STRINGSTRING
OLR19200.1 OLR19200.1 fadA fadA fadB fadB OLR19512.1 OLR19512.1 fadE fadE OLR20116.1 OLR20116.1 fadI fadI fadJ fadJ OLR20452.1 OLR20452.1 OLR21082.1 OLR21082.1 OLR21182.1 OLR21182.1 OLR21262.1 OLR21262.1 norV norV lplT lplT aas aas OLR18193.1 OLR18193.1 OLR18675.1 OLR18675.1 OLR18758.1 OLR18758.1 tsgA tsgA
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:
OLR19200.1Lactaldehyde reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (382 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. (387 aa)
fadBMultifunctional fatty acid oxidation complex subunit alpha; 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. (729 aa)
OLR19512.1isovaleryl-CoA dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (539 aa)
fadEacyl-CoA dehydrogenase; Functions in fatty acid oxidation; converts acyl-CoA and FAD to FADH2 and delta2-enoyl-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology. (817 aa)
OLR20116.1Zinc-binding dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (343 aa)
fadI3-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. (436 aa)
fadJMultifunctional fatty acid oxidation complex subunit alpha; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. (718 aa)
OLR20452.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. (402 aa)
OLR21082.1S-(hydroxymethyl)glutathione dehydrogenase/class III alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (372 aa)
OLR21182.1Bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (892 aa)
OLR21262.1long-chain-fatty-acid--CoA ligase; Derived by automated computational analysis using gene prediction method: Protein Homology. (572 aa)
norVNitric oxide reductase; Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase; In the N-terminal section; belongs to the zinc metallo- hydrolase group 3 family. (481 aa)
lplTLysophospholipid transporter LplT; Catalyzes the facilitated diffusion of 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) into the cell; Belongs to the major facilitator superfamily. LplT (TC 2.A.1.42) family. (397 aa)
aasBifunctional 2-acylglycerophosphoethanolamine acyltransferase/acyl-ACP synthetase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1; In the C-terminal section; belongs to the ATP-dependent AMP-binding enzyme family. (719 aa)
OLR18193.1acetyl-CoA acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
OLR18675.1L-fucose:H+ symporter permease; Derived by automated computational analysis using gene prediction method: Protein Homology. (443 aa)
OLR18758.1L-threonine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (383 aa)
tsgAMFS transporter TsgA; Derived by automated computational analysis using gene prediction method: Protein Homology. (394 aa)
Your Current Organism:
Enterobacter kobei
NCBI taxonomy Id: 208224
Other names: ATCC BAA-260, CCUG 49023, CIP 105566, DSM 13645, E. kobei, Enterobacter sp. 35730, Enterobacter sp. 42202, Enterobacter sp. 44593, Enterobacter sp. GN02186, Enterobacter sp. GN02204, Enterobacter sp. GN02225, Enterobacter sp. GN02266, Enterobacter sp. GN02275, Enterobacter sp. GN02366, Enterobacter sp. GN02454, Enterobacter sp. GN02825, Enterobacter sp. GN03191, JCM 8580, NIH group 21
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