{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0A6B7","secondaryAccessions":["P39171","P76581","P76992","Q8XA86"],"uniProtkbId":"ISCS_ECOLI","entryAudit":{"firstPublicDate":"2005-06-07","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-06-07","entryVersion":162,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8663056"}],"value":"Cysteine desulfurase IscS"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663056"}],"value":"2.8.1.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8663056"}],"value":"NifS protein homolog"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10600118"}],"value":"ThiI transpersulfidase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16387657"}],"value":"TusA transpersulfidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"}],"value":"iscS"},"synonyms":[{"value":"nuvC"},{"value":"yfhO"},{"value":"yzzO"}],"orderedLocusNames":[{"value":"b2530"},{"value":"JW2514"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10544286"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781558"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781607"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10829016"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10908675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387657"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22203963"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663056"}],"value":"Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto 'Cys-456' of ThiI and onto 'Cys-19' of TusA in transpersulfidation reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43892"},{"database":"Rhea","id":"RHEA-COMP:14737"},{"database":"Rhea","id":"RHEA-COMP:14739"},{"database":"ChEBI","id":"CHEBI:29917"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:57972"},{"database":"ChEBI","id":"CHEBI:64428"}],"ecNumber":"2.8.1.7","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663056"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10600118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387657"}],"value":"Treatment with N-ethylmaleimide inhibits sulfur transfer. Activated by ThiI and TusA"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":2.7,"unit":"uM","substrate":"L-cysteine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"}],"value":"kcat is 8.5 min(-1)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"10544286"}],"value":"Cofactor biosynthesis; iron-sulfur cluster biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387657"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22203963"}],"value":"Homodimer. The homodimer interacts with IscU and TusA, other S acceptors. Each subunit of the IscS dimer contacts a IscU monomer"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"P27838","geneName":"cyaY","intActId":"EBI-9146621"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"P0A9R4","geneName":"fdx","intActId":"EBI-767037"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"P0ACD4","geneName":"iscU","intActId":"EBI-561646"},"numberOfExperiments":12,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"P0A890","geneName":"tusA","intActId":"EBI-561780"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"P52197","geneName":"rhdA","intActId":"EBI-7906952"},"numberOfExperiments":2,"organismDiffer":true},{"interactantOne":{"uniProtKBAccession":"P0A6B7","intActId":"EBI-550055"},"interactantTwo":{"uniProtKBAccession":"Q1R8K8","geneName":"yfhJ","intActId":"EBI-15582429"},"numberOfExperiments":2,"organismDiffer":true}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000305"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"}],"value":"The C-terminus (residues 376-404) is important for interaction with IscU"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10781607"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10908675"}],"value":"Cells lacking this gene lose sulfurtransferase activity and require thiamine and nicotinic acid for growth. Under aerobic conditions the deletion of IscS causes an auxotrophy for thiamine and nicotinic acid, whereas under anaerobic conditions, only nicotinic acid s required"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Cysteine desulfurase IscS","featureId":"PRO_0000150264"},{"type":"Active site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8663056"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"via persulfide group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135","note":"ligand shared with IscU"}},{"type":"Modified residue","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12860127"}]},{"type":"Mutagenesis","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Loss of cysteine desulfurization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10739946"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Normal cysteine desulfurase activity, decreased binding to IscU, decreased sulfur transfer to IscU, decreased Fe-S cluster assembly.