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:
some 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
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[Homology]
Score
moaCCyclic pyranopterin monophosphate synthase; Catalyzes the conversion of (8S)-3',8-cyclo-7,8- dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP) (161 aa)    
Predicted Functional Partners:
moaA
Molybdopterin biosynthesis protein a; Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z)
 
 0.999
moaB
Inactive molybdopterin adenylyltransferase; May be involved in the biosynthesis of molybdopterin. Can bind GTP and has low GTPase activity. Can bind MPT, but has no MPT adenylyl transferase activity
 
 0.999
moaD
Molybdopterin synthase sulfur carrier subunit; Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin
 
 0.999
moaE
Molybdopterin synthase catalytic subunit; Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD
 0.999
moeA
Molybdopterin molybdenumtransferase; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP
 
 0.995
mog
Molybdochelatase incorporating molybdenum into molybdopterin; Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor
   
 0.991
mobB
GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP
   
 0.986
mobA
Molybdopterin-guanine dinucleotide synthase; Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor i [...]
   
 0.961
moeB
Molybdopterin-synthase adenylyltransferase; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD
 
  
 0.945
modA
Molybdate abc transporter periplasmic binding protein; Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell . Binds molybdate with high affinity in vitro and with a similar affinity in vivo Binds tungstate with high affinity in vitro Binds unnatural anion perrhenate with high affinity in vitro . Does not bind sulfate, phosphate, arsenate, selenate, chlorate, metavanadate, nitrate, perchlorate, permanganate or carbonate
 
   
 0.918
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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