Bacterial L-cysteine biosynthesis via O-acetyl-L-serine

A reusable two-step bacterial pathway in which serine O-acetyltransferase (CysE) converts L-serine and acetyl-CoA to O-acetyl-L-serine, followed by a pyridoxal-phosphate-dependent O-acetylserine sulfhydrylase that incorporates sulfide to produce L-cysteine. OAS-active CysK or CysM proteins can implement the terminal reaction. The route is distributed across bacterial lineages, but neither the gene names nor broad family membership establish substrate choice. Thiosulfate incorporation produces S-sulfocysteine and requires a further reduction; it is adjacent chemistry rather than the direct sulfide route. A regulatory cysteine synthase complex forms in some lineages but is not a required pathway assembly. Upstream sulfide generation and distinct O-phosphoserine/sulfur-carrier pathways lie outside this module.

MODULE:bacterial_cysteine_biosynthesis_via_o_acetylserineCOMPLETEABSTRACTMetabolic Pathwaymodules/bacterial_cysteine_biosynthesis_via_o_acetylserine.yaml
cysteine biosynthesis from serineGO:0019344
GO:0019344
L-cysteine biosynthetic process
GO:0019344 grounds the module. The route-specific term GO:0006535 (L-cysteine biosynthetic process from L-serine) is obsolete with replaced_by GO:0019344 since at least GO release 2026-03-25 and in every release since; a reviewed label alias in conf/oak_config.yaml had masked the obsoletion from validation. The O-acetylserine route is carried by the module structure rather than by the term.
PMID:10482527
Pathways of assimilative sulfur metabolism in Pseudomonas putida
Pseudomonas putida S-313 cell extracts showed substantial O-acetylserine sulfhydrylase activity, providing organism-level evidence that this terminal chemistry operates in P. putida.
PMID:42278617
Serine Acetyltransferase from Pseudomonas aeruginosa: Distinctive Features, Pleiotropic Roles, and Therapeutic Potential.
Biochemical and deletion analysis identifies PA3816/Q9HXI6 as the major Pseudomonas aeruginosa serine acetyltransferase, grounding the first reaction in a closely related Pseudomonas species.
PMID:41541697
De novo cysteine biosynthesis in Pseudomonas aeruginosa: Characterization of the two main cysteine synthase isoforms.
Biochemical and genetic analysis establishes CysK and CysM as partially redundant O-acetylserine sulfhydrylases with distinct sulfur-donor preferences in Pseudomonas aeruginosa.
PMID:41676964
Distinct contributions of O-acetylserine sulfhydrylases to cysteine biosynthesis in Pseudomonas aeruginosa
Direct PAO1 biochemical and genetic work supports partially redundant CysK/CysM roles and PaCysM thiosulfate preference. Binding assays detected no interaction of CysK with the tested endogenous CysE1 terminal peptide; PMID:42278617 separately found negligible reciprocal kinetic effects of the full-length enzymes.
file:ECOLI/cysE/cysE-ai-review.yaml
ECOLI CysE gene review
The E. coli K-12 CysE (P0A9D4) review accepts directly assayed serine O-acetyltransferase activity and membership of the cysteine synthase complex with CysK.
file:ECOLI/cysK/cysK-ai-review.yaml
ECOLI CysK gene review
The E. coli K-12 CysK (P0ABK5) review accepts directly assayed cysteine synthase activity as core and keeps L-cysteine desulfhydrase activity as a secondary, non-core activity.
file:ECOLI/cysM/cysM-ai-review.yaml
ECOLI CysM gene review
The E. coli K-12 CysM (P16703) review accepts directly assayed cysteine synthase activity as core.
file:PSEAE/cysE/cysE-ai-review.yaml
PSEAE CysE gene review
The P. aeruginosa PAO1 CysE (Q9HXI6) review accepts serine O-acetyltransferase activity from direct biochemistry and genetics and records that PaCysE does not functionally interact with CysK.
file:PSEAE/cysM/cysM-ai-review.yaml
PSEAE CysM gene review
The P. aeruginosa PAO1 CysM (Q9I526) review accepts cysteine synthase activity and proposes a thiosulfate-dependent S-sulfocysteine synthase activity for which GO has no term.
file:interpro/panther/PTHR42811/PTHR42811-review.yaml
PTHR42811 serine acetyltransferase family review
The PANTHER serine acetyltransferase family is functionally coherent; PAINT places serine O-acetyltransferase activity and cysteine biosynthesis at its family node PTN000602332 with no recorded loss.
file:interpro/panther/PTHR10314/PTHR10314-review.yaml
PTHR10314 cystathionine beta-synthase family review
The PANTHER PLP fold-type II family is heterogeneous (cysteine synthases, cystathionine beta-synthase, threonine synthase, cysteine desulfhydrase); cysteine synthase activity is placed at separate bacterial CysK and CysM nodes, which the module uses to distinguish its two variants.
file:PSEPK/cysE/cysE-ai-review.yaml
PSEPK CysE gene review
The exact Q88PL0 record and curated review ground serine O-acetylation in the KT2440 instance.
