thioredoxin pathway

MetaCyc:THIOREDOX-PWY

Thioredoxin pathway is a two-event redox cycle. NADPH-dependent thioredoxin reductase regenerates reduced thioredoxin from its active-site disulfide; reduced thioredoxin then supplies reducing equivalents to an oxidized carrier/client and becomes oxidized again. The native pathway contains both reactions and reciprocal ordering entries. Its explicitly listed microbial species are Escherichia coli MG1655 and Mycoplasmoides pneumoniae M129. Broader native taxonomic-range annotations and the widespread thioredoxin fold do not demonstrate the same physiological clients or regulation in every taxon. (MetaCyc:THIOREDOX-PWY; MetaCyc:THIOREDOXIN-REDUCT-NADPH-RXN; MetaCyc:THIOREDOXIN-RXN.) The complete native boundary has nine side occurrences, all with implicit coefficient one. THIOREDOXIN-REDUCT-NADPH-RXN is PHYSIOL-RIGHT-TO-LEFT: an oxidized thioredoxin + NADPH + H+ → a reduced thioredoxin + NADP+. THIOREDOXIN-RXN is RIGHT-TO-LEFT: a reduced thioredoxin + an oxidized electron carrier → an oxidized thioredoxin + a reduced two electron carrier. The latter event is marked physiologically relevant and orphan YES-PUTATIVE; neither native reaction declares spontaneous catalysis. Acceptor and Donor-H2 denote generic native carrier classes, without a single defined formula, structure or experimentally established universal client. (MetaCyc:THIOREDOXIN-REDUCT-NADPH-RXN; MetaCyc:THIOREDOXIN-RXN.) RHEA:20347 supplies an independent, explicitly oriented projection of the reductase event: whole [thioredoxin]-disulfide + NADPH(4−) + hydron → whole [thioredoxin]-dithiol + NADP(3−). Its source orientation is right-to-left relative to master RHEA:20345. RHEA-COMP:10700 and RHEA-COMP:10698 identify the whole carrier states; their reactive cysteine/cystine residues are not substitutes for the whole proteins. The native NADPH, NADP and PROTON originals explicitly unify CHEBI:57783, CHEBI:58349 and CHEBI:15378. The three reaction nodes therefore represent two biological events through source-specific projections, not three consecutive transformations. FAD is bound to reductase and is not a net consumed substrate. (MetaCyc:THIOREDOXIN-REDUCT-NADPH-RXN; RHEA:20347; MetaCyc:NADPH; MetaCyc:NADP; MetaCyc:PROTON.) The frozen PathBank SMP0002094/PW002082 diagram corroborates two events and a two-subunit E. coli TrxB complex. Its NADPH/NADP references use acid-form CHEBI:16474/CHEBI:18009 rather than the exact charge forms above, and both thioredoxin states share CHEBI:15033. Those state and charge distinctions are retained here. PathBank additionally marks its generic client event spontaneous; that source-specific flag is not transferred to the native physiological event or used to negate the protein-mediated evidence. (PathBank:SMP0002094.) The E. coli TrxB native complex contains two THIOREDOXIN-REDUCT-NADPH-MONOMER components. Its direct native name is absent, so the structural display identifies an unnamed protein complex; the linked enzymatic activity supplies its thioredoxin-reductase interpretation. The source attributes historical homodimer determination to E. coli B and describes one FAD per subunit. Electron flow is NADPH → FAD → the TrxB active-site disulfide → thioredoxin. The two-domain, two-stranded-linker organization and membership in the flavin-containing NADPH:disulfide-oxidoreductase family are native structural context, not proof that related family members share every substrate. (EcoCyc:THIOREDOXIN-REDUCT-NADPH-CPLX.) E. coli has sequence-level TrxA (UniProtKB:P0AA25) and TrxC (UniProtKB:P0AGG4), with separate native reduced and oxidized instances paired through their gene identities. The native reduced TrxA label is thioredoxin 1; the state follows from its Red-Thioredoxin parent and its reciprocal oxidized instance, rather than an added adjective. TrxC has a separate redox pair linked to its own gene. These native instances are neither the generic META classes nor the generic Rhea components. Native TrxC oxidation does not by itself assert oxidation of all six cysteines or loss of zinc. Current UniProt E. coli K12 taxon 83333, MG1655 taxon 511145 and experimental strains in individual papers remain distinct scopes. Independently retained META and ECOLI reduced instances share the TrxA/TrxC UniProt sequence links and have their own reciprocal gene-linked oxidized states. Context edges use this source-supported biological correspondence as a stated inference; they do not equate PGDB identifiers or instantiate the generic META carriers as one exclusive E. coli protein. (MetaCyc:THIOREDOX-PWY; EcoCyc:RED-THIOREDOXIN-MONOMER; EcoCyc:OX-THIOREDOXIN-MONOMER; EcoCyc:RED-THIOREDOXIN2-MONOMER; EcoCyc:OX-THIOREDOXIN2-MONOMER; MetaCyc:RED-THIOREDOXIN-MONOMER; MetaCyc:RED-THIOREDOXIN2-MONOMER; MetaCyc:OX-THIOREDOXIN-MONOMER; MetaCyc:OX-THIOREDOXIN2-MONOMER.) The 1997 primary abstract describes recombinant 139-residue TrxC with an extra 32-residue N-terminal region containing four additional cysteines. TrxC supports ribonucleotide reductase when combined with thioredoxin reductase and NADPH, and reduces insulin disulfides. DTT preincubation increases full-length activity but not that of an N-terminal deletion, and the additional domain contributes heat sensitivity. Its original vector/tag details remain unresolved here. Current UniProt TrxC catalytic annotations instead list direct NAD- and NADP-dependent protein-disulfide reactions without attached experimental citations. These conflicting direct-nucleotide annotations are retained as a source conflict; they do not establish pyridine-nucleotide reductase activity by TrxC alone. (UniProtKB:P0AGG4; PMID:9388228.) The full 2003 zinc study used deliberately untagged E. coli TrxC, avoiding a histidine-tag metal-binding confound. Genomic trxC was cloned into sequence-verified pET11a derivative pJFC67 and introduced into