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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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[Homology]
Score
metAAHomoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (307 aa)    
Predicted Functional Partners:
AMS42929.1
O-acetylhomoserine aminocarboxypropyltransferase; Pfam:pfam01053 Cys/Met metabolizm PLP-dependent enzyme.
 
 
 0.968
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
 
 
 0.959
AMS42314.1
Pfam:pfam00742 Homoserine dehydrogenase.
  
 
 0.955
AMS42304.1
Homoserine O-acetyltransferase; Pfam:pfam00561 alpha/beta hydrolase fold; Belongs to the AB hydrolase superfamily. MetX family.
     
  0.900
AMS39129.1
Homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent; 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.
  
  
 0.868
AMS41708.1
Pfam:pfam02219 Methylenetetrahydrofolate reductase; Belongs to the methylenetetrahydrofolate reductase family.
  
  
 0.868
AMS39505.1
Cystathionine beta-synthase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
    
 0.824
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
    
  0.817
AMS41455.1
Serine dehydratase; Pfam:pfam00291 Pyridoxal-phosphate dependent enzyme.
   
 
 0.816
ilvA
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.
   
 
 0.816
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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