STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
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 assimilation and metabolism. (924 aa)    
Predicted Functional Partners:
Mmc1_0969
PFAM: nitrogen regulatory protein P-II; KEGG: mag:amb0695 nitrogen regulatory protein PII; Belongs to the P(II) protein family.
 
 
 0.974
glnE
(Glutamate--ammonia-ligase) adenylyltransferase; Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal tra [...]
 
   
 0.791
Mmc1_0995
PFAM: nitrogen regulatory protein P-II; KEGG: cvi:CV4002 nitrogen regulatory protein P-II-2; Belongs to the P(II) protein family.
 
 
 
 0.740
Mmc1_0706
PFAM: glutamine amidotransferase, class-II; glutamate synthase, alpha subunit domain protein; ferredoxin-dependent glutamate synthase; glutamate synthase; KEGG: noc:Noc_1604 glutamate synthase (ferredoxin).
     
 0.593
Mmc1_3671
Signal transduction histidine kinase, nitrogen specific, NtrB; PFAM: ATP-binding region, ATPase domain protein domain protein; histidine kinase A domain protein domain protein; KEGG: gme:Gmet_2562 signal transduction histidine kinase, nitrogen specific, NtrB.
  
 
 
 0.542
cbiA
Cobyrinate a,c-diamide synthase; Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinate, using either L-glutamine or ammonia as the nitrogen source; Belongs to the CobB/CbiA family.
   
    0.513
Mmc1_3137
PFAM: Cobyrinic acid a,c-diamide synthase; CobB/CobQ domain protein glutamine amidotransferase; KEGG: mca:MCA2290 cobyrinic acid a,c-diamide synthase.
   
    0.513
Mmc1_0988
KEGG: rru:Rru_A2086 glutamine synthetase type I; TIGRFAM: glutamine synthetase, type I; PFAM: glutamine synthetase, catalytic region; glutamine synthetase, beta-Grasp.
 
   
 0.511
Mmc1_1417
TIGRFAM: UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; KEGG: cya:CYA_1015 UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase.
  
    0.511
bamA
Surface antigen (D15); Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
 
    0.482
Your Current Organism:
Magnetococcus marinus
NCBI taxonomy Id: 156889
Other names: M. marinus MC-1, Magnetococcus marinus MC-1, Magnetococcus marinus str. MC-1, Magnetococcus marinus strain MC-1, Magnetococcus sp. MC-1
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