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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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nadDNicotinate (nicotinamide) nucleotide adenylyltransferase; Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). (220 aa)    
Predicted Functional Partners:
rsfS
Iojap-like protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation.
 
  
 0.974
nadE
NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
  
 
 0.964
Deba_0844
Nicotinate phosphoribosyltransferase; Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D- ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Belongs to the NAPRTase family.
 
 
 0.954
nadK
ATP-NAD/AcoX 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.
 
 
 0.951
Deba_0027
COGs: COG0157 Nicotinate-nucleotide pyrophosphorylase; InterPro IPR002638:IPR004393:IPR013785; KEGG: bpt:Bpet0626 nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase; PRIAM: Nicotinate-nucleotide diphosphorylase (carboxylating); SPTR: A9I465 Nicotinate-mononucleotide pyrophosphorylase; TIGRFAM: nicotinate-nucleotide pyrophosphorylase; PFAM: Quinolinate phosphoribosyl transferase, C-terminal domain; Quinolinate phosphoribosyl transferase, N-terminal domain; TIGRFAM: nicotinate-nucleotide pyrophosphorylase; Belongs to the NadC/ModD family.
    
 0.939
cobB
Silent information regulator protein Sir2; COGs: COG0846 NAD-dependent protein deacetylase SIR2 family; InterPro IPR003000; KEGG: sfu:Sfum_3557 silent information regulator protein Sir2; PFAM: Silent information regulator protein Sir2; SPTR: A0LP75 Silent information regulator protein Sir2; PFAM: Sir2 family; Belongs to the sirtuin family. Class III subfamily.
   
 0.922
Deba_2660
Silent information regulator protein Sir2; COGs: COG0846 NAD-dependent protein deacetylase SIR2 family; InterPro IPR003000; KEGG: dal:Dalk_1098 silent information regulator protein Sir2; PFAM: Silent information regulator protein Sir2; SPTR: C8QW70 Silent information regulator protein Sir2; PFAM: Sir2 family.
   
 0.922
Deba_0469
NAD(+) diphosphatase; COGs: COG2816 NTP pyrophosphohydrolase containing a Zn-finger probably nucleic-acid-binding; InterProIPR015375:IPR015376:IPR000086:IPR015797:IPR 020084; KEGG: scl:sce4370 NADH pyrophosphatase; PFAM: NUDIX hydrolase; NADH pyrophosphatase-like; Zinc ribbon NADH pyrophosphatase; PRIAM: NAD(+) diphosphatase; SPTR: A9F2Z4 NADH pyrophosphatase; PFAM: NADH pyrophosphatase zinc ribbon domain; NUDIX domain.
     
 0.910
proA
Gamma-glutamyl phosphate reductase; Catalyzes the NADPH-dependent reduction of L-glutamate 5- phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. Belongs to the gamma-glutamyl phosphate reductase family.
  
  
 0.908
Deba_0953
MazG family protein; COGs: COG3956 Protein containing tetrapyrrole methyltransferase domain and MazG-like (predicted pyrophosphatase) domain; InterPro IPR004518:IPR011551; KEGG: scl:sce4803 hypothetical protein; PFAM: MazG nucleotide pyrophosphohydrolase; SPTR: A9FF91 Putative uncharacterized protein mazG; TIGRFAM: MazG family protein; PFAM: MazG nucleotide pyrophosphohydrolase domain; TIGRFAM: MazG family protein.
    
 0.907
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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