id: 290400
Other names: J. sp. CCS1
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