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11577100"}],"alternativeSequence":{}},{"type":"Sequence conflict","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["D"]}},{"type":"Sequence conflict","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["F"]}},{"type":"Sequence conflict","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"AS","alternativeSequences":["NA"]}},{"type":"Sequence conflict","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["L"]}},{"type":"Sequence conflict","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"P","alternativeSequences":["M"]}},{"type":"Sequence conflict","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["I"]}},{"type":"Sequence conflict","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"SA","alternativeSequences":["YL"]}},{"type":"Sequence conflict","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"in Ref. 4; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["V"]}},{"type":"Beta strand","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Turn","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Beta strand","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]},{"type":"Helix","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1P3W"}]}],"keywords":[{"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"9205837","citationType":"journal article","authors":["Yamamoto Y.","Aiba H.","Baba T.","Hayashi K.","Inada T.","Isono K.","Itoh T.","Kimura S.","Kitagawa M.","Makino K.","Miki T.","Mitsuhashi N.","Mizobuchi K.","Mori H.","Nakade S.","Nakamura Y.","Nashimoto H.","Oshima T.","Oyama S.","Saito N.","Sampei G.","Satoh Y.","Sivasundaram S.","Tagami H.","Takahashi H.","Takeda J.","Takemoto K.","Uehara K.","Wada C.","Yamagata S.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"9205837"},{"database":"DOI","id":"10.1093/dnares/4.2.91"}],"title":"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features.","publicationDate":"1997","journal":"DNA Res.","firstPage":"91","lastPage":"113","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9278503","citationType":"journal article","authors":["Blattner F.R.","Plunkett G. III","Bloch C.A.","Perna N.T.","Burland V.","Riley M.","Collado-Vides J.","Glasner J.D.","Rode C.K.","Mayhew G.F.","Gregor J.","Davis N.W.","Kirkpatrick H.A.","Goeden M.A.","Rose D.J.","Mau B.","Shao Y."],"citationCrossReferences":[{"database":"PubMed","id":"9278503"},{"database":"DOI","id":"10.1126/science.277.5331.1453"}],"title":"The complete genome sequence of Escherichia coli K-12.","publicationDate":"1997","journal":"Science","firstPage":"1453","lastPage":"1462","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"16738553","citationType":"journal article","authors":["Hayashi K.","Morooka N.","Yamamoto Y.","Fujita K.","Isono K.","Choi S.","Ohtsubo E.","Baba T.","Wanner B.L.","Mori H.","Horiuchi T."],"citationCrossReferences":[{"database":"PubMed","id":"16738553"},{"database":"DOI","id":"10.1038/msb4100049"}],"title":"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.","publicationDate":"2006","journal":"Mol. Syst. Biol.","firstPage":"E1","lastPage":"E5","volume":"2"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"K12 / W3110 / ATCC 27325 / DSM 5911","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"8663056","citationType":"journal article","authors":["Flint D.H."],"citationCrossReferences":[{"database":"PubMed","id":"8663056"},{"database":"DOI","id":"10.1016/s0021-9258(18)48580-8"}],"title":"Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase.","publicationDate":"1996","journal":"J. Biol. Chem.","firstPage":"16068","lastPage":"16074","volume":"271"},"referencePositions":["PROTEIN SEQUENCE OF 1-38; 43-66; 117-127; 212-219; 241-257; 319-339 AND 382-391","FUNCTION","CATALYTIC ACTIVITY","ACTIVE SITE"]},{"referenceNumber":5,"citation":{"id":"10600118","citationType":"journal article","authors":["Kambampati R.","Lauhon C.T."],"citationCrossReferences":[{"database":"PubMed","id":"10600118"},{"database":"DOI","id":"10.1021/bi991119r"}],"title":"IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA.","publicationDate":"1999","journal":"Biochemistry","firstPage":"16561","lastPage":"16568","volume":"38"},"referencePositions":["PROTEIN SEQUENCE OF 1-16","FUNCTION","COFACTOR","ACTIVITY REGULATION"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":6,"citation":{"id":"9298646","citationType":"journal article","authors":["Link A.J.","Robison K.","Church G.M."],"citationCrossReferences":[{"database":"PubMed","id":"9298646"},{"database":"DOI","id":"10.1002/elps.1150180807"}],"title":"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.","publicationDate":"1997","journal":"Electrophoresis","firstPage":"1259","lastPage":"1313","volume":"18"},"referencePositions":["PROTEIN SEQUENCE OF 1-12"],"referenceComments":[{"value":"K12 / EMG2","type":"STRAIN"}]},{"referenceNumber":7,"citation":{"id":"10739946","citationType":"journal article","authors":["Mihara H.","Kurihara T.","Yoshimura T.","Esaki N."],"citationCrossReferences":[{"database":"PubMed","id":"10739946"},{"database":"DOI","id":"10.1093/oxfordjournals.jbchem.a022641"}],"title":"Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions.","publicationDate":"2000","journal":"J. Biochem.","firstPage":"559","lastPage":"567","volume":"127"},"referencePositions":["PROTEIN