STRINGSTRING
Sare_0273 Sare_0273 nuoB1 nuoB1 Sare_0463 Sare_0463 nuoH nuoH nuoI nuoI Sare_0469 Sare_0469 nuoK nuoK Sare_0471 Sare_0471 Sare_0472 Sare_0472 nuoN nuoN Sare_0648 Sare_0648 Sare_0708 Sare_0708 Sare_0710 Sare_0710 Sare_0711 Sare_0711 nuoK-2 nuoK-2 Sare_0713 Sare_0713 Sare_0714 Sare_0714 nuoN-2 nuoN-2 Sare_0848 Sare_0848 Sare_0983 Sare_0983 ppk ppk Sare_1705 Sare_1705 Sare_1706 Sare_1706 Sare_1707 Sare_1707 Sare_2271 Sare_2271 Sare_2295 Sare_2295 Sare_2481 Sare_2481 Sare_2482 Sare_2482 Sare_3312 Sare_3312 ctaB ctaB Sare_3524 Sare_3524 Sare_3525 Sare_3525 Sare_3526 Sare_3526 Sare_3527 Sare_3527 Sare_3532 Sare_3532 atpC atpC atpD atpD atpG atpG atpA atpA atpH atpH atpF atpF atpE atpE atpB atpB Sare_4150 Sare_4150 Sare_4151 Sare_4151 nuoN-3 nuoN-3 Sare_4451 Sare_4451 Sare_4452 Sare_4452 nuoK-3 nuoK-3 Sare_4454 Sare_4454 nuoI-2 nuoI-2 nuoH-2 nuoH-2 Sare_4457 Sare_4457 Sare_4458 Sare_4458 Sare_4459 Sare_4459 nuoD1 nuoD1 nuoC nuoC nuoB2 nuoB2 nuoA nuoA Sare_4697 Sare_4697 nuoD2 nuoD2 ppa ppa
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:
Sare_0273PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: stp:Strop_0233 FAD-dependent pyridine nucleotide-disulphide oxidoreductase. (395 aa)
nuoB1NADH-quinone oxidoreductase, B subunit; 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. (188 aa)
Sare_0463NADH dehydrogenase (ubiquinone) 30 kDa 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 30 kDa subunit family. (235 aa)
nuoHNADH dehydrogenase (quinone); 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. (320 aa)
nuoI4Fe-4S ferredoxin iron-sulfur binding domain protein; 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. (216 aa)
Sare_0469NADH-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. (200 aa)
nuoKNADH-ubiquinone oxidoreductase chain 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. (118 aa)
Sare_0471KEGG: stp:Strop_0403 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (646 aa)
Sare_0472KEGG: stp:Strop_0404 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (503 aa)
nuoNNADH dehydrogenase (quinone); 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. (514 aa)
Sare_0648NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (125 aa)
Sare_0708NADH-ubiquinone/plastoquinone oxidoreductase chain 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. (114 aa)
Sare_0710PFAM: respiratory-chain NADH dehydrogenase subunit 1; KEGG: stp:Strop_0768 respiratory-chain NADH dehydrogenase, subunit 1. (309 aa)
Sare_0711Conserved hypothetical protein; 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. (187 aa)
nuoK-2NADH-ubiquinone oxidoreductase chain 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. (100 aa)
Sare_0713NADH dehydrogenase (quinone); PFAM: NADH/Ubiquinone/plastoquinone (complex I); KEGG: stp:Strop_0771 NADH dehydrogenase (quinone). (621 aa)
Sare_0714KEGG: stp:Strop_0772 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (496 aa)
nuoN-2NADH dehydrogenase (quinone); 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. (462 aa)
Sare_0848PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: stp:Strop_0905 FAD-dependent pyridine nucleotide-disulphide oxidoreductase. (441 aa)
Sare_0983Cytochrome c oxidase subunit I type; 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. (585 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. (769 aa)
Sare_1705TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: stp:Strop_1708 succinate dehydrogenase and fumarate reductase iron-sulfur protein. (251 aa)
Sare_1706KEGG: stp:Strop_1709 succinate dehydrogenase or fumarate reductase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein. (643 aa)
Sare_1707TIGRFAM: succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family; KEGG: stp:Strop_1710 succinate dehydrogenase (or fumarate reductase) cytochrome b subunit, b558 family. (230 aa)
Sare_2271PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: stp:Strop_2124 FAD-dependent pyridine nucleotide-disulphide oxidoreductase. (433 aa)
Sare_2295Cytochrome c oxidase subunit I type; 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. (666 aa)
Sare_2481KEGG: stp:Strop_2338 cytochrome d ubiquinol oxidase, subunit II; TIGRFAM: cytochrome d ubiquinol oxidase, subunit II; PFAM: cytochrome bd ubiquinol oxidase subunit II. (332 aa)
