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AEG49450.1 AEG49450.1 AEG47811.1 AEG47811.1 AEG47813.1 AEG47813.1 AEG47814.1 AEG47814.1 AEG47815.1 AEG47815.1 AEG47816.1 AEG47816.1 AEG47831.1 AEG47831.1 AEG47832.1 AEG47832.1 AEG47958.1 AEG47958.1 AEG48081.1 AEG48081.1 AEG48169.1 AEG48169.1 AEG48328.1 AEG48328.1 AEG48483.1 AEG48483.1 AEG48678.1 AEG48678.1 AEG48687.1 AEG48687.1 AEG48790.1 AEG48790.1 AEG48791.1 AEG48791.1 AEG48792.1 AEG48792.1 AEG48793.1 AEG48793.1 nuoN nuoN AEG48864.1 AEG48864.1 AEG48865.1 AEG48865.1 nuoK nuoK AEG48867.1 AEG48867.1 AEG48870.1 AEG48870.1 AEG48871.1 AEG48871.1 AEG48872.1 AEG48872.1 nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA AEG48911.1 AEG48911.1 AEG49003.1 AEG49003.1 AEG49046.1 AEG49046.1 AEG49091.1 AEG49091.1 AEG49147.1 AEG49147.1 AEG49249.1 AEG49249.1 AEG49255.1 AEG49255.1 AEG49334.1 AEG49334.1 AEG49384.1 AEG49384.1 AEG49386.1 AEG49386.1 AEG49795.1 AEG49795.1 AEG50111.1 AEG50111.1 AEG50112.1 AEG50112.1 AEG50116.1 AEG50116.1 AEG50161.1 AEG50161.1 AEG50320.1 AEG50320.1 AEG50321.1 AEG50321.1 AEG50322.1 AEG50322.1 AEG50403.1 AEG50403.1 AEG50469.1 AEG50469.1 AEG50684.1 AEG50684.1 AEG50835.1 AEG50835.1 AEG50996.1 AEG50996.1 AEG50997.1 AEG50997.1 AEG50999.1 AEG50999.1 AEG51016.1 AEG51016.1 AEG51017.1 AEG51017.1 AEG51018.1 AEG51018.1 AEG51165.1 AEG51165.1 AEG51183.1 AEG51183.1 AEG51235.1 AEG51235.1 AEG51302.1 AEG51302.1 AEG51303.1 AEG51303.1 AEG51304.1 AEG51304.1 AEG51316.1 AEG51316.1 AEG51378.1 AEG51378.1 AEG51418.1 AEG51418.1 AEG51537.1 AEG51537.1 AEG51546.1 AEG51546.1 azoR azoR AEG51615.1 AEG51615.1 AEG51635.1 AEG51635.1
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
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
AEG49450.1KEGG: sjp:SJA_C1-09050 putative cytochrome b561. (233 aa)
AEG47811.1PFAM: Cytochrome c, class I; KEGG: sjp:SJA_C1-11360 cytochrome c. (224 aa)
AEG47813.1PFAM: Cytochrome c oxidase, subunit III; KEGG: sjp:SJA_C1-11380 cytochrome c oxidase subunit III. (227 aa)
AEG47814.1PFAM: Cytochrome c oxidase, subunit III; KEGG: sjp:SJA_C1-11390 cytochrome c oxidase subunit III. (191 aa)
AEG47815.1PFAM: Cytochrome c oxidase, subunit I; KEGG: sjp:SJA_C1-11400 cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (572 aa)
AEG47816.1PFAM: Cytochrome c oxidase subunit II C-terminal; KEGG: sjp:SJA_C1-11410 cytochrome c oxidase subunit II. (289 aa)
AEG47831.1PFAM: Electron transfer flavoprotein, alpha/beta-subunit, N-terminal; KEGG: sjp:SJA_C1-11600 electron transfer flavoprotein beta subunit. (249 aa)
AEG47832.1PFAM: Electron transfer flavoprotein, alpha subunit, C-terminal; Electron transfer flavoprotein, alpha/beta-subunit, N-terminal; KEGG: sjp:SJA_C1-11610 electron transfer flavoprotein alpha subunit. (310 aa)
AEG47958.1TIGRFAM: Flavoprotein WrbA; HAMAP: Flavoprotein wrbA; KEGG: sjp:SJA_C1-15650 TrpR binding protein WrbA; PFAM: Flavodoxin/nitric oxide synthase. (199 aa)
AEG48081.1PFAM: Transglutaminase-like cysteine peptidase, predicted; KEGG: sjp:SJA_C1-22270 hypothetical protein. (353 aa)
AEG48169.1PFAM: Transglutaminase-like cysteine peptidase, predicted; KEGG: cse:Cseg_3991 transglutaminase family protein cysteine peptidase BTLCP. (311 aa)
AEG48328.1PFAM: Ferredoxin; KEGG: sjp:SJA_C1-21730 ferredoxin. (111 aa)
AEG48483.1Electron-transferring-flavoprotein dehydrogenase; Accepts electrons from ETF and reduces ubiquinone. (550 aa)
AEG48678.1Protein of unknown function DUF1271; PFAM: Ferredoxin soy-like; KEGG: rec:RHECIAT_PB0000258 putative ferredoxin protein. (63 aa)
AEG48687.1PFAM: Cytochrome c, class I; KEGG: sjp:SJA_C1-15940 cytochrome c. (124 aa)
AEG48790.1Ubiquinol oxidase, subunit II; KEGG: sjp:SJA_C1-20980 cytochrome o ubiquinol oxidase subunit II; TIGRFAM: Cytochrome o ubiquinol oxidase subunit II; PFAM: COX aromatic rich; Cytochrome c oxidase subunit II C-terminal. (370 aa)
AEG48791.1PFAM: Cytochrome c oxidase, subunit I; manually curated; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit I; KEGG: sjp:SJA_C1-20990 cytochrome o ubiquinol oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (666 aa)