file:PSEPK/cysK/cysK-ai-review.yaml
PSEPK CysK gene review
The exact Q88E95 record and curated review ground the CysK sulfide route in the KT2440 instance.
file:PSEPK/cysM/cysM-ai-review.yaml
PSEPK CysM gene review
The exact Q88MC0 record and curated review ground a CysM-family alternative for the same sulfide-dependent reaction in KT2440.
PMID:36148777
Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.
CysE forms OAS from serine and acetyl-CoA.
requiring L-serine and acetyl coenzyme A (acetyl-CoA) to produce O-acetylserine (OAS).
PMID:36148777
Combatting antimicrobial resistance via the cysteine biosynthesis pathway in bacterial pathogens.
CysK incorporates sulfide into OAS.
combines O-acetylserine with sulfide to produce cysteine
PMID:38257399
Challenges and Advances in the Bioproduction of L-Cysteine.
The thiosulfate route produces S-sulfocysteine before reduction to cysteine; it is not the two-step OAS/sulfide route.
OAS and thiosulfate into S-sulfocysteine, which is reduced into L-cysteine and sulfite by glutaredoxin (Grx1)
PMID:38931847
Amino Acid Biosynthesis Inhibitors in Tuberculosis Drug Discovery.
M. tuberculosis CysK1 is the OAS/sulfide enzyme; other cysteine synthase names need separate substrate checks.
CysK1, a bona fide PLP-dependent O-acetylserine sulfhydrylase encoded by the gene rv2334, which converts O-acetylserine and sulfide to Cys
PMID:42278617
Serine Acetyltransferase from Pseudomonas aeruginosa: Distinctive Features, Pleiotropic Roles, and Therapeutic Potential.
PAO1 CysE and CysK do not show the measured reciprocal activity coupling expected from a canonical CSC.
PaCysE did not measurably affect PaCysK activity, nor was its own activity significantly altered by PaCysK.
PMID:41676964
Distinct contributions of O-acetylserine sulfhydrylases to cysteine biosynthesis in Pseudomonas aeruginosa.
PaCysM favors thiosulfate, while PaCysK is adapted to sulfide; this is a preference rather than absolute exclusivity.
PaCysK primarily supports sulfide‐dependent cysteine biosynthesis, whereas PaCysM is specialized for thiosulfate utilization, consistent with their distinct catalytic properties.
PMID:41541697
De novo cysteine biosynthesis in Pseudomonas aeruginosa: Characterization of the two main cysteine synthase isoforms.
The thiosulfate branch requires an additional reduction after sulfocysteine formation.
S-sulfocysteine can subsequently be converted to cysteine by the action of glutaredoxins.
PMID:10482527
Pathways of assimilative sulfur metabolism in Pseudomonas putida.
The study compares P. putida S-313 with P. aeruginosa PAO1, not KT2440.
Cysteine and methionine biosynthesis was studied in Pseudomonas putida S-313 and Pseudomonas aeruginosa PAO1.
PMID:18842002
O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis.
Mtb CysM strongly favors OPS over OAS.
specificity of CysM for its amino acid substrate is more than 500-fold greater for O-phospho-L-serine than for O-acetyl-L-serine
PMID:18842002
O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis.
CysO-bound sulfur is strongly preferred over free bisulfide.
The specificity of CysM for this physiological sulfide equivalent is more than 3 orders of magnitude greater than that for bisulfide.
PMID:16104727
Reconstitution of a new cysteine biosynthetic pathway in Mycobacterium tuberculosis.
Mec+ releases free cysteine from the carrier-bound product of CysM.
A protease, Mec+, hydrolyzes the CysO-cysteine adduct to release cysteine and regenerate CysO.
PMID:38311199
Multi-oligomeric and catalytically compromised serine acetyltransferase and cysteine regulatory complex of Mycobacterium tuberculosis.
An experimentally reported Mtb regulatory complex reduces CysE activity, differing from the activation reported for other organisms.
significantly reduced in CRC state, in contrast to enhanced activity of SAT in CRC of other organisms.
PMID:18799456
Cysteine synthase (CysM) of Mycobacterium tuberculosis is an O-phosphoserine sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria.
The reported OAS/free-sulfide assay did not detect cysteine, leaving native complete-reaction capability unresolved rather than proving biochemical impossibility.
file:BACSU/cysK/cysK-source-analysis/primary-evidence.md
Direct Bacillus assay, regulatory-partner and construct checks; distinguishes independently active OAS enzymes from CymR-dependent transcriptional regulation.
file:MYCTU/cysM/cysM-source-analysis/18799456-assay-scope.md
The assay and construct limits of non-detected OAS/free-sulfide cysteine formation are explicit; native route exclusion is not an assertion of absolute chemical impossibility.
6Nodes
2Parts
1Variant Sets
3Variants
4Annotons
1Connections

