STRINGSTRING
gatD gatD guaAB guaAB gatE gatE nadE nadE SDW87511.1 SDW87511.1 guaAA guaAA gatB gatB cbiA cbiA SDX05831.1 SDX05831.1 purL purL SDX09976.1 SDX09976.1 gatC gatC gatA gatA purQ purQ purS purS carB carB carA carA
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:
gatDglutamyl-tRNA(Gln) amidotransferase subunit D; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (415 aa)
guaABGMP synthase (glutamine-hydrolyzing); Catalyzes the synthesis of GMP from XMP. (305 aa)
gatEglutamyl-tRNA(Gln) amidotransferase subunit E; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. (623 aa)
nadENH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. (277 aa)
SDW87511.1NAD+ synthase; Belongs to the NAD synthetase family. (282 aa)
guaAAGMP synthase (glutamine-hydrolysing); Catalyzes the synthesis of GMP from XMP. (189 aa)
gatBaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily. (504 aa)
cbiAHydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) /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. (439 aa)
SDX05831.1Asparagine synthase (glutamine-hydrolysing). (608 aa)
purLPhosphoribosylformylglycinamidine synthase subunit II; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to [...] (721 aa)
SDX09976.1Asparagine synthase (glutamine-hydrolysing). (364 aa)
gatCaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit C; Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatC family. (92 aa)
gatAaspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit A; Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln). (444 aa)
purQPhosphoribosylformylglycinamidine synthase subunit I; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to [...] (228 aa)
purSPhosphoribosylformylglycinamidine synthase; Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP- dependent manner. PurS interacts with PurQ and PurL and is thought to assist in [...] (84 aa)
carBCarbamoyl-phosphate synthase large subunit; Belongs to the CarB family. (1083 aa)
carACarbamoyl-phosphate synthase small subunit; Belongs to the CarA family. (348 aa)
Your Current Organism:
Haloarcula vallismortis
NCBI taxonomy Id: 28442
Other names: ATCC 29715, CGMCC 1.2048, DSM 3756, H. vallismortis, Halobacterium vallismortis, IFO 14741, JCM 8877, NBRC 14741, strain J. F. 54
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