BL21(DE3)pLysS; the expression paragraph describes BL21(DE3) harboring pJFC67. Aerobic LB expression at 37 °C used 0.5 mM IPTG and 0.8 mM ZnCl2. Sequential anion-exchange and size-exclusion purification produced protein reported as more than 95% pure. Fresh preparations contained six reduced cysteines and approximately one zinc per protein; ICP-HRMS reported 1.03 zinc/protein without other detected tested metals. Four N-terminal cysteines coordinate the metal, whereas selective active-site oxidation by GSSG leaves zinc bound. (PMID:12952960.) PMPS thiol modification released zinc, and DTT reversed the modification and restored binding. TPEN competition supports high affinity; EDTA was unsuitable for the affinity measurement because the authors report formation of a protein–zinc–EDTA complex as data not shown. Complete oxidation used a 40-fold excess of peroxide at 43 °C for two hours. Figure 4 compared 50 µM TrxC with 2 mM H2O2 at 23 °C and 43 °C; oxidation and zinc release were faster at 43 °C. A copper acceleration is described as data not shown. These forcing in-vitro conditions do not establish physiological zinc-center oxidation or a proven native stress switch. (PMID:12952960.) TrxB plus NADPH reduced all three disulfides in the fully oxidized TrxC preparation. A slow two-cysteine phase preceded faster reduction of the other four; assigning the first pair specifically to the catalytic cysteines was tentative. This auxiliary three-disulfide experiment does not alter the one-disulfide core stoichiometry. Zinc occupancy recovered to about 25% without added zinc and about 85% with added zinc. Oxidation changed hydrodynamic behavior, CD and protease sensitivity, but analytical ultracentrifugation found both preparations monomeric. Native-gel shifts or apparent size-exclusion masses therefore do not establish a stable native TrxC oligomer. (PMID:12952960.) Reduced apo-TrxC retained the same insulin-reduction rate as reduced zinc-bound TrxC in the DTT-driven assay: 130 µM insulin, 0.6 mM DTT and 1 µM thioredoxin at pH 7.0 and 25 °C. Both TrxC preparations were faster than TrxA under those conditions. Zinc binding is supported, but zinc was not required for this assay. A persistently oxidized zinc center could not be assayed because DTT and TrxB/NADPH reduced all six cysteines; that unmeasurable condition is not a demonstrated absence of an effect. The extent and function of zinc-center oxidation in vivo remained unresolved. Zinc found in a zinc-rich archaeal crystal or an engineered TrxA site does not establish a native TrxA zinc cofactor. (PMID:12952960.) The 2008 primary abstract reports different TrxA/TrxC redox potentials and active-site pKa values, with a four-zinc-cysteine-to-serine construct altering potential, pKa and thermostability. Native mentions of high-mass TrxC complexes under oxidative stress leave partners undefined. The 2000 abstract finds overlapping TrxA/TrxC functions among tested ribonucleotide-reductase, PAPS-reductase and DsbC-supporting assays; the 2003 full paper qualifies earlier DsbD/PAPS substitution as overexpression-dependent. The extension was dispensable for the tested functions, not for every possible client. A later methionine-sulfoxide study reports TrxC activity in vitro but failure of a metB1 trxA mutant to grow on methionine sulfoxide because of low TrxC expression in vivo. These results support conditional overlap, not complete physiological equivalence. (PMID:19073194; PMID:10644706; PMID:21570393.) Available primary abstracts show growth-phase and genetic-background dependence. Stationary-phase TrxA increases while TrxC remains approximately constant in the reported ELISA study, and loss of the thioredoxin system strongly induces Grx1. Thioredoxin and glutaredoxin pathways provide partially redundant reducing capacity; combined lesions can impair aerobic viability and can be rescued under particular reducing conditions. In the tested background any one of TrxA, TrxC or Grx1 supported aerobic growth. In trxB-deficient cells, oxidized thioredoxins can instead promote disulfide formation in engineered cytoplasmic alkaline phosphatase. Experimentally exported TrxA can also act as an oxidant in the periplasm. These construct- and background-specific role reversals do not redefine the default native reductive cycle. (PMID:11893749; PMID:9188456; PMID:9755155; PMID:9724776.) Engineered active-site variants demonstrate that redox potential, protein stability and partner recognition can be uncoupled. The available abstracts report variants that remain TrxB substrates yet differ in sulfate, methionine-sulfoxide and DsbC reduction. A Cys-Gly-Arg-Pro-Cys-Lys ring-expanded sequence retains some activity in vitro despite in-vivo inactivity; Cys-Ala-Cys is inefficient and forms intermolecular disulfides. Pro-to-Ser and Lys-to-Glu substitutions have their own assay-specific effects. Nonnatural replacement of cis-Pro76 by (4S)-fluoroproline accelerates rate-limiting folding isomerization, whereas the (4R) analogue has little effect in the intact structure. These engineered folding and catalytic observations are not additional native pathway events. (PMID:10464247; PMID:2187529; PMID:26382254.) The early TrxB cysteine-mutant activity report is materially corrected by the 1998 primary abstract: the original C138S preparation was a mixture containing wild-type enzyme, while the re-engineered C138S preparation had about 0.1% wild-type activity. Trapped mixed disulfides involving C135S/C138S TrxB and C35S TrxA support Cys138 initiation of thiol-disulfide interchange and acceptance of reducing equivalents from flavin. These are engineered trapping experiments, not permanent native assemblies. Historical mature-chain Cys135/Cys138 correspond to current initiator-containing TrxB Cys136/Cys139. Separate H245N/A and D139E/N/L mutant assays support a proposed Asp139 acid-base role; they do