STRINGSTRING
aspC_1 aspC_1 leuD leuD leuC leuC leuB leuB ilvC ilvC ilvH ilvH ilvB1 ilvB1 ilvD ilvD ilvA ilvA GCA_900049755_01138 GCA_900049755_01138 aruI aruI aspC_2 aspC_2 Csp1_14400 Csp1_14400 leuA leuA hicd hicd ycfT ycfT ilvE ilvE
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:
aspC_1Unannotated protein. (459 aa)
leuDUnannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (208 aa)
leuCUnannotated protein; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (507 aa)
leuBUnannotated protein. (353 aa)
ilvCUnannotated protein; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. (337 aa)
ilvHUnannotated protein. (168 aa)
ilvB1Unannotated protein. (618 aa)
ilvDUnannotated protein; Belongs to the IlvD/Edd family. (617 aa)
ilvAUnannotated protein; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. (512 aa)
GCA_900049755_01138Unannotated protein. (156 aa)
aruIUnannotated protein; Belongs to the TPP enzyme family. (402 aa)
aspC_2Unannotated protein. (419 aa)
Csp1_14400Unannotated protein. (197 aa)
leuAUnannotated protein; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily. (609 aa)
hicdUnannotated protein. (387 aa)
ycfTUnannotated protein. (355 aa)
ilvEUnannotated protein. (381 aa)
Your Current Organism:
Corynebacterium provencense
NCBI taxonomy Id: 1737425
Other names: C. provencense, CSUR P2161, Corynebacterium sp. SN15, DSM 101074, strain Marseille-P2161, strain SN15
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.