Derived QC

Recommended-field compliance

100.0% recommended fields populated

All recommended fields populated.

Module deep research

✗ none found

No MODULE:bacterial_cysteine_biosynthesis_via_o_acetylserine deep-research report alongside the module YAML.

Leaf nodes lacking representative members

✓ representative grounding skipped for abstract module.

Template conformance

✓ every declared conforms_to bundle matches its template motif.

Reaction chaining (advisory)

✓ every PRECEDES step chains, or its break is acknowledged via chaining_status.

  • serine_o_acetylation → sulfide_incorporation [NOT_CHECKED]
    O-acetyl-L-serine produced by serine O-acetyltransferase is the substrate consumed by either terminal sulfhydrylase variant.

Function consistency and core coverage

15 gene-function check(s) reflected in core functions · 0 conflict(s) · 3 evidence or coverage gap(s) (19 comparison(s))

Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.

AnnotonParticipantFunctionAssessment
cysE_activity CysE (Pseudomonas putida KT2440)
UniProtKB:Q88PL0
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity CysE (Escherichia coli K-12)
UniProtKB:P0A9D4
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity CysE (Pseudomonas aeruginosa PAO1)
UniProtKB:Q9HXI6
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity CysE (Campylobacter jejuni NCTC 11168)
UniProtKB:Q0PAC7
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity CysE (Bacillus subtilis 168)
UniProtKB:Q06750
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity CysE (Mycobacterium tuberculosis H37Rv)
UniProtKB:P95231
Family Representative
L-serine O-acetyltransferase activity
GO:0009001
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysK_activity CysK (Pseudomonas putida KT2440)
UniProtKB:Q88E95
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysK_activity CysK (Escherichia coli K-12)
UniProtKB:P0ABK5
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysK_activity CysK (Pseudomonas aeruginosa PAO1)
UniProtKB:Q9I0D3
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysK_activity CysK (Bacillus subtilis 168)
UniProtKB:P37887
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysK_activity CysK1 (Mycobacterium tuberculosis H37Rv)
UniProtKB:P9WP55
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysM_activity CysM (Pseudomonas putida KT2440)
UniProtKB:Q88MC0
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysM_activity CysM (Escherichia coli K-12)
UniProtKB:P16703
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysM_activity CysM (Pseudomonas aeruginosa PAO1)
UniProtKB:Q9I526
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
unplaced_oas_sulfhydrylase_activity CysM/Cj0912c (Campylobacter jejuni NCTC 11168)
UniProtKB:P71128
Family Representative
cysteine synthase activity
GO:0004124
Core Supported
The GO molecular function is reflected in core_functions (exact term or a reviewed subclass).
cysE_activity Serine acetyltransferase (CysE) family
PANTHER:PTHR42811
Family
L-serine O-acetyltransferase activity
GO:0009001
Family Supported
Family review supports GO:0009001 FAMILY_WIDE. Placed by PAINT at the family node with no recorded loss; bacterial, protist and plant members alike are serine acetyltransferases. The bacterial cysteine biosynthesis module grounds this step on the narrower InterPro CysE entry (IPR005881), which the PANTHER family contains.
cysK_activity CysK-type O-acetylserine sulfhydrylase (cysteine synthase A)
PANTHER:PTHR10314
Family
cysteine synthase activity
GO:0004124
Family Function Unreviewed
