STRINGSTRING
AEJ03158.1 AEJ03158.1 dsbD dsbD AEI99929.1 AEI99929.1 AEI99931.1 AEI99931.1 AEJ00174.1 AEJ00174.1 AEJ00251.1 AEJ00251.1 AEJ00271.1 AEJ00271.1 AEJ00272.1 AEJ00272.1 AEJ00276.1 AEJ00276.1 AEJ00280.1 AEJ00280.1 AEJ00454.1 AEJ00454.1 AEJ00506.1 AEJ00506.1 AEJ00598.1 AEJ00598.1 AEJ00599.1 AEJ00599.1 AEJ00614.1 AEJ00614.1 AEJ00629.1 AEJ00629.1 AEJ00670.1 AEJ00670.1 AEJ00717.1 AEJ00717.1 AEJ00720.1 AEJ00720.1 AEJ00936.1 AEJ00936.1 AEJ00990.1 AEJ00990.1 AEJ01185.1 AEJ01185.1 AEJ01428.1 AEJ01428.1 AEJ01429.1 AEJ01429.1 AEJ01430.1 AEJ01430.1 AEJ01432.1 AEJ01432.1 AEJ01467.1 AEJ01467.1 AEJ01515.1 AEJ01515.1 AEJ01519.1 AEJ01519.1 AEJ01663.1 AEJ01663.1 AEJ01674.1 AEJ01674.1 AEJ01757.1 AEJ01757.1 AEJ01855.1 AEJ01855.1 AEJ02027.1 AEJ02027.1 AEJ02046.1 AEJ02046.1 AEJ02299.1 AEJ02299.1 AEJ02301.1 AEJ02301.1 AEJ02466.1 AEJ02466.1 AEJ02648.1 AEJ02648.1 dsbB dsbB nuoN nuoN AEJ02672.1 AEJ02672.1 AEJ02673.1 AEJ02673.1 nuoK nuoK AEJ02675.1 AEJ02675.1 AEJ02678.1 AEJ02678.1 AEJ02679.1 AEJ02679.1 AEJ02680.1 AEJ02680.1 nuoD nuoD nuoC nuoC nuoB nuoB nuoA nuoA AEJ02697.1 AEJ02697.1 AEJ02724.1 AEJ02724.1 AEJ02725.1 AEJ02725.1 AEJ02796.1 AEJ02796.1 AEJ02808.1 AEJ02808.1 AEJ02853.1 AEJ02853.1 AEJ02854.1 AEJ02854.1 AEJ02855.1 AEJ02855.1 AEJ02894.1 AEJ02894.1 AEJ03024.1 AEJ03024.1 AEJ03058.1 AEJ03058.1 AEJ03115.1 AEJ03115.1 AEJ03148.1 AEJ03148.1 AEJ03154.1 AEJ03154.1 AEJ03157.1 AEJ03157.1 AEJ03188.1 AEJ03188.1 AEJ03206.1 AEJ03206.1 AEJ03207.1 AEJ03207.1 AEJ03271.1 AEJ03271.1
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.
