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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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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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speESpermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. (315 aa)    
Predicted Functional Partners:
speH
S-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily.
 
 0.999
AFY39232.1
Agmatinase; PFAM: Arginase family; TIGRFAM: agmatinase; COGs: COG0010 Arginase/agmatinase/formimionoglutamate hydrolase arginase family; InterPro IPR005925:IPR006035; KEGG: syp:SYNPCC7002_A1109 agmatinase, putative; PFAM: Ureohydrolase; PRIAM: Agmatinase; SPTR: Agmatinase, putative; TIGRFAM: Putative agmatinase; Belongs to the arginase family.
 
 
 0.952
mtnP
Methylthioadenosine phosphorylase; Catalyzes the reversible phosphorylation of S-methyl-5'- thioadenosine (MTA) to adenine and 5-methylthioribose-1-phosphate. Involved in the breakdown of MTA, a major by-product of polyamine biosynthesis. Responsible for the first step in the methionine salvage pathway after MTA has been generated from S-adenosylmethionine. Has broad substrate specificity with 6-aminopurine nucleosides as preferred substrates; Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.
  
 
 0.945
AFY36898.1
Agmatinase; PFAM: Arginase family; TIGRFAM: agmatinase; COGs: COG0010 Arginase/agmatinase/formimionoglutamate hydrolase arginase family; InterPro IPR006035; KEGG: mar:MAE_18840 agmatinase; PFAM: Ureohydrolase; PRIAM: Agmatinase; SPTR: Arginase family; Belongs to the arginase family.
  
 
 0.933
AFY40247.1
Agmatinase; PFAM: Arginase family; TIGRFAM: agmatinase; arginase; COGs: COG0010 Arginase/agmatinase/formimionoglutamate hydrolase arginase family; InterPro IPR006035; KEGG: syp:SYNPCC7002_A1751 arginase/agmatinase family protein; PFAM: Ureohydrolase; PRIAM: Agmatinase; SPTR: Arginase/agmatinase family protein; Belongs to the arginase family.
  
 
 0.933
AFY36764.1
PFAM: Multi-copper polyphenol oxidoreductase laccase; TIGRFAM: uncharacterized protein, YfiH family; COGs: COG1496 conserved hypothetical protein; InterPro IPR003730; KEGG: syp:SYNPCC7002_A0954 hypothetical protein; PFAM: Multi-copper polyphenol oxidoreductase, laccase; SPTR: Putative uncharacterized protein; TIGRFAM: Multi-copper polyphenol oxidoreductase, laccase; Belongs to the multicopper oxidase YfiH/RL5 family.
    
  0.900
AFY38143.1
PFAM: Orn/Lys/Arg decarboxylase, C-terminal domain; Orn/Lys/Arg decarboxylase, major domain; COGs: COG1982 Arginine/lysine/ornithine decarboxylase; InterPro IPR000310:IPR008286; KEGG: syp:SYNPCC7002_A1159 Orn/Lys/Arg decarboxylase; PFAM: Orn/Lys/Arg decarboxylase, major domain; Orn/Lys/Arg decarboxylase, C-terminal; PRIAM: Arginine decarboxylase; SPTR: Orn/Lys/Arg decarboxylase.
  
 0.670
metK
Methionine adenosyltransferase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
  
  
 0.471
pyrG
CTP synthase; Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
  
    0.467
nnrD
YjeF-related protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epi [...]
  
  
 0.464
Your Current Organism:
Leptolyngbya sp. PCC7376
NCBI taxonomy Id: 111781
Other names: Enugrolinea bermudensis PCC 7376, L. sp. PCC 7376, Leptolyngbya PCC7376, Leptolyngbya sp. PCC 7376
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