Family review leaves GO:0004124 UNRESOLVED. Exact OAS plus free sulfide cysteine synthase activity is supported in particular bacterial CysK, OAS-active CysM and eukaryotic OAS-TL members. PAINT places it at PTN000034535, PTN008497439 and PTN000034468, respectively. The broader cysteine-biosynthesis BP at the family root does not establish ancestral OAS substrate chemistry. SF194 includes both CBS and CysK proteins; SF162 includes OAS-active CysM proteins and OPS/CysO-specialized M. tuberculosis P9WP53, whose complete OAS/free-sulfide turnover remains unresolved. Neither family nor subfamily alone therefore defines a safe scope for this exact activity. Positive node and member evidence is retained. CBS proteins, threonine synthases and SF135 cysteine desulfhydrases have distinct demonstrated functions; the former scope-carving member entries are archived verbatim in the notes. This is not a claim that cysteine synthase activity is false family-wide. The exact historical exception objects and a separate P9WP53 over-annotation case are restored in the linked structured scope proof. They cannot be placed in active member_exceptions under UNRESOLVED without violating current checker semantics. SF194 is not a safe wholesale substitute: it also includes the CBS clade; the eukaryotic OAS-TL node spans 28 subfamilies. This unresolved enum describes the coarse family/subfamily boundary, not doubt about the supported E. coli or PAO1 activities.
cysM_activity CysM-type O-acetylserine sulfhydrylase (cysteine synthase B)
PANTHER:PTHR10314
Family
cysteine synthase activity
GO:0004124
Family Function Unreviewed
Family review leaves GO:0004124 UNRESOLVED. Exact OAS plus free sulfide cysteine synthase activity is supported in particular bacterial CysK, OAS-active CysM and eukaryotic OAS-TL members. PAINT places it at PTN000034535, PTN008497439 and PTN000034468, respectively. The broader cysteine-biosynthesis BP at the family root does not establish ancestral OAS substrate chemistry. SF194 includes both CBS and CysK proteins; SF162 includes OAS-active CysM proteins and OPS/CysO-specialized M. tuberculosis P9WP53, whose complete OAS/free-sulfide turnover remains unresolved. Neither family nor subfamily alone therefore defines a safe scope for this exact activity. Positive node and member evidence is retained. CBS proteins, threonine synthases and SF135 cysteine desulfhydrases have distinct demonstrated functions; the former scope-carving member entries are archived verbatim in the notes. This is not a claim that cysteine synthase activity is false family-wide. The exact historical exception objects and a separate P9WP53 over-annotation case are restored in the linked structured scope proof. They cannot be placed in active member_exceptions under UNRESOLVED without violating current checker semantics. SF194 is not a safe wholesale substitute: it also includes the CBS clade; the eukaryotic OAS-TL node spans 28 subfamilies. This unresolved enum describes the coarse family/subfamily boundary, not doubt about the supported E. coli or PAO1 activities.
unplaced_oas_sulfhydrylase_activity Experimentally supported OAS/sulfide enzyme within PTHR10314; exact PAINT branch unresolved
PANTHER:PTHR10314
Family
cysteine synthase activity
GO:0004124
Family Function Unreviewed
Family review leaves GO:0004124 UNRESOLVED. Exact OAS plus free sulfide cysteine synthase activity is supported in particular bacterial CysK, OAS-active CysM and eukaryotic OAS-TL members. PAINT places it at PTN000034535, PTN008497439 and PTN000034468, respectively. The broader cysteine-biosynthesis BP at the family root does not establish ancestral OAS substrate chemistry. SF194 includes both CBS and CysK proteins; SF162 includes OAS-active CysM proteins and OPS/CysO-specialized M. tuberculosis P9WP53, whose complete OAS/free-sulfide turnover remains unresolved. Neither family nor subfamily alone therefore defines a safe scope for this exact activity. Positive node and member evidence is retained. CBS proteins, threonine synthases and SF135 cysteine desulfhydrases have distinct demonstrated functions; the former scope-carving member entries are archived verbatim in the notes. This is not a claim that cysteine synthase activity is false family-wide. The exact historical exception objects and a separate P9WP53 over-annotation case are restored in the linked structured scope proof. They cannot be placed in active member_exceptions under UNRESOLVED without violating current checker semantics. SF194 is not a safe wholesale substitute: it also includes the CBS clade; the eukaryotic OAS-TL node spans 28 subfamilies. This unresolved enum describes the coarse family/subfamily boundary, not doubt about the supported E. coli or PAO1 activities.

