{"gene":"PF3D7_1208300","run_date":"2026-09-08T16:26:55","timeline":{"discoveries":[{"year":2021,"finding":"Ligand-dependent knockdown of mACP (PF3D7_1208300) is lethal to P. falciparum parasites, demonstrating an essential FASII-independent function. Decyl-ubiquinone temporarily rescued parasites from death, indicating a dominant dysfunction of the mitochondrial electron transport chain (ETC) upon mACP depletion.","method":"Conditional (ligand-dependent) knockdown with parasite viability assay and chemical rescue with decyl-ubiquinone","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Strong — conditional knockdown with defined lethal phenotype, chemical rescue with decyl-ubiquinone providing mechanistic specificity, published in peer-reviewed journal","pmids":["34612205"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"mACP (PF3D7_1208300) physically binds and stabilizes the Isd11-Nfs1 complex required for mitochondrial Fe-S cluster biosynthesis, despite lacking the 4-phosphopantetheine (Ppant) prosthetic group that mediates this interaction in other eukaryotes. Knockdown of mACP causes loss of Nfs1 and the Rieske Fe-S protein in ETC complex III.","method":"Biochemical pulldown/binding studies; conditional knockdown followed by immunoblot detection of Nfs1 and Rieske Fe-S protein levels","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal biochemical binding studies combined with functional knockdown demonstrating downstream loss of Fe-S pathway components, multiple orthogonal methods in one study","pmids":["34612205"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"mACP (PF3D7_1208300) lacks the 4-phosphopantetheine (Ppant) prosthetic group, making it divergent from canonical eukaryotic mACP proteins and decoupling mitochondrial Fe-S cluster biogenesis from fatty acid synthesis (FASII) activity in Plasmodium parasites.","method":"Sequence and biochemical characterization establishing absence of Ppant group","journal":"eLife","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — biochemical characterization in single lab but corroborated by functional studies showing Ppant-independent Isd11-Nfs1 binding","pmids":["34612205"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"mACP (PF3D7_1208300) was used as a negative control (mitochondrial HA-tagged protein) in immunoprecipitation experiments for PfHO interactor identification, confirming its mitochondrial localization and utility as a mitochondrial control, and showing it does not co-purify with apicoplast-specific PfHO interactors.","method":"Anti-HA immunoprecipitation followed by tandem mass spectrometry (negative control experiment)","journal":"eLife","confidence":"Low","confidence_rationale":"Tier 3 / Weak — mACP used only as a negative/control pulldown; the finding about mACP itself is its mitochondrial localization confirmed indirectly, single use as control","pmids":["39660822"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"finding":"Conditional depletion of the Rieske Fe-S protein (PfRieske) in P. falciparum resulted in loss of PfRieske protein, consistent with the earlier observation that mACP (PF3D7_1208300) knockdown causes secondary loss of PfRieske, confirming the pathway: mACP stabilizes Fe-S biogenesis → Fe-S clusters → Rieske protein → ETC complex III.","method":"Conditional knockdown of PfRieske with immunoblot; cited in context of previously established mACP-Rieske epistatic relationship","journal":"International journal of molecular sciences","confidence":"Low","confidence_rationale":"Tier 3 / Weak — mACP-specific finding is cited as prior work; this paper provides indirect epistatic support but does not directly experiment on mACP","pmids":["39273187"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"P. falciparum mACP (PF3D7_1208300) is a divergent mitochondrial acyl carrier protein that lacks the canonical 4-phosphopantetheine prosthetic group and therefore has no fatty acid synthesis function; instead, it is essential for parasite survival by directly binding and stabilizing the Isd11-Nfs1 complex required for mitochondrial Fe-S cluster biogenesis, and its depletion causes secondary loss of the Rieske Fe-S protein in ETC complex III and dominant dysfunction of the mitochondrial electron transport chain."},"narrative":{"mechanistic_narrative":"mACP (PF3D7_1208300) is a divergent mitochondrial acyl carrier protein in Plasmodium falciparum that has been repurposed away from fatty acid synthesis to serve an essential role in mitochondrial Fe-S cluster biogenesis [PMID:34612205]. Unlike canonical eukaryotic mitochondrial ACPs, mACP lacks the 4-phosphopantetheine (Ppant) prosthetic group, decoupling it from FASII activity, yet it still directly binds and stabilizes the Isd11-Nfs1 cysteine desulfurase complex that initiates Fe-S cluster assembly [PMID:34612205]. Conditional knockdown of mACP is lethal and causes secondary loss of Nfs1 and of the Rieske Fe-S protein of ETC complex III, producing a dominant defect in the mitochondrial electron transport chain that is transiently rescued by decyl-ubiquinone [PMID:34612205]. Beyond this Fe-S biogenesis and ETC-stabilization role, no additional mechanistic function of mACP has been characterized in the available corpus.","teleology":[{"year":2021,"claim":"It was unknown