STRINGSTRING
moaC moaC thiS thiS AJF84470.1 AJF84470.1 AJF84720.1 AJF84720.1 AJF84723.1 AJF84723.1 moaD moaD trmU trmU AJF85855.1 AJF85855.1 AJF85894.1 AJF85894.1 moaB moaB thiI thiI AJF86051.1 AJF86051.1 moaA moaA AJF87071.1 AJF87071.1
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:
moaCMolybdenum cofactor biosynthesis protein C; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP); Belongs to the MoaC family. (170 aa)
thiSThiamine biosynthesis protein ThiS; Derived by automated computational analysis using gene prediction method: Protein Homology. (67 aa)
AJF84470.1Thiamine biosynthesis protein MoeB; Catalyzes the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD or ThiS in the molybdopterin or thiamin pyrophosphate biosynthesis pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. (336 aa)
AJF84720.1Thiamine biosynthesis protein MoeB; Catalyzes the formation of a high-energy acyladenylate intermediate and subsequently to the formation of a thiocarboxylate at the C termini of MoaD or ThiS in the molybdopterin or thiamin pyrophosphate biosynthesis pathways; Derived by automated computational analysis using gene prediction method: Protein Homology. (339 aa)
AJF84723.1Molybdenum cofactor biosynthesis protein MoaE; Derived by automated computational analysis using gene prediction method: Protein Homology. (157 aa)
moaDMolybdenum cofactor biosynthesis protein MoaD; Derived by automated computational analysis using gene prediction method: Protein Homology. (77 aa)
trmUThiouridylase; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. (371 aa)
AJF85855.1Cysteine desulfurase; Derived by automated computational analysis using gene prediction method: Protein Homology. (379 aa)
AJF85894.1Cysteine desulfurase; Catalyzes the removal of elemental sulfur from cysteine to produce alanine; involved in NAD biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology. (395 aa)
moaBMolybdenum cofactor biosynthesis protein B; May be involved in the biosynthesis of molybdopterin. Belongs to the MoaB/Mog family. (171 aa)
thiIThiamine biosynthesis protein ThiI; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. (401 aa)
AJF86051.1Cysteine desulfurase; Derived by automated computational analysis using gene prediction method: Protein Homology. (381 aa)
moaAMolybdenum cofactor biosynthesis protein A; Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate. (341 aa)
AJF87071.1Molybdenum cofactor synthesis protein 3; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)
Your Current Organism:
Bacillus atrophaeus
NCBI taxonomy Id: 1452
Other names: ATCC 49337, B. atrophaeus, Bacillus atriphaeus, Bacillus sp. S2 BC-2, Bacillus subtilis DSM 2277, Bacillus subtilis DSM 675, CCUG 28524, CIP 107159, DSM 7264, IFO 15539, JCM 9070, LMG 16797, LMG:16797, NBRC 15539, NRRL NRS-213
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