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
hemHFerrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (340 aa)    
Predicted Functional Partners:
hemG
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
 
 
 0.996
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
  
 0.979
ABK71061.1
Conserved hypothetical protein; Identified by match to protein family HMM PF06778.
  
 0.965
ABK72276.1
Chelatase; Identified by match to protein family HMM PF00092; match to protein family HMM PF01078; match to protein family HMM PF07728.
  
 
 0.946
ABK73730.1
Magnesium chelatase.
 
 
 0.936
cyoE
Protoheme IX farnesyltransferase; Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group.
   
 
 0.930
bfrB
Ferritin family protein; Iron-storage protein that displays ferroxidase activity, catalyzing the oxidation of Fe(2+) ions into Fe(3+) ions, that can then be deposited as a ferric-oxide mineral core within the central cavity of the protein complex.
  
 
 0.927
bfr
Bacterioferritin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex; Belongs to the bacterioferritin family.
   
 
 0.925
inhA
[NADH] enoyl-[acyl-carrier-protein] reductase; Enoyl-ACP reductase of the type II fatty acid syntase (FAS- II) system, which is involved in the biosynthesis of mycolic acids, a major component of mycobacterial cell walls. Catalyzes the NADH-dependent reduction of the double bond of 2-trans- enoyl-[acyl-carrier protein], an essential step in the fatty acid elongation cycle of the FAS-II pathway. Shows preference for long-chain fatty acyl thioester substrates (>C16), and can also use 2-trans-enoyl-CoAs as alternative substrates (By similarity). The mycobacterial FAS-II system utilizes th [...]
 
  
 0.920
fabG-3
3-oxoacyl-(acyl-carrier-protein) reductase; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis; Belongs to the short-chain dehydrogenases/reductases (SDR) family.
  
  
 0.840
Your Current Organism:
Mycolicibacterium smegmatis
NCBI taxonomy Id: 246196
Other names: M. smegmatis MC2 155, Mycobacterium smegmatis MC2 155, Mycolicibacterium smegmatis MC2 155
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