STRINGSTRING
bioF bioF bioA bioA fabG fabG bioH bioH fabZ fabZ A4SQW3_AERS4 A4SQW3_AERS4 rrmA rrmA fabG-3 fabG-3 A4SI85_AERS4 A4SI85_AERS4 fabF fabF fabB fabB A4SK47_AERS4 A4SK47_AERS4 A4SJH0_AERS4 A4SJH0_AERS4 A4SJH6_AERS4 A4SJH6_AERS4 fabF-2 fabF-2 A4SJI5_AERS4 A4SJI5_AERS4 fabG-2 fabG-2 A4SJI7_AERS4 A4SJI7_AERS4 birA birA pcm pcm A4SM70_AERS4 A4SM70_AERS4 bioD bioD bioC bioC bioB bioB
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:
bioFUnannotated protein; 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. (398 aa)
bioAUnannotated protein; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (424 aa)
fabGUnannotated protein; Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. Belongs to the short-chain dehydrogenases/reductases (SDR) family. (244 aa)
bioHUnannotated protein; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. (254 aa)
fabZUnannotated protein; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (153 aa)
A4SQW3_AERS4Unannotated protein. (327 aa)
rrmAUnannotated protein. (266 aa)
fabG-3Unannotated protein. (249 aa)
A4SI85_AERS4Unannotated protein. (249 aa)
fabFUnannotated protein; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. (413 aa)
fabBUnannotated protein; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (403 aa)
A4SK47_AERS4Unannotated protein. (306 aa)
A4SJH0_AERS4Unannotated protein. (239 aa)
A4SJH6_AERS4Unannotated protein. (123 aa)
fabF-2Unannotated protein; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (393 aa)
A4SJI5_AERS4Unannotated protein. (153 aa)
fabG-2Unannotated protein. (241 aa)
A4SJI7_AERS4Unannotated protein; Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (408 aa)
birAUnannotated protein; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (321 aa)
pcmUnannotated protein; Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. (205 aa)
A4SM70_AERS4Unannotated protein. (191 aa)
bioDUnannotated protein; 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. (226 aa)
bioCUnannotated protein; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. (270 aa)
bioBUnannotated protein; 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. (362 aa)
Your Current Organism:
Aeromonas salmonicida
NCBI taxonomy Id: 29491
Other names: A. salmonicida subsp. salmonicida, Aeromonas salmonicida salmonicida, Aeromonas salmonicida subsp. salmonicida
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.