not establish H245 as an obligatory catalytic base. D139N impairs the thioredoxin oxidative half-reaction despite retained surrogate pyridine-nucleotide transfer. (PMID:2644268; PMID:9655349; PMID:8136348.) Turnover and fluorescence abstracts support multiple redox/cofactor states and alternating flavin-oxidizing/flavin-reducing conformations, with a proposed ternary-complex mechanism. Wild-type oxidized and nucleotide-bound C138S crystals show flavin-oxidizing states with a nonproductive distant pyridine ring; the later flavin-reducing structure demonstrates domain rotation. Phenylmercuric acetate, nucleotide analogues, glycerol and temperature belong to experimental conditions. The 2009 study models the catalytic cycle from wild-type TrxB FO and engineered mixed-disulfide FR structures and tests TrxA Arg73 and Lys36 through R73G, R73D and K36A substitutions. These TrxA mutants are impaired to different extents in reduction by TrxB; computed intermediates are not separately observed native turnover structures. (PMID:8664260; PMID:8114095; PMID:10947986; PMID:11567095; PMID:19585660.) The original 1F6M deposition resolves the construct details behind the 2000 structural result. Its TrxB chains carry C135S and its TrxA chains carry C35S in mature-chain numbering, with trapped TrxB Cys138–TrxA Cys32 disulfides. Exact sequence comparison to retained current UniProt originals places these substitutions at TrxB C136S and TrxA C36S after the initiator-methionine offset. The deposited nucleotide is 3-aminopyridine-adenine-dinucleotide phosphate, not native NADPH. Two deposited tetrameric assemblies each contain two reductase and two thioredoxin chains; four copies of each protein in the asymmetric unit are not native homodimer stoichiometry. Source and host are E. coli, with strain and vector unspecified. (PMID:10947986; DOI:10.2210/pdb1f6m/pdb.) The original 1CL0 deposition describes TrxB expressed in E. coli A326, with vector PSL350 and plasmid PTRR301. FAD and the active-site disulfide were reduced by sodium dithionite after crystallization. Its deposited biological assembly is dimeric, whereas the asymmetric unit contains one protein chain and one FAD. The mature chain matches retained UniProt P0A9P4 exactly after removal of the initiating methionine; the source gene strain is unspecified. This chemically reduced crystal does not measure a native steady-state conformational population. (PMID:8114095; DOI:10.2210/pdb1cl0/pdb.) The Mycoplasma primary abstract reports partially purified M. pneumoniae and M. capricolum systems that use NADPH rather than NADH and prefer homologous thioredoxins; tested E. coli and Bacillus subtilis thioredoxins failed as heterologous substrates. M129 TrxA P75512 is 102 residues and TrxB P75531 is 315 residues in issuing sequence records. Reviewed M129 FAD, assembly and location annotations are explicitly by similarity, not direct M129 structural experiments. A protective role against oxidative stress was proposed rather than demonstrated by those substrate-specificity assays. The M. capricolum strain/protein identities are not guessed or merged with M129. (PMID:9202470; UniProtKB:P75512; UniProtKB:P75531.) TrxA structural abstracts describe subtle, localized differences between reduced and oxidized solution structures near Cys32/Cys35. An earlier NMR report describes larger local differences; the studies do not establish one universal inter-residue distance for every state. The reduced TrxA solution structure has a five-strand central beta-sheet, so the native generic four-sheet fold description is not used as an exact whole-protein count. An oxidized crystal contains an active-site disulfide and two independent molecules. Copper and methylpentanediol used for crystal growth/packing are not evidence of obligatory native TrxA copper binding or a physiological homodimer. (PMID:7812718; PMID:2193685; PMID:2181145.) trxA regulation is condition- and promoter-specific. The cAMP study used trxA-lac translational fusions in pMC1403; switching glucose to lactose or adding cAMP reduced reporter synthesis. The effect was absent in a crp mutant and in a fusion lacking the plausible cAMP-CRP site, and chromosomal trxA expression also decreased with exogenous cAMP. The native REG0-6357 object assigns repression to the cAMP-CRP complex at trxAp1. Separately, pKO100/pJEL170 promoter fusions showed growth-rate dependence and ppGpp/RelA-linked induction during stationary phase and amino-acid starvation; RpoS was not required in those tests. These observations concern transcription, not direct inhibition or activation of the TrxA redox-active protein by those metabolites. (PMID:9175752; PMID:10760563.) Oxidized OxyR binds the trxC promoter and activates expression in the 2000 primary abstract. Double-thioredoxin mutants were more resistant to high peroxide yet more diamide-sensitive, illustrating stress-specific effects. Native regulation records retain direct promoter linkage and their cited binding/expression evidence. A genome-wide OxyR/SoxRS study used ChIP-exo and RNA sequencing; its accessible abstract does not independently enumerate trxC, so the exact target association remains native-attributed where that paper is cited. Similarly, a genome-wide RACE/pyrosequencing TSS abstract does not independently identify the native trxB row. A source object without a named local regulator is not evidence that trxB is unregulated. (PMID:10644706; EcoCyc:REG0-6358; PMID:26279566; PMID:19838305.) The 2019 full study supports a distinct OxyR persulfidation response: sulfane sulfur modifies C199 and activates trxC reporters, while sulfide alone fails. C199S/C208S and the double mutant lose reporter activity; four other cysteine-to-alanine substitutions retain it. C208 is required although a C199–C208 crosslink was not detected, leaving its precise role unresolved. Purified OxyR was His-tagged and