whether the mitochondrial ACP of P. falciparum had an essential role independent of fatty acid synthesis; conditional knockdown established that mACP is essential and that its loss primarily disables the mitochondrial ETC.","evidence":"Ligand-dependent conditional knockdown with viability assay and chemical rescue by decyl-ubiquinone","pmids":["34612205"],"confidence":"High","gaps":["Does not identify the direct molecular target whose loss disables the ETC","Transient nature of decyl-ubiquinone rescue not mechanistically resolved"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"The molecular basis of mACP essentiality was unresolved; binding and knockdown studies showed mACP physically stabilizes the Isd11-Nfs1 Fe-S biogenesis complex and that its depletion causes loss of Nfs1 and the Rieske Fe-S protein, defining a Fe-S biogenesis-to-complex III pathway.","evidence":"Biochemical pulldown/binding studies plus conditional knockdown with immunoblot for Nfs1 and Rieske Fe-S protein","pmids":["34612205"],"confidence":"High","gaps":["Structural basis of Ppant-independent Isd11-Nfs1 binding not resolved","Whether mACP participates in other Fe-S client maturation steps unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Whether mACP retained the canonical ACP prosthetic group was unclear; biochemical characterization established that mACP lacks the 4-phosphopantetheine group, explaining its decoupling from FASII and its divergence from canonical mitochondrial ACPs.","evidence":"Sequence and biochemical characterization of the absence of the Ppant group","pmids":["34612205"],"confidence":"Medium","gaps":["Single-lab biochemical assignment","Structural consequences of Ppant absence for the Isd11-Nfs1 interface not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"mACP's subcellular assignment was tested indirectly when it served as an HA-tagged mitochondrial negative control in an apicoplast interactor screen, confirming its mitochondrial residence and that it does not co-purify with apicoplast proteins.","evidence":"Anti-HA immunoprecipitation with tandem mass spectrometry, using mACP as a negative control","pmids":["39660822"],"confidence":"Low","gaps":["mACP was not the subject of study, only a control","No new mACP-specific interactors defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2024,"claim":"The proposed mACP-to-Rieske epistatic pathway gained indirect support when conditional depletion of the Rieske Fe-S protein reproduced the loss of PfRieske consistent with the pathway placing mACP upstream of complex III Fe-S maturation.","evidence":"Conditional knockdown of PfRieske with immunoblot, interpreted in the context of prior mACP work","pmids":["39273187"],"confidence":"Low","gaps":["No direct experimentation on mACP in this study","Epistasis inferred from citation rather than co-perturbation"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How mACP mechanistically substitutes for the Ppant-dependent ACP contacts of canonical eukaryotes to stabilize Isd11-Nfs1, and whether it has any Fe-S client roles beyond the Rieske protein, remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No structure of the mACP-Isd11-Nfs1 interface","Full set of Fe-S clients downstream of mACP unknown","Mechanism of ETC dominance upon mACP loss not fully defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Isd11-Nfs1 cysteine desulfurase complex (binding/stabilizing partner)"],"partners":["ISD11","NFS1","RIESKE FE-S PROTEIN (PFRIESKE, DOWNSTREAM-DEPENDENT)"],"other_free_text":["Divergent mitochondrial ACP lacking the 4-phosphopantetheine prosthetic group, uncoupling it from FASII [#2].","Essential; conditional knockdown is lethal and transiently rescued by decyl-ubiquinone, indicating dominant ETC dysfunction [#0].","Knockdown causes secondary loss of Nfs1 and the complex III Rieske Fe-S protein [#1]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"34612205","id":"PMC_34612205","title":"Divergent acyl carrier protein decouples mitochondrial Fe-S cluster biogenesis from fatty acid synthesis in malaria parasites.","date":"2021","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/34612205","citation_count":18,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["mACP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39660822","id":"","title":"Malaria parasites require a divergent heme oxygenase for apicoplast gene expression and biogenesis.","date":"2024","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/39660822","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["mACP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39273187","id":"","title":"Plasmodium falciparum Mitochondrial Complex III, the Target of Atovaquone, Is Essential for Progression to the Transmissible Sexual Stages.","date":"2024","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/39273187","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["mACP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"39207139","id":"","title":"The Toxoplasma gondii mitochondrial transporter ABCB7L is essential for the biogenesis of cytosolic and nuclear iron-sulfur cluster proteins and cytosolic