{"gene":"PF3D7_0727200","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2013,"finding":"NFS1 (IscS, PF3D7_0727200) and its effector Isd11 localize exclusively to the mitochondrion in P. falciparum, as determined by subcellular fractionation/localization experiments, indicating that NFS1 cannot contribute to apicoplast Fe-S cluster synthesis (the apicoplast uses the Suf pathway instead).","method":"Subcellular localization experiments (complementation assay, compartment-specific analysis)","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment with functional inference, single lab, complementation assay used for SufS activity but localization is the primary finding for NFS1","pmids":["24086138"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"NFS1 (PF3D7_0727200) forms a cysteine desulfurase complex with PfIsd11 and PfIscU in the mitochondrion. The desulfurase-scaffold complex assembles around a PfIscS (NFS1) tetramer rather than the canonical dimer seen in bacteria, yeast, and humans, resulting in a symmetric hetero-hexamer of composition 2×(2PfIscS–2PfIsd11–2PfIscU).","method":"Biochemical complex reconstitution, small angle X-ray scattering (SAXS), spectral studies, confirmed mitochondrial targeting","journal":"Molecular microbiology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — SAXS structural analysis combined with biochemical reconstitution and spectroscopy in a single focused study on PfIscS (NFS1)","pmids":["34032321"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"NFS1 (PF3D7_0727200) functions as cysteine desulfurase within the mitochondrial ISC pathway; PfIscU in complex with NFS1–PfIsd11 can directly assemble [4Fe-4S] clusters without prior [2Fe-2S] formation, and PfIscU transfers [4Fe-4S] directly to apo-aconitase B, bypassing the intermediary conversion step seen in other organisms.","method":"In vitro Fe-S cluster assembly assay, cluster transfer assay to apo-aconitase B","journal":"Molecular microbiology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in vitro enzymatic reconstitution with defined substrates and direct transfer assay, single lab with multiple orthogonal methods","pmids":["34032321"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"finding":"Plasmodium falciparum mitochondrial acyl carrier protein (mACP) physically binds and stabilizes the Isd11–NFS1 (PF3D7_0727200) complex required for 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 protein and loss of the Rieske Fe-S protein in ETC complex III.","method":"Biochemical binding studies (co-purification), ligand-dependent knockdown of mACP with proteomic readout (loss of Nfs1 and Rieske protein)","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal biochemical binding assay plus genetic knockdown with defined molecular phenotype (loss of NFS1 protein and downstream Fe-S protein), single lab with two orthogonal methods","pmids":["34612205"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"NFS1 (PF3D7_0727200) is the mitochondrial cysteine desulfurase of P. falciparum that forms the core of the ISC Fe-S cluster biosynthesis machinery: it assembles as an unusual tetramer with Isd11 and the scaffold protein IscU into a symmetric hetero-hexamer, directly synthesises [4Fe-4S] clusters without a [2Fe-2S] intermediate, and its stability depends on physical interaction with the divergent mitochondrial acyl carrier protein (mACP) in a phosphopantetheine-independent manner, linking mACP to mitochondrial Fe-S biogenesis and electron transport chain integrity."},"narrative":{"mechanistic_narrative":"NFS1 (PF3D7_0727200) is the mitochondrial cysteine desulfurase that constitutes the catalytic core of the iron-sulfur cluster (ISC) biosynthesis machinery in Plasmodium falciparum, localizing exclusively to the mitochondrion and therefore not contributing to apicoplast Fe-S cluster synthesis, which relies on the separate Suf pathway [PMID:24086138]. NFS1 assembles with the effector protein PfIsd11 and the scaffold PfIscU into an unusual symmetric hetero-hexamer built around an NFS1 tetramer (2×(2PfIscS–2PfIsd11–2PfIscU)), in contrast to the canonical dimeric desulfurase seen in bacteria, yeast, and humans [PMID:34032321]. Within this complex NFS1 supplies sulfur for de novo Fe-S cluster assembly, and PfIscU directly generates [4Fe-4S] clusters and transfers them to apo-aconitase B without passing through a [2Fe-2S] intermediate, bypassing a conversion step required in other organisms [PMID:34032321]. The stability of the NFS1–Isd11 complex depends on physical interaction with the divergent mitochondrial acyl carrier protein (mACP), which binds and stabilizes NFS1 despite lacking the 4-phosphopantetheine group that mediates this interaction elsewhere; mACP knockdown depletes NFS1 protein and the Rieske Fe-S subunit of electron transport chain complex III, coupling NFS1-dependent Fe-S biogenesis to mitochondrial respiratory integrity [PMID:34612205].","teleology":[{"year":2013,"claim":"Establishing where NFS1 acts was the first step