SEQUENCE OF 1-9","MUTAGENESIS OF CYS-328"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":8,"citation":{"id":"10544286","citationType":"journal article","authors":["Takahashi Y.","Nakamura M."],"citationCrossReferences":[{"database":"PubMed","id":"10544286"},{"database":"DOI","id":"10.1093/oxfordjournals.jbchem.a022535"}],"title":"Functional assignment of the ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 gene cluster involved in the assembly of Fe-S clusters in Escherichia coli.","publicationDate":"1999","journal":"J. Biochem.","firstPage":"917","lastPage":"926","volume":"126"},"referencePositions":["FUNCTION","PATHWAY"],"referenceComments":[{"value":"C41(DE3)","type":"STRAIN"}]},{"referenceNumber":9,"citation":{"id":"10781558","citationType":"journal article","authors":["Kiyasu T.","Asakura A.","Nagahashi Y.","Hoshino T."],"citationCrossReferences":[{"database":"PubMed","id":"10781558"},{"database":"DOI","id":"10.1128/jb.182.10.2879-2885.2000"}],"title":"Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli.","publicationDate":"2000","journal":"J. Bacteriol.","firstPage":"2879","lastPage":"2885","volume":"182"},"referencePositions":["FUNCTION"],"referenceComments":[{"value":"ATCC 33694 / HB101","type":"STRAIN"}]},{"referenceNumber":10,"citation":{"id":"10781607","citationType":"journal article","authors":["Lauhon C.T.","Kambampati R."],"citationCrossReferences":[{"database":"PubMed","id":"10781607"},{"database":"DOI","id":"10.1074/jbc.m002680200"}],"title":"The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamine, and NAD.","publicationDate":"2000","journal":"J. Biol. Chem.","firstPage":"20096","lastPage":"20103","volume":"275"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12 / MC1061 / ATCC 53338 / DSM 7140","type":"STRAIN"}]},{"referenceNumber":11,"citation":{"id":"10829016","citationType":"journal article","authors":["Lacourciere G.M.","Mihara H.","Kurihara T.","Esaki N.","Stadtman T.C."],"citationCrossReferences":[{"database":"PubMed","id":"10829016"},{"database":"DOI","id":"10.1074/jbc.m000926200"}],"title":"Escherichia coli NifS-like proteins provide selenium in the pathway for the biosynthesis of selenophosphate.","publicationDate":"2000","journal":"J. Biol. Chem.","firstPage":"23769","lastPage":"23773","volume":"275"},"referencePositions":["FUNCTION IN SELENIUM DELIVERY"],"referenceComments":[{"value":"MBO8","type":"STRAIN"}]},{"referenceNumber":12,"citation":{"id":"10908675","citationType":"journal article","authors":["Schwartz C.J.","Djaman O.","Imlay J.A.","Kiley P.J."],"citationCrossReferences":[{"database":"PubMed","id":"10908675"},{"database":"DOI","id":"10.1073/pnas.160261497"}],"title":"The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli.","publicationDate":"2000","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9009","lastPage":"9014","volume":"97"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE"],"referenceComments":[{"value":"K12 / MG1655 / ATCC 47076","type":"STRAIN"}]},{"referenceNumber":13,"citation":{"id":"11577100","citationType":"journal article","authors":["Urbina H.D.","Silberg J.J.","Hoff K.G.","Vickery L.E."],"citationCrossReferences":[{"database":"PubMed","id":"11577100"},{"database":"DOI","id":"10.1074/jbc.m106907200"}],"title":"Transfer of sulfur from IscS to IscU during Fe/S cluster assembly.","publicationDate":"2001","journal":"J. Biol. Chem.","firstPage":"44521","lastPage":"44526","volume":"276"},"referencePositions":["FUNCTION IN SULFUR TRANSFER","INTERACTION WITH ISCU","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","DOMAIN","MUTAGENESIS OF 376-SER--HIS-404"],"referenceComments":[{"value":"K12","type":"STRAIN"}]},{"referenceNumber":14,"citation":{"id":"16387657","citationType":"journal article","authors":["Ikeuchi Y.","Shigi N.","Kato J.","Nishimura A.","Suzuki T."],"citationCrossReferences":[{"database":"PubMed","id":"16387657"},{"database":"DOI","id":"10.1016/j.molcel.2005.11.001"}],"title":"Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions.","publicationDate":"2006","journal":"Mol. Cell","firstPage":"97","lastPage":"108","volume":"21"},"referencePositions":["FUNCTION","SUBUNIT","ACTIVITY REGULATION"]},{"referenceNumber":15,"citation":{"id":"22203963","citationType":"journal article","authors":["Kim J.H.","Tonelli M.","Markley J.L."],"citationCrossReferences":[{"database":"PubMed","id":"22203963"},{"database":"DOI","id":"10.1073/pnas.1114372109"}],"title":"Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase.","publicationDate":"2012","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"454","lastPage":"459","volume":"109"},"referencePositions":["FUNCTION","SUBUNIT"]},{"referenceNumber":16,"citation":{"id":"12860127","citationType":"journal article","authors":["Cupp-Vickery J.R.","Urbina H.","Vickery L.E."],"citationCrossReferences":[{"database":"PubMed","id":"12860127"},{"database":"DOI","id":"10.1016/s0022-2836(03)00690-9"}],"title":"Crystal structure of IscS, a cysteine desulfurase from Escherichia coli.","publicationDate":"2003","journal":"J. Mol. Biol.","firstPage":"1049","lastPage":"1059","volume":"330"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE","PYRIDOXAL PHOSPHATE AT LYS-206","COFACTOR","SUBUNIT","ACTIVE SITE"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U00096","properties":[{"key":"ProteinId","value":"AAT48142.