STRINGSTRING
thrA thrA purU purU lysC lysC glnD glnD spoT spoT serA serA relA relA gcvR gcvR pheA pheA ilvH ilvH tyrR tyrR
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.
Node Color
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:
thrABifunctional aspartokinase/homoserine dehydrogenase I (AKI-HDI) [Includes: Aspartokinase I; Homoserine dehydrogenase I ]; In the C-terminal section; belongs to the homoserine dehydrogenase family. (801 aa)
purUFormyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (282 aa)
lysCLysine-sensitive aspartokinase III; Aspartate kinase; Belongs to the aspartokinase family. (450 aa)
glnDprotein-P-II uridylyltransferase; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. (885 aa)
spoTGuanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (707 aa)
serAD-3-phosphoglycerate dehydrogenase (PGDH), D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding. (412 aa)
relAGTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. (749 aa)
gcvRGlycine cleavage system transcriptional repressor (Gcv operon repressor), Amino acid-binding ACT. (183 aa)
pheAP-protein [Includes: Chorismate mutase (CM); Prephenate dehydratase (PDT)], Bifunctional chorismate mutase/prephenate dehydratase. (386 aa)
ilvHAcetolactate synthase isozyme III small subunit (AHAS-III) (Acetohydroxy-acid synthase III small subunit) (ALS-III). (163 aa)
tyrRTranscriptional regulatory protein tyrR; RNA polymerase sigma factor 54, interaction, Sigma-54 interaction domain, phageshock_pspF: psp operon transcriptional activator PspF. (521 aa)
Your Current Organism:
Erwinia amylovora
NCBI taxonomy Id: 665029
Other names: E. amylovora CFBP1430, Erwinia amylovora CFBP1430, Erwinia amylovora str. CFBP1430, Erwinia amylovora strain CFBP1430
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