STRINGSTRING
aspC aspC ord ord ArcB ArcB speA speA speH speH speE speE speB speB bltD bltD aspB aspB proC proC aldH aldH PatA PatA pepI pepI prdF prdF prdB prdB prdA prdA proC1 proC1 pflD-2 pflD-2 SpeA2 SpeA2
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:
aspCAspartate aminotransferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant PMID:24568651. (394 aa)
ord2,4-diaminopentanoate dehydrogenase. (355 aa)
ArcBPutative ornithine cyclodeaminase. (329 aa)
speAArginine decarboxylase. (491 aa)
speHS-adenosylmethionine decarboxylase proenzyme; Catalyzes the decarboxylation of S-adenosylmethionine to S- adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine; Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily. (137 aa)
speESpermidine synthase; Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. (283 aa)
speBAgmatinase (Agmatine ureohydrolase) (AUH); Belongs to the arginase family. (292 aa)
bltDDiamine N-acetyltransferase. (146 aa)
aspBAspartate aminotransferase (AspAT) (Transaminase A); Experimentally verified as part of mature spore proteome PMID:19542279. (398 aa)
proCPyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (267 aa)
aldHAldehyde dehydrogenase (aldehyde:NAD+ oxidoreductase); Belongs to the aldehyde dehydrogenase family. (454 aa)
PatAPutative pyridoxal phosphate-dependent transferase. (399 aa)
pepIProline iminopeptidase (Proline aminopeptidase) (PIP), peptidase S33 family; Releases the N-terminal proline from various substrates. Belongs to the peptidase S33 family. (293 aa)
prdFProline racemase; Strong B-cell mitogen. Plays an important role in the regulation of intra- and extracellular amino acid pools, allowing the bacterium to profit from host precursors and enzymatic pathways (By similarity). (335 aa)
prdBProline reductase (selenocysteine); Experimentally verified as part of mature spore proteome PMID:19542279. (241 aa)
prdAD-proline reductase proprotein prdA; Experimentally verified as part of mature spore proteome PMID:19542279. (626 aa)
proC1Pyrroline-5-carboxylate reductase; Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. (267 aa)
pflD-2Pyruvate formate-lyase. (789 aa)
SpeA2Putative arginine decarboxylase. (469 aa)
Your Current Organism:
Clostridioides difficile
NCBI taxonomy Id: 272563
Other names: C. difficile 630, Clostridioides difficile 630, Clostridium difficile 630, Clostridium difficile 630 (epidemic type X), Clostridium difficile str. 630, Clostridium difficile strain 630, Peptoclostridium difficile 630
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