STRINGSTRING
purD purD Bsel_0708 Bsel_0708 purK purK Bsel_1433 Bsel_1433 Bsel_1434 Bsel_1434 carB carB sucC sucC ddl ddl carB-2 carB-2 Bsel_2272 Bsel_2272
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:
purDTIGRFAM: phosphoribosylamine/glycine ligase; KEGG: vfm:VFMJ11_2513 phosphoribosylamine--glycine ligase; PFAM: Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase, N-domain; Phosphoribosylglycinamide synthetase, C-domain; protein of unknown function DUF201; ATP-grasp domain protein; Belongs to the GARS family. (422 aa)
Bsel_0708D-alanine--D-alanine ligase domain protein; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (714 aa)
purKPhosphoribosylaminoimidazole carboxylase, ATPase subunit; Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). (381 aa)
Bsel_1433PFAM: RimK domain protein ATP-grasp; KEGG: apa:APP7_0562 ribosomal protein S6 modification protein. (291 aa)
Bsel_1434alpha-L-glutamate ligase, RimK family; KEGG: hap:HAPS_0258 ribosomal protein S6 modification protein, glutamic acid ligase; TIGRFAM: alpha-L-glutamate ligase, RimK family; PFAM: RimK domain protein ATP-grasp; protein of unknown function DUF201; Belongs to the RimK family. (310 aa)
carBKEGG: dal:Dalk_3481 carbamoyl-phosphate synthase, large subunit; TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; ATP-dependent carboxylate-amine ligase domain protein ATP-grasp; protein of unknown function DUF201; RimK domain protein ATP-grasp; MGS domain protein; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein; Belongs to the CarB family. (1071 aa)
sucCsuccinyl-CoA synthetase, beta subunit; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. (387 aa)
ddlD-alanine/D-alanine ligase; Cell wall formation; Belongs to the D-alanine--D-alanine ligase family. (359 aa)
carB-2KEGG: ppd:Ppro_2524 carbamoyl-phosphate synthase, large subunit; TIGRFAM: carbamoyl-phosphate synthase, large subunit; PFAM: Carbamoyl-phosphate synthase L chain ATP-binding; RimK domain protein ATP-grasp; Carbamoyl-phosphate synthetase large chain oligomerisation; Carbamoyl-phosphate synthetase large chain domain protein. (1079 aa)
Bsel_2272acetyl-CoA carboxylase, biotin carboxylase; This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. (453 aa)
Your Current Organism:
Bacillus selenitireducens
NCBI taxonomy Id: 439292
Other names: Bacillus selenitireducens MLS10, [. selenitireducens MLS10, [Bacillus] selenitireducens MLS10
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.