{"gene":"PF3D7_0206100","run_date":"2026-09-07T10:55:51","timeline":{"discoveries":[{"year":2013,"finding":"SufE (PF3D7_0206100) localizes exclusively to the apicoplast of P. falciparum, as established by subcellular localization experiments, and functions as the partner of SufS in sulfur acquisition for the Suf Fe-S cluster synthesis pathway.","method":"Subcellular localization (live imaging/fractionation) and complementation assay demonstrating SufS cysteine desulfurase activity","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiment and functional complementation assay in single lab, two orthogonal methods","pmids":["24086138"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"finding":"SufE (PF3D7_0206100) localizes exclusively to the apicoplast in P. falciparum, forms a complex with PfSufS detectable in vivo (Co-IP), and greatly enhances the cysteine desulfurase activity of PfSufS in vitro; structural modeling places conserved cysteine residues of the two proteins in proximity to allow sulfide transfer from the PLP-bound active site of PfSufS.","method":"Subcellular localization, in vivo Co-immunoprecipitation, in vitro cysteine desulfurase activity assay, and structural modeling","journal":"Antimicrobial agents and chemotherapy","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal/in vivo Co-IP combined with biochemical activity assay and localization, multiple orthogonal methods in a single rigorous study","pmids":["24709262"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"finding":"In P. berghei, targeted gene deletion of SufE (the ortholog of PF3D7_0206100) was refractory, demonstrating it is essential for asexual blood-stage survival in vivo; fluorescent tagging of endogenous SufE confirmed apicoplast localization.","method":"Targeted gene deletion (experimental genetics) and endogenous fluorescent tagging with localization imaging","journal":"PloS one","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean genetic KO attempt (refractory deletion) with direct localization, single lab, two methods","pmids":["24586983"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2019,"finding":"In P. vivax clinical isolates, SufE interacts in vitro with SufS to form a SufSE complex responsible for sulfur mobilization in the apicoplast; the mobilized sulfur then assembles on the scaffold protein PvSufA, demonstrating conservation of the SufSE sulfur-transfer mechanism across Plasmodium species.","method":"In vitro protein interaction assay and in vitro Fe-S cluster assembly assay using P. vivax clinical isolate proteins","journal":"Experimental parasitology","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — in vitro interaction and assembly assay, single lab, single study, clinical isolate material adds some variability","pmids":["30721667"],"is_preprint":false,"attribution":[{"species":"Plasmodium vivax","strain":""}]},{"year":2023,"finding":"Deletion of SufS in P. falciparum (using a chemical bypass) leads to disruption of the apicoplast organelle and loss of the organellar genome, a phenotype not shared by deletion of other Fe-S pathway components; this apicoplast maintenance role of SufS is driven by its provision of sulfur to MnmA (a tRNA-modifying enzyme localized to the apicoplast) rather than solely by its role in Fe-S biosynthesis. SufE's role is implied as part of the sulfur acquisition step upstream of this dual function, but the 2023 study primarily characterizes SufS's dual role rather than SufE independently.","method":"Conditional gene deletion (chemical bypass method), organelle and genome integrity assays, complementation with bacterial MnmA and cognate desulfurase","journal":"eLife","confidence":"Low","confidence_rationale":"Tier 2 / Weak — rigorous study of SufS dual function; SufE (PF3D7_0206100) itself is not independently characterized beyond its established partnership with SufS in sulfur acquisition","pmids":["37166116"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"SufE (PF3D7_0206100) is an apicoplast-localized cysteine desulfuration protein in Plasmodium falciparum (and its orthologs in P. berghei and P. vivax) that forms an essential complex with the cysteine desulfurase SufS, greatly enhancing SufS enzymatic activity and enabling sulfide transfer for the first step of apicoplast Fe-S cluster biosynthesis via the SUF pathway; it is essential for parasite blood-stage survival, as gene deletion is refractory in P. berghei."