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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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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glnEProbable [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 si [...] (893 aa)    
Predicted Functional Partners:
glnD
Putative protein-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 fixation and metabolism.
 
   
 0.803
glnA
Glutamine synthetase I (GS) plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine. Similar to pir|G83005 (70%) and to pir|AJECQ (66%). Pfam (PF00120): Glutamine synthetase, catalytic domain Pfam (PF03951): Glutamine synthetase, beta-Grasp domain; High confidence in function and specificity.
 
   
 0.711
azo1292
Adenylate cyclase; Conserved hypothetical protein,40% identity to TrEMBL;Q88AR4 Has PF01928|CYTH domain(IPR008172);These sequences are functionally identified as members of the adenylate cyclase family, which catalyses the conversion of ATP to 3',5'-cyclic AMP and pyrophosphate. Has PF05235:CHAD domain(IPR007899);The CHAD domain is an alpha-helical domain functionally associated with the CYTH domains. It has conserved histidines that may chelate metals.
       0.687
azo1295
Conserved hypothetical carbon-nitrogen hydrolase. Homolog to bb1933 of B. bronchiseptica (trembl|Q7WL17). InterPro: Carbon-nitrogen hydrolase (IPR003010) Pfam: Carbon-nitorgen hydrolase no signal peptide no TMHs; Conserved hypothetical protein.
     
 0.646
hrpA
ATP-dependent helicase hrpA. Not yet known. InterPro: DEAD/DEAH box helicase; High confidence in function and specificity.
  
   
 0.621
nadE
NAD(+) synthase (glutamine-hydrolyzing); Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
     
 0.583
azo1294
Conserved hypothetical protein. Homology to cv2096 of C. violaceum of 32% (trembl|Q7NW94(SRS) no domains predicted no signal peptide 1 TMHs.
       0.580
tldD
Probable TldD protein. Homology to tldD of E. coli of 59% (sprot|TLDD_ECOLI). Suppresses the inhibitory activity of the carbon storage regulator (csrA). Pfam: putative modulator of DNA gyrase no signal peptide no TMHs; Function unclear.
  
    0.551
sixA
Putative phosphohistidine phosphatase, SixA. TIGRFAM: TIGR00249; sixA. Phosphohistidine phosphatase sixA (EC 3.1.3.-) (RX6). EXHIBITS PHOSPHOHISTIDINE PHOSPHATASE ACTIVITY TOWARDS THE HPT DOMAIN OF THE ARCB SENSOR INVOLVED IN THE MULTISTEP HIS- ASP PHOSPHORELAY; Specificity unclear.
       0.475
guaA
GMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP.
     
 0.474
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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