Gene-review completeness (15/15 grounded genes reviewed)

14 complete review(s) · 1 with deep research · 0 missing review · 14 reviewed but lacking deep research

Gene Review Complete Deep research
cysE P0A9D4 ✓ ✓ ✗
cysE P95231 ✓ ✓ ✗
cysE Q06750 ✓ ✓ ✗
cysE Q0PAC7 ✓ ✓ ✗
cysE Q88PL0 ✓ ✓ ✗
cysE Q9HXI6 ✓ ✓ ✗
cysK P0ABK5 ✓ ✓ ✗
cysK P37887 ✓ ✓ ✗
cysK Q88E95 ✓ ✓ ✓
cysK Q9I0D3 ✓ ✓ ✗
cysK1 P9WP55 ✓ 13/14 ✗
cysM P16703 ✓ ✓ ✗
cysM P71128 ✓ ✓ ✗
cysM Q88MC0 ✓ ✓ ✗
cysM Q9I526 ✓ ✓ ✗

Details

Context
bacteria that implement the O-acetylserine plus sulfide routeNCBITaxon:2
Bacterial L-cysteine biosynthesis via O-acetyl-L-serineMetabolic Pathwaybacterial_cysteine_biosynthesis_via_o_acetylserine
cysteine biosynthesis from serineGO:0019344
Context
bacteria that implement the O-acetylserine plus sulfide routeNCBITaxon:2

The taxon context denotes a reusable bacterial route, not universal possession or dependence. Sulfate uptake and reduction supply sulfide upstream. Thiosulfate incorporation into OAS produces S-sulfocysteine and requires downstream reduction, so it cannot silently replace the stated sulfide chemistry. CysK and CysM names describe diverse proteins: mycobacterial CysM prefers O-phosphoserine and CysO thiocarboxylate, whereas Campylobacter CysM uses OAS and strongly favors sulfide. Minor in-vitro side reactions do not automatically define a physiological module implementation. The cysteine synthase complex is regulatory context: CysE-tail occupation inhibits the CysK active site, and the enterobacterial interaction cannot be assumed in Pseudomonas or Bacillus. PTHR42811 grounds serine acetyltransferase; heterogeneous PTHR10314 contains both relevant OAS enzymes and proteins with other substrates/functions. PAINT node membership must therefore be combined with a gene review that establishes the route-specific core activity. The CysK node PTN000034535 includes bacterial CysK exemplars, but CysM node PTN008497439 also contains M. tuberculosis P9WP53; it cannot alone qualify a native OAS-route implementation. Absence of a representative from the cached tree is not evidence for absence of family membership. Campylobacter Cj0912c is retained as an explicitly unplaced OAS-active alternative: its CysM symbol and CysK-like signature do not establish either existing PAINT node. Fifteen positive member exemplars span E. coli, Pseudomonas, Bacillus, Campylobacter and Mycobacterium; a sixteenth gene review assesses Mtb CysM as a mechanistically distinct comparator. Mtb regulatory-complex formation has direct support in PMID:38311199, but exact full-length construct and assembly details remain unresolved; its CysE activity is reduced, so regulatory direction is not universal. Bacillus instead has directly demonstrated CymR-CysK regulation, while tested CysE-CysK association is negative. Quoted biochemical results, genetic evidence, family inference and construct/strain limits are distinguished. An intact enzyme panel describes supported capacity, not measured native flux or whole-genome completeness.

Connections

Part 1: serine O-acetylation
Formation of O-acetyl-L-serineReactionserine_o_acetylation

Annotons

Serine O-acetyltransferase activity
cysE_activity
Participant: Family: Serine acetyltransferase (CysE) family
Family:
Serine acetyltransferase (CysE) familyPANTHER:PTHR42811
Representative Members: CysE (Pseudomonas putida KT2440)UniProtKB:Q88PL0 CysE (Escherichia coli K-12)UniProtKB:P0A9D4 CysE (Pseudomonas aeruginosa PAO1)UniProtKB:Q9HXI6 CysE (Campylobacter jejuni NCTC 11168)UniProtKB:Q0PAC7 CysE (Bacillus subtilis 168)UniProtKB:Q06750 CysE (Mycobacterium tuberculosis H37Rv)UniProtKB:P95231

Function

L-serine O-acetyltransferase activityGO:0009001
Substrates: L-serineCHEBI:33384 acetyl-CoACHEBI:57288
Products: O-acetyl-L-serineCHEBI:58340 coenzyme ACHEBI:57287

Transfers an acetyl group from acetyl-CoA to L-serine to form O-acetyl-L-serine, the carbon skeleton consumed by the terminal sulfhydrylation step.