},"narrative":{"mechanistic_narrative":"SufE (PF3D7_0206100) is an apicoplast-localized cysteine desulfuration protein of Plasmodium falciparum that serves as the sulfur-transfer partner in the first, sulfur-acquisition step of the apicoplast SUF pathway for Fe-S cluster biosynthesis [PMID:24086138, PMID:24709262]. It localizes exclusively to the apicoplast and forms an in vivo complex with the cysteine desulfurase SufS (PfSufS), greatly enhancing SufS enzymatic activity; structural modeling positions conserved cysteine residues of the two proteins in proximity, consistent with sulfide transfer from the PLP-bound active site of SufS to SufE [PMID:24709262]. This SufSE partnership is conserved across Plasmodium species: in P. vivax clinical-isolate proteins, the SufSE complex mobilizes sulfur that is subsequently assembled onto the scaffold protein PvSufA in vitro [PMID:30721667]. The pathway is essential for blood-stage survival, as targeted deletion of the SufE ortholog in P. berghei was refractory [PMID:24586983]. Beyond its established partnership with SufS in the sulfur-acquisition step, SufE has not been independently characterized in the available corpus; the downstream apicoplast-maintenance functions of sulfur mobilization (Fe-S assembly and MnmA-dependent tRNA modification) have been attributed to SufS rather than to SufE itself [PMID:37166116].","teleology":[{"year":2013,"claim":"Establishing where SufE acts and whether it participates in sulfur acquisition answered whether the parasite's SUF pathway operates in the apicoplast and identified SufE as SufS's functional partner.","evidence":"Subcellular localization and complementation assay demonstrating SufS cysteine desulfurase activity in P. falciparum","pmids":["24086138"],"confidence":"Medium","gaps":["Did not resolve the biochemical mechanism of sulfur transfer between SufE and SufS","No direct measurement of SufE's effect on SufS kinetics"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"claim":"Whether SufE physically partners SufS in vivo and how it contributes catalytically was resolved by showing complex formation and enhancement of desulfurase activity, defining SufE as an activator of sulfide mobilization.","evidence":"In vivo Co-immunoprecipitation, in vitro cysteine desulfurase activity assay, localization, and structural modeling in P. falciparum","pmids":["24709262"],"confidence":"High","gaps":["Structural model of the cysteine-to-cysteine sulfide relay not experimentally confirmed by a solved structure","Stoichiometry and dynamics of the SufSE complex not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2014,"claim":"Whether SufE is genetically essential was addressed in P. berghei, where refractory deletion established the sulfur-acquisition step as indispensable for asexual blood-stage growth.","evidence":"Targeted gene deletion and endogenous fluorescent tagging in P. berghei","pmids":["24586983"],"confidence":"Medium","gaps":["Refractory deletion does not distinguish which downstream function (Fe-S assembly vs other) drives essentiality","No conditional knockdown to define the terminal phenotype of SufE loss"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2019,"claim":"Whether the SufSE sulfur-transfer mechanism is conserved and feeds a downstream scaffold was tested in P. vivax, showing the SufSE complex mobilizes sulfur that assembles onto SufA.","evidence":"In vitro protein interaction and Fe-S cluster assembly assays using P. vivax clinical-isolate proteins","pmids":["30721667"],"confidence":"Medium","gaps":["In vitro reconstitution using clinical-isolate material adds variability and does not establish in vivo flux","SufE's specific contribution to SufA loading not isolated from SufS"],"attribution":[{"species":"Plasmodium vivax","strain":""}]},{"year":2023,"claim":"Whether the sulfur-acquisition step has functions beyond Fe-S biosynthesis was examined via SufS, revealing a dual role including MnmA-dependent tRNA modification for apicoplast maintenance, with SufE implied as the upstream partner but not independently dissected.","evidence":"Conditional deletion (chemical bypass), organelle and genome integrity assays, and complementation with bacterial MnmA and cognate desulfurase in P. falciparum","pmids":["37166116"],"confidence":"Low","gaps":["SufE (PF3D7_0206100) itself was not independently characterized in this study beyond its partnership with SufS","Whether SufE contributes specifically to the MnmA-directed sulfur branch is untested","No SufE-specific conditional deletion phenotype reported"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"The independent, SufE-specific determinants of sulfur-transfer selectivity — whether SufE channels sulfur preferentially toward Fe-S assembly versus MnmA-dependent tRNA thiolation — remain unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No SufE conditional knockdown defining the terminal