STRINGSTRING
nuoA nuoA nuoB nuoB nuoC nuoC nuoD nuoD nuoH nuoH UFO1_0730 UFO1_0730 nuoK nuoK UFO1_0733 UFO1_0733 UFO1_0734 UFO1_0734 nuoN nuoN UFO1_1384 UFO1_1384 UFO1_1385 UFO1_1385 UFO1_1400 UFO1_1400 UFO1_2355 UFO1_2355 UFO1_3062 UFO1_3062 UFO1_3063 UFO1_3063 UFO1_3064 UFO1_3064 UFO1_3927 UFO1_3927 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB UFO1_4345 UFO1_4345 UFO1_4372 UFO1_4372 UFO1_4373 UFO1_4373 ppk ppk
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:
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 a menaquinone. 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. (120 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 a menaquinone. 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. (171 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 a menaquinone. 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. (160 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 a menaquinone. 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. (365 aa)
nuoHNAD(P)H-quinone oxidoreductase subunit 1; 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. (346 aa)
UFO1_0730PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; KEGG: nuoI, proton-translocating NADH-ubiquinone oxidoreductase, 23 kd, chain i. (158 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 a menaquinone. 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)
UFO1_0733TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; KEGG: nuoL, proton-translocating NADH-ubiquinone oxidoreductase subunit l; PFAM: NADH/Ubiquinone/plastoquinone (complex I), NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein. (634 aa)
UFO1_0734TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; KEGG: nuoM, proton-translocating NADH-ubiquinone oxidoreductase subunit m; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (511 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 a menaquinone. 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. (471 aa)
UFO1_1384KEGG: NADH dehydrogenase (quinone); PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit. (158 aa)
UFO1_1385PFAM: Respiratory-chain NADH dehydrogenase domain 51 kDa subunit, Soluble ligand binding domain-containing protein, NADH ubiquinone oxidoreductase, F subunit, iron sulfur binding protein; KEGG: NADH:ubiquinone oxidoreductase, NADH-binding (51 kD) subunit; SMART: NADH ubiquinone oxidoreductase, F subunit, iron sulfur binding protein. (432 aa)
UFO1_1400PFAM: phosphoesterase RecJ domain protein, DHHA2 domain protein, DRTGG domain protein, CBS domain containing protein; KEGG: Inorganic diphosphatase; SMART: CBS domain containing protein. (545 aa)
UFO1_2355KEGG: HAD family hydrolase; TIGRFAM: HAD-superfamily hydrolase, subfamily IA, variant 1, HAD-superfamily hydrolase, subfamily IA, variant 3. (213 aa)
UFO1_3062TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: sdhB, putative succinate dehydrogenase iron-sulfur subunit; PFAM: Succinate dehydogenase/fumarate reductase N-terminal, 4Fe-4S ferredoxin, iron-sulpur binding domain-containing protein. (252 aa)
UFO1_3063TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; KEGG: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein, Fumarate reductase/succinate dehydrogenase flavoprotein-like protein. (583 aa)
UFO1_3064PFAM: succinate dehydrogenase cytochrome b subunit; KEGG: sdhC, hypothetical protein. (204 aa)
UFO1_3927NADH dehydrogenase (ubiquinone); KEGG: putative oxidoreductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domain, FAD-dependent pyridine nucleotide-disulfide oxidoreductase. (417 aa)
atpCATP synthase epsilon chain; Produces ATP from ADP in the presence of a proton gradient across the membrane. (135 aa)
atpDATP synthase 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. (470 aa)
atpGATP synthase gamma chain; 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. (282 aa)
atpAATP synthase subunit alpha; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. (508 aa)
atpHATP synthase subunit delta; 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. (188 aa)
atpFATP synthase subunit b; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family. (167 aa)
atpEATP synthase subunit c; 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. (83 aa)
atpBATP synthase subunit a; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family. (226 aa)
UFO1_4345NADH dehydrogenase (ubiquinone); KEGG: putative oxidoreductase; PFAM: Pyridine nucleotide-disulphide oxidoreductase, FAD/NAD(P)-binding domain, FAD-dependent pyridine nucleotide-disulfide oxidoreductase. (418 aa)
UFO1_4372KEGG: cytochrome d ubiquinol oxidase, subunit II; TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II. (334 aa)
UFO1_4373PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: cytochrome bd ubiquinol oxidase subunit I. (462 aa)
ppkPolyphosphate kinase; 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. (684 aa)
Your Current Organism:
Pelosinus sp. UFO1
NCBI taxonomy Id: 484770
Other names: P. sp. UFO1, Pelosinus lilaceae
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.