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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
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second shell of interactors
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filled nodes:
a 3D structure is known or predicted
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[Homology]
Score
hisZATP phosphoribosyltransferase regulatory subunit; Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine. (392 aa)    
Predicted Functional Partners:
hisG
ATP phosphoribosyltransferase; Catalyzes the condensation of ATP and 5-phosphoribose 1- diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. Belongs to the ATP phosphoribosyltransferase family. Short subfamily.
 
 0.975
hisI
PFAM: Phosphoribosyl-AMP cyclohydrolase; Phosphoribosyl-ATP pyrophosphohydrolase-like; TIGRFAM: Phosphoribosyl-ATP pyrophosphohydrolase; HAMAP: Phosphoribosyl-ATP pyrophosphohydrolase; Histidine biosynthesis bifunctional protein HisIE; KEGG: pmf:P9303_18291 bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP pyrophosphatase protein; In the N-terminal section; belongs to the PRA-CH family.
  
 
 0.937
prs
Ribose-phosphate pyrophosphokinase; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
    
 0.858
EHA63430.1
KEGG: pmf:P9303_15251 heat shock protein 90; PFAM: ATPase-like, ATP-binding domain; Heat shock protein Hsp90, C-terminal; SMART: ATPase-like, ATP-binding domain.
 
 
   0.810
aspS
aspartyl-tRNA synthetase; Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn); Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
  
  
 0.781
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.
       0.698
EHA63427.1
PFAM: Inositol monophosphatase; KEGG: pmt:PMT0699 inositol phosphatase/fructose-1,6-bisphosphatase.
  
    0.693
EHA63426.1
PFAM: Ferredoxin; KEGG: pmf:P9303_29191 ferredoxin, PetF like protein.
       0.687
pheT
TIGRFAM: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial; KEGG: pmf:P9303_14801 phenylalanyl-tRNA synthetase subunit beta; HAMAP: Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial.
  
  
 0.652
metG
Methionyl-tRNA synthetase; Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
  
 
 0.598
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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