phenotype","No solved SufSE structure confirming the modeled sulfide relay","SufE's partitioning between downstream sulfur-acceptor pathways unmeasured"],"attribution":[]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["SufSE cysteine desulfurase / sulfur-transfer complex (SufE + SufS)"],"partners":["SUFS (CYSTEINE DESULFURASE, DIRECT PARTNER ENHANCING ITS ACTIVITY)","SUFA (FE-S SCAFFOLD PROTEIN; DOWNSTREAM SULFUR ACCEPTOR, SHOWN IN P. VIVAX)"],"other_free_text":["SufE is essential for asexual blood-stage survival; deletion of its ortholog in P. berghei was refractory.","The SufSE sulfur-transfer mechanism is conserved across P. falciparum, P. berghei, and P. vivax.","Downstream apicoplast-maintenance roles (Fe-S assembly and MnmA-dependent tRNA modification) have been characterized for the partner SufS rather than for SufE itself."]}},"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":["SufE"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24709262","id":"PMC_24709262","title":"Sulfur mobilization for Fe-S cluster assembly by the essential SUF pathway in the Plasmodium falciparum apicoplast and its inhibition.","date":"2014","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/24709262","citation_count":40,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PfSufE"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"24586983","id":"PMC_24586983","title":"Identification of vital and dispensable sulfur utilization factors in the Plasmodium apicoplast.","date":"2014","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24586983","citation_count":27,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"37166116","id":"PMC_37166116","title":"The Plasmodium falciparum apicoplast cysteine desulfurase provides sulfur for both iron-sulfur cluster assembly and tRNA modification.","date":"2023","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/37166116","citation_count":13,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30721667","id":"PMC_30721667","title":"Functional analysis of iron-sulfur cluster biogenesis (SUF pathway) from Plasmodium vivax clinical isolates.","date":"2019","source":"Experimental parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/30721667","citation_count":7,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["SufE"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":5400,"output_tokens":1488,"usd":0.01926,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6470,"output_tokens":2714,"usd":0.0501,"stage2_stop_reason":"end_turn"},"total_usd":0.06936,"stage1_batch_id":"msgbatch_01DbiymDmubkPpYvdbAu5a7V","stage2_batch_id":"msgbatch_012TbrWvMRH129T7PQ4SmvrJ","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"SufE (PF3D7_0206100) localizes exclusively to the apicoplast of P. falciparum, as established by subcellular localization experiments, and functions as the partner of SufS in sulfur acquisition for the Suf Fe-S cluster synthesis pathway.\",\n      \"method\": \"Subcellular localization (live imaging/fractionation) and complementation assay demonstrating SufS cysteine desulfurase activity\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiment and functional complementation assay in single lab, two orthogonal methods\",\n      \"pmids\": [\"24086138\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"SufE (PF3D7_0206100) localizes exclusively to the apicoplast in P. falciparum, forms a complex with PfSufS detectable in vivo (Co-IP), and greatly enhances the cysteine desulfurase activity of PfSufS in vitro; structural modeling places conserved cysteine residues of the two proteins in proximity to allow sulfide transfer from the PLP-bound active site of PfSufS.\",\n      \"method\": \"Subcellular localization, in vivo Co-immunoprecipitation, in vitro cysteine desulfurase activity assay, and structural modeling\",\n      \"journal\": \"Antimicrobial agents and chemotherapy\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal/in vivo Co-IP combined with biochemical activity assay and localization, multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"24709262\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"In P. berghei, targeted gene deletion of SufE (the ortholog of PF3D7_0206100) was refractory, demonstrating it is essential for asexual blood-stage survival in vivo; fluorescent tagging of endogenous SufE confirmed apicoplast localization.