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MMAR_1069 MMAR_1069 MMAR_1068 MMAR_1068 xylB xylB MMAR_1067 MMAR_1067 secY secY MMAR_2598 MMAR_2598 adk adk mapA mapA
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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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colored nodes:
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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Edges represent protein-protein associations
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
MMAR_1069O-methyltransferase; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity. (316 aa)    
Predicted Functional Partners:
MMAR_1068
O-methyltransferase; Exhibits S-adenosyl-L-methionine-dependent methyltransferase activity.
 
    
0.780
xylB
D-xylulose-kinase (xylulokinase), XylB; Phosphorylates D-xylulose [catalytic activity: ATP + D-xylulose = ADP + D-xylulose 5-phosphate].
      
 0.608
MMAR_1067
Conserved protein.
      
 0.608
secY
Preprotein translocase, SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
       0.508
MMAR_2598
Conserved hypothetical protein; Belongs to the long-chain O-acyltransferase family.
      
 0.474
adk
Adenylate kinase (ATP-AMP transphosphorylase), Adk; Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism; Belongs to the adenylate kinase family.
       0.472
mapA
Methionine aminopeptidase, MapA; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
       0.472
Your Current Organism:
Mycobacterium marinum
NCBI taxonomy Id: 216594
Other names: M. marinum M, Mycobacterium marinum M, Mycobacterium marinum str. M, Mycobacterium marinum strain M
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