expressed in BL21(DE3); reporter responses depend on dose and aerobic/anaerobic conditions. TrxA overexpression alone did not lower the sulfane-sulfur signal, whereas combined TrxA/TrxB overexpression lowered it during log phase. TrxC overexpression rescued the tested oxyR-defective phenotype. These engineered feedback results do not supply a homogeneous additional H2Sn core reaction or establish that all OxyR activation involves the same oxidized state. (PMID:31421411.) Switching dissolved oxygen from 30% to 300% air saturation produced strain-dependent transcriptional responses in the 2013 full study. AB1157 trxC increased 2.2-fold, while its PN134 sodA sodB mutant increased 3.2-fold and grew more slowly. MG1655 primarily showed a SoxRS response with little OxyR response. MG1655 was grown in defined mineral medium with 8 g/L glucose; AB1157 and PN134 used supplemented modified LB with 4 g/L glucose. Transcript samples were collected at 0, 5, 10 and 40 minutes after the oxygen shift. These different parental backgrounds, media and sampling times limit generalization; high oxygen is not universal strong activation of trxC. (PMID:23497217.) The 2026 ArsR study associates lower TrxB abundance under arsenite with AW3110, a W3110-derived strain lacking the entire arsRBC operon, compared with a complemented strain or MG1655. The supplement explicitly contains TrxB rows. This does not demonstrate direct ArsR binding to, or direct activation of, trxB. Whole-operon deletion, W3110 versus MG1655 background, an altered complementation promoter, and comparisons involving 100 µM mutant versus 1 mM high wild-type exposure remain confounders. The association is retained as proteomic context rather than a direct regulatory edge. (DOI:10.3390/proteomes14010001.) The 2023 full study finds that low-micromolar peroxide can activate OxyR and induce trxC/grxA/trxB without widespread protein-thiol damage in growing E. coli. In an Hpx-minus ΔkatG ΔkatE ΔahpCF background, additional ΔgrxA ΔtrxC caused no added long-culture growth defect and sometimes a small advantage; substantial Pdf, Tdh or IPMI repair defects were not found. Table 1 assigns trxC 20-fold, grxA 30-fold and trxB 3-fold induction, while body/caption wording differs for the trxC 20/30 value; no universal exact fold is inferred. The PhoA reporter on pAID135 lacks export-signal residues 2–22, and residual activity can reflect a small periplasmic fraction. Earlier differential-thiol-trapping experiments used DHB4 versus WP570 ΔtrxA with 4 mM H2O2 or 1 mM diamide, a different regime. Modified spots and other proteomic capture hits are candidate or indirect effects, not a verified list of direct thioredoxin catalytic clients. (PMID:38152379; PMID:15502869; PMID:15004283.) Adjacent thioredoxin electron flow can pass through DsbD to periplasmic DsbC. This transmembrane relay does not place native TrxA freely in the periplasm and is not an extra member reaction of the native two-event pathway. The 2009 DsbD abstract reports cysteine-substitution and alkylation-accessibility comparisons of oxidized and reduced DsbD beta-domain transmembrane segments. Accessibility at the tested positions in TM1-TM4 was unchanged between those redox states, supporting a relatively static conformation while leaving possible changes during thioredoxin interaction unresolved. A separate PAPS-reductase/TrxA crystal captures a mixed disulfide; full construct details remain unresolved from its abstract, so Cys239 involvement is not promoted into a permanent native assembly. Crosslinking/immunoelectron microscopy in W3110 and overproducing SK3981 reported an inner-membrane-adjacent thioredoxin fraction without specific periplasmic labeling. It supports contextual membrane association, not an integral-membrane identity or an exclusively bulk-cytosolic population. (PMID:9352906; PMID:19258316; PMID:17352498; PMID:3294802.) Other substrate and physiological contexts remain separate from the generic client identity. The YchF abstract reports oxidation-dependent disulfide dimerization with lower ATPase activity and TrxA-dependent dimer dissociation/activity recovery in vitro, plus cellular crosslinking; exact mutant and crosslinking constructs require its unavailable full body before sequence-state edges can be assigned. TrxB-dependent selenium incorporation into formate dehydrogenase H under anaerobic low-salt conditions does not establish direct selenite reduction by TrxB. TrxA/TrxB/NADPH together support IscA iron binding and delivery for IscU cluster assembly in vitro, with IscA/IscS/cysteine context; direct IscU iron binding is not supported. Oxidized Grx4 can be a direct TrxB substrate, whereas Grx1 reduces glutathionylated Grx4; the engineered CGFC Grx4 variant lacks HED activity. That adjacent branch bypasses thioredoxin and is not silently substituted for the native cycle. (PMID:26160547; PMID:18182386; PMID:15985427; PMID:15833738.) In-vitro anthracycline redox cycling, ROS and DNA-damage enhancement by the E. coli thioredoxin system are distinct from endogenous microbial substrate requirements; A549-cell treatment observations are heterologous. Thioredoxin and TrxB can assist refolding or protect selected unfolded proteins, including cysteine-free targets, without an additional disulfide-reduction event. Active dimeric TrxB produced in a cell-free system with added FAD does not prove in-vivo regulation by FAD availability. A Salmonella AhpF N-terminal 207-residue fusion to E. coli TrxB acquired AhpC reductase activity while retaining thioredoxin reductase activity; C129/132S and C342/345S variants distinguish its engineered centers. AhpC specificity in that chimera is not transferred to unmodified TrxB. (PMID:15290096; PMID:12549977; PMID:14960309; PMID:10913298.) Primary Figure 1C of the 2012 mutagenesis study explicitly lists trxB among the SIM-network genes and marks it with