Cysteine synthesis from O-acetylserine
Reactome:R-MTU-936721
The Mycobacterium tuberculosis O-acetylserine route joins CysH/Sir sulfate reduction with CysE serine acetylation and CysK1-dependent cysteine synthesis. The outdated CysK2 O-acetylserine reaction is excluded: CysK2 uses a distinct O-phosphoserine route. Native thioredoxin and ferredoxin states and PLP-bearing CysK1 are retained. Reactome chemical forms include sulfurous acid, sulfide(2-) and acetic acid; this graph does not claim physiological protonation or complete stoichiometric balance.
- Pathway type
- biopax pathway
- Organism scope
Pathway network
33 nodes · 69 asserted directed edges
Arrows show recorded subject → object relationships, not necessarily metabolic flow. Select a node for details or an arrow for evidence. Scroll, zoom or find a node to explore.
- Reaction / activity
- Chemical / cofactor
- Protein / complex
- Cell / process context
- Solid arrow: mechanistic relation
- Dashed arrow: membership, location or cofactor relation
Components and activities
| Node | Kind or role | Source direction |
|---|---|---|
Mycobacterium tuberculosisNCBITaxon:1773 | taxon | |
5'-adenylyl sulfate(2-)CHEBI:58243 | small molecule | |
hydronCHEBI:15378 | small molecule | |
sulfurous acidCHEBI:48854 | small molecule | |
adenosine 5'-monophosphate(2-)CHEBI:456215 | small molecule | |
tetra-mu3-sulfido-tetrairon(1+)CHEBI:33723 | cofactor | |
waterCHEBI:15377 | small molecule | |
sulfide(2-)CHEBI:15138 | small molecule | |
tetra-mu3-sulfido-tetrairon(2+)CHEBI:33722 | cofactor | |
sirohemeCHEBI:28599 | cofactor | |
acetyl-CoA(4-)CHEBI:57288 | small molecule | |
L-serine zwitterionCHEBI:33384 | small molecule | |
O-acetyl-L-serineCHEBI:17981 | small molecule | |
coenzyme A(4-)CHEBI:57287 | small molecule | |
acetic acidCHEBI:15366 | small molecule | |
L-cysteine zwitterionCHEBI:35235 | small molecule | |
Trx(red.)Reactome:R-MTU-936674 | protein | |
TrxA(ox.)Reactome:R-MTU-1222293 | protein | |
CysHReactome:R-MTU-936694 | protein | |
FdxReactome:R-MTU-937262 | protein | |
SirReactome:R-MTU-936705 | protein | |
CysEReactome:R-MTU-936604 | protein | |
PXLP-K44-CysK1Reactome:R-MTU-936587 | protein | |
CysH holoenzymeReactome:R-MTU-936704 | complex | |
Iron Sulfur ClusterReactome:R-ALL-70986 | cofactor | |
Fdx(red.)Reactome:R-MTU-937263 | complex | |
Fdx(ox.)Reactome:R-MTU-937267 | complex | |
Sir holoenzymeReactome:R-MTU-936607 | complex | |
CysK1 dimerReactome:R-MTU-936755 | complex | |
cytosolGO:0005829 | cellular component | |
sulfite results from reduction of APSReactome:R-MTU-936655 | molecular activity | left to right |
sulfite is reduced to sulfideReactome:R-MTU-936703 | molecular activity | left to right |
acetylation of serineReactome:R-MTU-936615 | molecular activity | left to right |
deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 | molecular activity | left to right |
Mechanistic edges
| Subject | Predicate and description | Object | Evidence |
|---|---|---|---|
5'-adenylyl sulfate(2-)CHEBI:58243 | consumes | sulfite results from reduction of APSReactome:R-MTU-936655 |
|
Trx(red.)Reactome:R-MTU-936674 | consumes | sulfite results from reduction of APSReactome:R-MTU-936655 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | produces | hydronCHEBI:15378 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | produces | TrxA(ox.)Reactome:R-MTU-1222293 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | produces | sulfurous acidCHEBI:48854 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | produces | adenosine 5'-monophosphate(2-)CHEBI:456215 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | occurs_in | cytosolGO:0005829 |
|
hydronCHEBI:15378 | consumes | sulfite is reduced to sulfideReactome:R-MTU-936703 |
|
sulfurous acidCHEBI:48854 | consumes | sulfite is reduced to sulfideReactome:R-MTU-936703 |
|
Fdx(red.)Reactome:R-MTU-937263 | consumes | sulfite is reduced to sulfideReactome:R-MTU-936703 |
|
