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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
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[Homology]
Score
AMF96464.1Mononuclear molybdenum enzyme YedY; In Escherichia coli this periplasmic enzyme was found to encode the periplasmic catalytic subunit of an oxidoreductase; requires inner membrane anchor protein YedZ; Derived by automated computational analysis using gene prediction method: Protein Homology. (334 aa)    
Predicted Functional Partners:
msrQ
Sulfoxide reductase heme-binding subunit YedZ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalyti [...]
 
  
 0.998
coxB
Cytochrome B559 subunit alpha; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
   
 
 0.735
CcoP
Cytochrome C oxidase Cbb3; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.638
AMG00040.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.638
AMG00666.1
Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.638
AMG00927.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.638
mobB
Molybdopterin-guanine dinucleotide biosynthesis protein MobB; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.
 
 
 
 0.567
moeA
Molybdenum cofactor biosynthesis protein MoaA; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family.
 
 
 
 0.481
moaE
Molybdopterin synthase catalytic subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
   
 0.463
AMG01405.1
Methionine sulfoxide reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.437
Your Current Organism:
Vibrio harveyi
NCBI taxonomy Id: 669
Other names: ATCC 14126, Achromobacter harveyi, Beneckea harveyi, Beneckea neptuna, CAIM 513, CCUG 28584, CECT 525, CIP 103192, DSM 19623, IFO 15634, LMG 4044, LMG:4044, Lucibacterium harveyi, NBRC 15634, NCCB 80033, NCTC 12970, Photobacterium harveyi, Pseudomonas harveyi, V. harveyi, Vibrio carchariae, Vibrio sp. HENC-01, Vibrio sp. HENC-02, Vibrio sp. PG 001, Vibrio sp. PG 002, Vibrio sp. PG 006, Vibrio sp. PG 007, Vibrio trachuri
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