AEG48792.1KEGG: sjp:SJA_C1-21000 cytochrome o ubiquinol oxidase subunit III; TIGRFAM: Cytochrome o ubiquinol oxidase, subunit III; PFAM: Cytochrome c oxidase, subunit III. (207 aa)
AEG48793.1KEGG: sjp:SJA_C1-21010 cytochrome o ubiquinol oxidase operon protein CyoD; TIGRFAM: Cytochrome o ubiquinol oxidase subunit IV; PFAM: Cytochrome C oxidase subunit IV prokaryotic. (133 aa)
nuoNNAD(P)H-quinone oxidoreductase 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 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. (478 aa)
AEG48864.1TIGRFAM: NADH-quinone oxidoreductase, chain M; KEGG: sjp:SJA_C1-13350 NADH dehydrogenase I chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (523 aa)
AEG48865.1TIGRFAM: NADH-plastoquinone oxidoreductase, chain 5; KEGG: sjp:SJA_C1-13340 NADH dehydrogenase I chain L; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal; NADH dehydrogenase subunit 5, C-terminal. (681 aa)
nuoKNAD(P)H-quinone oxidoreductase 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 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. (101 aa)
AEG48867.1NADH-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. (203 aa)
AEG48870.1NADH-quinone oxidoreductase, chain 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. (668 aa)
AEG48871.1NADH-quinone oxidoreductase, F subunit; 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. (438 aa)
AEG48872.1TIGRFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; KEGG: sjp:SJA_C1-13260 NADH dehydrogenase I chain E; PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit. (222 aa)
nuoDNAD(P)H-quinone oxidoreductase 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; Belongs to the complex I 49 kDa subunit family. (411 aa)
nuoCNAD(P)H-quinone oxidoreductase subunit J; 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. (258 aa)
nuoBNAD(P)H-quinone oxidoreductase 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. (184 aa)
nuoANAD(P)H-quinone oxidoreductase 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 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. (124 aa)
AEG48911.1KEGG: sjp:SJA_C1-15170 putative MFS permease. (579 aa)
AEG49003.1KEGG: sjp:SJA_C1-23920 hypothetical protein. (414 aa)
AEG49046.1TIGRFAM: Succinate dehydrogenase/fumarate reductase iron-sulphur protein; KEGG: sjp:SJA_C1-24370 succinate dehydrogenase iron-sulfur protein; PFAM: Ferredoxin. (262 aa)
AEG49091.1PFAM: ETC complex I subunit conserved region; KEGG: sjp:SJA_C1-27710 putative oxidoreductase. (92 aa)
AEG49147.14Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (112 aa)
AEG49249.1Cytochrome b561; KEGG: sjp:SJA_C1-08090 cytochrome b561; Belongs to the UPF0312 family. (410 aa)
AEG49255.1PFAM: Ferredoxin; KEGG: sjp:SJA_C1-08030 ferredoxin. (105 aa)
AEG49334.1KEGG: sjp:SJA_C1-27540 hypothetical protein. (185 aa)
AEG49384.1TIGRFAM: Succinate dehydrogenase, flavoprotein subunit; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit; KEGG: sjp:SJA_C1-10730 succinate dehydrogenase/fumarate reductase flavoprotein subunit; PFAM: Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; Fumarate reductase/succinate dehydrogenase flavoprotein, C-terminal; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (609 aa)
AEG49386.1KEGG: sjp:SJA_C1-10710 succinate dehydrogenase/fumarate reductase cytochrome b subunit; TIGRFAM: Succinate dehydrogenase, cytochrome b556 subunit; PFAM: Succinate dehydrogenase, cytochrome b subunit. (131 aa)
AEG49795.1Nitrate reductase; KEGG: mgi:Mflv_1778 molydopterin dinucleotide-binding region; PFAM: Molybdopterin oxidoreductase Fe4S4 region; Molybdopterin oxidoreductase; Molydopterin dinucleotide-binding region; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (725 aa)
AEG50111.1Cytochrome 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). (336 aa)
AEG50112.1Cytochrome c oxidase, subunit I; 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. (555 aa)
AEG50116.1PFAM: Cytochrome c oxidase, subunit III; KEGG: sjp:SJA_C1-06740 cytochrome c oxidase subunit III. (276 aa)