superscript E, defined in the caption as decreased sigma-E activity in the secondary screen. This supports a mutant-screen association with stress-induced mutagenesis and sigma-E response, not direct TrxB catalysis of DNA repair or direct RpoE regulation. The linked supplemental file remains inaccessible, so exact trxB strain, magnitude and rescue details are not independently verified here. The 2011 kinetic-regulation work instead models competing thioredoxin reactions with literature-derived parameters; its nonlinear responses remain model predictions, not additional measured physiological edges. (PMID:23224554; PMID:21266044.) TrxA also acts as a redox-independent processivity factor for T7 DNA polymerase. This interaction does not add DNA polymerization to the two-event redox cycle. Current UniProt subunit prose refers to T3 despite the cited/interaction T7 scope; that discrepancy is retained. Human thioredoxin fails to support T7 growth/processivity despite structural similarity, and E. coli–human chimeras and L95 variants identify an interface determinant. Homology alone therefore does not transfer the phage-specific function to all thioredoxins. (PMID:20080681; PMID:30265524.) The 2024 full TreX study provides a separate redox-independent chaperone example. Cysteine-free TreX requires reduced TrxA for folding, solubility and ADP-ribosyltransferase activity rather than TrxA redox turnover per substrate. ΔtrxA protects cells and ΔtrxB partly protects. TrxA C33A/C36A, W32A, I61D, D62A and I76D variants impair the measured interaction or activity; the numbering includes the initiating methionine relative to classic C32/C35 nomenclature. E. coli and X. bovienii homologs, their measured sequence similarity, affinity tags and tag-cleavage preparations remain distinct. Delivery was tested with an engineered E. coli CDI chimera carrying Xenorhabdus toxin/immunity genes, not a demonstration of native Xenorhabdus T6SS delivery. TreX E100A/E102A trapping, Strep/His tags, TEV removal and TriX-containing complexes qualify the structures; T130C/R118C engineering did not eliminate TrxA dependence. Proposed Scabin ancestry and modeled homolog behavior remain hypotheses. (PMID:39613764.) Export-reporter selections show that altered TrxA folding can permit post-translational export, conditional on the signal sequence and mutation. Exported G74S improves PhoA oxidation without restoring FlgI-dependent motility, supporting changed substrate specificity rather than a universal oxidative gain. These constructs do not redefine native localization. Constant-pH molecular-dynamics methodology using thioredoxin contributes computational structural context without establishing a new microbial physiological reaction, regulator or phenotype. (PMID:16357193; PMID:18003618; PMID:36190807.) Historical native purification and sequencing references distinguish E. coli B from the affinity-purified E. coli 011-prime preparation. Their full bodies remain unavailable here; current issuing sequence identities do not retrospectively establish an exact MG1655 preparation or undisclosed tags in those experiments. The generic native background also describes thiol-redox systems across archaea and eukaryotes, but that comparison is review-level context rather than a blanket organism assertion for this record. (PMID:14245401; PMID:330529; PMID:4883076.) Identity conflicts are explicitly rejected: P0A850 is trigger factor rather than TrxB; EG11022 is trmA rather than trxA; CHEBI:17992 is sucrose rather than ppGpp; reactive CHEBI cysteine/cystine residues do not identify whole thioredoxins. Two historical native trxAp3 citations resolve to unrelated cardiac-imaging and rat-satiety articles and do not support promoter biology. OxyR is a transcriptional regulator; the 2003 discussion's isolated sigma-factor wording is not adopted. Unknown clients, unverified stable complexes, the unresolved zinc-center physiological function and unavailable older construct details remain evidence gaps rather than fabricated identities or causal links. (UniProtKB:P0AGG4; PMID:9175752.) The sulfane-sulfur study used a prepared H2Sn mixture with chain lengths 2–8, rather than one uniquely identified chemical species. Native-promoter mkate reporters were carried in pTrcHis2A derivatives, and oxyR complementation used PlacI. Promoter induction used early-log cells at OD600 0.5 with 600 µM H2Sn for two hours; anaerobic RT-qPCR used OD600 0.4 with 200 µM for 60 minutes; growth plates used 100 µM. These separate assay regimes are not merged into one physiological dose. (PMID:31421411.) Four retained native regulation originals annotate inhibition of the TrxB enzymatic activity by hydrogen cyanide, cadmium dichloride, p-mercuribenzoate and arsenite. They cite the 1964 E. coli B purification study; p-mercuribenzoate is described as strong and arsenite as moderate inhibition. These are native source annotations assigned to the ECOLI activity, not independently verified MG1655 experiments. The linked compound originals identify hydrogen cyanide and arsenite(1-); exact assay dose, pH-dependent speciation, preparation and reversibility remain unresolved because both renewed primary-body requests failed. No endogenous physiological control by these compounds is inferred. (EcoCyc:REG0-10687; EcoCyc:REG0-9797; EcoCyc:REG0-9025; EcoCyc:REG0-9024; PMID:14245401.)

Pathway type

thiol redox homeostasis

Organism scope

• Escherichia coli str. K-12 substr. MG1655 NCBITaxon:511145
• Mycoplasmoides pneumoniae M129 NCBITaxon:272634

Read the source YAML

Components and activities

Mechanistic edges

References

