STRINGSTRING
SEB60609.1 SEB60609.1 SEB60992.1 SEB60992.1 SEB61996.1 SEB61996.1 SEB62210.1 SEB62210.1 SEB64496.1 SEB64496.1 SEB65689.1 SEB65689.1 SEB65758.1 SEB65758.1 SEB66376.1 SEB66376.1 SEB97842.1 SEB97842.1 fadA fadA fadB fadB SEC10752.1 SEC10752.1 SEC10921.1 SEC10921.1 SEC11436.1 SEC11436.1 SEC34702.1 SEC34702.1 SEC90147.1 SEC90147.1 SED25181.1 SED25181.1 SED33691.1 SED33691.1 SED37461.1 SED37461.1 SED39019.1 SED39019.1 SED41443.1 SED41443.1 SED42118.1 SED42118.1 SED46424.1 SED46424.1 SED58783.1 SED58783.1 SED59027.1 SED59027.1 SED64493.1 SED64493.1 SED65212.1 SED65212.1 SED65730.1 SED65730.1
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:
SEB60609.1Enoyl-CoA hydratase/carnithine racemase. (261 aa)
SEB60992.1fatty-acyl-CoA synthase. (617 aa)
SEB61996.1enoyl-CoA hydratase. (250 aa)
SEB62210.1acetyl-CoA C-acetyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (402 aa)
SEB64496.1Short chain enoyl-CoA hydratase /Enoyl-CoA hydratase; Belongs to the enoyl-CoA hydratase/isomerase family. (263 aa)
SEB65689.1Enoyl-CoA hydratase/carnithine racemase. (368 aa)
SEB65758.1Short chain enoyl-CoA hydratase; Belongs to the enoyl-CoA hydratase/isomerase family. (257 aa)
SEB66376.1enoyl-CoA hydratase. (270 aa)
SEB97842.12-oxoglutaroyl-CoA hydrolase. (267 aa)
fadA3-ketoacyl-CoA thiolase; Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. (391 aa)
fadBShort chain enoyl-CoA hydratase; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (715 aa)
SEC10752.1enoyl-CoA hydratase. (229 aa)
SEC10921.1Short chain enoyl-CoA hydratase. (714 aa)
SEC11436.1citronellyl-CoA synthetase. (612 aa)
SEC34702.1Enoyl-CoA hydratase/carnithine racemase. (249 aa)
SEC90147.1Citronellol/citronellal dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (274 aa)
SED25181.1Enoyl-CoA hydratase/carnithine racemase. (370 aa)
SED33691.1acetyl-CoA acyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (394 aa)
SED37461.1Enoyl-CoA hydratase/carnithine racemase. (263 aa)
SED39019.1Citronellol/citronellal dehydrogenase. (289 aa)
SED41443.1Enoyl-CoA hydratase. (260 aa)
SED42118.1Short chain enoyl-CoA hydratase; Belongs to the enoyl-CoA hydratase/isomerase family. (257 aa)
SED46424.1hydroxymethylglutaryl-CoA lyase. (299 aa)
SED58783.1Short chain enoyl-CoA hydratase; Belongs to the enoyl-CoA hydratase/isomerase family. (258 aa)
SED59027.1acetyl-CoA C-acetyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (400 aa)
SED64493.1enoyl-CoA hydratase. (272 aa)
SED65212.1acetyl-CoA C-acetyltransferase; Belongs to the thiolase-like superfamily. Thiolase family. (395 aa)
SED65730.1crotonobetainyl-CoA hydratase; Belongs to the enoyl-CoA hydratase/isomerase family. (258 aa)
Your Current Organism:
Pseudomonas mohnii
NCBI taxonomy Id: 395600
Other names: Arthrobacter sp. BDR2P2B2-M, CCUG 53115, DSM 18327, P. mohnii, Pseudomonas mohnii Camara et al. 2007, strain IpA-2
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