PP_3130 protein (Pseudomonas putida KT2440) - STRING interaction network

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.

Knowledge-based Evidence

from curated databases

textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Input:

Neighborhood

Gene Fusion

Co-occurrence

Co-expression

Experiments

Databases

Textmining

[Homology]

Score

PP_3130

Homologs of previously reported genes of unknown function. (868 aa)

Predicted Functional Partners:

nuoC

0.954

PP_3131

0.834

PP_0103

0.681

gltB

0.634

nuoA

0.628

PP_0550

0.624

nuoN

0.598

PP_3132

0.589

nuoB

0.559

galE

0.557

Your Current Organism:

Pseudomonas putida KT2440

NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440

Export your current network:

... as a bitmap image:

download

file format is 'PNG': portable network graphic

... as a high-resolution bitmap:

download

same PNG format, but at higher resolution

... as a vector graphic:

download

SVG: scalable vector graphic - can be opened and edited in Illustrator, CorelDraw, Dia, etc

... as short tabular text output:

download

TSV: tab separated values - can be opened in Excel and Cytoscape (lists only one-way edges: A-B)

... as tabular text output:

download

TSV: tab separated values - can be opened in Excel (lists reciprocal edges: A-B,B-A)

... as an XML summary:

download

structured XML interaction data, according to the 'PSI-MI' data standard

... protein node degrees:

download

node degree of proteins in your network (given the current score cut-off)

... network coordinates:

download

a flat-file format describing the coordinates and colors of nodes in the network

... protein sequences:

download

MFA: multi-fasta format - containing the aminoacid sequences in the network

... protein annotations:

download

a tab-delimited file describing the names, domains and descriptions of proteins in your network

... functional annotations:

download

a tab-delimited file containing all known functional terms of proteins in your network

Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
PP_0103	PP_0550	PP_0103	PP_0550	Cytochrome c oxidase subunit 2; 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).	Homologs of previously reported genes of unknown function.	0.864
PP_0103	PP_3130	PP_0103	PP_3130	Cytochrome c oxidase subunit 2; 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).	Homologs of previously reported genes of unknown function.	0.681
PP_0103	nuoA	PP_0103	PP_4119	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit A; 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.	0.979
PP_0103	nuoB	PP_0103	PP_4120	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase 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 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.	0.938
PP_0103	nuoC	PP_0103	PP_4121	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit C/D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.	0.997
PP_0103	nuoN	PP_0103	PP_4131	Cytochrome c oxidase subunit 2; 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).	NADH-quinone oxidoreductase subunit 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 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.	0.975
PP_0550	PP_0103	PP_0550	PP_0103	Homologs of previously reported genes of unknown function.	Cytochrome c oxidase subunit 2; 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).	0.864
PP_0550	PP_3130	PP_0550	PP_3130	Homologs of previously reported genes of unknown function.	Homologs of previously reported genes of unknown function.	0.624
PP_0550	gltB	PP_0550	PP_5076	Homologs of previously reported genes of unknown function.	L-glutamate synthase(NADPH) alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Glutamate family.	0.488
PP_0550	nuoA	PP_0550	PP_4119	Homologs of previously reported genes of unknown function.	NADH-quinone oxidoreductase subunit A; 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.	0.838
PP_0550	nuoB	PP_0550	PP_4120	Homologs of previously reported genes of unknown function.	NADH-quinone oxidoreductase 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 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.	0.948
PP_0550	nuoC	PP_0550	PP_4121	Homologs of previously reported genes of unknown function.	NADH-quinone oxidoreductase subunit C/D; 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; In the N-terminal section; belongs to the complex I 30 kDa subunit family.	0.999
PP_0550	nuoN	PP_0550	PP_4131	Homologs of previously reported genes of unknown function.	NADH-quinone oxidoreductase subunit 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 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.	0.812
PP_3130	PP_0103	PP_3130	PP_0103	Homologs of previously reported genes of unknown function.	Cytochrome c oxidase subunit 2; 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).	0.681
PP_3130	PP_0550	PP_3130	PP_0550	Homologs of previously reported genes of unknown function.	Homologs of previously reported genes of unknown function.	0.624
PP_3130	PP_3131	PP_3130	PP_3131	Homologs of previously reported genes of unknown function.	Homologs of previously reported genes of unknown function.	0.834
PP_3130	PP_3132	PP_3130	PP_3132	Homologs of previously reported genes of unknown function.	Putative Polysaccharide transporter; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology.	0.589
PP_3130	galE	PP_3130	PP_3129	Homologs of previously reported genes of unknown function.	UDP-glucose 4-epimerase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the NAD(P)-dependent epimerase/dehydratase family.	0.557
PP_3130	gltB	PP_3130	PP_5076	Homologs of previously reported genes of unknown function.	L-glutamate synthase(NADPH) alpha subunit; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Aminoacidbiosynthesis : Glutamate family.	0.634
PP_3130	nuoA	PP_3130	PP_4119	Homologs of previously reported genes of unknown function.	NADH-quinone oxidoreductase subunit A; 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.	0.628