• PMID:10464247 Importance of redox potential for the in vivo function of the cytoplasmic disulfide reductant thioredoxin from Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:10644706 Thioredoxin 2 is involved in the oxidative stress response in Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:10760563 Growth-phase regulation of the Escherichia coli thioredoxin gene. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:10913298 Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:10947986 Twists in catalysis: alternating conformations of Escherichia coli thioredoxin reductase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:11567095 Exploring the conformational equilibrium of E. coli thioredoxin reductase: characterization of two catalytically important states by ultrafast flavin fluorescence spectroscopy. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:11893749 Protein levels of Escherichia coli thioredoxins and glutaredoxins and their relation to null mutants, growth phase, and function. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:12549977 Chaperone properties of Escherichia coli thioredoxin and thioredoxin reductase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:14245401 ENZYMATIC SYNTHESIS OF DEOXYRIBONUCLEOTIDES.V. PURIFICATION AND PROPERTIES OF THIOREDOXIN REDUCTASE FROM ESCHERICHIA COLI B. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:14960309 Cell-free production of active E. coli thioredoxin reductase and glutathione reductase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:15004283 Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:15290096 Redox-cycling of anthracyclines by thioredoxin system: increased superoxide generation and DNA damage. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:15833738 A novel monothiol glutaredoxin (Grx4) from Escherichia coli can serve as a substrate for thioredoxin reductase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:15985427 Thioredoxin reductase system mediates iron binding in IscA and iron delivery for the iron-sulfur cluster assembly in IscU. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:16357193 A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:17352498 3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:18003618 Laboratory evolution of Escherichia coli thioredoxin for enhanced catalysis of protein oxidation in the periplasm reveals a phylogenetically conserved substrate specificity determinant. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:18182386 Selenite assimilation into formate dehydrogenase H depends on thioredoxin reductase in Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:19073194 The zinc center influences the redox and thermodynamic properties of Escherichia coli thioredoxin 2. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:19258316 Two snapshots of electron transport across the membrane: insights into the structure and function of DsbD. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:19585660 Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:19838305 Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:20080681 Thioredoxin suppresses microscopic hopping of T7 DNA polymerase on duplex DNA. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:21570393 Thioredoxin 2 from Escherichia coli is not involved in vivo in the recycling process of methionine sulfoxide reductase activities. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:2181145 Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:2187529 Characterization of Escherichia coli thioredoxins with altered active site residues. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:2193685 Three-dimensional solution structure of the reduced form of Escherichia coli thioredoxin determined by nuclear magnetic resonance spectroscopy. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:26160547 Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:26279566 Genome-wide Reconstruction of OxyR and SoxRS Transcriptional Regulatory Networks under Oxidative Stress in Escherichia coli K-12 MG1655. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:26382254 Acceleration of the Rate-Limiting Step of Thioredoxin Folding by Replacement of its Conserved cis-Proline with (4 S)-Fluoroproline. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:2644268 Characterization of two active site mutations of thioredoxin reductase from Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:30265524 Hydrophobic Residue in Escherichia coli Thioredoxin Critical for the Processivity of T7 DNA Polymerase. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:3294802 Association of thioredoxin with the inner membrane and adhesion sites in Escherichia coli. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:330529 Purification of thioredoxin, thioredoxin reductase, and glutathione reductase by affinity chromatography. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:36190807 Extending the Stochastic Titration CpHMD to CHARMM36m. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:4883076 Thioredoxin. 6. The amino acid sequence of the protein from escherichia coli B. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:7812718 High-resolution solution structures of oxidized and reduced Escherichia coli thioredoxin. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:8114095 Crystal structure of Escherichia coli thioredoxin reductase refined at 2 A resolution. Implications for a large conformational change during catalysis. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:8136348 Potential active-site base of thioredoxin reductase from Escherichia coli: examination of histidine245 and aspartate139 by site-directed mutagenesis. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:8664260 Enzyme-monitored turnover of Escherichia coli thioredoxin reductase: insights for catalysis. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9175752 Expression of the Escherichia coli thioredoxin gene is negatively regulated by cyclic AMP. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9188456 The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9352906 Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9388228 Cloning, expression, and characterization of a novel Escherichia coli thioredoxin. