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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
ahcyAdenosylhomocysteinase; May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine. (462 aa)    
Predicted Functional Partners:
metE
5-methyltetrahydropteroyltriglutamate-homocystei ne methyltra; Catalyzes the transfer of a methyl group from 5- methyltetrahydrofolate to homocysteine resulting in methionine formation; Belongs to the vitamin-B12 independent methionine synthase family.
 
 
 0.975
ABO_1324
5-methyltetrahydrofolate--homocysteine methyltransferase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
  
 
 0.964
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
  
 0.925
mtaD
Conserved hypothetical protein; Catalyzes the deamination of 5-methylthioadenosine and S- adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L- homocysteine, respectively. Is also able to deaminate adenosine. Belongs to the metallo-dependent hydrolases superfamily. MTA/SAH deaminase family.
 
 
 0.922
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
 
 
 0.914
metY
(O-acetylhomoserine sulfhydrylase, O-acetylhomoserine (thiol)-lyase, oah sulfhydrylase, homocysteine synthase) identified by sequence similarity; identified by match to PFAM protein family HMMPF01053; putative InterPro: Cys/Met metabolism pyridoxal-phosphate-dependent enzymes; High confidence in function and specificity.
     
 0.911
dsm
C-5 cytosine-specific DNA methylase family protein; DNA-cytosine methyltransferase identified by sequence similarity; putative InterPro: C-5 cytosine-specific DNA methylase; Specificity unclear.
     
 0.903
cysK
(cysteine synthase A, O-acetylserine sulfhydrylase A, O- acetylserine (thiol)-lyase A, sulfate starvation-induced protein 5) identified by sequencesimilarity; putative InterPro: Pyridoxal-5-phosphate-dependent enzymes beta family; High confidence in function and specificity; Belongs to the cysteine synthase/cystathionine beta- synthase family.
  
 0.841
hom
Homoserine dehydrogenase; Identified by sequence similarity; putative identified by match to PFAM protein family HMMPF00742 InterPro: Homoserine dehydrogenase; High confidence in function and specificity.
   
 
  0.814
ilvA
Threonine dehydratase, biosynthetic; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA.
  
 
 0.803
Your Current Organism:
Alcanivorax borkumensis
NCBI taxonomy Id: 393595
Other names: A. borkumensis SK2, Alcanivorax borkumensis SK2, Alcanivorax borkumensis str. SK2, Alcanivorax borkumensis strain SK2
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