STRINGSTRING
glnD glnD ilvA ilvA Meso_1489 Meso_1489 Meso_0946 Meso_0946 purU purU Meso_1922 Meso_1922 Meso_4087 Meso_4087 Meso_3001 Meso_3001 Meso_3161 Meso_3161
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:
glnDUTP-GlnB uridylyltransferase, GlnD; 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 fixation and metabolism. (912 aa)
ilvAL-threonine ammonia-lyase; 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. (418 aa)
Meso_1489TIGRFAM: acetolactate synthase, small subunit; PFAM: amino acid-binding ACT; KEGG: mlo:mll1432 acetolactate synthase small subunit. (190 aa)
Meso_0946(p)ppGpp synthetase I, SpoT/RelA; 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. (745 aa)
purUFormyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (286 aa)
Meso_1922PFAM: homoserine dehydrogenase amino acid-binding ACT homoserine dehydrogenase, NAD-binding; KEGG: mlo:mll0934 homoserine dehydrogenase. (436 aa)
Meso_4087PFAM: prephenate dehydratase amino acid-binding ACT; KEGG: bmb:BruAb1_0037 PheA, prephenate dehydratase. (290 aa)
Meso_3001TIGRFAM: aspartate kinase aspartate kinase, monofunctional class; PFAM: aspartate/glutamate/uridylate kinase amino acid-binding ACT; KEGG: bmb:BruAb1_1850 aspartate kinase, monofunctional class; Belongs to the aspartokinase family. (424 aa)
Meso_3161TIGRFAM: D-3-phosphoglycerate dehydrogenase; PFAM: amino acid-binding ACT D-isomer specific 2-hydroxyacid dehydrogenase, catalytic region D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding; KEGG: mlo:mll3875 phosphoglycerate dehydrogenase. (532 aa)
Your Current Organism:
Chelativorans sp. BNC1
NCBI taxonomy Id: 266779
Other names: C. sp. BNC1, Mesorhizobium sp. BNC1
Server load: low (20%) [HD]