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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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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
AMS41845.1Precorrin-2 C20-methyltransferase; Pfam:pfam00590 Tetrapyrrole (Corrin/Porphyrin) Methylases; Belongs to the precorrin methyltransferase family. (250 aa)    
Predicted Functional Partners:
AMS41844.1
precorrin-3B C17-methyltransferase; Pfam:pfam00590 Tetrapyrrole (Corrin/Porphyrin) Methylases.
 
 0.999
AMS41846.1
Pfam:pfam02570 Precorrin-8X methylmutase.
 
  
 0.993
AMS41847.1
Cobalamin biosynthesis protein CobG; Pfam:pfam03460 Nitrite/Sulfite reductase ferredoxin-like half domain.
 
 
 0.993
AMS41842.1
Precorrin-6Y C(5,15)-methyltransferase (Decarboxylating); Pfam:pfam00590 Tetrapyrrole (Corrin/Porphyrin) Methylases.
 
  
 0.979
AMS41840.1
Precorrin-4 C11-methyltransferase; Pfam:pfam00590 Tetrapyrrole (Corrin/Porphyrin) Methylases; Belongs to the precorrin methyltransferase family.
 
  
 0.971
AMS41843.1
Pfam:pfam02571 Precorrin-6x reductase CbiJ/CobK.
 
  
 0.965
AMS41848.1
Cobalt chelatase; Pfam:pfam02514 CobN/Magnesium Chelatase.
 
  
 0.963
AMS39211.1
Siroheme synthase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme.
 
 
 0.958
AMS41838.1
uroporphyrin-III C-methyltransferase; Pfam:pfam00590 Tetrapyrrole (Corrin/Porphyrin) Methylases.
 
 
 0.942
cobQ
Cobyric acid synthase; Catalyzes amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide. NH(2) groups are provided by glutamine, and one molecule of ATP is hydrogenolyzed for each amidation. Belongs to the CobB/CobQ family. CobQ subfamily.
 
  
 0.936
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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