STRINGSTRING
OBX08667.1 OBX08667.1 OBX08144.1 OBX08144.1 OBX07518.1 OBX07518.1 pheA pheA OBX06975.1 OBX06975.1 thrA thrA OBX05320.1 OBX05320.1 ilvH ilvH glnD glnD relA relA
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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
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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:
OBX08667.1Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology. (525 aa)
OBX08144.1Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0237 family. (90 aa)
OBX07518.13-phosphoglycerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (412 aa)
pheAChorismate mutase; Catalyzing the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. (383 aa)
OBX06975.1Guanosine-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. (712 aa)
thrAAspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. (815 aa)
OBX05320.1Aspartate kinase; Catalyzes the formation of 4-phospho-L-aspartate from L-aspartate and ATP; functions in amino acid biosynthesis; lysine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family. (450 aa)
ilvHAcetolactate synthase 3 regulatory subunit; With IlvI catalyzes the formation of 2-acetolactate from pyruvate, the small subunit is required for full activity and valine sensitivity; E.coli produces 3 isoenzymes of acetolactate synthase which differ in specificity to substrates, valine sensitivity and affinity for cofactors; also known as acetolactate synthase 3 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (165 aa)
glnDprotein-PII 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 metabolism. (876 aa)
relA(p)ppGpp synthetase; 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. (741 aa)
Your Current Organism:
Gallibacterium salpingitidis
NCBI taxonomy Id: 505341
Other names: CCUG 15564, CCUG 36325, G. salpingitidis, Gallibacterium salpingitidis Bisgaard et al. 2009, Gallibacterium sp. 18469/18, Gallibacterium sp. 19987/2, Gallibacterium sp. BK1010/1, Gallibacterium sp. F150, NCTC 11414, strain F150
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