STRINGSTRING
aspC aspC bioF bioF bioA bioA AFJ47797.1 AFJ47797.1 cadA1 cadA1 gabT gabT metC metC cadA2 cadA2 hemL hemL speF speF tyrB tyrB rffA rffA metB metB kbl kbl AFJ45895.1 AFJ45895.1 gcvP gcvP speC speC AFJ45738.1 AFJ45738.1 AFJ49013.1 AFJ49013.1 ygjG ygjG goaG goaG argD argD AFJ45184.1 AFJ45184.1 glyA glyA csdA csdA iscS iscS yfdZ yfdZ yfbQ yfbQ AFJ46500.1 AFJ46500.1 arnB arnB hisC hisC sufS sufS AFJ47034.1 AFJ47034.1 ydcR1 ydcR1 malY malY AFJ47421.1 AFJ47421.1 serC serC ltaE ltaE
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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
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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:
aspCAspartate transaminase. (397 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. (385 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. (429 aa)
AFJ47797.1Putative aminotransferase in cobalamin synthesis. (364 aa)
cadA1RNA methyltransferase; Subunit of lysine decarboxylase. (737 aa)
gabT4-aminobutyrate aminotransferase-like aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (427 aa)
metCCystathionine beta-lyase. (393 aa)
cadA2RNA methyltransferase; Subunit of lysine decarboxylase. (715 aa)
hemLGlutamate-1-semialdehyde 2,1-aminomutase. (426 aa)
speFOrnithine decarboxylase; Inducible. (722 aa)
tyrBAromatic-amino-acid aminotransferase. (397 aa)
rffATDP-4-oxo-6-deoxy-D-glucose transaminase; Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D- galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D- Glc4O) and L-glutamate; Belongs to the DegT/DnrJ/EryC1 family. (376 aa)
metBCystathionine gamma-synthase. (386 aa)
kbl2-amino-3-ketobutyrate coenzyme A ligase; Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. (398 aa)
AFJ45895.1Putative aminotransferase. (395 aa)
gcvPGlycine cleavage system P protein; 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. (929 aa)
speCOrnithine decarboxylase; Constitutive. (712 aa)
AFJ45738.1Cystathionine beta-lyase. (403 aa)
AFJ49013.1Putative serine palmitoyltransferase. (391 aa)
ygjGPutative ornithine 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. (465 aa)
goaG4-aminobutyrate transaminase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (422 aa)
argDAcetylornithine aminotransferase; Involved in both the arginine and lysine biosynthetic pathways; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (407 aa)
AFJ45184.1Biodegradative arginine decarboxylase. (756 aa)
glyASerine 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)
csdACysteine sulfinate desulfinase; PfkB domain protein. (401 aa)
iscSCysteine 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. (404 aa)
yfdZPutative aminotransferase; Classes I and II. (402 aa)
yfbQPutative aminotransferase. (404 aa)
AFJ46500.1Putative aminotransferase YbdL. (386 aa)
arnBPutative UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase; Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides; Belongs to the DegT/DnrJ/EryC1 family. ArnB subfamily. (379 aa)
hisCHistidinol-phosphate aminotransferase HisC; Permease; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (360 aa)
sufSSelenocysteine lyase; 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)
AFJ47034.1Diaminobutyrate--2-oxoglutarate transaminase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (466 aa)
ydcR1Transcriptional regulator; GntR family/aminotransferase, classes I and II. (476 aa)
malYBifunctional: PLP-dependent beta-cystathionase; Repressor of maltose regulon through interaction with MalT. (395 aa)
AFJ47421.1Aminotransferase; Classes I and II. (378 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)
ltaELow-specificity L-threonine aldolase. (334 aa)
Your Current Organism:
Shimwellia blattae
NCBI taxonomy Id: 630626
Other names: Escherichia blattae CIP 104942, Escherichia blattae DSM 4481, Escherichia blattae NBRC 105725, S. blattae DSM 4481 = NBRC 105725, Shimwellia blattae CIP 104942, Shimwellia blattae DSM 4481, Shimwellia blattae DSM 4481 = NBRC 105725, Shimwellia blattae NBRC 105725, Shimwellia blattae NBRC 105725 = DSM 4481
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