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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
azo3817Conserved hypothetical protein. Homology to slr1189 of Synechocystis of 43% (trembl|P74718). Pfam: Homocystein S-transferase. no signal peptide. no TMHs. (313 aa)    
Predicted Functional Partners:
metH
Probable methionine synthase; 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.
   
 
 0.925
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.
     
 0.670
metZ
Cys/Met metabolism pyridoxal-phosphate-dependent enzyme; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
  
 
 0.629
azo3816
Putative AraC family transcriptional regulator,; Family membership.
 
     0.611
metF
5,10-methylenetetrahydrofolate reductase (FADH2; 510-methylenetetrahydrofolate reductase InterPro: Methylenetetrahydrofolate reductase fadh2: 510-methylenetetrahydrofolate reductase; High confidence in function and specificity; Belongs to the methylenetetrahydrofolate reductase family.
   
 
 0.607
hom
Homoserine dehydrogenase catalyzes NAD-dependent reduction of aspartate beta-semialdehyde into homoserine. This reaction is the third step in a pathway leading from aspartate to homoserine. Similar to TREMBL:Q9RAM9 (77%) and to pir|DEPSHA(PIR (Georgetown University) (56%). Pfam: Homoserine dehydrogenase; High confidence in function and specificity.
   
 
 0.577
lysC
Aspartate kinase (AK) catalyzes the phosphorylation of aspartate. The product of this reaction can then be used in the biosynthesis of lysine or in the pathway leading to homoserine, which participates in the biosynthesis of threonine, isoleucine and methionine. Similar to trembl|Q8RU02 (80%) and to pir|C83531 (74%). Pfam (PF00696): Amino acid kinase family Pfam (PF01842): two ACT domain; High confidence in function and specificity; Belongs to the aspartokinase family.
     
 0.574
azo1737
Conserved hypothetical membrane protein. Homology to ebA6987 of Azoarcus sp. EbN1 of 62% (gnl|keqq|eba:ebA6987(KEGG)). no domains predicted. no signal peptide. 4 TMHs; Conserved hypothetical protein.
     
 0.554
tyrB
Probable aromatic-amino-acid aminotransferase. Homology to tyrB of E. coli of 52% (sprot|TYRB_ECO). Is involved in biosynthesis of phe, tyr, asp and leu. Catalyse the reactiion: an aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + l-glutamate. Pfam: Aminotransferase class I and II no signal peptide no TMHs; High confidence in function and specificity.
     
 0.548
ilvA
Probable threonine dehydratase; 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.
     
 0.514
Your Current Organism:
Azoarcus sp. BH72
NCBI taxonomy Id: 62928
Other names: A. sp. BH72
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