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hemL protein (Synechococcus elongatus PCC7942) - STRING interaction network
"hemL" - annotation not available in Synechococcus elongatus PCC7942
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second shell of interactors
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
hemLannotation not available (453 aa)    
Predicted Functional Partners:
hemA
Glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl- tRNA(Glu) to glutamate 1-semialdehyde (GSA) (438 aa)
 
  0.998
hemB
Delta-aminolevulinic acid dehydratase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity) (326 aa)
 
 
  0.997
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps (320 aa)
 
   
  0.969
hemD
Uroporphyrinogen-III synthase; Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III (264 aa)
 
 
  0.957
chlD
Magnesium-chelatase subunit ChlD; Involved in chlorophyll biosynthesis; introduces a magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX (677 aa)
     
   
  0.865
gltX
Glutamate--tRNA ligase; Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction- glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu) (481 aa)
   
   
  0.861
hemE
Uroporphyrinogen decarboxylase; Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III (354 aa)
 
   
  0.859
ABB56678.1
annotation not available (75 aa)
              0.845
chlL
Light-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 (286 aa)
           
  0.770
chlN
Light-independent protochlorophyllide reductase subunit N; 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 (466 aa)
           
  0.769
Your Current Organism:
Synechococcus elongatus PCC7942
NCBI taxonomy Id: 1140
Other names: Anacystis nidulans R2, S. elongatus PCC 7942, Synechococcus elongatus PCC 7942, Synechococcus elongatus PCC7942, Synechococcus leopoliensis UTEX 2434, Synechococcus leopoliensis strain PCC 7942, Synechococcus sp. IAM M-200, Synechococcus sp. PCC 7942
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