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aspC aspC metK metK speH speH speE speE CAJ67761.1 CAJ67761.1 serA serA hom1 hom1 dapG dapG aspB aspB sseA sseA hom2 hom2 cysK cysK cysE cysE cysM cysM metY metY metA metA lysC lysC CAJ68967.2 CAJ68967.2 CAJ68974.2 CAJ68974.2 ldh ldh CAJ69267.1 CAJ69267.1 PatB1 PatB1 AspD AspD mtnN mtnN PatB2 PatB2 CAJ69591.1 CAJ69591.1 CAJ69620.1 CAJ69620.1 PatA PatA malY malY CAJ70040.1 CAJ70040.1 sdaB sdaB asd asd PatB3 PatB3 mdeA mdeA MetH MetH luxS luxS
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
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aspCAspartate aminotransferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant PMID:24568651. (394 aa)
metKS-adenosylmethionine synthetase; Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme. (397 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)
CAJ67761.1Putative phage DNA modification methylase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. (357 aa)
serAPutative D-3-phosphoglycerate dehydrogenase; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (313 aa)
hom1Homoserine dehydrogenase. (401 aa)
dapGAspartokinase 1 (Aspartokinase I) (1spartate kinase I); Belongs to the aspartokinase family. (407 aa)
aspBAspartate aminotransferase (AspAT) (Transaminase A); Experimentally verified as part of mature spore proteome PMID:19542279. (398 aa)
sseA3-mercaptopyruvate sulfurtransferase. (283 aa)
hom2Homoserine dehydrogenase. (405 aa)
cysKO-acetyl-serine thiol-lyase A (O-acetyl-sulfhydrylase)(OAS-TL); Experimentally verified as part of mature spore proteome PMID:19542279. (302 aa)
cysESerine acetyltransferase (SAT); Experimentally verified through Mass Spectrometry as part of Spo0A regulated proteome: down-regulated in Spo0A mutant PMID:24568651. (196 aa)
cysMO-acetylserine (thiol)-lyase (O-acetylserine sulfhydrylase) (OAS-TL). (320 aa)
metYO-acetylhomoserine sulfhydrylase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: down-regulated in Spo0A mutant PMID:24568651. (421 aa)
metAHomoserine O-succinyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (296 aa)
lysCAspartokinase; Belongs to the aspartokinase family. (397 aa)
CAJ68967.2Amidohydrolase. (468 aa)
CAJ68974.2Putative metal-dependent hydrolase. (464 aa)
ldhL-lactate dehydrogenase (L-LDH); Catalyzes the conversion of lactate to pyruvate. (322 aa)
CAJ69267.1Putative pyridoxal phosphate-dependent transferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant PMID:24568651. (419 aa)
PatB1Putative aminotransferase. (392 aa)
AspDPutative L-aspartate-beta-decarboxylase; Experimentally verified as part of mature spore proteome PMID:19542279. (542 aa)
mtnNMTA/SAH nucleosidase (5'-methylthioadenosine nucleosidase) (S-adenosylhomocysteine nucleosidase); Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- methylthioribose and S-ribosylhomocysteine, respectively. Belongs to the PNP/UDP phosphorylase family. MtnN subfamily. (232 aa)
PatB2Putative pyridoxal phosphate-dependent transferase. (396 aa)
CAJ69591.1Putative amidohydrolase. (454 aa)
CAJ69620.1Putative pyridoxal phosphate-dependent transferase. (388 aa)
PatAPutative pyridoxal phosphate-dependent transferase. (399 aa)
malYBifunctional protein: cystathionine beta-lyase / repressor. (394 aa)
CAJ70040.1Putative DNA-methyltransferase; Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family. (541 aa)
sdaBL-serine dehydratase; Experimentally verified as part of mature spore proteome PMID:19542279; Belongs to the iron-sulfur dependent L-serine dehydratase family. (397 aa)
asdAspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (333 aa)
PatB3Putative pyridoxal phosphate-dependent transferase (PLP-dependent transferase). (395 aa)
mdeAMethionine gamma-lyase. (384 aa)
MetHPutative homocysteine S-methyltransferase. (793 aa)
luxSS-ribosylhomocysteine lyase (Autoinducer-2 production protein luxS) (AI-2 synthesis protein); Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Belongs to the LuxS family. (151 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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