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cysI cysI ytkP ytkP mccA mccA mccB mccB cysH cysH metC metC metI metI yitB yitB cysE cysE cysK cysK yxeP yxeP cysJ cysJ thrC thrC yxeK yxeK yxeL yxeL
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
Predicted Interactions
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textmining
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cysISulfite reductase (hemoprotein beta-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate (Probable); Belongs to the nitrite and sulfite reductase 4Fe-4S domain family. (571 aa)
ytkPPutative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (311 aa)
mccACystathionine beta-synthase for the reverse transsulfuration pathway; Catalyzes the conversion of O-acetylserine and homocysteine to cystathionine. (307 aa)
mccBCystathionine gamma-lyase and homocysteine gamma-lyase for reverse transsulfuration pathway; Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. (379 aa)
cysH(phospho)adenosine phosphosulfate reductase; Reduction of activated sulfate into sulfite. (233 aa)
metCCystathionine beta-lyase; Catalyzes the transformation of cystathionine into homocysteine. Also exhibits cysteine desulfhydrase activity in vitro, producing sulfide from cysteine; Belongs to the trans-sulfuration enzymes family. (390 aa)
metICystathionine gamma-synthase and O-acetylhomoserine thiolyase; Catalyzes the formation of L-cystathionine from O-acetyl-L- homoserine and L-cysteine. Cannot use O-succinyl-L-homoserine as substrate. Also exhibits O-acetylhomoserine thiolyase activity, catalyzing the synthesis of L-homocysteine from O-acetyl-L-homoserine and sulfide. (373 aa)
yitBPutative phospho-adenylylsulfate sulfotransferase; Reduction of activated sulfate into sulfite; Belongs to the PAPS reductase family. CysH subfamily. (236 aa)
cysESerine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa)
cysKCysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. (308 aa)
yxePPutative amidohydrolase; Probably catalyzes the deacetylation of N-acetylcysteine (NAC) to acetate and cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Belongs to the peptidase M20 family. (380 aa)
cysJSulfite reductase (flavoprotein alpha-subunit); Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component (Probable). (605 aa)
thrCThreonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa)
yxeKPutative monooxygenase; Probably catalyzes the oxygenation of the 2-position of the succinyl moiety of N-acetyl-S-(2-succino)cysteine, causing a spontaneous elimination reaction of the resulting hemithioketal that generates oxaloacetate and N-acetylcysteine (NAC). Is involved in a S- (2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine; Belongs to the NtaA/SnaA/SoxA(DszA) monooxygenase family. (441 aa)
yxeLPutative acetyltransferase; Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation; Belongs to the acetyltransferase family. (165 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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