STRINGSTRING
CAJ70573.1 CAJ70573.1 aspC aspC CAJ67574.1 CAJ67574.1 iscS1 iscS1 speA speA CAJ67835.1 CAJ67835.1 CAJ67914.1 CAJ67914.1 iscS2 iscS2 aspB aspB CAJ68270.1 CAJ68270.1 hisC hisC gcvTPA gcvTPA gcvPB gcvPB metY metY CAJ68848.1 CAJ68848.1 argM argM gabT gabT hisC-2 hisC-2 CAJ69139.1 CAJ69139.1 CD630_22850 CD630_22850 CAJ69267.1 CAJ69267.1 CAJ69309.1 CAJ69309.1 PatB1 PatB1 selA selA CAJ69388.1 CAJ69388.1 AspD AspD CAJ69419.1 CAJ69419.1 ltaE ltaE CobD1 CobD1 SufS2 SufS2 PatB2 PatB2 glyA glyA CAJ69620.1 CAJ69620.1 PatA PatA glyA1 glyA1 phnXW phnXW malY malY SufS1 SufS1 CAJ70252.1 CAJ70252.1 cobD cobD PatB3 PatB3 SpeA2 SpeA2 mdeA mdeA DgaE DgaE
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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
Node Content
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
Others
textmining
co-expression
protein homology
Your Input:
CAJ70573.1Putative aminotransferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant PMID:24568651. Experimentally verified as part of mature spore proteome PMID:19542279. (398 aa)
aspCAspartate aminotransferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant PMID:24568651. (394 aa)
CAJ67574.1Putative pyridoxal phosphate-dependent aminotransferase. (365 aa)
iscS1Cysteine desulfurase. (383 aa)
speAArginine decarboxylase. (491 aa)
CAJ67835.1Putative serine-pyruvate aminotransferase. (358 aa)
CAJ67914.1Putative aminotransferase. (484 aa)
iscS2Cysteine desulfurase; Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (397 aa)
aspBAspartate aminotransferase (AspAT) (Transaminase A); Experimentally verified as part of mature spore proteome PMID:19542279. (398 aa)
CAJ68270.1Transcriptional regulator, GntR family. (482 aa)
hisCHistidinol-phosphate aminotransferase (Imidazole acetol-phosphate transaminase); Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (349 aa)
gcvTPABi-functional glycine dehydrogenase/aminomethyl transferase protein; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. N-terminal subunit subfamily. (824 aa)
gcvPBGlycine decarboxylase; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein; Belongs to the GcvP family. C-terminal subunit subfamily. (485 aa)
metYO-acetylhomoserine sulfhydrylase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: down-regulated in Spo0A mutant PMID:24568651. (421 aa)
CAJ68848.1Aluminum resistance protein. (426 aa)
argMSuccinylornithine transaminase (ACOAT); Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. ArgD subfamily. (395 aa)
gabT4-aminobutyrate aminotransferase; Experimentally verified through Mass Spectrometry as part of Spo0A regulated proteome: up-regulated in Spo0A mutant PMID:24568651. Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (441 aa)
hisC-2Histidinol-phosphate aminotransferase; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. Histidinol-phosphate aminotransferase subfamily. (367 aa)
CAJ69139.1Transcriptional regulator, GntR family. (460 aa)
CD630_22850Fragment of putative beta-lactamase inducer (C-terminal region). (461 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)
CAJ69309.1Putative pyridoxal phosphate-dependent transferase. (402 aa)
PatB1Putative aminotransferase. (392 aa)
selAL-seryl-tRNA(Sec) selenium transferase; Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. (467 aa)
CAJ69388.1Putative pyridoxal phosphate-dependent transferase; Experimentally verified through RNA-seq as part of Spo0A regulated transcriptome: up-regulated in Spo0A mutant. Experimentally verified through Mass Spectrometry as part of Spo0A regulated proteome: up-regulated in Spo0A mutant PMID:24568651. (367 aa)
AspDPutative L-aspartate-beta-decarboxylase; Experimentally verified as part of mature spore proteome PMID:19542279. (542 aa)
CAJ69419.1Aminotransferase, alanine--glyoxylate transaminase. (380 aa)
ltaELow specificity L-threonine aldolase. (344 aa)
CobD1Putative threonine-phosphate decarboxylase. (358 aa)
SufS2Putative cysteine desulfurase family protein. (380 aa)
PatB2Putative pyridoxal phosphate-dependent transferase. (396 aa)
glyASerine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (414 aa)
CAJ69620.1Putative pyridoxal phosphate-dependent transferase. (388 aa)
PatAPutative pyridoxal phosphate-dependent transferase. (399 aa)
glyA1Serine hydroxymethyltransferase (Serine methylase) (SHMT); Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. (418 aa)
phnXWBifunctional phosphonoacetaldehyde hydrolase/aminoethylphosphonate transaminase; Involved in phosphonate degradation; In the N-terminal section; belongs to the HAD-like hydrolase superfamily. PhnX family. (636 aa)
malYBifunctional protein: cystathionine beta-lyase / repressor. (394 aa)
SufS1Putative aminotransferase; Experimentally verified as part of mature spore proteome PMID:19542279. (424 aa)
CAJ70252.1Transcriptional regulator, GntR family. (471 aa)
cobDThreonine-phosphate decarboxylase (L-threonine-O-3-phosphate decarboxylase), CobD/CbiB family. (356 aa)
PatB3Putative pyridoxal phosphate-dependent transferase (PLP-dependent transferase). (395 aa)
SpeA2Putative arginine decarboxylase. (469 aa)
mdeAMethionine gamma-lyase. (384 aa)
DgaEPutative selenocysteine synthase. (369 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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