in defining its pathway role, since Plasmodium compartmentalizes Fe-S synthesis between mitochondrion and apicoplast; localizing NFS1 to the mitochondrion assigned it exclusively to the ISC pathway.","evidence":"subcellular localization/complementation experiments in P. falciparum","pmids":["24086138"],"confidence":"Medium","gaps":["Does not establish the catalytic activity or complex composition of NFS1","Does not identify downstream Fe-S recipient proteins"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"The architecture of the desulfurase machine was unknown; reconstitution and SAXS revealed that NFS1 assembles into a tetramer-based hetero-hexamer with Isd11 and IscU, distinguishing the parasite complex from the canonical dimeric form.","evidence":"biochemical complex reconstitution, SAXS, and spectral studies in P. falciparum","pmids":["34032321"],"confidence":"High","gaps":["No atomic-resolution structure of the hexamer","Functional consequence of the tetrameric versus dimeric arrangement not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"Whether the parasite follows the canonical stepwise Fe-S assembly route was open; in vitro assays showed the NFS1-containing complex enables direct [4Fe-4S] assembly and transfer to apo-aconitase B, bypassing a [2Fe-2S] intermediate.","evidence":"in vitro Fe-S cluster assembly and cluster transfer assays to apo-aconitase B","pmids":["34032321"],"confidence":"High","gaps":["Full range of physiological Fe-S recipient proteins not defined","Mechanism of direct [4Fe-4S] formation not resolved structurally"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"The determinants of NFS1 stability and its link to mitochondrial function were unclear; mACP was shown to bind and stabilize the Isd11–NFS1 complex in a phosphopantetheine-independent manner, with its depletion causing loss of NFS1 and the Rieske Fe-S protein.","evidence":"co-purification binding studies and ligand-dependent mACP knockdown with proteomic readout in P. falciparum","pmids":["34612205"],"confidence":"High","gaps":["Structural basis of Ppant-independent mACP binding to NFS1 not defined","Whether mACP regulates NFS1 catalytic activity beyond stabilizing its abundance is untested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The full spectrum of NFS1-dependent Fe-S apoprotein clients, the regulation of desulfurase activity in vivo, and a high-resolution structure of the tetrameric complex remain to be established.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No atomic structure of the NFS1 hetero-hexamer","In vivo essentiality and phenotype of NFS1 depletion not directly reported in this corpus","Complete Fe-S client repertoire beyond aconitase B and the Rieske protein unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Symmetric hetero-hexameric cysteine desulfurase complex 2x(2PfIscS-2PfIsd11-2PfIscU) [#1]","NFS1-Isd11 complex stabilized by mitochondrial acyl carrier protein (mACP) [#3]"],"partners":["PFISD11 [#0, #1, #3]","PFISCU (SCAFFOLD) [#1, #2]","MITOCHONDRIAL ACYL CARRIER PROTEIN (MACP) [#3]","APO-ACONITASE B (FE-S CLUSTER RECIPIENT) [#2]"],"other_free_text":["Assembles as an unusual tetramer rather than the canonical desulfurase dimer [#1]","Supports direct [4Fe-4S] cluster synthesis, bypassing a [2Fe-2S] intermediate [#2]","mACP stabilizes NFS1 despite lacking the 4-phosphopantetheine prosthetic group; mACP loss depletes NFS1 and the ETC complex III Rieske Fe-S protein [#3]","Restricted to the mitochondrial ISC pathway and does not act in apicoplast (Suf pathway) Fe-S synthesis [#0]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24086138","id":"PMC_24086138","title":"The suf iron-sulfur cluster synthesis pathway is required for apicoplast maintenance in malaria parasites.","date":"2013","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/24086138","citation_count":92,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"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":["NFS1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"34032321","id":"PMC_34032321","title":"[Fe-S] biogenesis and unusual assembly of the ISC scaffold complex in the Plasmodium falciparum mitochondrion.","date":"2021","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/34032321","citation_count":11,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37202779","id":"PMC_37202779","title":"Prevalence of mutations in the cysteine desulfurase IscS (Pfnfs1) gene in recurrent Plasmodium falciparum infections following artemether-lumefantrine (AL) and dihydroartemisinin-piperaquine (DP) treatment in Matayos, Western Kenya.","date":"2023","source":"Malaria journal","url":"https://pubmed.ncbi.nlm.nih.gov/37202779","citation_count":2,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["cysteine desulfurase IscS","PfNFS1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38520842","id":"PMC_38520842","title":"Absence of association between Pfnfs1 mutation and in vitro susceptibility to lumefantrine in Plasmodium