AEG50161.1PFAM: Flavodoxin/nitric oxide synthase; KEGG: cak:Caul_0456 flavodoxin/nitric oxide synthase. (192 aa)
AEG50320.1Ubiquinol-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)
AEG50321.1Cytochrome b/b6 domain 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. (439 aa)
AEG50322.1PFAM: Cytochrome c1; KEGG: sjp:SJA_C1-30510 ubiquinol-cytochrome c reductase cytochrome c1 subunit. (282 aa)
AEG50403.1KEGG: met:M446_2760 hypothetical protein. (592 aa)
AEG50469.1PFAM: Cytochrome c, class I; KEGG: sjp:SJA_C1-28980 cytochrome c. (205 aa)
AEG50684.1PFAM: Ferredoxin; KEGG: nar:Saro_1115 ferredoxin. (105 aa)
AEG50835.1KEGG: swi:Swit_2022 indolepyruvate ferredoxin oxidoreductase; PFAM: Pyruvate/ketoisovalerate oxidoreductase. (1143 aa)
AEG50996.1TIGRFAM: Cytochrome c oxidase cbb3-type, subunit I; KEGG: sjp:SJA_C2-00670 cb-type cytochrome c oxidase subunit I; PFAM: Cytochrome c oxidase, subunit I; Belongs to the heme-copper respiratory oxidase family. (552 aa)
AEG50997.1KEGG: sjp:SJA_C2-00680 cb-type cytochrome c oxidase subunit II; TIGRFAM: Cytochrome C oxidase, monohaem subunit/FixO; PFAM: Cytochrome C oxidase, monohaem subunit/FixO. (248 aa)
AEG50999.1Cytochrome c oxidase, cbb3-type, subunit III; C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex. (295 aa)
AEG51016.1PFAM: Cytochrome c oxidase, subunit I; KEGG: rlt:Rleg2_5243 cytochrome c oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (615 aa)
AEG51017.1KEGG: rlt:Rleg2_5242 cytochrome c oxidase subunit III. (202 aa)
AEG51018.1PFAM: Cytochrome c, class I; KEGG: sus:Acid_6904 cytochrome c, class I. (140 aa)
AEG51165.1PFAM: Ferredoxin; KEGG: swi:Swit_0363 ferredoxin. (105 aa)
AEG51183.1PFAM: Ferredoxin; KEGG: swi:Swit_0285 ferredoxin. (106 aa)
AEG51235.1PFAM: Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; KEGG: swi:Swit_0325 3-ketosteroid-delta-1-dehydrogenase. (550 aa)
AEG51302.1PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; KEGG: sjp:SJA_C2-01610 NAD-dependent formate dehydrogenase gamma subunit. (155 aa)
AEG51303.1NADH dehydrogenase (quinone); KEGG: sjp:SJA_C2-01620 NAD-dependent formate dehydrogenase beta subunit; PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding. (526 aa)
AEG51304.1KEGG: sjp:SJA_C2-01630 NAD-dependent formate dehydrogenase alpha subunit; TIGRFAM: Formate dehydrogenase, alpha subunit; PFAM: Molybdopterin oxidoreductase; NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; Ferredoxin; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; Molybdopterin oxidoreductase Fe4S4 region; Molydopterin dinucleotide-binding region. (948 aa)
AEG51316.1PFAM: Blue (type 1) copper domain; KEGG: gur:Gura_2109 hypothetical protein. (135 aa)
AEG51378.1Protein of unknown function DUF1271; PFAM: Ferredoxin soy-like; KEGG: sjp:SJA_C2-04950 putative ferredoxin. (70 aa)
AEG51418.1Nitrate reductase; KEGG: tcu:Tcur_2187 molybdopterin oxidoreductase; PFAM: Molybdopterin oxidoreductase; Molybdopterin oxidoreductase Fe4S4 region; Molydopterin dinucleotide-binding region; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (732 aa)
AEG51537.1KEGG: sjp:SJA_C2-00180 putative cytochrome c. (105 aa)
AEG51546.1PFAM: Cytochrome c, class I; KEGG: sjp:SJA_C2-01840 putative cytochrome c. (129 aa)
azoRFMN-dependent NADH-azoreductase; 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. (205 aa)
AEG51615.1PFAM: Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal; KEGG: ppf:Pput_3118 fumarate reductase/succinate dehydrogenase flavoprotein domain-containing protein. (558 aa)
AEG51635.1Succinate dehydrogenase; KEGG: rsk:RSKD131_4248 tricarballylate dehydrogenase; PFAM: Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal. (509 aa)
Your Current Organism:
Sphingobium chlorophenolicum
NCBI taxonomy Id: 690566
Other names: FLAVOBACTERIUM SP. (STRAIN ATCC 39723), Flavobacterium sp. (ATCC 39723), Flavobacterium sp. ATCC 39723, S. chlorophenolicum L-1, Sphingobium chlorophenolicum ATCC 39723, Sphingobium chlorophenolicum L-1, Sphingobium chlorophenolicum str. L-1, Sphingobium chlorophenolicum strain L-1
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