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
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[Homology]
Score
lipA-2Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. (293 aa)    
Predicted Functional Partners:
lipB
Lipoate-protein ligase B; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate- dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
 
 0.997
AFZ47505.1
PFAM: Biotin/lipoate A/B protein ligase family; COGs: COG0095 Lipoate-protein ligase A; InterPro IPR004143; KEGG: mar:MAE_41170 biotin/lipoate A/B protein ligase family protein; PFAM: biotin/lipoate A/B protein ligase; SPTR: Biotin/lipoate A/B protein ligase family protein.
 
 
 0.937
lipA
Lipoic acid synthetase; Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
  
  
 
0.906
gcvH
Glycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein.
 
 
 0.753
AFZ48264.1
FAD linked oxidase domain protein; PFAM: FAD binding domain; COGs: COG0277 FAD/FMN-containing dehydrogenase; InterPro IPR006094:IPR016166; KEGG: cyh:Cyan8802_1443 FAD linked oxidase domain protein; PFAM: FAD linked oxidase domain protein; SPTR: FAD linked oxidase domain protein.
       0.508
gcvP
Glycine dehydrogenase (decarboxylating) beta subunit; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family.
  
  
 0.485
AFZ48262.1
PFAM: MatE; TIGRFAM: putative efflux protein, MATE family; COGs: COG0534 Na+-driven multidrug efflux pump; InterPro IPR002528; KEGG: syn:slr0896 hypothetical protein; PFAM: multi antimicrobial extrusion protein MatE; SPTR: MATE efflux family protein; TIGRFAM: MATE efflux family protein.
     
 0.478
AFZ48454.1
Catalytic domain-containing protein of components of various dehydrogenase complexes; PFAM: 2-oxoacid dehydrogenases acyltransferase (catalytic domain); e3 binding domain; Biotin-requiring enzyme; TIGRFAM: pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form; COGs: COG0508 Pyruvate/2-oxoglutarate dehydrogenase complex dihydrolipoamide acyltransferase (E2) protein; InterPro IPR000089:IPR004167:IPR001078:IPR003016; KEGG: syp:SYNPCC7002_A0110 branched-chain alpha-keto acid dehydrogenase subunit E2; PFAM: catalytic domain-containing protein of components of various [...]
 
  
 0.414
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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