falciparum.","date":"2024","source":"International journal for parasitology. Drugs and drug resistance","url":"https://pubmed.ncbi.nlm.nih.gov/38520842","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["cysteine desulfurase IscS","PfNFS1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5634,"output_tokens":1326,"usd":0.018396,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6248,"output_tokens":2579,"usd":0.047857,"stage2_stop_reason":"end_turn"},"total_usd":0.066253,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"NFS1 (IscS, PF3D7_0727200) and its effector Isd11 localize exclusively to the mitochondrion in P. falciparum, as determined by subcellular fractionation/localization experiments, indicating that NFS1 cannot contribute to apicoplast Fe-S cluster synthesis (the apicoplast uses the Suf pathway instead).\",\n      \"method\": \"Subcellular localization experiments (complementation assay, compartment-specific analysis)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment with functional inference, single lab, complementation assay used for SufS activity but localization is the primary finding for NFS1\",\n      \"pmids\": [\"24086138\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"NFS1 (PF3D7_0727200) forms a cysteine desulfurase complex with PfIsd11 and PfIscU in the mitochondrion. The desulfurase-scaffold complex assembles around a PfIscS (NFS1) tetramer rather than the canonical dimer seen in bacteria, yeast, and humans, resulting in a symmetric hetero-hexamer of composition 2×(2PfIscS–2PfIsd11–2PfIscU).\",\n      \"method\": \"Biochemical complex reconstitution, small angle X-ray scattering (SAXS), spectral studies, confirmed mitochondrial targeting\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — SAXS structural analysis combined with biochemical reconstitution and spectroscopy in a single focused study on PfIscS (NFS1)\",\n      \"pmids\": [\"34032321\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"NFS1 (PF3D7_0727200) functions as cysteine desulfurase within the mitochondrial ISC pathway; PfIscU in complex with NFS1–PfIsd11 can directly assemble [4Fe-4S] clusters without prior [2Fe-2S] formation, and PfIscU transfers [4Fe-4S] directly to apo-aconitase B, bypassing the intermediary conversion step seen in other organisms.\",\n      \"method\": \"In vitro Fe-S cluster assembly assay, cluster transfer assay to apo-aconitase B\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in vitro enzymatic reconstitution with defined substrates and direct transfer assay, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"34032321\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Plasmodium falciparum mitochondrial acyl carrier protein (mACP) physically binds and stabilizes the Isd11–NFS1 (PF3D7_0727200) complex required for 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 protein and loss of the Rieske Fe-S protein in ETC complex III.\",\n      \"method\": \"Biochemical binding studies (co-purification), ligand-dependent knockdown of mACP with proteomic readout (loss of Nfs1 and Rieske protein)\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal biochemical binding assay plus genetic knockdown with defined molecular phenotype (loss of NFS1 protein and downstream Fe-S protein), single lab with two orthogonal methods\",\n      \"pmids\": [\"34612205\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"NFS1 (PF3D7_0727200) is the mitochondrial cysteine desulfurase of P. falciparum that forms the core of the ISC Fe-S cluster biosynthesis machinery: it assembles as an unusual tetramer with Isd11 and the scaffold protein IscU into a symmetric hetero-hexamer, directly synthesises [4Fe-4S] clusters without a [2Fe-2S] intermediate, and its stability depends on physical interaction with the divergent mitochondrial acyl carrier protein (mACP) in a phosphopantetheine-independent manner, linking mACP to mitochondrial Fe-S biogenesis and electron transport chain integrity.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"NFS1 (PF3D7_0727200) is the mitochondrial cysteine desulfurase that constitutes the catalytic core of the iron-sulfur cluster (ISC) biosynthesis machinery in Plasmodium falciparum, localizing exclusively to the mitochondrion and therefore not contributing to apicoplast Fe-S cluster synthesis, which relies on the separate Suf pathway [#0]. NFS1 assembles with the effector protein PfIsd11 and the scaffold PfIscU into an unusual symmetric hetero-hexamer built around an NFS1 tetramer (2×(2PfIscS–2PfIsd11–2PfIscU)), in contrast to the canonical dimeric desulfurase seen in bacteria, yeast, and humans [#1]. Within this complex NFS1 supplies sulfur for de novo Fe-S cluster assembly, and PfIscU directly generates [4Fe-4S] clusters and transfers them to apo-aconitase B without passing through a [2Fe-2S] intermediate, bypassing a conversion step required in other organisms [#2]. The stability of the NFS1–Isd11 complex depends on physical interaction with the divergent mitochondrial acyl carrier protein (mACP), which binds and stabilizes NFS1 despite lacking the 4-phosphopantetheine group that mediates this interaction elsewhere; mACP knockdown depletes NFS1 protein and the Rieske Fe-S subunit of electron transport chain complex III, coupling NFS1-dependent Fe-S biogenesis to mitochondrial respiratory integrity [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Establishing where NFS1 acts was the first step in defining its pathway role, since Plasmodium compartmentalizes Fe-S synthesis between mitochondrion and apicoplast; localizing NFS1 to the mitochondrion assigned it exclusively to the ISC pathway.