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gabT gabT ltaE ltaE glyA-I glyA-I bioF bioF aruC aruC PP_0486 PP_0486 selA selA PP_0596 PP_0596 metB metB glyA-II glyA-II alaC alaC iscS-I iscS-I PP_0858 PP_0858 hisC hisC gcvP-I gcvP-I PP_1109 PP_1109 mdeA mdeA csdA csdA dapC dapC cobC cobC serC serC alaA alaA tyrB tyrB metZ metZ spuC-I spuC-I phnW phnW iscS-II iscS-II PP_2528 PP_2528 PP_2542 PP_2542 PP_2552 PP_2552 PP_2588 PP_2588 PP_2642 PP_2642 PP_2782 PP_2782 PP_2799 PP_2799 PP_2800 PP_2800 PP_2829 PP_2829 PP_2948 PP_2948 PP_3361 PP_3361 PP_3544 PP_3544 amaC amaC PP_3718 PP_3718 aruH aruH PP_3750 PP_3750 aspC aspC PP_4108 PP_4108 ldcC ldcC PP_4154 PP_4154 PP_4197 PP_4197 pvdN pvdN pvdH pvdH PP_4348 PP_4348 PP_4350 PP_4350 PP_4421 PP_4421 PP_4429 PP_4429 astC astC PP_4594 PP_4594 PP_4692 PP_4692 hemL hemL bioA bioA spuC-II spuC-II gcvP-II gcvP-II yjiR yjiR PP_5342 PP_5342
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:
gabT4-aminobutyrate aminotransferase; Catalyzes the conversion of 5-aminovalerate to 5- oxopentanoate. (425 aa)
ltaELow specificity L-threonine aldolase; Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. (346 aa)
glyA-ISerine 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)
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. (390 aa)
aruCAcetylornithine aminotransferase 2; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Glutamate family; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (426 aa)
PP_0486Transcriptional regulator, GntR family. (474 aa)
selASelenocysteine synthase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (475 aa)
PP_0596Omega-amino acid--pyruvate aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (448 aa)
metBCystathionine gamma-synthase. (423 aa)
glyA-IISerine 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)
alaCAminotransferase; Function of strongly homologous gene; enzyme; Regulatory functions. (402 aa)
iscS-ICysteine desulfurase; 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; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (404 aa)
PP_0858Putative methionine/glutamine aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (382 aa)
hisCHistidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (348 aa)
gcvP-IGlycine 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 (By similarity); Belongs to the GcvP family. (951 aa)
PP_1109Transcriptional regulator, GntR family. (446 aa)
mdeAMethionine gamma-lyase; Function experimentally demonstrated in the studied strain; enzyme; Fattyacidandphospholipidmetabolism : Degradation. (398 aa)
csdAProbable cysteine desulfurase; Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine. (401 aa)
dapCN-succinyl-L,L-diaminopimelate aminotransferase alternative; Function of strongly homologous gene; enzyme; Aminoacidbiosynthesis : Aspartate family. (398 aa)
cobCSubunit of adenosylcobinamide-phosphate synthase beta component; Function experimentally demonstrated in the studied genus; enzyme; Biosynthesis of cofactors, prosthetic groups, and carriers. (330 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. (361 aa)
alaAGlutamate-pyruvate aminotransferase; Function of homologous gene experimentally demonstrated in an other organism; enzyme. (403 aa)
tyrBAromatic-amino-acid aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aspartate family. (398 aa)
metZO-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide. (403 aa)
spuC-IPolyamine:pyruvate transaminase; Function experimentally demonstrated in the studied genus; enzyme; Central intermediary metabolism; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (452 aa)
phnW2-aminoethylphosphonate--pyruvate transaminase; Involved in phosphonate degradation; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. PhnW subfamily. (368 aa)
iscS-IICysteine desulfurase; Function of strongly homologous gene; enzyme. (405 aa)
PP_2528O-acetylhomoserine (thiol)-lyase; Function of homologous gene experimentally demonstrated in an other organism; enzyme; Fattyacidandphospholipidmetabolism : Degradation. (425 aa)
PP_2542Transcriptional regulator, GntR family. (474 aa)
PP_2552DOPA decarboxylase. (470 aa)
PP_2588Aminotransferase, class III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (460 aa)
PP_2642Transcriptional regulator, GntR family. (496 aa)
PP_2782Pyridoxalphosphate dependent aminotransferase, class III. (959 aa)
PP_2799Aminotransferase, class III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (459 aa)
PP_2800Putative Diaminobutyrate-2-oxoglutarate transaminase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (417 aa)
PP_2829Transcriptional regulator, GntR family. (452 aa)
PP_2948Transcriptional regulator, GntR family. (460 aa)
PP_3361Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity. (1015 aa)
PP_3544Transcriptional regulator, GntR family. (469 aa)
amaCD-lysine aminotransferase; Function experimentally demonstrated in the studied strain; enzyme; Aminoacidbiosynthesis : Aromatic amino acid family. (398 aa)
PP_3718Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (470 aa)
aruHArginine--pyruvate transaminase AruH. (396 aa)
PP_3750Transcriptional regulator, GntR family. (477 aa)
aspCAminotransferase; Function experimentally demonstrated in the studied species; enzyme; Biologicalprocesses : Scavenge (Catabolism). (402 aa)
PP_4108Putative 4-aminobutyrate aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (416 aa)
ldcCLysine decarboxylase; Function experimentally demonstrated in the studied genus; enzyme; Energymetabolism : Amino acids and amines. (749 aa)
PP_4154Putative class 3 aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity. (976 aa)
PP_4197Transcriptional regulator, GntR family. (530 aa)
pvdNPyoverdine biosynthesis related protein; Function of strongly homologous gene; putative enzyme; Fattyacidandphospholipidmetabolism : Biosynthesis. (428 aa)
pvdHDiaminobutyrate-2-oxoglutarate transaminase; Function experimentally demonstrated in the studied genus; enzyme; Fattyacidandphospholipidmetabolism : Biosynthesis; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (452 aa)
PP_4348Putative Cystathionine beta-lyase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (364 aa)
PP_4350Aminotransferase, class V, NifS/IscS family. (387 aa)
PP_4421Putative aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (463 aa)
PP_4429Transcriptional regulator, GntR family. (466 aa)
astCSuccinylornithine transaminase/acetylornithine aminotransferase; Function experimentally demonstrated in the studied genus; enzyme; Aminoacidbiosynthesis : Glutamate family; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (406 aa)
PP_4594Putative Cystathionine gamma-synthase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology. (393 aa)
PP_4692Putative aspartate/tyrosine/aromatic aminotransferase; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Unknownfunction : Enzymes of unknown specificity. (390 aa)
hemLGlutamate-1-semialdehyde 2,1-aminomutase. (427 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. (468 aa)
spuC-IIPolyamine:pyruvate transaminase; Function experimentally demonstrated in the studied genus; enzyme; Central intermediary metabolism; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (453 aa)
gcvP-IIGlycine 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 (By similarity); Belongs to the GcvP family. (957 aa)
yjiRPutative regulator; Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator; Transcription. (496 aa)
PP_5342Transcriptional regulator, GntR family. (509 aa)
Your Current Organism:
Pseudomonas putida KT2440
NCBI taxonomy Id: 160488
Other names: P. putida KT2440, Pseudomonas putida (strain KT2440), Pseudomonas putida str. KT2440
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