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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Edges represent protein-protein associations
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experimentally determined
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[Homology]
Score
EHA63371.1PFAM: Glucose-inhibited division protein A-related; KEGG: pmt:PMT0742 hypothetical protein. (608 aa)    
Predicted Functional Partners:
petC
Cytochrome b6-f complex iron-sulfur subunit; Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
  
 0.978
ndhH
NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 0.962
fumC
Fumarate hydratase class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
  
 0.950
EHA61798.1
TIGRFAM: 2-methylcitrate synthase/citrate synthase type I; KEGG: pmf:P9303_26921 citrate synthase; PFAM: Citrate synthase-like; Belongs to the citrate synthase family.
  
 0.932
EHA63429.1
4Fe-4S ferredoxin iron-sulfur binding domain-containing protein; Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
  
 0.928
ndhI
NAD(P)H-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient; Belongs to the complex I 23 kDa subunit family.
  
 0.928
ndhJ
NAD(P)H-quinone oxidoreductase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration.
   
 0.904
gcvP
Glycine dehydrogenase (decarboxylating); The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
   
  
 0.894
ndhK
NAD(P)H-quinone oxidoreductase subunit K; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon-concentration; Belongs to the complex I 20 kDa subunit family.
   
 0.874
EHA63514.1
Conserved hypothetical protein CHP00730; PFAM: Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG; KEGG: pmn:PMN2A_0462 putative DapE gene and orf2.
     
 0.869
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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