STRINGSTRING
purQ purQ pyrG pyrG cobQ cobQ carA carA AKB12265.1 AKB12265.1 AKB12350.1 AKB12350.1 AKB12407.1 AKB12407.1 AKB12544.1 AKB12544.1 pdxT pdxT AKB12755.1 AKB12755.1 hisH hisH AKB13055.1 AKB13055.1 guaAA guaAA cbiA cbiA cbiA-2 cbiA-2 AKB14266.1 AKB14266.1 AKB14267.1 AKB14267.1
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:
purQPhosphoribosylformylglycinamidine synthase, glutamine amidotransferase subunit; 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 a [...] (232 aa)
pyrGCTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. (534 aa)
cobQCobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily. (485 aa)
carACarbamoyl-phosphate synthase small chain; Belongs to the CarA family. (369 aa)
AKB12265.1Anthranilate synthase, amidotransferase component. (201 aa)
AKB12350.1ThiJ/PfpI family protein. (167 aa)
AKB12407.1Glutamine amidotransferase class-I. (231 aa)
AKB12544.1ThiJ/PfpI family protein. (180 aa)
pdxTPyridoxine biosynthesis glutamine amidotransferase, glutaminase subunit; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (199 aa)
AKB12755.1ThiJ/PfpI family protein. (158 aa)
hisHImidazole glycerol phosphate synthase amidotransferase subunit; IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR. The resulting ammonia molecule is channeled to the active site of HisF. (198 aa)
AKB13055.1Catalase. (735 aa)
guaAAGMP synthase (glutamine-hydrolyzing), amidotransferase subunit; Catalyzes the synthesis of GMP from XMP. (189 aa)
cbiACobyrinic acid 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. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. (439 aa)
cbiA-2Cobyrinic acid 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. Involved in the biosynthesis of the unique nickel-containing tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M reductase (MCR), which plays a key role in methanogenesis and anaerobic methane oxidation. Catalyzes the ATP- dependent amidation of the two carboxylate groups at positions a and c of Ni-sirohydrochlorin, using L-glutamine or ammonia as the nitrogen source. (495 aa)
AKB14266.1Hypothetical protein. (626 aa)
AKB14267.1Hypothetical protein. (817 aa)
Your Current Organism:
Methanosarcina thermophila
NCBI taxonomy Id: 523844
Other names: M. thermophila TM-1, Methanosarcina thermophila OCM 12, Methanosarcina thermophila TM-1, Methanosarcina thermophila str. TM-1, Methanosarcina thermophila strain TM-1
Server load: low (14%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.