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
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[Homology]
Score
chlLLight-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein; 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. (288 aa)    
Predicted Functional Partners:
chlN
Light-independent protochlorophyllide reductase, N 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 (ChlN-ChlB) is the catalytic component of the complex.
 
 0.998
chlB
Light-independent protochlorophyllide reductase, B 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 (ChlN-ChlB) is the catalytic component of the complex.
 
 0.998
Tery_0876
TIGRFAM: bacteriochlorophyll/chlorophyll synthetase chlorophyll synthase, ChlG; PFAM: UbiA prenyltransferase; KEGG: ana:all4480 chlorophyll synthase 33 kD subunit.
 
 
 0.973
Tery_0742
PFAM: coenzyme F420 hydrogenase/dehydrogenase beta subunit-like; KEGG: ana:all1601 coenzyme F420 hydrogenase.
 
  
  0.964
Tery_0109
NADPH-protochlorophyllide oxidoreductase / chlorophyll synthase; Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).
     
 0.952
acsF
Mg-protoporphyrin IX monomethyl ester (oxidative) cyclase; Catalyzes the formation of the isocyclic ring in chlorophyll biosynthesis. Mediates the cyclase reaction, which results in the formation of divinylprotochlorophyllide (Pchlide) characteristic of all chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester (MgPMME); Belongs to the AcsF family.
 
  
 0.900
Tery_4133
TIGRFAM: nitrogenase cofactor biosynthesis protein NifB; PFAM: Dinitrogenase iron-molybdenum cofactor biosynthesis Radical SAM; KEGG: ava:Ava_3912 nitrogenase cofactor biosynthesis protein NifB.
 
  
 0.849
Tery_4148
KEGG: ava:Ava_0243 molybdate ABC transporter, permease protein; TIGRFAM: molybdate ABC transporter, inner membrane subunit; PFAM: binding-protein-dependent transport systems inner membrane component ABC transporter related; SMART: ATPase.
  
  
 0.808
Tery_0459
PFAM: PUCC protein major facilitator superfamily MFS_1; KEGG: syn:sll1906 hypothetical protein that may be an assembly factor for photosynthetic complex.
 
    0.782
Tery_1823
TIGRFAM: geranylgeranyl reductase; PFAM: monooxygenase, FAD-binding; KEGG: ava:Ava_1497 geranylgeranyl reductase.
  
  
 0.762
Your Current Organism:
Trichodesmium erythraeum
NCBI taxonomy Id: 203124
Other names: T. erythraeum IMS101, Trichodesmium erythraeum IMS101, Trichodesmium erythraeum str. IMS101, Trichodesmium erythraeum strain IMS101, Trichodesmium sp. IMS101
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