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Sps_00540 Sps_00540 Sps_01408 Sps_01408 Sps_01409 Sps_01409 Sps_01835 Sps_01835 ilvA ilvA ilvD ilvD ilvE ilvE Sps_03126 Sps_03126 Sps_03127 Sps_03127 Sps_03128 Sps_03128 Sps_03227 Sps_03227 leuD leuD leuC leuC leuB leuB leuA leuA
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.
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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:
Sps_00540'PFAM: Glutamate/Leucine/Phenylalanine/Valine dehydrogenase; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain'. (344 aa)
Sps_01408Acetolactate synthase, large subunit; 'PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain'; 'TIGRFAM: acetolactate synthase, large subunit, biosynthetic type'. (573 aa)
Sps_01409PFAM: Small subunit of acetolactate synthase; ACT domain; 'TIGRFAM: acetolactate synthase, small subunit'. (164 aa)
Sps_01835Valine-pyruvate aminotransferase apoenzyme; PFAM: Aminotransferase class I and II. (416 aa)
ilvAL-threonine ammonia-lyase; 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. (516 aa)
ilvDPFAM: Dehydratase family; TIGRFAM: dihydroxy-acid dehydratase; Belongs to the IlvD/Edd family. (616 aa)
ilvEBranched chain amino acid aminotransferase apoenzyme; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (307 aa)
Sps_03126Acetolactate synthase, small subunit; PFAM: ACT domain. (75 aa)
Sps_03127Acetolactate synthase, large subunit; 'PFAM: Thiamine pyrophosphate enzyme, central domain; Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; Thiamine pyrophosphate enzyme, C-terminal TPP binding domain'; 'TIGRFAM: acetolactate synthase, large subunit, biosynthetic type'. (579 aa)
Sps_03128Ketol-acid reductoisomerase; 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. (521 aa)
Sps_03227PFAM: Aminotransferase class IV; 'TIGRFAM: branched-chain amino acid aminotransferase, group II'. (362 aa)
leuD3-isopropylmalate dehydratase, small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (201 aa)
leuC3-isopropylmalate dehydratase, large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. (466 aa)
leuB3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. (364 aa)
leuA2-isopropylmalate synthase; 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 1 subfamily. (523 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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