STRINGSTRING
APD08830.1 APD08830.1 APD08836.1 APD08836.1 APD08884.1 APD08884.1 APD08615.1 APD08615.1 APD08424.1 APD08424.1 APD08423.1 APD08423.1 APD08261.1 APD08261.1 APD08260.1 APD08260.1 APD08930.1 APD08930.1 APD09215.1 APD09215.1 APD09216.1 APD09216.1 APD09218.1 APD09218.1 APD09250.1 APD09250.1 APD09251.1 APD09251.1 APD09282.1 APD09282.1 APD09473.1 APD09473.1 APD09475.1 APD09475.1 APD09476.1 APD09476.1 APD09706.1 APD09706.1 nuoI nuoI APD09712.1 APD09712.1 APD09713.1 APD09713.1 APD09714.1 APD09714.1 nuoB nuoB APD09851.1 APD09851.1 APD09889.1 APD09889.1 sdhB sdhB APD08625.1 APD08625.1 APD08633.1 APD08633.1 APD08639.1 APD08639.1 APD08640.1 APD08640.1 dgk dgk dck dck
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:
APD08830.1Cytochrome C SoxX. (186 aa)
APD08836.1Cytochrome C-552. (148 aa)
APD08884.1Cytochrome C-552 like protein. (231 aa)
APD08615.1Hypothetical protein. (383 aa)
APD08424.1Ba3-type cytochrome C oxidase polypeptide I; Belongs to the heme-copper respiratory oxidase family. (562 aa)
APD08423.1Ba3-type cytochrome C oxidase polypeptide II. (168 aa)
APD08261.1NADH-quinone oxidoreductase subunit 1. (490 aa)
APD08260.1NADH-quinone oxidoreductase subunit 3. (200 aa)
APD08930.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase FolK. (159 aa)
APD09215.1Cytochrome C. (241 aa)
APD09216.1Cytochrome C. (160 aa)
APD09218.1Quinol-cytochrome C reductase cytochrome b subunit. (420 aa)
APD09250.1Cytochrome Caa3 oxidase subunit I; Belongs to the heme-copper respiratory oxidase family. (791 aa)
APD09251.1Cytochrome Caa3 oxidase subunit IIC; 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). (337 aa)
APD09282.1Cytochrome C-552. (142 aa)
APD09473.1Class III cytochrome C family protein. (211 aa)
APD09475.1Hypothetical protein. (172 aa)
APD09476.1Hypothetical protein. (170 aa)
APD09706.1NADH-quinone oxidoreductase subunit 13. (469 aa)
nuoINADH-quinone oxidoreductase subunit 9; 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. (182 aa)
APD09712.1NADH-quinone oxidoreductase subunit 3; 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. (783 aa)
APD09713.1NADH-quinone oxidoreductase subunit 1; 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. (437 aa)
APD09714.1NADH-quinone oxidoreductase subunit 2. (181 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. 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. (181 aa)
APD09851.1Cytochrome C-552. (125 aa)
APD09889.1Succinate dehydrogenase cytochrome subunit. (121 aa)
sdhBSuccinate dehydrogenase iron-sulfur subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (232 aa)
APD08625.1Cytochrome C-552. (262 aa)
APD08633.1Cytochrome C-552. (142 aa)
APD08639.1Ba3-type cytochrome C oxidase polypeptide II. (180 aa)
APD08640.1Ba3-type cytochrome C oxidase polypeptide I. (561 aa)
dgkDeoxyguanosine kinase. (199 aa)
dckDeoxyadenosine/deoxycytidine kinase. (202 aa)
Your Current Organism:
Thermus brockianus
NCBI taxonomy Id: 56956
Other names: JCM 11602, NCIB 12676, NCIB:12676, NCIMB 12676, T. brockianus, strain YS38
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