{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A0F7RJ52","secondaryAccessions":["E9QVX2","E9QVX3","Q6HZY6","Q6KTW5","Q81RQ9"],"uniProtkbId":"ASBA_BACAN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":36,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bacillus anthracis","taxonId":1392,"lineage":["Bacteria","Bacillati","Bacillota","Bacilli","Caryophanales","Bacillaceae","Bacillus","Bacillus cereus group"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Spermidine-citrate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19259597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}],"value":"6.3.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Petrobactin biosynthesis protein AsbA"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"14756782"}],"value":"asbA"},"orderedLocusNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAT31100.1"}],"value":"GBAA_1981"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14756782"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16875672"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189355"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19259597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}],"value":"Involved in the biosynthesis of petrobactin, a catecholate siderophore that functions in both iron acquisition and virulence (PubMed:16875672, PubMed:17189355, PubMed:22408253). Catalyzes the ATP-dependent condensation of citric acid and spermidine to form N(8)-citryl-spermidine (PubMed:17579415, PubMed:19259597, PubMed:22408253). It can also catalyze the condensation of several di- and triamine analogs of spermidine with citric acid and the condensation of the citric acid analog tricarballylic acid with spermidine (PubMed:19259597). Required for growth in iron-depleted medium and for full virulence in a mouse model of infection (PubMed:14756782)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"spermidine + citrate + ATP = N(8)-citryl-spermidine + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:63808"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16947"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57834"},{"database":"ChEBI","id":"CHEBI:149586"},{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17579415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19259597"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":5.65,"unit":"mM","substrate":"citric acid","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}],"value":"kcat is 0.89 sec(-1)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189355"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22408253"}],"value":"Siderophore biosynthesis; petrobactin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14756782"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16875672"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17189355"}],"value":"Deletion of the gene leads to a decrease in siderophore production during iron-depleted growth and attenuates growth (PubMed:14756782). The deletion mutant cannot produce petrobactin on iron-depleted medium (PubMed:16875672, PubMed:17189355). Mutant produces the petrobactin precursor 3,4-dihydroxybenzoyl (3,4-DHB) and bacillibactin (PubMed:16875672). The deletion mutant is severely attenuated for growth in macrophages and virulence in mice (PubMed:14756782). In vitro analysis show that mutants grow to a very limited extent as vegetative cells in iron-depleted medium but are not able to outgrow from spores under the same culture conditions (PubMed:17189355)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19259597"}],"value":"The ability of the enzyme to catalyze condensation of citric acid with several di- and triamine analogs of spermidine suggests that it may be a versatile biocatalyst for the preparation of highly enantiomerically-enriched citrate derivatives via a novel type of desymmetrization process"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the IucA/IucC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":602,"modifier":"EXACT"}},"description":"Spermidine-citrate ligase","featureId":"PRO_0000450623"},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81RQ8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81RQ8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q81RQ8"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"18952800","citationType":"journal article","authors":["Ravel J.","Jiang L.","Stanley S.T.","Wilson M.R.","Decker R.S.","Read T.D.","Worsham P.","Keim P.S.","Salzberg S.L.","Fraser-Liggett C.M.","Rasko D.A."],"citationCrossReferences":[{"database":"PubMed","id":"18952800"},{"database":"DOI","id":"10.1128/jb.01347-08"}],"title":"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.","publicationDate":"2009","journal":"J. 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