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coaD protein (Methylobacter tundripaludum) - STRING interaction network
"coaD" - Phosphopantetheine adenylyltransferase in Methylobacter tundripaludum
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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coaDPhosphopantetheine adenylyltransferase; Reversibly transfers an adenylyl group from ATP to 4’- phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate; Belongs to the bacterial CoaD family (161 aa)    
Predicted Functional Partners:
Mettu_1831
Coenzyme A biosynthesis bifunctional protein CoaBC; Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4’-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4’-phosphopantotheine; In the C-terminal section; belongs to the PPC synthetase family (396 aa)
 
 
  0.933
coaE
Dephospho-CoA kinase; Catalyzes the phosphorylation of the 3’-hydroxyl group of dephosphocoenzyme A to form coenzyme A; Belongs to the CoaE family (200 aa)
 
 
  0.933
Mettu_3674
Ribosomal RNA small subunit methyltransferase D; Specifically methylates the guanine in position 966 of 16S rRNA in the assembled 30S particle (185 aa)
 
        0.905
nadE
Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source (536 aa)
 
   
  0.884
coaX
Type III pantothenate kinase; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis (243 aa)
 
   
  0.874
Mettu_3672
PFAM- 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; KEGG- psp-PSPPH_4790 ferredoxin, 4Fe-4S (76 aa)
   
        0.853
nadK
NAD kinase; Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2’-hydroxyl of the adenosine moiety of NAD to yield NADP (301 aa)
       
  0.789
glmU
Bifunctional protein GlmU; Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5- monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain (488 aa)
 
 
  0.789
nadD
Probable nicotinate-nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (210 aa)
       
  0.764
Mettu_0078
KEGG- nhl-Nhal_3853 mutator MutT protein; TIGRFAM- Mutator MutT protein; PFAM- Thiamine monophosphate synthase; NUDIX hydrolase domain (307 aa)
            0.741
Your Current Organism:
Methylobacter tundripaludum
NCBI taxonomy Id: 697282
Other names: M. tundripaludum SV96, Methylobacter sp. SV96, Methylobacter tundripaludum, Methylobacter tundripaludum DSM 17260, Methylobacter tundripaludum SV96, Methylobacter tundripaludum str. SV96, Methylobacter tundripaludum strain SV96
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