STRINGSTRING
ADO47343.1 ADO47343.1 ADO47321.1 ADO47321.1 ADO47189.1 ADO47189.1 lysA lysA ADO47129.1 ADO47129.1 ADO47111.1 ADO47111.1 ADO47079.1 ADO47079.1 ADO47017.1 ADO47017.1 ADO46918.1 ADO46918.1 patA patA ADO46858.1 ADO46858.1 ADO46831.1 ADO46831.1 argD argD ADO46636.1 ADO46636.1 ADO46631.1 ADO46631.1 ADO46596.1 ADO46596.1 ADO46590.1 ADO46590.1 ADO46562.1 ADO46562.1 dsdA dsdA ADO46307.1 ADO46307.1 ADO46563.1 ADO46563.1 ADO46323.1 ADO46323.1 kbl kbl ADO46447.1 ADO46447.1 ADO46520.1 ADO46520.1 ADO46521.1 ADO46521.1 ADO50580.1 ADO50580.1 ADO50565.1 ADO50565.1 ADO50502.1 ADO50502.1 ilvA ilvA ADO50380.1 ADO50380.1 ADO50350.1 ADO50350.1 ADO50349.1 ADO50349.1 ADO50048.1 ADO50048.1 ADO49955.1 ADO49955.1 ADO49898.1 ADO49898.1 ADO49889.1 ADO49889.1 hemL hemL btuF btuF ADO49742.1 ADO49742.1 dxs dxs ADO49587.1 ADO49587.1 ADO49578.1 ADO49578.1 ADO49454.1 ADO49454.1 ADO49432.1 ADO49432.1 ADO49347.1 ADO49347.1 bioA bioA bioF bioF ADO49166.1 ADO49166.1 serC serC ADO49105.1 ADO49105.1 ADO49098.1 ADO49098.1 ADO49033.1 ADO49033.1 ADO48945.1 ADO48945.1 ADO48877.1 ADO48877.1 ADO48834.1 ADO48834.1 argD-2 argD-2 ADO48687.1 ADO48687.1 ADO48640.1 ADO48640.1 ADO48565.1 ADO48565.1 ADO48480.1 ADO48480.1 ADO48462.1 ADO48462.1 sufS sufS ADO48285.1 ADO48285.1 ADO48255.1 ADO48255.1 ADO48014.1 ADO48014.1 ADO48013.1 ADO48013.1 ADO48012.1 ADO48012.1 ADO47994.1 ADO47994.1 glmS glmS glmE glmE hisC hisC menD menD ADO47700.1 ADO47700.1 ADO47625.1 ADO47625.1 ADO47620.1 ADO47620.1 ADO47600.1 ADO47600.1 eutC eutC ADO47582.1 ADO47582.1 ADO47524.1 ADO47524.1 iscS iscS glyA glyA
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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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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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Edges represent protein-protein associations
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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
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ADO47343.1PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; KEGG: ect:ECIAI39_2453 cystathionine gamma-synthase (CGS) (O-succinylhomoserine (thiol)-lyase). (408 aa)
ADO47321.1Transcriptional regulator, GntR family with aminotransferase domain; KEGG: cko:CKO_04020 hypothetical protein; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (450 aa)
ADO47189.1PFAM: aminotransferase class V; KEGG: enc:ECL_04136 cysteine sulfinate desulfinase. (401 aa)
lysADiaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (420 aa)
ADO47129.1Folate-binding protein YgfZ; Folate-binding protein involved in regulating the level of ATP-DnaA and in the modification of some tRNAs. It is probably a key factor in regulatory networks that act via tRNA modification, such as initiation of chromosomal replication; Belongs to the tRNA-modifying YgfZ family. (327 aa)
ADO47111.1TIGRFAM: methylmalonyl-CoA mutase, large subunit; KEGG: ect:ECIAI39_3331 methylmalonyl-CoA mutase; PFAM: methylmalonyl-CoA mutase; cobalamin B12-binding domain protein. (714 aa)
ADO47079.1Alanine racemase domain protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which is involved in PLP homeostasis. (239 aa)
ADO47017.1KEGG: cko:CKO_04402 cystathionine beta-lyase; TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein. (395 aa)
ADO46918.1PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein; KEGG: enc:ECL_02361 cystathionine gamma-lyase. (382 aa)
patAPutrescine aminotransferase; Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4- aminobutanal. Also functions as a cadaverine transaminase in a a L- lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. (459 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)
ADO46831.1PFAM: aminotransferase class I and II; KEGG: cko:CKO_04539 hypothetical protein. (392 aa)
argDSuccinylornithine transaminase family; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (407 aa)
ADO46636.1KEGG: ecx:EcHS_A3571 hypothetical protein. (363 aa)
ADO46631.1PFAM: alanine racemase domain protein; KEGG: cko:CKO_04801 hypothetical protein. (387 aa)
ADO46596.1Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. (797 aa)
ADO46590.1Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. (815 aa)
ADO46562.1Transcriptional regulator, GntR family with aminotransferase domain; KEGG: spe:Spro_4307 transcriptional regulator; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (492 aa)
dsdATIGRFAM: D-serine ammonia-lyase; KEGG: enc:ECL_00023 D-serine deaminase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (434 aa)