\",\n      \"method\": \"Targeted gene deletion (experimental genetics) and endogenous fluorescent tagging with localization imaging\",\n      \"journal\": \"PloS one\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic KO attempt (refractory deletion) with direct localization, single lab, two methods\",\n      \"pmids\": [\"24586983\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"In P. vivax clinical isolates, SufE interacts in vitro with SufS to form a SufSE complex responsible for sulfur mobilization in the apicoplast; the mobilized sulfur then assembles on the scaffold protein PvSufA, demonstrating conservation of the SufSE sulfur-transfer mechanism across Plasmodium species.\",\n      \"method\": \"In vitro protein interaction assay and in vitro Fe-S cluster assembly assay using P. vivax clinical isolate proteins\",\n      \"journal\": \"Experimental parasitology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — in vitro interaction and assembly assay, single lab, single study, clinical isolate material adds some variability\",\n      \"pmids\": [\"30721667\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium vivax\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Deletion of SufS in P. falciparum (using a chemical bypass) leads to disruption of the apicoplast organelle and loss of the organellar genome, a phenotype not shared by deletion of other Fe-S pathway components; this apicoplast maintenance role of SufS is driven by its provision of sulfur to MnmA (a tRNA-modifying enzyme localized to the apicoplast) rather than solely by its role in Fe-S biosynthesis. SufE's role is implied as part of the sulfur acquisition step upstream of this dual function, but the 2023 study primarily characterizes SufS's dual role rather than SufE independently.\",\n      \"method\": \"Conditional gene deletion (chemical bypass method), organelle and genome integrity assays, complementation with bacterial MnmA and cognate desulfurase\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 2 / Weak — rigorous study of SufS dual function; SufE (PF3D7_0206100) itself is not independently characterized beyond its established partnership with SufS in sulfur acquisition\",\n      \"pmids\": [\"37166116\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"SufE (PF3D7_0206100) is an apicoplast-localized cysteine desulfuration protein in Plasmodium falciparum (and its orthologs in P. berghei and P. vivax) that forms an essential complex with the cysteine desulfurase SufS, greatly enhancing SufS enzymatic activity and enabling sulfide transfer for the first step of apicoplast Fe-S cluster biosynthesis via the SUF pathway; it is essential for parasite blood-stage survival, as gene deletion is refractory in P. berghei.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"SufE (PF3D7_0206100) is an apicoplast-localized cysteine desulfuration protein of Plasmodium falciparum that serves as the sulfur-transfer partner in the first, sulfur-acquisition step of the apicoplast SUF pathway for Fe-S cluster biosynthesis [#0, #1]. It localizes exclusively to the apicoplast and forms an in vivo complex with the cysteine desulfurase SufS (PfSufS), greatly enhancing SufS enzymatic activity; structural modeling positions conserved cysteine residues of the two proteins in proximity, consistent with sulfide transfer from the PLP-bound active site of SufS to SufE [#1]. This SufSE partnership is conserved across Plasmodium species: in P. vivax clinical-isolate proteins, the SufSE complex mobilizes sulfur that is subsequently assembled onto the scaffold protein PvSufA in vitro [#3]. The pathway is essential for blood-stage survival, as targeted deletion of the SufE ortholog in P. berghei was refractory [#2]. Beyond its established partnership with SufS in the sulfur-acquisition step, SufE has not been independently characterized in the available corpus; the downstream apicoplast-maintenance functions of sulfur mobilization (Fe-S assembly and MnmA-dependent tRNA modification) have been attributed to SufS rather than to SufE itself [#4].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Establishing where SufE acts and whether it participates in sulfur acquisition answered whether the parasite's SUF pathway operates in the apicoplast and identified SufE as SufS's functional partner.\",\n      \"evidence\": \"Subcellular localization and complementation assay demonstrating SufS cysteine desulfurase activity in P. falciparum\",\n      \"pmids\": [\"24086138\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Did not resolve the biochemical mechanism of sulfur transfer between SufE and SufS\",\n        \"No direct measurement of SufE's effect on SufS kinetics\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether SufE physically partners SufS in vivo and how it contributes catalytically was resolved by showing complex formation and enhancement of desulfurase activity, defining SufE as an activator of sulfide mobilization.