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Nmar_1732 protein (Nitrosopumilus maritimus) - STRING interaction network
"Nmar_1732" - KEGG: pab:PAB1318 nicotinamide-nucleotide adenylyltransferase in Nitrosopumilus maritimus
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
Nmar_1732KEGG- pab-PAB1318 nicotinamide-nucleotide adenylyltransferase; TIGRFAM- cytidyltransferase-related domain; PFAM- cytidylyltransferase (164 aa)    
Predicted Functional Partners:
nadE
NH(3)-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source (237 aa)
 
   
  0.928
Nmar_1237
Nicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA); Belongs to the NadC/ModD family (272 aa)
         
  0.924
Nmar_0921
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 (332 aa)
   
 
  0.910
Nmar_0440
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 (278 aa)
   
 
  0.907
Nmar_0960
KEGG- pas-Pars_0405 nicotinamide-nucleotide adenylyltransferase; TIGRFAM- cytidyltransferase-related domain; PFAM- cytidylyltransferase; Citrate lyase ligase domain protein (176 aa)
   
   
 
0.814
Nmar_1730
Peptidyl-prolyl cis-trans isomerase; PFAM- peptidylprolyl isomerase FKBP-type; KEGG- iho-Igni_0058 peptidylprolyl isomerase, FKBP-type (248 aa)
 
          0.782
Nmar_1731
Serine--pyruvate transaminase; PFAM- aminotransferase class V; KEGG- mvn-Mevan_1378 serine--pyruvate transaminase (381 aa)
              0.713
rtcA
RNA 3’-terminal phosphate cyclase; Catalyzes the conversion of 3’-phosphate to a 2’,3’- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps- (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3’P to produce RNA- N3’PP5’A; (C) and attack of the adjacent 2’-hydroxyl on the 3’- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (338 aa)
 
          0.700
Nmar_1054
PFAM- PilT protein domain protein; KH type 1 domain protein; SMART- KH domain protein; Nucleotide binding protein PINc; KEGG- mja-MJ1533 hypothetical protein (605 aa)
   
          0.411
Nmar_1091
PFAM- transcriptional regulator TrmB; KEGG- neq-NEQ098 predicted transcription regulator (386 aa)
   
          0.408
Your Current Organism:
Nitrosopumilus maritimus
NCBI taxonomy Id: 436308
Other names: N. maritimus SCM1, Nitrosopumilus maritimus, Nitrosopumilus maritimus SCM1, Nitrosopumilus maritimus str. SCM1, Nitrosopumilus maritimus strain SCM1, Seattle Aquarium strain SCM1
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