translation.","date":"2024","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/39207139","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["mACP"],"competing_organism_flag":true,"competing_organism_match":"Toxoplasma","competing_organism_only":true}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6744,"output_tokens":1463,"usd":0.021088,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6483,"output_tokens":2509,"usd":0.04757,"stage2_stop_reason":"end_turn"},"total_usd":0.068658,"stage1_batch_id":"msgbatch_01NE1MTa8x1hW7Lo4tAaNzY1","stage2_batch_id":"msgbatch_0141vaQdeFvbo2q39AinvXM9","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"Ligand-dependent knockdown of mACP (PF3D7_1208300) is lethal to P. falciparum parasites, demonstrating an essential FASII-independent function. Decyl-ubiquinone temporarily rescued parasites from death, indicating a dominant dysfunction of the mitochondrial electron transport chain (ETC) upon mACP depletion.\",\n      \"method\": \"Conditional (ligand-dependent) knockdown with parasite viability assay and chemical rescue with decyl-ubiquinone\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — conditional knockdown with defined lethal phenotype, chemical rescue with decyl-ubiquinone providing mechanistic specificity, published in peer-reviewed journal\",\n      \"pmids\": [\"34612205\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"mACP (PF3D7_1208300) physically binds and stabilizes the Isd11-Nfs1 complex required for mitochondrial Fe-S cluster biosynthesis, despite lacking the 4-phosphopantetheine (Ppant) prosthetic group that mediates this interaction in other eukaryotes. Knockdown of mACP causes loss of Nfs1 and the Rieske Fe-S protein in ETC complex III.\",\n      \"method\": \"Biochemical pulldown/binding studies; conditional knockdown followed by immunoblot detection of Nfs1 and Rieske Fe-S protein levels\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal biochemical binding studies combined with functional knockdown demonstrating downstream loss of Fe-S pathway components, multiple orthogonal methods in one study\",\n      \"pmids\": [\"34612205\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"mACP (PF3D7_1208300) lacks the 4-phosphopantetheine (Ppant) prosthetic group, making it divergent from canonical eukaryotic mACP proteins and decoupling mitochondrial Fe-S cluster biogenesis from fatty acid synthesis (FASII) activity in Plasmodium parasites.\",\n      \"method\": \"Sequence and biochemical characterization establishing absence of Ppant group\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — biochemical characterization in single lab but corroborated by functional studies showing Ppant-independent Isd11-Nfs1 binding\",\n      \"pmids\": [\"34612205\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"mACP (PF3D7_1208300) was used as a negative control (mitochondrial HA-tagged protein) in immunoprecipitation experiments for PfHO interactor identification, confirming its mitochondrial localization and utility as a mitochondrial control, and showing it does not co-purify with apicoplast-specific PfHO interactors.\",\n      \"method\": \"Anti-HA immunoprecipitation followed by tandem mass spectrometry (negative control experiment)\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — mACP used only as a negative/control pulldown; the finding about mACP itself is its mitochondrial localization confirmed indirectly, single use as control\",\n      \"pmids\": [\"39660822\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"Conditional depletion of the Rieske Fe-S protein (PfRieske) in P. falciparum resulted in loss of PfRieske protein, consistent with the earlier observation that mACP (PF3D7_1208300) knockdown causes secondary loss of PfRieske, confirming the pathway: mACP stabilizes Fe-S biogenesis → Fe-S clusters → Rieske protein → ETC complex III.\",\n      \"method\": \"Conditional knockdown of PfRieske with immunoblot; cited in context of previously established mACP-Rieske epistatic relationship\",\n      \"journal\": \"International journal of molecular sciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — mACP-specific finding is cited as prior work; this paper provides indirect epistatic support but does not directly experiment on mACP\",\n      \"pmids\": [\"39273187\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"P. falciparum mACP (PF3D7_1208300) is a divergent mitochondrial acyl carrier protein that lacks the canonical 4-phosphopantetheine prosthetic group and therefore has no fatty acid synthesis function; instead, it is essential for parasite survival by directly binding and stabilizing the Isd11-Nfs1 complex required for mitochondrial Fe-S cluster biogenesis, and its depletion causes secondary loss of the Rieske Fe-S protein in ETC complex III and dominant dysfunction of the mitochondrial electron transport chain.