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
ADO46518.1PFAM: phosphate transporter; KEGG: cko:CKO_04941 hypothetical protein. (498 aa)    
Predicted Functional Partners:
ADO47995.1
TIGRFAM: siroheme synthase; KEGG: aha:AHA_4121 siroheme synthase.
 
  
 0.657
cysG
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.
  
  
 0.608
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.
  
  
 0.608
ADO47428.1
KEGG: kva:Kvar_1155 phospholipase D/transphosphatidylase; PFAM: phospholipase D/Transphosphatidylase; SMART: phospholipase D/Transphosphatidylase.
  
     0.564
ADO46519.1
PFAM: HI0933 family protein; KEGG: enc:ECL_04910 hypothetical protein.
  
    0.552
ADO48687.1
KEGG: ent:Ent638_2136 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein; TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase, catalytic domain; Pyruvate-flavodoxin oxidoreductase, EKR domain; thiamine pyrophosphate TPP-binding domain-containing protein.
     
 0.543
hisB
TIGRFAM: histidinol-phosphatase; histidinol-phosphate phosphatase family protein; hydrolase, HAD-superfamily, subfamily IIIA; KEGG: cko:CKO_00763 imidazole glycerol-phosphate dehydratase/histidinol phosphatase; PFAM: imidazoleglycerol-phosphate dehydratase; In the N-terminal section; belongs to the histidinol- phosphatase family.
     
 0.513
ADO46763.1
KEGG: kpu:KP1_4936 glutamate synthase subunit alpha; PFAM: ferredoxin-dependent glutamate synthase; glutamine amidotransferase class-II; glutamate synthase; glutamate synthase alpha subunit domain protein.
  
  
 0.480
ppk
Polyphosphate kinase; Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Belongs to the polyphosphate kinase 1 (PPK1) family.
     
 0.447
ADO50658.1
Phosphate ABC transporter, periplasmic phosphate-binding protein; Part of the ABC transporter complex PstSACB involved in phosphate import; Belongs to the PstS family.
     
 0.447
Your Current Organism:
Enterobacter lignolyticus
NCBI taxonomy Id: 701347
Other names: Enterobacter lignolyticus SCF1, [. lignolyticus SCF1, [Enterobacter] lignolyticus SCF1
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