ADO46307.1KEGG: enc:ECL_00034 acetolactate synthase catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. (562 aa)
ADO46563.1KEGG: ent:Ent638_3864 4-aminobutyrate aminotransferase; TIGRFAM: 4-aminobutyrate aminotransferase; PFAM: aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (421 aa)
ADO46323.1KEGG: kpu:KP1_5432 2-aminoethylphosphonate transport system periplasmic binding component; TIGRFAM: 2-aminoethylphosphonate ABC transporter, 2-aminoethylphosphonate binding protein; PFAM: extracellular solute-binding protein family 1. (337 aa)
kbl2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
ADO46447.1PFAM: aminotransferase class I and II; KEGG: enc:ECL_00194 valine--pyruvate transaminase. (419 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)
ADO50580.1PFAM: MOSC domain containing protein; 3-alpha domain protein; KEGG: kpn:KPN_04218 hypothetical protein. (224 aa)
ADO50565.1O-succinylhomoserine (thiol)-lyase; KEGG: cro:ROD_38041 cystathionine gamma-synthase; TIGRFAM: O-succinylhomoserine (thiol)-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein. (386 aa)
ADO50502.1Manually curated; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; KEGG: enc:ECL_05014 acetolactate synthase 2 catalytic subunit; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. (548 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)
ADO50380.1Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. (1227 aa)
ADO50350.1Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (359 aa)
ADO50349.1Aromatic-amino-acid transaminase; KEGG: enc:ECL_00312 aromatic amino acid aminotransferase; PFAM: aminotransferase class I and II. (397 aa)
ADO50048.1Transcriptional regulator, GntR family with aminotransferase domain; KEGG: kpu:KP1_0709 putative aminotransferase; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (470 aa)
ADO49955.1TIGRFAM: threonine synthase; KEGG: cko:CKO_03383 threonine synthase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (428 aa)
ADO49898.1KEGG: kpe:KPK_4675 thiamine transporter substrate binding subunit; TIGRFAM: thiamine ABC transporter, periplasmic binding protein; ABC transporter, periplasmic binding protein, thiB subfamily; PFAM: extracellular solute-binding protein family 1. (327 aa)
ADO49889.1KEGG: kpe:KPK_4659 acetolactate synthase 3 catalytic subunit; TIGRFAM: acetolactate synthase, large subunit, biosynthetic type; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein. (574 aa)
hemLKEGG: kva:Kvar_4212 glutamate-1-semialdehyde-2,1-aminomutase; TIGRFAM: glutamate-1-semialdehyde-2,1-aminomutase; PFAM: aminotransferase class-III. (426 aa)
btuFPeriplasmic binding protein; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. (266 aa)
ADO49742.1KEGG: glycoxylate carboligase GclA; TIGRFAM: glyoxylate carboligase; PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; Belongs to the TPP enzyme family. (579 aa)
dxsDeoxyxylulose-5-phosphate synthase; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP); Belongs to the transketolase family. DXPS subfamily. (620 aa)
ADO49587.1KEGG: kpu:KP1_1294 putative GntR-family transcriptional regulator; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (475 aa)
ADO49578.1KEGG: kpe:KPK_4241 transcriptional regulator, GntR family/aminotransferase family protein; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (486 aa)
ADO49454.1Amino acid adenylation domain protein; KEGG: kpe:KPK_3973 enterobactin synthase subunit F; TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Thioesterase. (1289 aa)
ADO49432.1PFAM: aminotransferase class I and II; KEGG: kva:Kvar_3722 aminotransferase class I and II. (386 aa)
ADO49347.1TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; KEGG: kpu:KP1_1687 2-oxoglutarate dehydrogenase E1 component; PFAM: Transketolase central region; dehydrogenase E1 component. (935 aa)
bioAAdenosylmethionine-8-amino-7-oxononanoate aminotransferase; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (435 aa)
bioF8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. (384 aa)
ADO49166.1PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: cko:CKO_02209 pyruvate dehydrogenase; Belongs to the TPP enzyme family. (572 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)
ADO49105.1Aspartate transaminase; KEGG: esa:ESA_02414 aromatic amino acid aminotransferase; PFAM: aminotransferase class I and II. (396 aa)
ADO49098.1PFAM: MOSC domain containing protein; MOSC domain protein beta barrel domain protein; ferredoxin; KEGG: sea:SeAg_B1018 MOSC domain protein. (369 aa)