sulfite is reduced to sulfideReactome:R-MTU-936703 | produces | waterCHEBI:15377 |
|
sulfite is reduced to sulfideReactome:R-MTU-936703 | produces | sulfide(2-)CHEBI:15138 |
|
sulfite is reduced to sulfideReactome:R-MTU-936703 | produces | Fdx(ox.)Reactome:R-MTU-937267 |
|
sulfite is reduced to sulfideReactome:R-MTU-936703 | occurs_in | cytosolGO:0005829 |
|
acetyl-CoA(4-)CHEBI:57288 | consumes | acetylation of serineReactome:R-MTU-936615 |
|
L-serine zwitterionCHEBI:33384 | consumes | acetylation of serineReactome:R-MTU-936615 |
|
acetylation of serineReactome:R-MTU-936615 | produces | O-acetyl-L-serineCHEBI:17981 |
|
acetylation of serineReactome:R-MTU-936615 | produces | coenzyme A(4-)CHEBI:57287 |
|
acetylation of serineReactome:R-MTU-936615 | occurs_in | cytosolGO:0005829 |
|
sulfide(2-)CHEBI:15138 | consumes | deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 |
|
O-acetyl-L-serineCHEBI:17981 | consumes | deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 |
|
deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 | produces | acetic acidCHEBI:15366 |
|
deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 | produces | L-cysteine zwitterionCHEBI:35235 |
|
deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 | occurs_in | cytosolGO:0005829 |
|
CysH holoenzymeReactome:R-MTU-936704 | catalyzes | sulfite results from reduction of APSReactome:R-MTU-936655 |
|
Sir holoenzymeReactome:R-MTU-936607 | catalyzes Reactome assigns this Sir holoenzyme to sulfite reduction. PMID17644602 assayed purified M. tuberculosis SirA with methyl viologen; its deletion physiology was in M. smegmatis, not direct validation of this particular ferredoxin pair. | sulfite is reduced to sulfideReactome:R-MTU-936703 |
|
CysEReactome:R-MTU-936604 | catalyzes Direct recombinant H37Rv CysE characterization supersedes the source comment that direct biochemical evidence was unavailable. | acetylation of serineReactome:R-MTU-936615 |
|
CysK1 dimerReactome:R-MTU-936755 | catalyzes | deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 |
|
sulfide(2-)CHEBI:15138 | located_in | cytosolGO:0005829 |
|
waterCHEBI:15377 | located_in | cytosolGO:0005829 |
|
adenosine 5'-monophosphate(2-)CHEBI:456215 | located_in | cytosolGO:0005829 |
|
sulfurous acidCHEBI:48854 | located_in | cytosolGO:0005829 |
|
hydronCHEBI:15378 | located_in | cytosolGO:0005829 |
|
L-cysteine zwitterionCHEBI:35235 | located_in | cytosolGO:0005829 |
|
acetic acidCHEBI:15366 | located_in | cytosolGO:0005829 |
|
coenzyme A(4-)CHEBI:57287 | located_in | cytosolGO:0005829 |
|
O-acetyl-L-serineCHEBI:17981 | located_in | cytosolGO:0005829 |
|
L-serine zwitterionCHEBI:33384 | located_in | cytosolGO:0005829 |
|
acetyl-CoA(4-)CHEBI:57288 | located_in | cytosolGO:0005829 |
|
5'-adenylyl sulfate(2-)CHEBI:58243 | located_in | cytosolGO:0005829 |
|
CysEReactome:R-MTU-936604 | located_in | cytosolGO:0005829 |
|
TrxA(ox.)Reactome:R-MTU-1222293 | located_in | cytosolGO:0005829 |
|
Trx(red.)Reactome:R-MTU-936674 | located_in | cytosolGO:0005829 |
|
CysK1 dimerReactome:R-MTU-936755 | has_part | PXLP-K44-CysK1Reactome:R-MTU-936587 |
|
CysK1 dimerReactome:R-MTU-936755 | located_in | cytosolGO:0005829 |
|
PXLP-K44-CysK1Reactome:R-MTU-936587 | located_in | cytosolGO:0005829 |
|
Sir holoenzymeReactome:R-MTU-936607 | has_part | sirohemeCHEBI:28599 |
|
Sir holoenzymeReactome:R-MTU-936607 | has_part | Iron Sulfur ClusterReactome:R-ALL-70986 |
|
Sir holoenzymeReactome:R-MTU-936607 | has_part | SirReactome:R-MTU-936705 |
|
Sir holoenzymeReactome:R-MTU-936607 | located_in | cytosolGO:0005829 |
|
SirReactome:R-MTU-936705 | located_in | cytosolGO:0005829 |
|
Iron Sulfur ClusterReactome:R-ALL-70986 | located_in | cytosolGO:0005829 |
|
sirohemeCHEBI:28599 | located_in | cytosolGO:0005829 |
|
Fdx(ox.)Reactome:R-MTU-937267 | has_part | FdxReactome:R-MTU-937262 |
|
