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AMA50804.1 AMA50804.1 AMA52180.1 AMA52180.1 AMA52181.1 AMA52181.1 AMA52769.1 AMA52769.1 qcrB qcrB AMA53208.1 AMA53208.1 AMA53209.1 AMA53209.1 sdhB sdhB sdhC sdhC AMA54022.1 AMA54022.1 qoxB qoxB AMA54323.1 AMA54323.1 AMA50739.1 AMA50739.1 AMA50740.1 AMA50740.1
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:
AMA50804.12-amino-4-hydroxy-6- hydroxymethyldihydropteridine pyrophosphokinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (167 aa)
AMA52180.1Cytochrome B; 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). (356 aa)
AMA52181.1Cytochrome ubiquinol 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. (622 aa)
AMA52769.1Cytochrome C oxidase Cbb3; Component of the menaquinol-cytochrome c reductase complex. (255 aa)
qcrBCytochrome b6; Electron transport protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (224 aa)
AMA53208.1Protease; Derived by automated computational analysis using gene prediction method: Protein Homology. (422 aa)
AMA53209.1Peptidase U32; Derived by automated computational analysis using gene prediction method: Protein Homology. (309 aa)
sdhBPart of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (253 aa)
sdhCSuccinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (202 aa)
AMA54022.1Derived by automated computational analysis using gene prediction method: Protein Homology. (112 aa)
qoxBCytochrome ubiquinol oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. (649 aa)
AMA54323.1Cytochrome ubiquinol oxidase subunit II; Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Subunit II transfers the electrons from a quinol to the binuclear center of the catalytic subunit I. (318 aa)
AMA50739.1Deoxycytidine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (217 aa)
AMA50740.1Deoxyguanosine kinase; Derived by automated computational analysis using gene prediction method: Protein Homology. (207 aa)
Your Current Organism:
Bacillus subtilis inaquosorum
NCBI taxonomy Id: 483913
Other names: B. subtilis subsp. inaquosorum, BGSC 3A28, Bacillus subtilis subsp. inaquosorum, Bacillus subtilis subsp. inaquosorum Rooney et al. 2009, DSM 22148, KCTC 13429, NRRL B-23052
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