STRINGSTRING
purU purU Sps_01409 Sps_01409 Sps_01987 Sps_01987 glnD glnD purU-2 purU-2 Sps_02407 Sps_02407 Sps_02414 Sps_02414 glnD-2 glnD-2 Sps_02853 Sps_02853 Sps_03318 Sps_03318 Sps_03664 Sps_03664 Sps_04110 Sps_04110
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:
purUFormyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (288 aa)
Sps_01409PFAM: Small subunit of acetolactate synthase; ACT domain; 'TIGRFAM: acetolactate synthase, small subunit'. (164 aa)
Sps_01987PFAM: ACT domain. (166 aa)
glnDUTP--GlnB (protein PII) 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 metabolism. (857 aa)
purU-2Formyltetrahydrofolate deformylase; Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). (277 aa)
Sps_02407Aspartate kinase; 'PFAM: Homoserine dehydrogenase; Homoserine dehydrogenase, NAD binding domain; ACT domain; Amino acid kinase family'; TIGRFAM: aspartate kinase; In the C-terminal section; belongs to the homoserine dehydrogenase family. (821 aa)
Sps_02414Chorismate mutase; PFAM: Prephenate dehydratase; Chorismate mutase type II; DAHP synthetase I family; 'TIGRFAM: chorismate mutase domain of proteobacterial P-protein, clade 1'. (660 aa)
glnD-2UTP--GlnB (protein PII) 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 metabolism. (867 aa)
Sps_02853'PFAM: D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain; ACT domain; D-isomer specific 2-hydroxyacid dehydrogenase, catalytic domain'. (409 aa)
Sps_03318(p)ppGpp synthetase, RelA/SpoT family; 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. (701 aa)
Sps_03664Transcriptional regulator, TyrR; PFAM: ACT domain; Sigma-54 interaction domain. (534 aa)
Sps_04110(p)ppGpp synthetase, RelA/SpoT family; 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. (734 aa)
Your Current Organism:
Shewanella psychrophila
NCBI taxonomy Id: 225848
Other names: CGMCC 1.6159, JCM 13876, S. psychrophila, Shewanella psychrophila Xiao et al. 2007 emend. Thorell et al. 2019, Shewanella sp. WP2, strain WP2
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