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
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family. (336 aa)    
Predicted Functional Partners:
bioD
Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.
 
 
 0.998
AFY32069.1
PFAM: Biotin/lipoate A/B protein ligase family; TIGRFAM: birA, biotin-[acetyl-CoA-carboxylase] ligase region; COGs: COG0340 Biotin-(acetyl-CoA carboxylase) ligase; InterPro IPR004143:IPR004408; KEGG: npu:Npun_F0057 biotin--acetyl-CoA-carboxylase ligase; PFAM: Biotin/lipoate A/B protein ligase; SPTR: Biotin acetyl-CoA carboxylase ligase; TIGRFAM: Biotin--acetyl-CoA-carboxylase ligase.
  
 
 0.938
AFY35278.1
8-amino-7-oxononanoate synthase; Catalyzes the decarboxylative condensation of pimeloyl-[acyl- carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide.
  
 0.927
AFY31581.1
PFAM: Aminotransferase class-III; TIGRFAM: 4-aminobutyrate aminotransferase, prokaryotic type; COGs: COG0160 4-aminobutyrate aminotransferase and related aminotransferase; HAMAP: Acetylornithine/succinyldiaminopimelate aminotransferase; InterPro IPR005814; KEGG: npu:Npun_F1941 4-aminobutyrate aminotransferase; PFAM: Aminotransferase class-III; PRIAM: Acetylornithine transaminase; SPTR: Aminotransferase class-III; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.
 
    
 0.668
AFY35154.1
PFAM: BioY family; COGs: COG1268 conserved hypothetical protein; InterPro IPR003784; KEGG: npu:Npun_R0890 BioY protein; PFAM: BioY protein; SPTR: BioY protein; manually curated.
 
  
 0.589
argD
PFAM: Aminotransferase class-III; TIGRFAM: acetylornithine and succinylornithine transaminases; COGs: COG4992 Ornithine/acetylornithine aminotransferase; HAMAP: Acetylornithine/succinyldiaminopimelate aminotransferase; InterPro IPR005814:IPR004636; KEGG: npu:Npun_R4958 acetylornithine aminotransferase; PFAM: Aminotransferase class-III; PRIAM: Acetylornithine transaminase; SPTR: N-acetylornithine aminotransferase; TIGRFAM: Acetylornithine/succinylornithine aminotransferase; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily.
 
 
  
 0.588
thiC
Hydroxymethylpyrimidine synthase; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. Belongs to the ThiC family.
 
  
 0.587
thiG
Thiazole-phosphate synthase; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S.
 
  
 0.529
nadA
Quinolinate synthetase; Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
  
  
 0.508
AFY34535.1
Urea carboxylase; PFAM: Carbamoyl-phosphate synthase L chain, ATP binding domain; Biotin carboxylase C-terminal domain; Allophanate hydrolase subunit 2; Carbamoyl-phosphate synthase L chain, N-terminal domain; Allophanate hydrolase subunit 1; Biotin-requiring enzyme; TIGRFAM: urea carboxylase; biotin-dependent carboxylase uncharacterized domain; COGs: COG4770 Acetyl/propionyl-CoA carboxylase alpha subunit; InterProIPR014084:IPR003778:IPR005482:IPR003833:IPR 005481:IPR005479:IPR000089; KEGG: cyn:Cyan7425_2304 UreA carboxylase; PFAM: Allophanate hydrolase subunit 2; Carbamoyl-phosphate s [...]
  
  
 0.477
Your Current Organism:
Calothrix sp. PCC7507
NCBI taxonomy Id: 99598
Other names: C. sp. PCC 7507, Calothrix sp. PCC 7507
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