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AP009048","properties":[{"key":"ProteinId","value":"BAA16424.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_001295373.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP009789.1"}]},{"database":"RefSeq","id":"YP_026169.1","properties":[{"key":"NucleotideSequenceId","value":"NC_000913.3"}]},{"database":"PDB","id":"1P3W","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A/B=1-404"}]},{"database":"PDBsum","id":"1P3W","properties":[{"key":"Description","value":"-"}]},{"database":"AlphaFoldDB","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"EMDB","id":"EMD-67634","properties":[{"key":"Description","value":"-"}]},{"database":"SASBDB","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"BioGRID","id":"4263511","properties":[{"key":"Interactions","value":"617"}]},{"database":"BioGRID","id":"851343","properties":[{"key":"Interactions","value":"3"}]},{"database":"ComplexPortal","id":"CPX-2136","properties":[{"key":"EntryName","value":"L-cysteine desulfurase complex"}]},{"database":"ComplexPortal","id":"CPX-2139","properties":[{"key":"EntryName","value":"iscS-tusA cysteine desulfurase complex"}]},{"database":"ComplexPortal","id":"CPX-2140","properties":[{"key":"EntryName","value":"iscS-thiI sulfurtransferase complex"}]},{"database":"ComplexPortal","id":"CPX-2141","properties":[{"key":"EntryName","value":"iscS-iscU iron-sulfur cluster assembly complex"}]},{"database":"DIP","id":"DIP-29109N","properties":[{"key":"Description","value":"-"}]},{"database":"FunCoup","id":"P0A6B7","properties":[{"key":"Number of interactors","value":"882"}]},{"database":"IntAct","id":"P0A6B7","properties":[{"key":"Interactions","value":"47"}]},{"database":"MINT","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"511145.b2530","properties":[{"key":"Description","value":"-"}]},{"database":"jPOST","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"511145-b2530","properties":[{"key":"Description","value":"-"}]},{"database":"EnsemblBacteria","id":"AAT48142","properties":[{"key":"ProteinId","value":"AAT48142"},{"key":"GeneId","value":"b2530"}]},{"database":"GeneID","id":"67175948","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"93774606","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"947004","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecj:JW2514","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"eco:b2530","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ecoc:C3026_14020","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1411691.4.peg.4204","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"EchoBASE","id":"EB2542","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1104","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"HOGENOM","id":"CLU_003433_0_2_6","properties":[{"key":"Description","value":"-"}]},{"database":"InParanoid","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"OMA","id":"KGLYWAR","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"OrthoDB","id":"9808002at2","properties":[{"key":"Description","value":"-"}]},{"database":"PhylomeDB","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"EcoCyc:G7325-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:G7325-MONOMER","properties":[{"key":"Description","value":"-"}]},{"database":"SABIO-RK","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00266","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000000625","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"AbasyAtlas","id":"P0A6B7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"18304323"}]},{"database":"GO","id":"GO:1990330","properties":[{"key":"GoTerm","value":"C:IscS-IscU complex"},{"key":"GoEvidenceType","value":"NAS:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"20404999"}]},{"database":"GO","id":"GO:1990329","properties":[{"key":"GoTerm","value":"C:IscS-TusA complex"},{"key":"GoEvidenceType","value":"IPI:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"16387657"}]},{"database":"GO","id":"GO:1990221","properties":[{"key":"GoTerm","value":"C:L-cysteine desulfurase complex"},{"key":"GoEvidenceType","value":"IPI:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"10753862"},{"evidenceCode":"ECO:0000353","source":"PubMed","id":"12860127"}]},{"database":"GO","id":"GO:1990228","properties":[{"key":"GoTerm","value":"C:sulfurtransferase complex"},{"key":"GoEvidenceType","value":"IPI:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000353","source":"PubMed","id":"10753862"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031071","properties":[{"key":"GoTerm","value":"F:cysteine