\",\n      \"evidence\": \"subcellular localization/complementation experiments in P. falciparum\",\n      \"pmids\": [\"24086138\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not establish the catalytic activity or complex composition of NFS1\", \"Does not identify downstream Fe-S recipient proteins\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The architecture of the desulfurase machine was unknown; reconstitution and SAXS revealed that NFS1 assembles into a tetramer-based hetero-hexamer with Isd11 and IscU, distinguishing the parasite complex from the canonical dimeric form.\",\n      \"evidence\": \"biochemical complex reconstitution, SAXS, and spectral studies in P. falciparum\",\n      \"pmids\": [\"34032321\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No atomic-resolution structure of the hexamer\", \"Functional consequence of the tetrameric versus dimeric arrangement not tested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Whether the parasite follows the canonical stepwise Fe-S assembly route was open; in vitro assays showed the NFS1-containing complex enables direct [4Fe-4S] assembly and transfer to apo-aconitase B, bypassing a [2Fe-2S] intermediate.\",\n      \"evidence\": \"in vitro Fe-S cluster assembly and cluster transfer assays to apo-aconitase B\",\n      \"pmids\": [\"34032321\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Full range of physiological Fe-S recipient proteins not defined\", \"Mechanism of direct [4Fe-4S] formation not resolved structurally\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The determinants of NFS1 stability and its link to mitochondrial function were unclear; mACP was shown to bind and stabilize the Isd11–NFS1 complex in a phosphopantetheine-independent manner, with its depletion causing loss of NFS1 and the Rieske Fe-S protein.\",\n      \"evidence\": \"co-purification binding studies and ligand-dependent mACP knockdown with proteomic readout in P. falciparum\",\n      \"pmids\": [\"34612205\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Structural basis of Ppant-independent mACP binding to NFS1 not defined\", \"Whether mACP regulates NFS1 catalytic activity beyond stabilizing its abundance is untested\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The full spectrum of NFS1-dependent Fe-S apoprotein clients, the regulation of desulfurase activity in vivo, and a high-resolution structure of the tetrameric complex remain to be established.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"No atomic structure of the NFS1 hetero-hexamer\", \"In vivo essentiality and phenotype of NFS1 depletion not directly reported in this corpus\", \"Complete Fe-S client repertoire beyond aconitase B and the Rieske protein unknown\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0031071\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"GO:0016226\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005739\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016226\", \"supporting_discovery_ids\": [1, 2, 3]}\n    ],\n    \"complexes\": [\n      \"Symmetric hetero-hexameric cysteine desulfurase complex 2x(2PfIscS-2PfIsd11-2PfIscU) [#1]\",\n      \"NFS1-Isd11 complex stabilized by mitochondrial acyl carrier protein (mACP) [#3]\"\n    ],\n    \"partners\": [\n      \"PfIsd11 [#0, #1, #3]\",\n      \"PfIscU (scaffold) [#1, #2]\",\n      \"mitochondrial acyl carrier protein (mACP) [#3]\",\n      \"apo-aconitase B (Fe-S cluster recipient) [#2]\"\n    ],\n    \"other_free_text\": [\n      \"Assembles as an unusual tetramer rather than the canonical desulfurase dimer [#1]\",\n      \"Supports direct [4Fe-4S] cluster synthesis, bypassing a [2Fe-2S] intermediate [#2]\",\n      \"mACP stabilizes NFS1 despite lacking the 4-phosphopantetheine prosthetic group; mACP loss depletes NFS1 and the ETC complex III Rieske Fe-S protein [#3]\",\n      \"Restricted to the mitochondrial ISC pathway and does not act in apicoplast (Suf pathway) Fe-S synthesis [#0]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0727200","name":null,"product":"cysteine desulfurase IscS","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0211300","name":null,"product":"cysteine desulfurase IscS, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0211800","name":null,"product":"cysteine desulfurase IscS, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"NFS1","evaluation":null}