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
hemHProtoporphyrin ferrochelatase; Catalyzes the ferrous insertion into protoporphyrin IX. Belongs to the ferrochelatase family. (362 aa)    
Predicted Functional Partners:
APA99875.1
Protoporphyrinogen oxidase; Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
 
 
 0.997
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III.
 
  
 0.976
APA99872.1
KEGG: nno:NONO_c52570 chlorite dismutase.
  
 0.970
chlD
Magnesium chelatase; Involved in bacteriochlorophyll biosynthesi; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. Belongs to the Mg-chelatase subunits D/I family; KEGG: nno:NONO_c55210 magnesium chelatase subunit D.
  
 
 0.949
hmoX
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Belongs to the heme oxygenase family; KEGG: sgr:SGR_5243 heme oxygenase.
 
  
 0.940
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.
   
 
 0.923
APB00682.1
Mediates copper resistance by sequestration of copper in the periplasm along with the copper-binding protein CopC. May have oxidase activity. Belongs to the multicopper oxidase family. CopA subfamily.
   
 
 0.922
ftnA
Bacterial non-heme ferritin; Iron-storage protein.
    
 0.918
hemG
Protoporphyrinogen IX dehydrogenase (menaquinone); KEGG: msv:Mesil_0168 menaquinone-dependent protoporphyrinogen oxidase.
    
 0.911
APA98350.1
Protoporphyrinogen IX dehydrogenase (menaquinone); KEGG: nbr:O3I_018085 menaquinone-dependent protoporphyrinogen oxidase.
    
 0.911
Your Current Organism:
Nocardia seriolae
NCBI taxonomy Id: 37332
Other names: ATCC 43993, CCUG 46828, CIP 104778, DSM 44129, IFO 15557, JCM 3360, N. seriolae, NBRC 15557
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