\",\n      \"evidence\": \"In vivo Co-immunoprecipitation, in vitro cysteine desulfurase activity assay, localization, and structural modeling in P. falciparum\",\n      \"pmids\": [\"24709262\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural model of the cysteine-to-cysteine sulfide relay not experimentally confirmed by a solved structure\",\n        \"Stoichiometry and dynamics of the SufSE complex not defined\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether SufE is genetically essential was addressed in P. berghei, where refractory deletion established the sulfur-acquisition step as indispensable for asexual blood-stage growth.\",\n      \"evidence\": \"Targeted gene deletion and endogenous fluorescent tagging in P. berghei\",\n      \"pmids\": [\"24586983\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Refractory deletion does not distinguish which downstream function (Fe-S assembly vs other) drives essentiality\",\n        \"No conditional knockdown to define the terminal phenotype of SufE loss\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Whether the SufSE sulfur-transfer mechanism is conserved and feeds a downstream scaffold was tested in P. vivax, showing the SufSE complex mobilizes sulfur that assembles onto SufA.\",\n      \"evidence\": \"In vitro protein interaction and Fe-S cluster assembly assays using P. vivax clinical-isolate proteins\",\n      \"pmids\": [\"30721667\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"In vitro reconstitution using clinical-isolate material adds variability and does not establish in vivo flux\",\n        \"SufE's specific contribution to SufA loading not isolated from SufS\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium vivax\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Whether the sulfur-acquisition step has functions beyond Fe-S biosynthesis was examined via SufS, revealing a dual role including MnmA-dependent tRNA modification for apicoplast maintenance, with SufE implied as the upstream partner but not independently dissected.\",\n      \"evidence\": \"Conditional deletion (chemical bypass), organelle and genome integrity assays, and complementation with bacterial MnmA and cognate desulfurase in P. falciparum\",\n      \"pmids\": [\"37166116\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"SufE (PF3D7_0206100) itself was not independently characterized in this study beyond its partnership with SufS\",\n        \"Whether SufE contributes specifically to the MnmA-directed sulfur branch is untested\",\n        \"No SufE-specific conditional deletion phenotype reported\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The independent, SufE-specific determinants of sulfur-transfer selectivity — whether SufE channels sulfur preferentially toward Fe-S assembly versus MnmA-dependent tRNA thiolation — remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No SufE conditional knockdown defining the terminal phenotype\",\n        \"No solved SufSE structure confirming the modeled sulfide relay\",\n        \"SufE's partitioning between downstream sulfur-acceptor pathways unmeasured\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0044540\", \"supporting_discovery_ids\": [0, 1, 3]},\n      {\"term_id\": \"GO:0097163\", \"supporting_discovery_ids\": [1, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020011\", \"supporting_discovery_ids\": [0, 1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0016226\", \"supporting_discovery_ids\": [0, 1, 3]}\n    ],\n    \"complexes\": [\n      \"SufSE cysteine desulfurase / sulfur-transfer complex (SufE + SufS)\"\n    ],\n    \"partners\": [\n      \"SufS (cysteine desulfurase, direct partner enhancing its activity)\",\n      \"SufA (Fe-S scaffold protein; downstream sulfur acceptor, shown in P. vivax)\"\n    ],\n    \"other_free_text\": [\n      \"SufE is essential for asexual blood-stage survival; deletion of its ortholog in P. berghei was refractory.\",\n      \"The SufSE sulfur-transfer mechanism is conserved across P. falciparum, P. berghei, and P. vivax.\",\n      \"Downstream apicoplast-maintenance roles (Fe-S assembly and MnmA-dependent tRNA modification) have been characterized for the partner SufS rather than for SufE itself.\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0206100","name":null,"product":"cysteine desulfuration protein SufE","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0303800","name":null,"product":"cysteine desulfuration protein SufE","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0414800","name":null,"product":"cysteine desulfuration protein SufE, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"SufE","evaluation":null}