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
Databases
Textmining
[Homology]
Score
hemLTIGRFAM: glutamate-1-semialdehyde-2,1-aminomutase; PFAM: aminotransferase class-III; KEGG: eca:ECA3307 glutamate-1-semialdehyde aminotransferase. (426 aa)    
Predicted Functional Partners:
PC1_4049
Porphobilinogen synthase; PFAM: delta-aminolevulinic acid dehydratase; KEGG: eca:ECA0203 delta-aminolevulinic acid dehydratase; Belongs to the ALAD family.
 
 
 0.993
hemA
glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
 
 0.988
hemC
Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family.
 
  
 0.933
PC1_0573
PFAM: KR domain protein; Acyl transferase; Beta-ketoacyl synthase; short-chain dehydrogenase/reductase SDR; phosphopantetheine-binding; KEGG: sil:SPO0849 non-ribosomal peptide synthase.
    
 0.922
PC1_0576
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; KEGG: scl:sce4135 hybrid polyketide synthase/nonribosomal peptide synthetase; Belongs to the ATP-dependent AMP-binding enzyme family.
    
 0.879
PC1_2728
TIGRFAM: uroporphyrin-III C-methyltransferase; PFAM: Uroporphyrin-III C/tetrapyrrole (Corrin/Porphyrin) methyltransferase; KEGG: eca:ECA2989 uroporphyrin-III C-methyltransferase; Belongs to the precorrin methyltransferase family.
 
   
 0.808
PC1_0572
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; Thioesterase; phosphopantetheine-binding; condensation domain protein; KEGG: mxa:MXAN_4000 non-ribosomal peptide synthetase.
  
 
 0.789
PC1_0468
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; KEGG: eca:ECA0483 putative non-ribosomal peptide synthetase; Belongs to the ATP-dependent AMP-binding enzyme family.
  
 
 0.762
cysG-2
uroporphyrin-III C-methyltransferase; Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. Belongs to the precorrin methyltransferase family. In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family.
   
 0.750
PC1_0578
TIGRFAM: amino acid adenylation domain protein; PFAM: AMP-dependent synthetase and ligase; phosphopantetheine-binding; condensation domain protein; KEGG: rso:RS05859 peptide synthetase protein; Belongs to the ATP-dependent AMP-binding enzyme family.
 
 
 0.745
Your Current Organism:
Pectobacterium carotovorum
NCBI taxonomy Id: 561230
Other names: P. carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum str. PC1, Pectobacterium carotovorum subsp. carotovorum strain PC1
Server load: low (40%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.