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:
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
mptEConserved hypothetical protein; Catalyzes the transfer of diphosphate from ATP to 6- hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6-hydroxymethyl- 7,8-dihydropterin diphosphate (6-HMDP); Belongs to the archaeal 6-HMPDK family. (241 aa)    
Predicted Functional Partners:
mptD
Conserved hypothetical protein; Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) to 6-hydroxymethyl-7,8-dihydropterin (6-HMD).
 
  
 0.994
MJ_0301
Conserved hypothetical protein; Catalyzes the condensation of 6-hydroxymethyl-7,8- dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)- aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin-6- methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin (H4MPT). To a lesser extent, is able to condense beta-RFA-P with another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to form 7,8-dihydropterin- 6-methyl-1-(4-aminophenyl)-1-deoxy-D-ribitol. Dephosphorylated beta- RFA-P is not a substrate; [...]
    
  0.903
MJ_0448
Conserved hypothetical protein; Similar to PID:577190 percent identity: 29.38; identified by sequence similarity; putative; Belongs to the metallo-beta-lactamase superfamily.
    
  0.903
mptB
Cmp-binding-factor 1 isolog; Cyclic phosphodiesterase that hydrolyzes the cyclic phosphate of 7,8-dihydroneopterin 2',3'-cyclic phosphate (H2N-cP) and converts it to a mixture of 7,8-dihydroneopterin 2'-phosphate (H2N-2'P) and 7,8- dihydroneopterin 3'-phosphate (H2N-3'P). Is also able to utilize other phosphodiesters as substrates in vitro: hydrolysis of bis-pNPP and pNPPC produces nitrophenyl phosphate, and that of 2',3'-cAMP produces 3'-AMP. ATP, 3',5'-cAMP, GTP, 3',5'-cGMP, and 4',5'-cFMN cannot serve as substrates.
      
 0.821
mch
N5,N10-methenyl-tetrahydromethanopterin cyclohydrolase (mch); Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+); Belongs to the MCH family.
       0.724
purB
Adenylosuccinate lyase (purB); Similar to GB:J02732 SP:P12047 PID:143366 GB:AL009126 percent identity: 42.51; identified by sequence similarity; putative.
  
   
 0.685
mptA
Conserved hypothetical protein; Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate, the first intermediate in the biosynthesis of coenzyme methanopterin. It is also able to utilize a variety of GTP analogs as substrates, including GDP, beta,gamma-methylene-GTP and GTP-[gamma- thio]; Belongs to the GTP cyclohydrolase IV family.
 
   
 0.652
MJ_1633
Conserved hypothetical protein; Similar to GP:1652055 percent identity: 37.46; identified by sequence similarity; putative.
       0.586
MJ_1032
Conserved hypothetical protein; Similar to GB:AE000782 percent identity: 34.62; identified by sequence similarity; putative.
 
     0.554
MJ_0831
Conserved hypothetical protein; Similar to GB:AE000666 percent identity: 35.87; identified by sequence similarity; putative; To M.jannaschii MJ0977.
  
     0.544
Your Current Organism:
Methanocaldococcus jannaschii
NCBI taxonomy Id: 243232
Other names: M. jannaschii DSM 2661, Methanocaldococcus jannaschii DSM 2661, Methanocaldococcus jannaschii str. DSM 2661, Methanococcus jannaschii DSM 2661
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