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:
AEJ03158.1KEGG: nit:NAL212_0198 cytochrome c class I. (108 aa)
dsbDThiol:disulfide interchange protein dsbD; Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps. Belongs to the thioredoxin family. DsbD subfamily. (645 aa)
AEI99929.1PFAM: Blue (type 1) copper domain; KEGG: nit:NAL212_0178 blue (type 1) copper domain-containing protein. (150 aa)
AEI99931.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_0180 cytochrome c class I. (155 aa)
AEJ00174.1KEGG: nmu:Nmul_A1577 hypothetical protein; TIGRFAM: Conserved hypothetical protein CHP02284; PFAM: Protein of unknown function DUF2383. (153 aa)
AEJ00251.1KEGG: nit:NAL212_3151 hypothetical protein. (173 aa)
AEJ00271.1Cytochrome 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). (273 aa)
AEJ00272.1Cytochrome 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. (528 aa)
AEJ00276.1PFAM: Cytochrome c oxidase, subunit III; KEGG: nit:NAL212_0528 cytochrome-c oxidase. (285 aa)
AEJ00280.1PFAM: FAD-linked oxidase, C-terminal; FAD linked oxidase, N-terminal; KEGG: nit:NAL212_0532 D-lactate dehydrogenase (cytochrome). (457 aa)
AEJ00454.1Rubredoxin-type Fe(Cys)4 protein; KEGG: pag:PLES_57451 rubredoxin 2; manually curated; PFAM: Rubredoxin-type Fe(Cys)4 protein. (54 aa)
AEJ00506.1KEGG: nit:NAL212_2775 hypothetical protein. (687 aa)
AEJ00598.1KEGG: nit:NAL212_2582 cytochrome c class I. (239 aa)
AEJ00599.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_2581 gluconate 2-dehydrogenase (acceptor). (430 aa)
AEJ00614.1KEGG: nit:NAL212_0950 hypothetical protein. (691 aa)
AEJ00629.1PFAM: Di-haem cytochrome c peroxidase; KEGG: net:Neut_1521 cytochrome-c peroxidase. (351 aa)
AEJ00670.1PFAM: Di-haem cytochrome c peroxidase; KEGG: nit:NAL212_2175 cytochrome-c peroxidase. (330 aa)
AEJ00717.1KEGG: nit:NAL212_2775 hypothetical protein. (685 aa)
AEJ00720.1KEGG: nit:NAL212_1785 succinate dehydrogenase and fumarate reductase iron-sulfur protein; TIGRFAM: Succinate dehydrogenase/fumarate reductase iron-sulphur protein; PFAM: Ferredoxin. (231 aa)
AEJ00936.14Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. (107 aa)
AEJ00990.1PFAM: Multicopper oxidase, type 2; KEGG: nit:NAL212_2853 multicopper oxidase type 2. (327 aa)
AEJ01185.1PFAM: NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding; Ferredoxin; KEGG: mca:MCA2725 NAD-reducing hydrogenase, gamma subunit. (243 aa)
AEJ01428.1KEGG: nhl:Nhal_2893 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (501 aa)
AEJ01429.1KEGG: nhl:Nhal_2894 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (530 aa)
AEJ01430.1NADH/Ubiquinone/plastoquinone (complex I); PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal; KEGG: nhl:Nhal_2895 NADH/ubiquinone/plastoquinone (complex I). (522 aa)
AEJ01432.1KEGG: nhl:Nhal_2897 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (490 aa)
AEJ01467.1PFAM: Di-haem cytochrome c peroxidase; KEGG: nit:NAL212_1277 di-heme cytochrome c peroxidase. (734 aa)
AEJ01515.1PFAM: Rubredoxin-type Fe(Cys)4 protein; KEGG: nit:NAL212_0552 rubredoxin-type Fe(Cys)4 protein. (62 aa)
AEJ01519.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_0556 cytochrome c class I. (214 aa)
AEJ01663.1PFAM: Di-haem cytochrome c peroxidase; KEGG: net:Neut_1521 cytochrome-c peroxidase. (350 aa)
AEJ01674.1KEGG: neu:NE1179 putative transmembrane protein. (169 aa)
AEJ01757.1PFAM: Glutaredoxin 2; KEGG: nit:NAL212_1019 glutaredoxin 2. (96 aa)
AEJ01855.1PFAM: Nickel-dependent hydrogenase, large subunit; KEGG: mca:MCA0114 NAD-reducing hydrogenase, beta subunit; Belongs to the [NiFe]/[NiFeSe] hydrogenase large subunit family. (491 aa)
AEJ02027.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_2331 cytochrome c class I. (103 aa)
AEJ02046.1KEGG: hch:HCH_04215 hypothetical protein. (603 aa)
AEJ02299.1KEGG: nit:NAL212_2002 succinate dehydrogenase, cytochrome b556 subunit; TIGRFAM: Succinate dehydrogenase, cytochrome b556 subunit; PFAM: Succinate dehydrogenase, cytochrome b subunit. (129 aa)
