close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Mvan_3849TIGRFAM: amino acid adenylation domain; PFAM: AMP-dependent synthetase and ligase; condensation domain protein; phosphopantetheine-binding; Non-ribosomal peptide synthetase; KEGG: mmc:Mmcs_3470 amino acid adenylation. (1149 aa)    
Predicted Functional Partners:
Mvan_3124
PFAM: beta-ketoacyl synthase; acyl transferase domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR; KEGG: mbo:Mb2959 phenolpthiocerol synthesis type-I polyketide synthase PpsD.
 
 0.999
Mvan_3126
PFAM: beta-ketoacyl synthase; acyl transferase domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR; KEGG: mmc:Mmcs_2835 beta-ketoacyl synthase.
 
 0.999
Mvan_3842
PFAM: MbtH domain protein; KEGG: mmc:Mmcs_3463 MbtH-like protein.
 
 
 0.999
Mvan_3846
PFAM: acyl transferase domain protein; NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR; KEGG: mmc:Mmcs_3467 acyl transferase region.
 
 0.999
Mvan_3847
PFAM: beta-ketoacyl synthase; KEGG: mmc:Mmcs_3468 beta-ketoacyl synthase; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family.
 
 0.999
Mvan_5640
Mycolic acid condensase; PFAM: beta-ketoacyl synthase; Thioesterase; acyl transferase domain protein; phosphopantetheine-binding; KEGG: mmc:Mmcs_5010 beta-ketoacyl synthase.
 
 0.998
Mvan_0269
PFAM: beta-ketoacyl synthase; acyl transferase domain protein; NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase, zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR; KEGG: mmc:Mmcs_0244 beta-ketoacyl synthase.
 
 0.997
Mvan_1003
PFAM: beta-ketoacyl synthase; acyl transferase domain protein; NAD-dependent epimerase/dehydratase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; Alcohol dehydrogenase, zinc-binding domain protein; Alcohol dehydrogenase GroES domain protein; KR; KEGG: mpa:MAP2230c hypothetical protein.
 
 0.997
Mvan_3125
PFAM: beta-ketoacyl synthase; acyl transferase domain protein; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KR; KEGG: mmc:Mmcs_2833 beta-ketoacyl synthase.
 
 0.997
Mvan_3850
PFAM: AMP-dependent synthetase and ligase; KEGG: mmc:Mmcs_3471 AMP-dependent synthetase and ligase.
 
0.997
Your Current Organism:
Mycolicibacterium vanbaalenii
NCBI taxonomy Id: 350058
Other names: M. vanbaalenii PYR-1, Mycobacterium sp. PYR-1, Mycobacterium vanbaalenii DSM 7251, Mycobacterium vanbaalenii PYR-1, Mycolicibacterium vanbaalenii DSM 7251, Mycolicibacterium vanbaalenii PYR-1
Server load: low (24%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.