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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
purMTIGRFAM: phosphoribosylformylglycinamidine cyclo-ligase; KEGG: nmn:NMCC_1133 phosphoribosylaminoimidazole synthetase; PFAM: AIR synthase related protein domain protein; AIR synthase related protein. (360 aa)    
Predicted Functional Partners:
purN
Phosphoribosylglycinamide formyltransferase; Catalyzes the transfer of a formyl group from 10- formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
  
 0.999
purD
TIGRFAM: phosphoribosylamine/glycine ligase; KEGG: mei:Msip34_0380 phosphoribosylamine/glycine ligase; PFAM: Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, N-domain; Phosphoribosylglycinamide synthetase, C-domain; Belongs to the GARS family.
  
 0.998
purL
Phosphoribosylformylglycinamidine synthase; Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
  
 
 0.997
purF
Amidophosphoribosyltransferase; Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine; In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family.
  
 0.997
purC
TIGRFAM: phosphoribosylaminoimidazole-succinocarboxamide synthase; KEGG: mei:Msip34_0489 phosphoribosylaminoimidazole-succinocarboxamide synthase; PFAM: SAICAR synthetase.
 
  
 0.985
purH
SMART: AICARFT/IMPCHase bienzyme formylation region; MGS domain protein; TIGRFAM: phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; KEGG: nmu:Nmul_A0133 bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase; PFAM: AICARFT/IMPCHase bienzyme formylation region; MGS domain protein.
 
  
 0.985
purE
Phosphoribosylaminoimidazole carboxylase, catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
 
 0.978
purE-2
Phosphoribosylaminoimidazole carboxylase, catalytic subunit; Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
 
 
 0.978
Slit_0953
TIGRFAM: adenylosuccinate lyase; KEGG: mei:Msip34_0992 adenylosuccinate lyase; PFAM: Adenylosuccinate lyase domain protein; fumarate lyase; Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
  
 
 0.931
purT
Phosphoribosylglycinamide formyltransferase 2; Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate; Belongs to the PurK/PurT family.
  
  
 0.872
Your Current Organism:
Sideroxydans lithotrophicus
NCBI taxonomy Id: 580332
Other names: S. lithotrophicus ES-1, Sideroxydans lithotrophicus ES-1, Sideroxydans lithotrophicus str. ES-1, Sideroxydans lithotrophicus strain ES-1, iron-oxidizing lithotroph ES-1
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