ADO49033.1KEGG: cro:ROD_34021 putative diaminopropionate ammonia-lyase; TIGRFAM: diaminopropionate ammonia-lyase; PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit. (399 aa)
ADO48945.1KEGG: kva:Kvar_3286 aminodeoxychorismate lyase; TIGRFAM: aminodeoxychorismate lyase; PFAM: aminotransferase class IV. (271 aa)
ADO48877.1PFAM: Pyridoxal-5'-phosphate-dependent protein beta subunit; KEGG: pct:PC1_2250 serine/threonine dehydratase. (322 aa)
ADO48834.1Glycogen/starch/alpha-glucan phosphorylase; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. (805 aa)
argD-2Succinylornithine transaminase family; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 aa)
ADO48687.1KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein. (1174 aa)
ADO48640.1Transcriptional regulator, GntR family with aminotransferase domain; KEGG: kpn:KPN_01929 transcription regulator GntR; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (481 aa)
ADO48565.1KEGG: etr:ETAE_0786 glutamate decarboxylase and related PLP-dependent protein. (570 aa)
ADO48480.1PFAM: aminotransferase class I and II; KEGG: enc:ECL_02037 putative aminotransferase. (389 aa)
ADO48462.1PFAM: aminotransferase class I and II; KEGG: kpn:KPN_01511 bifunctional PLP-dependent beta-cystathionase; repressor of maltose regulon through interaction with MalT. (390 aa)
sufSCysteine desulfurase, SufS subfamily; Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L- selenocysteine. Selenocysteine lyase activity is however unsure in vivo. (406 aa)
ADO48285.1KEGG: pmr:PMI0626 cystathionine beta-lyase; TIGRFAM: cystathionine beta-lyase; PFAM: Cys/Met metabolism pyridoxal-phosphate-dependent protein. (390 aa)
ADO48255.1Alanine racemase; Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids; Belongs to the alanine racemase family. (356 aa)
ADO48014.1Glycerol dehydratase; KEGG: cko:CKO_00796 hypothetical protein; PFAM: dehydratase large subunit. (554 aa)
ADO48013.1PFAM: dehydratase medium subunit; KEGG: ses:SARI_00846 hypothetical protein. (221 aa)
ADO48012.1PFAM: dehydratase small subunit; KEGG: cro:ROD_21281 propanediol utilization dehydratase, small subunit. (173 aa)
ADO47994.1KEGG: xne:XNC1_1146 threonine-phosphate decarboxylase (L-threonine-O-3-phosphate decarboxylase); TIGRFAM: L-threonine-O-3-phosphate decarboxylase; PFAM: aminotransferase class I and II. (370 aa)
glmSMethylaspartate mutase, S subunit; Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (149 aa)
glmEMethylaspartate mutase, E subunit; Catalyzes the carbon skeleton rearrangement of L-glutamate to L-threo-3-methylaspartate ((2S,3S)-3-methylaspartate). (481 aa)
hisCKEGG: ent:Ent638_2633 histidinol-phosphate aminotransferase; TIGRFAM: histidinol-phosphate aminotransferase; PFAM: aminotransferase class I and II; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (353 aa)
menD2-succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylic acid synthase/2-oxoglutarate decarboxylase; Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2- succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Belongs to the TPP enzyme family. MenD subfamily. (556 aa)
ADO47700.1PFAM: aminotransferase class I and II; KEGG: enc:ECL_03634 putative aminotransferase. (404 aa)
ADO47625.1PFAM: aminotransferase class I and II; KEGG: enc:ECL_03723 aminotransferase. (401 aa)
ADO47620.1PFAM: thiamine pyrophosphate TPP-binding domain-containing protein; thiamine pyrophosphate central domain-containing protein; KEGG: kpu:KP1_3993 putative pyruvate decarboxylase. (553 aa)
ADO47600.1Transcriptional regulator, GntR family with aminotransferase domain; KEGG: kpu:KP1_4015 putative regulatory protein; PFAM: regulatory protein GntR HTH; aminotransferase class I and II; SMART: regulatory protein GntR HTH. (435 aa)
eutCKEGG: cko:CKO_00346 ethanolamine ammonia-lyase small subunit; PFAM: Ethanolamine ammonia-lyase light chain; Belongs to the EutC family. (298 aa)
ADO47582.1KEGG: cro:ROD_23981 ethanolamine ammonia-lyase heavy chain; PFAM: Ethanolamine ammonia lyase large subunit. (453 aa)
ADO47524.1PFAM: thiamine pyrophosphate central domain-containing protein; thiamine pyrophosphate TPP-binding domain-containing protein; KEGG: eic:NT01EI_2136 putative malonic semialdehyde oxidative decarboxylase; Belongs to the TPP enzyme family. (641 aa)
iscSCysteine desulfurase IscS; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. (404 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)
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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