Fdx(ox.)Reactome:R-MTU-937267 | has_part Retained as partial source composition, without the source cluster stoichiometry. UniProt P9WNE7 annotates one [4Fe-4S] and one [3Fe-4S] cluster by similarity; this edge does not assert complete composition. | tetra-mu3-sulfido-tetrairon(2+)CHEBI:33722 |
|
Fdx(ox.)Reactome:R-MTU-937267 | located_in | cytosolGO:0005829 |
|
tetra-mu3-sulfido-tetrairon(1+)CHEBI:33723 | located_in | cytosolGO:0005829 |
|
tetra-mu3-sulfido-tetrairon(2+)CHEBI:33722 | located_in | cytosolGO:0005829 |
|
FdxReactome:R-MTU-937262 | located_in | cytosolGO:0005829 |
|
Fdx(red.)Reactome:R-MTU-937263 | has_part | FdxReactome:R-MTU-937262 |
|
Fdx(red.)Reactome:R-MTU-937263 | has_part Retained as partial source composition, without the source cluster stoichiometry. UniProt P9WNE7 annotates one [4Fe-4S] and one [3Fe-4S] cluster by similarity; this edge does not assert complete composition. | tetra-mu3-sulfido-tetrairon(1+)CHEBI:33723 |
|
Fdx(red.)Reactome:R-MTU-937263 | located_in | cytosolGO:0005829 |
|
CysH holoenzymeReactome:R-MTU-936704 | has_part | Iron Sulfur ClusterReactome:R-ALL-70986 |
|
CysH holoenzymeReactome:R-MTU-936704 | has_part | CysHReactome:R-MTU-936694 |
|
CysH holoenzymeReactome:R-MTU-936704 | located_in | cytosolGO:0005829 |
|
CysHReactome:R-MTU-936694 | located_in | cytosolGO:0005829 |
|
sulfite results from reduction of APSReactome:R-MTU-936655 | provides_input_for Source-ordered material transfer through CHEBI:48854; no regulatory sign or stoichiometric coefficient is asserted. | sulfite is reduced to sulfideReactome:R-MTU-936703 |
|
sulfite is reduced to sulfideReactome:R-MTU-936703 | provides_input_for Source-ordered material transfer through CHEBI:15138; no regulatory sign or stoichiometric coefficient is asserted. | deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 |
|
acetylation of serineReactome:R-MTU-936615 | provides_input_for Source-ordered material transfer through CHEBI:17981; no regulatory sign or stoichiometric coefficient is asserted. | deacetylation of O-acetylserine and sulfhydrylation using CysK1Reactome:R-MTU-936642 |
|
References
PMID:120724415'-adenosinephosphosulfate lies at a metabolic branch point in mycobacteriaPMID:16008502A conserved mechanism for sulfonucleotide reductionPMID:17644602Sulfite reduction in mycobacteriaPMID:15917234Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active sitePMID:17567578Structural insights into catalysis and inhibition of O-acetylserine sulfhydrylase from Mycobacterium tuberculosis. Crystal structures of the enzyme alpha-aminoacrylate intermediate and an enzyme-inhibitor complexPMID:16436075Functional analysis of L-serine O-acetyltransferase from Corynebacterium glutamicumPMID:19376862Functional genomics reveals extended roles of the Mycobacterium tuberculosis stress response factor sigmaHPMID:17970225Drug targets in mycobacterial sulfur metabolismReactome:R-MTU-936721BioPAX source pathway Reactome:R-MTU-936721 (source version: Reactome release 97)PMID:25022854CysK2 from Mycobacterium tuberculosis Is an O-Phospho-L-Serine-Dependent S-Sulfocysteine SynthasePMID:23483228Identification and characterization of serine acetyltransferase encoded by the Mycobacterium tuberculosis Rv2335 geneUniProtKB:P9WNE7UniProtKB P9WNE7 ferredoxin cofactor annotations (source version: retrieved 2026-10-07; release not exposed)
Curation history
- Codex
- CREATE — Curate Reactome:R-MTU-936721 with native physical states and reviewed chemistry
Added 4 reactions and 69 edges from hash-pinned Reactome release 97. Complete source projection and edge-disposition ledger are in research/source_discovery/2026-10-07-reactome. Preserve modified, redox and cleaved protein states; exclude unsupported sulfur charging and CysK2/OAS chemistry where relevant; correct GTP coupling in sulfate activation. Exact source and primary-evidence limitations are explicit. Native and closed-schema validation passed before writing. Hidden/ignored-file deduplication included.
- CREATE — Curate Reactome:R-MTU-936721 with native physical states and reviewed chemistry