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query proteins and first shell of interactors
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second shell of interactors
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bchFPossible 2-vinyl bacteriochlorophillide hydratase BchF subunit (AB034704). (161 aa)    
Predicted Functional Partners:
bchN
Protochlorophyllide reductase subunit BchN; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
 
 
 0.999
bchX
Bacteriochlorophyllide reductase subunit BchX; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished; Belongs to the NifH/BchL/ChlL family.
 
 
 0.997
bchZ
Bacteriochlorophyllide reductase subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
  
 
 0.997
bchG
Geranylgeranyl bacteriochlorophyll synthase.
 
 
 0.997
bchB
Protochlorophyllide reductase BchB subunit; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (BchN-BchB) is the catalytic component of the complex.
 
  
 0.997
bchL
Protochlorophyllide reductase iron-sulfur ATP-binding protein BchL; Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The L component serves as a unique electron donor to the NB-component of the complex, and binds Mg-ATP.
 
 
 0.997
bchC
2-desacetyl-2-hydroxyethyl bacteriochlorophyllide a dehydrogenase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
 
 
 0.995
bchY
Bacteriochlorophyllide reductase subunit BchY; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
  
 
 0.995
bchH
Magnesium-protoporphyrin O-methyltransferase BchH subunit; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
 
  
 0.988
bchM
Mg-protoporphyrin IX methyl transferase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished.
 
  
 0.984
Your Current Organism:
Rhodopseudomonas palustris CGA009
NCBI taxonomy Id: 258594
Other names: R. palustris CGA009, Rhodopseudomonas palustris str. CGA009, Rhodopseudomonas palustris strain CGA009
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