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9655349 Formation and properties of mixed disulfides between thioredoxin reductase from Escherichia coli and thioredoxin: evidence that cysteine-138 functions to initiate dithiol-disulfide interchange and to accept the reducing equivalent from reduced flavin. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9724776 The reductive enzyme thioredoxin 1 acts as an oxidant when it is exported to the Escherichia coli periplasm. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9755155 Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• PMID:9202470 The thioredoxin reductase system of mycoplasmas. (source version: Retained Europe PMC core metadata; primary abstract inspected where supplied. No full primary body is implied by database indexing or metadata.)
• DOI:10.3390/proteomes14010001 Beyond Repression: ArsR Functions as a Global Activator of Metabolic and Redox Responses in Escherichia coli (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:38152379 Evidence that protein thiols are not primary targets of intracellular reactive oxygen species in growing Escherichia coli (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:39613764 Thioredoxin 1 moonlights as a chaperone for an interbacterial ADP-ribosyltransferase toxin (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:21266044 The logic of kinetic regulation in the thioredoxin system (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:23497217 Escherichia coli avoids high dissolved oxygen stress by activation of SoxRS and manganese-superoxide dismutase (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:15502869 Protein Thiol Modifications Visualized In Vivo (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:31421411 OxyR senses sulfane sulfur and activates the genes for its removal in Escherichia coli (source version: Inspected full primary JATS body retained verbatim; preparation, organism, methods, negative results and cited-background scope are distinguished.)
• PMID:12952960 Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. (source version: Full primary eight-page author-hosted PDF retained and inspected; untagged recombinant TrxC; core catalytic disulfide distinguished from all-six-cysteine oxidation.)
• PMID:23224554 Identity and function of a large gene network underlying mutagenic repair of DNA breaks. (source version: Inspected primary HTML and Figure 1C; original linked figure SHA256 fb1742d21adae587b90b64d8d8f1a72b9edce81987861c0ab9c473060c08d025. Supplemental PDF request returned challenge HTML, so detailed strain/quantitative tables are not claimed inspected.)
• DOI:10.2210/pdb1f6m/pdb Original PDB 1F6M structure deposition (source version: Issuing mmCIF original acquired 2026-10-12; exact entity/construct/sequence/assembly fields inspected. A structure deposition does not imply inspection of its cited full paper.)
• DOI:10.2210/pdb1cl0/pdb Original PDB 1CL0 structure deposition (source version: Issuing mmCIF original acquired 2026-10-12; exact entity/construct/sequence/assembly fields inspected. A structure deposition does not imply inspection of its cited full paper.)
• MetaCyc:THIOREDOX-PWY thioredoxin pathway (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:THIOREDOXIN-REDUCT-NADPH-RXN THIOREDOXIN-REDUCT-NADPH-RXN (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:THIOREDOXIN-RXN THIOREDOXIN-RXN (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:Red-Thioredoxin a reduced thioredoxin (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:Ox-Thioredoxin an oxidized thioredoxin (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:Acceptor an oxidized electron carrier (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:Donor-H2 a reduced two electron carrier (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:NADPH NADPH (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:NADP NADP+ (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• MetaCyc:PROTON H+ (source version: Native META PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:THIOREDOX-PWY thioredoxin pathway (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:THIOREDOXIN-REDUCT-NADPH-CPLX THIOREDOXIN-REDUCT-NADPH-CPLX (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:THIOREDOXIN-REDUCT-NADPH-MONOMER thioredoxin reductase (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:THIOREDOXIN-REDUCT-NADPH-ENZRXN thioredoxin reductase (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:RED-THIOREDOXIN-MONOMER thioredoxin 1 (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:OX-THIOREDOXIN-MONOMER oxidized thioredoxin (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:RED-THIOREDOXIN2-MONOMER reduced thioredoxin 2 (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:OX-THIOREDOXIN2-MONOMER oxidized thioredoxin 2 (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:REG0-6357 REG0-6357 (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:REG0-6358 REG0-6358 (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:CPLX0-226 CRP-cyclic-AMP DNA-binding transcriptional dual regulator (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:PC00004 DNA-binding transcriptional dual regulator CRP (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:PD00257 DNA-binding transcriptional dual regulator CRP (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:CAMP cyclic-AMP (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:PD00214 DNA-binding transcriptional dual regulator OxyR (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• EcoCyc:TU0-3104 trxC (source version: Native ECOLI PGDB 27.0; exact retained whole XML original acquired 2026-10-12; structured assertions are native annotations, not automatic readings of cited papers.)
