STRINGSTRING
dsdA dsdA kbl kbl tdh tdh gpmI gpmI ghrB ghrB ADO46520.1 ADO46520.1 ADO46521.1 ADO46521.1 ADO46522.1 ADO46522.1 asd asd ADO46858.1 ADO46858.1 ADO46863.1 ADO46863.1 ADO46918.1 ADO46918.1 ADO46919.1 ADO46919.1 ADO47114.1 ADO47114.1 gcvT gcvT gcvH gcvH gcvP gcvP ADO47194.1 ADO47194.1 ADO47428.1 ADO47428.1 glyA glyA ADO47553.1 ADO47553.1 ADO48234.1 ADO48234.1 ADO48561.1 ADO48561.1 ADO48675.1 ADO48675.1 trpB trpB trpA trpA ghrA ghrA serC serC ADO49167.1 ADO49167.1 gpmA gpmA ADO49745.1 ADO49745.1 ADO49853.1 ADO49853.1 ADO49920.1 ADO49920.1 ADO49955.1 ADO49955.1 thrB thrB ADO49957.1 ADO49957.1 gpmB gpmB ADO49986.1 ADO49986.1 ADO50375.1 ADO50375.1 ilvA ilvA ADO50564.1 ADO50564.1
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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
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
dsdATIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (434 aa)
kbl2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
tdhL-threonine 3-dehydrogenase; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate; Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)
gpmIPhosphoglycerate mutase, 2,3-bisphosphoglycerate-independent; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (515 aa)
ghrBD-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. GhrB subfamily. (323 aa)
ADO46520.1PFAM: Pyridoxal-dependent decarboxylase; KEGG: ebi:EbC_22090 L-2,4-diaminobutyrate decarboxylase. (487 aa)
ADO46521.12,4-diaminobutyrate 4-transaminase; KEGG: pct:PC1_2060 diaminobutyrate--2-oxoglutarate aminotransferase; TIGRFAM: 2,4-diaminobutyrate 4-transaminase; PFAM: aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (460 aa)
ADO46522.1TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; KEGG: ssn:SSON_4202 aspartate kinase III; PFAM: aspartate/glutamate/uridylate kinase; Belongs to the aspartokinase family. (453 aa)
asdAspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (368 aa)
ADO46858.1Pyridoxal-5'-phosphate-dependent protein beta subunit; 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. (329 aa)
ADO46863.1TIGRFAM: L-serine dehydratase 1; KEGG: cko:CKO_04512 hypothetical protein; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
ADO46918.1PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; KEGG: enc:ECL_02361 cystathionine gamma-lyase. (382 aa)
ADO46919.1KEGG: enc:ECL_02360 cystathionine beta-synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; CBS domain containing protein; SMART: CBS domain containing protein. (457 aa)
ADO47114.1PFAM: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase catalytic region; amino acid-binding ACT domain protein; KEGG: kpu:KP1_4635 D-3-phosphoglycerate dehydrogenase. (410 aa)
gcvTGlycine cleavage system T protein; The glycine cleavage system catalyzes the degradation of glycine. (364 aa)
gcvHGlycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (129 aa)
gcvPGlycine dehydrogenase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. (957 aa)
ADO47194.1TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_3250 L-serine dehydratase 1; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. (455 aa)
ADO47428.1KEGG: kva:Kvar_1155 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase. (451 aa)
glyAGlycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (417 aa)
ADO47553.1TIGRFAM: glycerate kinase; KEGG: stt:t0367 hypothetical protein; PFAM: glycerate kinase; Belongs to the glycerate kinase type-1 family. (379 aa)
ADO48234.1TIGRFAM: L-serine dehydratase 1; KEGG: ent:Ent638_2383 L-serine ammonia-lyase; PFAM: serine dehydratase alpha chain; serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. (454 aa)
ADO48561.1PFAM: short-chain dehydrogenase/reductase SDR; KEGG: ent:Ent638_1939 3-hydroxy acid dehydrogenase; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (249 aa)
ADO48675.1KEGG: kva:Kvar_2900 primary-amine oxidase; PFAM: Copper amine oxidase domain-containing protein; Copper amine oxidase N3-terminal; copper amine oxidase-like domain-containing protein; Copper amine oxidase N2-terminal. (755 aa)
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (397 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (269 aa)
ghrAD-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. (312 aa)
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (362 aa)
ADO49167.1KEGG: ent:Ent638_1386 L-threonine aldolase; PFAM: aromatic amino acid beta-eliminating lyase/threonine aldolase. (333 aa)
gpmAPhosphoglycerate mutase 1 family; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. (250 aa)
ADO49745.1TIGRFAM: glycerate kinase; KEGG: glycerate kinase GclK; PFAM: glycerate kinase; Belongs to the glycerate kinase type-1 family. (379 aa)
ADO49853.1KEGG: sed:SeD_A0167 dihydrolipoamide dehydrogenase; TIGRFAM: dihydrolipoamide dehydrogenase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region. (474 aa)
ADO49920.1PFAM: D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding; D-isomer specific 2-hydroxyacid dehydrogenase catalytic region; KEGG: kpe:KPK_4701 D-isomer specific 2-hydroxyacid dehydrogenase family protein. (315 aa)
ADO49955.1TIGRFAM: threonine synthase; KEGG: cko:CKO_03383 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (428 aa)
thrBHomoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa)
ADO49957.1Aspartate kinase; KEGG: kpu:KP1_0820 bifunctional aspartokinase I/homeserine dehydrogenase I; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. (820 aa)
gpmBPFAM: Phosphoglycerate mutase; KEGG: kpn:KPN_04850 phosphoglycerate mutase; Belongs to the phosphoglycerate mutase family. GpmB subfamily. (215 aa)
ADO49986.1TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); KEGG: ect:ECIAI39_4920 phosphoserine phosphatase; PFAM: Haloacid dehalogenase domain protein hydrolase. (323 aa)
ADO50375.1TIGRFAM: aspartate kinase; aspartate kinase, monofunctional class; KEGG: cko:CKO_03894 aspartate kinase III; PFAM: aspartate/glutamate/uridylate kinase; amino acid-binding ACT domain protein; Belongs to the aspartokinase family. (449 aa)
ilvAThreonine dehydratase, biosynthetic; 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. (514 aa)
ADO50564.1Aspartate kinase; KEGG: cko:CKO_03054 bifunctional aspartate kinase II/homoserine dehydrogenase II; TIGRFAM: aspartate kinase; PFAM: homoserine dehydrogenase; aspartate/glutamate/uridylate kinase; homoserine dehydrogenase NAD-binding; In the C-terminal section; belongs to the homoserine dehydrogenase family. (810 aa)
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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