AEJ02301.1KEGG: nit:NAL212_2000 succinate dehydrogenase, flavoprotein subunit; TIGRFAM: Succinate dehydrogenase, flavoprotein subunit; 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. (587 aa)
AEJ02466.1KEGG: gvi:gll0213 hypothetical protein; PFAM: Cell surface receptor IPT/TIG; SMART: Cell surface receptor IPT/TIG. (637 aa)
AEJ02648.1PFAM: Copper resistance D; Cytochrome c, class I; KEGG: nit:NAL212_1916 copper resistance D domain-containing protein. (673 aa)
dsbBDisulfide bond formation protein B; Required for disulfide bond formation in some periplasmic proteins. Acts by oxidizing the DsbA protein; Belongs to the DsbB family. (157 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. (481 aa)
AEJ02672.1KEGG: nit:NAL212_2729 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: NADH-quinone oxidoreductase, chain M; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase. (494 aa)
AEJ02673.1KEGG: nit:NAL212_2730 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: NADH-plastoquinone oxidoreductase, chain 5; PFAM: NADH:ubiquinone/plastoquinone oxidoreductase; NADH:ubiquinone oxidoreductase, chain 5/L, N-terminal. (646 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)
AEJ02675.1NADH-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. (201 aa)
AEJ02678.1NADH-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. (803 aa)
AEJ02679.1NADH-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. (425 aa)
AEJ02680.1KEGG: nit:NAL212_2737 NADH-quinone oxidoreductase, E subunit; TIGRFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit; PFAM: NADH:ubiquinone oxidoreductase, 24kDa subunit. (158 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. (417 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. (206 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. (158 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. (118 aa)
AEJ02697.1PFAM: FAD-linked oxidase, C-terminal; FAD linked oxidase, N-terminal; KEGG: nit:NAL212_2160 D-lactate dehydrogenase (cytochrome). (484 aa)
AEJ02724.1KEGG: nit:NAL212_0143 cytochrome c family protein. (171 aa)
AEJ02725.1PFAM: Transglutaminase-like; KEGG: hypothetical protein. (499 aa)
AEJ02796.1KEGG: nit:NAL212_2764 hypothetical protein. (599 aa)
AEJ02808.1PFAM: NADPH-dependent FMN reductase; KEGG: pna:Pnap_0016 NADPH-dependent FMN reductase. (375 aa)
AEJ02853.1PFAM: Cytochrome c1; KEGG: nit:NAL212_2479 cytochrome c1. (240 aa)
AEJ02854.1Cytochrome b/b6 domain-containing 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. (411 aa)
AEJ02855.1Ubiquinol-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. (202 aa)
AEJ02894.1KEGG: ade:Adeh_2940 hypothetical protein. (479 aa)
AEJ03024.1KEGG: nit:NAL212_2961 multicopper oxidase type 1. (615 aa)
AEJ03058.1KEGG: net:Neut_1845 putative transmembrane protein. (169 aa)
AEJ03115.1KEGG: nit:NAL212_0639 hypothetical protein. (183 aa)
AEJ03148.1PFAM: Multicopper oxidase, type 3; Multicopper oxidase, type 2; KEGG: nit:NAL212_0279 multicopper oxidase type 3. (933 aa)
AEJ03154.1Electron transport complex, RnfABCDGE type, B subunit; Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane. Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB subfamily. (227 aa)
AEJ03157.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_0199 cytochrome c class I. (109 aa)
AEJ03188.1PFAM: Cytochrome c, class I; KEGG: nit:NAL212_3121 cytochrome c, class I. (102 aa)
AEJ03206.1KEGG: neu:NE1179 putative transmembrane protein. (169 aa)
AEJ03207.1PFAM: Di-haem cytochrome c peroxidase; KEGG: net:Neut_1521 cytochrome-c peroxidase. (350 aa)
AEJ03271.1PFAM: Copper resistance D; Cytochrome c, class I; KEGG: neu:NE2058 cytochrome c, class IC:cytochrome c, class I. (673 aa)
Your Current Organism:
Nitrosomonas sp. Is79A3
NCBI taxonomy Id: 261292
Other names: N. sp. Is79A3
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.