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"mACP (PF3D7_1208300) is a divergent mitochondrial acyl carrier protein in Plasmodium falciparum that has been repurposed away from fatty acid synthesis to serve an essential role in mitochondrial Fe-S cluster biogenesis [#0, #1]. Unlike canonical eukaryotic mitochondrial ACPs, mACP lacks the 4-phosphopantetheine (Ppant) prosthetic group, decoupling it from FASII activity, yet it still directly binds and stabilizes the Isd11-Nfs1 cysteine desulfurase complex that initiates Fe-S cluster assembly [#1, #2]. Conditional knockdown of mACP is lethal and causes secondary loss of Nfs1 and of the Rieske Fe-S protein of ETC complex III, producing a dominant defect in the mitochondrial electron transport chain that is transiently rescued by decyl-ubiquinone [#0, #1]. Beyond this Fe-S biogenesis and ETC-stabilization role, no additional mechanistic function of mACP has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"It was unknown whether the mitochondrial ACP of P. falciparum had an essential role independent of fatty acid synthesis; conditional knockdown established that mACP is essential and that its loss primarily disables the mitochondrial ETC.\",\n      \"evidence\": \"Ligand-dependent conditional knockdown with viability assay and chemical rescue by decyl-ubiquinone\",\n      \"pmids\": [\"34612205\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not identify the direct molecular target whose loss disables the ETC\", \"Transient nature of decyl-ubiquinone rescue not mechanistically resolved\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The molecular basis of mACP essentiality was unresolved; binding and knockdown studies showed mACP physically stabilizes the Isd11-Nfs1 Fe-S biogenesis complex and that its depletion causes loss of Nfs1 and the Rieske Fe-S protein, defining a Fe-S biogenesis-to-complex III pathway.\",\n      \"evidence\": \"Biochemical pulldown/binding studies plus conditional knockdown with immunoblot for Nfs1 and Rieske Fe-S protein\",\n      \"pmids\": [\"34612205\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of Ppant-independent Isd11-Nfs1 binding not resolved\", \"Whether mACP participates in other Fe-S client maturation steps unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Whether mACP retained the canonical ACP prosthetic group was unclear; biochemical characterization established that mACP lacks the 4-phosphopantetheine group, explaining its decoupling from FASII and its divergence from canonical mitochondrial ACPs.\",\n      \"evidence\": \"Sequence and biochemical characterization of the absence of the Ppant group\",\n      \"pmids\": [\"34612205\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Single-lab biochemical assignment\", \"Structural consequences of Ppant absence for the Isd11-Nfs1 interface not defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"mACP's subcellular assignment was tested indirectly when it served as an HA-tagged mitochondrial negative control in an apicoplast interactor screen, confirming its mitochondrial residence and that it does not co-purify with apicoplast proteins.\",\n      \"evidence\": \"Anti-HA immunoprecipitation with tandem mass spectrometry, using mACP as a negative control\",\n      \"pmids\": [\"39660822\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"mACP was not the subject of study, only a control\", \"No new mACP-specific interactors defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"The proposed mACP-to-Rieske epistatic pathway gained indirect support when conditional depletion of the Rieske Fe-S protein reproduced the loss of PfRieske consistent with the pathway placing mACP upstream of complex III Fe-S maturation.\",\n      \"evidence\": \"Conditional knockdown of PfRieske with immunoblot, interpreted in the context of prior mACP work\",\n      \"pmids\": [\"39273187\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No direct experimentation on mACP in this study\", \"Epistasis inferred from citation rather than co-perturbation\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How mACP mechanistically substitutes for the Ppant-dependent ACP contacts of canonical eukaryotes to stabilize Isd11-Nfs1, and whether it has any Fe-S client roles beyond the Rieske protein, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No structure of the mACP-Isd11-Nfs1 interface\", \"Full set of Fe-S clients downstream of mACP unknown\", \"Mechanism of ETC dominance upon mACP loss not fully defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0051537\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016226\", \"supporting_discovery_ids\": [1, 4]},\n      {\"term_id\": \"GO:0022900\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\n      \"Isd11-Nfs1 cysteine desulfurase complex (binding/stabilizing partner)\"\n    ],\n    \"partners\": [\n      \"Isd11\",\n      \"Nfs1\",\n      \"Rieske Fe-S protein (PfRieske, downstream-dependent)\"\n    ],\n    \"other_free_text\": [\n      \"Divergent mitochondrial ACP lacking the 4-phosphopantetheine prosthetic group, uncoupling it from FASII [#2].\",\n      \"Essential; conditional knockdown is lethal and transiently rescued by decyl-ubiquinone, indicating dominant ETC dysfunction [#0].\",\n      \"Knockdown causes secondary loss of Nfs1 and the complex III Rieske Fe-S protein [#1].\"\n    ]\n  }\n}\n```","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1208300","name":null,"product":"acyl carrier protein, mitochondrial","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0606800","name":null,"product":"acyl carrier protein, mitochondrial, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1308200","name":null,"product":"acyl carrier protein, mitochondrial, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"mACP","evaluation":null}