• PathBank:SMP0002094 Thioredoxin Pathway; frozen PathBank member PW002082.owl (source version: Exact member SHA of retained whole BioPAX ZIP b3a9b9557d4147fac0159d178a27c13cc1180729eae9ccb4fb32abebb1656f44; original member PW002082.owl; state/charge/spontaneity differences retained.)
• RHEA:20347 [thioredoxin]-disulfide + NADPH + H(+) => [thioredoxin]-dithiol + NADP(+) (source version: Rhea release 142; issuing complete RDF gzip, exact directional side links and whole polypeptide components; reactive residues remain separate.)
• RHEA-COMP:10698 [thioredoxin]-dithiol (source version: Rhea release 142; issuing complete RDF gzip, exact directional side links and whole polypeptide components; reactive residues remain separate.)
• RHEA-COMP:10700 [thioredoxin]-disulfide (source version: Rhea release 142; issuing complete RDF gzip, exact directional side links and whole polypeptide components; reactive residues remain separate.)
• UniProtKB:P0AA25 Thioredoxin 1 (source version: Reviewed issuing record entry version 175, sequence version 2; annotation date 2026-09-02. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• UniProtKB:P0AGG4 Thioredoxin 2 (source version: Reviewed issuing record entry version 139, sequence version 1; annotation date 2026-06-10. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• UniProtKB:P0A9P4 Thioredoxin reductase (source version: Reviewed issuing record entry version 154, sequence version 2; annotation date 2026-09-02. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• UniProtKB:P75512 Thioredoxin (source version: Reviewed issuing record entry version 128, sequence version 1; annotation date 2026-06-10. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• UniProtKB:P75531 Thioredoxin reductase (source version: Reviewed issuing record entry version 143, sequence version 1; annotation date 2026-06-10. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• UniProtKB:P0ACQ4 DNA-binding transcriptional dual regulator OxyR (source version: Reviewed issuing record entry version 144, sequence version 1; annotation date 2026-09-02. Evidence codes, inference and explicit annotation conflicts remain scoped.)
• Entrez:947062 trxC gene, Escherichia coli MG1655 (source version: Exact issuing NCBI Gene EFetch XML retrieved 2026-10-12; gene/locus/taxon and EcoCyc cross-reference verified.)
• Entrez:948289 trxA gene, Escherichia coli MG1655 (source version: Exact issuing NCBI Gene EFetch XML retrieved 2026-10-12; gene/locus/taxon and EcoCyc cross-reference verified.)
• Entrez:949054 trxB gene, Escherichia coli MG1655 (source version: Exact issuing NCBI Gene EFetch XML retrieved 2026-10-12; gene/locus/taxon and EcoCyc cross-reference verified.)
• EcoCyc:TU0-3102 trxA (source version: Native PGDB27.0; exact retained whole XML original acquired 2026-10-12.)
• MetaCyc:GUANOSINE-5DP-3DP ppGpp (source version: Native PGDB27.0; exact retained whole XML original acquired 2026-10-12.)
• EcoCyc:CCI-CYTOSOL-GN cytosol (source version: Native PGDB27.0; exact retained whole XML original acquired 2026-10-12.)
• EcoCyc:CCI-PM-BAC-NEG-GN inner membrane (source version: Native PGDB27.0; exact retained whole XML original acquired 2026-10-12.)
• MetaCyc:RED-THIOREDOXIN-MONOMER thioredoxin 1 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• MetaCyc:OX-THIOREDOXIN-MONOMER oxidized thioredoxin (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• MetaCyc:RED-THIOREDOXIN2-MONOMER reduced thioredoxin 2 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• MetaCyc:OX-THIOREDOXIN2-MONOMER oxidized thioredoxin 2 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:THIOREDOXIN-REDUCT-NADPH-RXN THIOREDOXIN-REDUCT-NADPH-RXN (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• MetaCyc:THIOREDOXIN-REDUCT-NADPH-ENZRXN thioredoxin reductase (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:REG0-10687 REG0-10687 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:HCN hydrogen cyanide (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:REG0-9797 REG0-9797 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:CPD0-1355 dichlorocadmium (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:REG0-9025 REG0-9025 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:CPD-7388 p-mercuribenzoate (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:REG0-9024 REG0-9024 (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)
• EcoCyc:CPD-763 arsenite (source version: Native PGDB27.0; exact whole original acquired 2026-10-12. Source-specific identifiers remain distinct.)