STRINGSTRING
mtnD mtnD AGA85857.1 AGA85857.1 mtnA mtnA AGA87696.1 AGA87696.1 AGA86636.1 AGA86636.1 AGA86450.1 AGA86450.1 speE speE AGA87158.1 AGA87158.1 AGA84924.1 AGA84924.1 AGA86448.1 AGA86448.1 metZ metZ
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
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[Homology]
Score
mtnDHypothetical protein, contains double-stranded beta-helix domain; Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4- methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway. (181 aa)    
Predicted Functional Partners:
AGA85857.1
PFAM: Aminotransferase class I and II.
     
 0.915
mtnA
Methylthioribose-1-phosphate isomerase; Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
 
 
 0.832
AGA87696.1
Ribulose-5-phosphate 4-epimerase-like epimerase or aldolase; PFAM: Class II Aldolase and Adducin N-terminal domain.
  
  
 0.788
AGA86636.1
Methionine synthase (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.
  
  
 0.682
AGA86450.1
Arabinose efflux permease family protein; PFAM: Nucleoside H+ symporter.
     
 0.648
speE
Spermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
 
   
 0.646
AGA87158.1
Methylthioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
 
 
 
 0.538
AGA84924.1
PFAM: Methylenetetrahydrofolate reductase; TIGRFAM: 5,10-methylenetetrahydrofolate reductase, prokaryotic form; Belongs to the methylenetetrahydrofolate reductase family.
   
  
 0.528
AGA86448.1
Hypothetical protein.
  
    0.496
metZ
O-succinylhomoserine sulfhydrylase; Catalyzes the formation of L-homocysteine from O-succinyl-L- homoserine (OSHS) and hydrogen sulfide.
   
  
 0.475
Your Current Organism:
Pseudomonas stutzeri
NCBI taxonomy Id: 644801
Other names: P. stutzeri RCH2, Pseudomonas stutzeri RCH2, Pseudomonas stutzeri str. RCH2, Pseudomonas stutzeri strain RCH2
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