Part 2: sulfide incorporation
Formation of L-cysteine from O-acetyl-L-serine and sulfideReactionsulfide_incorporation
Variant set: O-acetylserine sulfhydrylase variant by enzyme family variant (One Or More)
CysK-type O-acetylserine sulfhydrylaseReactioncysK_variant

Annotons

CysK-type cysteine synthase activity
cysK_activity
Participant: Family: CysK-type O-acetylserine sulfhydrylase (cysteine synthase A)
Family:
CysK-type O-acetylserine sulfhydrylase (cysteine synthase A)PANTHER:PTHR10314
Representative Members: CysK (Pseudomonas putida KT2440)UniProtKB:Q88E95 CysK (Escherichia coli K-12)UniProtKB:P0ABK5 CysK (Pseudomonas aeruginosa PAO1)UniProtKB:Q9I0D3 CysK (Bacillus subtilis 168)UniProtKB:P37887 CysK1 (Mycobacterium tuberculosis H37Rv)UniProtKB:P9WP55

Function

cysteine synthase activityGO:0004124
Substrates: O-acetyl-L-serineCHEBI:58340 hydrosulfideCHEBI:29919
Products: L-cysteineCHEBI:35235 acetateCHEBI:30089
Cofactors: pyridoxal 5'-phosphateCHEBI:597326

PLP-dependent incorporation of sulfide into O-acetyl-L-serine to produce L-cysteine.

CysM-type O-acetylserine sulfhydrylaseReactioncysM_variant

Annotons

CysM-type cysteine synthase activity
cysM_activity
Participant: Family: CysM-type O-acetylserine sulfhydrylase (cysteine synthase B)
Family:
CysM-type O-acetylserine sulfhydrylase (cysteine synthase B)PANTHER:PTHR10314
Representative Members: CysM (Pseudomonas putida KT2440)UniProtKB:Q88MC0 CysM (Escherichia coli K-12)UniProtKB:P16703 CysM (Pseudomonas aeruginosa PAO1)UniProtKB:Q9I526

Function

cysteine synthase activityGO:0004124
Substrates: O-acetyl-L-serineCHEBI:58340 hydrosulfideCHEBI:29919
Products: L-cysteineCHEBI:35235 acetateCHEBI:30089
Cofactors: pyridoxal 5'-phosphateCHEBI:597326

Alternative PLP-dependent OAS/sulfide chemistry established for the reviewed CysM proteins in this branch. Assayed PAO1 CysM also favors thiosulfate, yielding S-sulfocysteine; donor preference is not assumed for unassayed KT2440 CysM. Neither the name nor PTHR10314/SF162 membership qualifies the OPS/CysO route of mycobacterial CysM. The Campylobacter implementation has unresolved PAINT placement and is represented separately.

Experimentally supported OAS sulfhydrylase with unresolved PAINT placementReactionunplaced_oas_sulfhydrylase_variant

Annotons

OAS/sulfide cysteine synthase activity
unplaced_oas_sulfhydrylase_activity
Participant: Family: Experimentally supported OAS/sulfide enzyme within PTHR10314; exact PAINT branch unresolved
Family:
Experimentally supported OAS/sulfide enzyme within PTHR10314; exact PAINT branch unresolvedPANTHER:PTHR10314
Representative Members: CysM/Cj0912c (Campylobacter jejuni NCTC 11168)UniProtKB:P71128

Function

cysteine synthase activityGO:0004124
Substrates: O-acetyl-L-serineCHEBI:58340 hydrosulfideCHEBI:29919
Products: L-cysteineCHEBI:35235 acetateCHEBI:30089
Cofactors: pyridoxal 5'-phosphateCHEBI:597326

NCTC11168 Cj0912c, named CysM, is directly assayed as an OAS/sulfide enzyme and has the CysK-associated IPR005859 signature. Neither name nor signature establishes descent from PTN000034535 or PTN008497439; this implementation remains unplaced relative to those nodes. It uses the same reaction, not a new tissue- or organism-specific pathway.