Sare_2482PFAM: cytochrome bd ubiquinol oxidase subunit I; KEGG: stp:Strop_2339 cytochrome bd ubiquinol oxidase, subunit I. (470 aa)
Sare_3312PFAM: cytochrome oxidase assembly; KEGG: stp:Strop_3085 cytochrome oxidase assembly. (325 aa)
ctaBProtoheme IX farnesyltransferase; 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. (317 aa)
Sare_3524PFAM: Cytochrome b/b6 domain; KEGG: stp:Strop_3292 cytochrome b/b6, N-terminal domain. (536 aa)
Sare_3525PFAM: Rieske [2Fe-2S] domain protein; KEGG: stp:Strop_3293 Rieske (2Fe-2S) domain protein. (361 aa)
Sare_3526PFAM: cytochrome c class I; KEGG: stp:Strop_3294 cytochrome c, class I. (277 aa)
Sare_3527PFAM: cytochrome c oxidase subunit III; KEGG: stp:Strop_3295 cytochrome c oxidase, subunit III. (199 aa)
Sare_3532Cytochrome 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). (323 aa)
atpCH+transporting two-sector ATPase delta/epsilon subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. (94 aa)
atpDATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. (485 aa)
atpGATP synthase F1, gamma subunit; 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. (309 aa)
atpAATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family. (550 aa)
atpHATP synthase F1, delta subunit; 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; Belongs to the ATPase delta chain family. (274 aa)
atpFATP synthase F0, B subunit; 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. (179 aa)
atpEH+transporting two-sector ATPase C subunit; 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. (77 aa)
atpBATP synthase F0, A subunit; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. (265 aa)
Sare_4150PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase; KEGG: stp:Strop_3768 succinate dehydrogenase. (637 aa)
Sare_4151TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; KEGG: stp:Strop_3769 succinate dehydrogenase and fumarate reductase iron-sulfur protein. (366 aa)
nuoN-3Proton-translocating NADH-quinone oxidoreductase, chain 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 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. (517 aa)
Sare_4451KEGG: stp:Strop_4053 proton-translocating NADH-quinone oxidoreductase, chain M; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain M; PFAM: NADH/Ubiquinone/plastoquinone (complex I). (510 aa)
Sare_4452KEGG: stp:Strop_4054 proton-translocating NADH-quinone oxidoreductase, chain L; TIGRFAM: proton-translocating NADH-quinone oxidoreductase, chain L; PFAM: NADH-Ubiquinone oxidoreductase (complex I) chain 5/L domain protein; NADH/Ubiquinone/plastoquinone (complex I). (651 aa)
nuoK-3NADH-ubiquinone oxidoreductase chain 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. (105 aa)
Sare_4454NADH-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. (256 aa)
nuoI-2NADH-quinone oxidoreductase, chain I; 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. (211 aa)
nuoH-2NADH dehydrogenase (quinone); 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. (448 aa)
Sare_4457NADH-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. (839 aa)
Sare_4458NADH-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. (443 aa)
Sare_4459TIGRFAM: NADH-quinone oxidoreductase, E subunit; PFAM: NADH dehydrogenase (ubiquinone) 24 kDa subunit; KEGG: stp:Strop_4061 NADH-quinone oxidoreductase, E subunit. (305 aa)
nuoD1NADH dehydrogenase I, D subunit; 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. (441 aa)
nuoCNADH (or F420H2) 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 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. (245 aa)
nuoB2NADH-quinone oxidoreductase, B subunit; 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. (226 aa)
nuoANADH-ubiquinone/plastoquinone oxidoreductase chain 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. (121 aa)
Sare_4697PFAM: UbiA prenyltransferase; KEGG: stp:Strop_4267 UbiA prenyltransferase; Belongs to the UbiA prenyltransferase family. (303 aa)
nuoD2NADH dehydrogenase (quinone); 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. (385 aa)
ppaInorganic diphosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (168 aa)
Your Current Organism:
Salinispora arenicola
NCBI taxonomy Id: 391037
Other names: S. arenicola CNS-205, Salinispora arenicola CNS-205, Salinispora arenicola str. CNS-205, Salinispora arenicola strain CNS-205
Server load: low (32%) [HD]