desulfurase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10739946"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10600118"}]},{"database":"GO","id":"GO:0009000","properties":[{"key":"GoTerm","value":"F:selenocysteine lyase activity"},{"key":"GoEvidenceType","value":"IDA:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10739946"}]},{"database":"GO","id":"GO:0097163","properties":[{"key":"GoTerm","value":"F:sulfur carrier activity"},{"key":"GoEvidenceType","value":"EXP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10739946"}]},{"database":"GO","id":"GO:0044571","properties":[{"key":"GoTerm","value":"P:[2Fe-2S] cluster assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009589","properties":[{"key":"GoTerm","value":"P:detection of UV"},{"key":"GoEvidenceType","value":"NAS:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10753862"}]},{"database":"GO","id":"GO:0016226","properties":[{"key":"GoTerm","value":"P:iron-sulfur cluster assembly"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"10393315"}]},{"database":"GO","id":"GO:0019448","properties":[{"key":"GoTerm","value":"P:L-cysteine catabolic process"},{"key":"GoEvidenceType","value":"IDA:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10739946"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10753862"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"16387657"}]},{"database":"GO","id":"GO:0016261","properties":[{"key":"GoTerm","value":"P:L-selenocysteine catabolic process"},{"key":"GoEvidenceType","value":"IDA:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10739946"}]},{"database":"GO","id":"GO:0072348","properties":[{"key":"GoTerm","value":"P:sulfur compound transport"},{"key":"GoEvidenceType","value":"IDA:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"10739946"}]},{"database":"GO","id":"GO:0009228","properties":[{"key":"GoTerm","value":"P:thiamine biosynthetic process"},{"key":"GoEvidenceType","value":"NAS:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10753862"}]},{"database":"GO","id":"GO:0002937","properties":[{"key":"GoTerm","value":"P:tRNA 4-thiouridine biosynthesis"},{"key":"GoEvidenceType","value":"IMP:EcoCyc"}],"evidences":[{"evidenceCode":"ECO:0000315","source":"PubMed","id":"10781607"}]},{"database":"GO","id":"GO:0002143","properties":[{"key":"GoTerm","value":"P:tRNA wobble position uridine thiolation"},{"key":"GoEvidenceType","value":"IDA:ComplexPortal"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"16387657"}]},{"database":"DisProt","id":"DP03813","properties":[{"key":"Description","value":"-"}]},{"database":"FunFam","id":"3.40.640.10:FF:000003","properties":[{"key":"EntryName","value":"Cysteine desulfurase IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000002","properties":[{"key":"EntryName","value":"Cysteine desulfurase IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00331","properties":[{"key":"EntryName","value":"Cys_desulf_IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000192","properties":[{"key":"EntryName","value":"Aminotrans_V_dom"}]},{"database":"InterPro","id":"IPR020578","properties":[{"key":"EntryName","value":"Aminotrans_V_PyrdxlP_BS"}]},{"database":"InterPro","id":"IPR010240","properties":[{"key":"EntryName","value":"Cys_deSase_IscS"}]},{"database":"InterPro","id":"IPR016454","properties":[{"key":"EntryName","value":"Cysteine_dSase"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR02006","properties":[{"key":"EntryName","value":"IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002806","properties":[{"key":"EntryName","value":"PRK02948.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010611","properties":[{"key":"EntryName","value":"PRK14012.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11601:SF34","properties":[{"key":"EntryName","value":"CYSTEINE DESULFURASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11601","properties":[{"key":"EntryName","value":"CYSTEINE DESULFURYLASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00266","properties":[{"key":"EntryName","value":"Aminotran_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005572","properties":[{"key":"EntryName","value":"NifS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00595","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLPIYLDYSATTPVDPRVAEKMMQFMTMDGTFGNPASRSHRFGWQAEEAVDIARNQIADLVGADPREIVFTSGATESDNLAIKGAANFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLAPQRNGIIDLKELEAAMRDDTILVSIMHVNNEIGVVQDIAAIGEMCRARGIIYHVDATQSVGKLPIDLSQLKVDLMSFSGHKIYGPKGIGALYVRRKPRVRIEAQMHGGGHERGMRSGTLPVHQIVGMGEAYRIAKEEMATEMERLRGLRNRLWNGIKDIEEVYLNGDLEHGAPNILNVSFNYVEGESLIMALKDLAVSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYTIELVRKSIGRLRDLSPLWEMYKQGVDLNSIEWAHH","length":404,"molWeight":45090,"crc64":"1E4F2E6F9CD266B0","md5":"858F1FE35D5F51A75188C72882269FE8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"INTERACTION":6,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":6,"Modified residue":1,"Mutagenesis":2,"Sequence conflict":8,"Beta strand":11,"Turn":10,"Helix":17},"uniParcId":"UPI000003121D"}}