{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G3ESV0","uniProtkbId":"FATB2_CUPVI","entryAudit":{"firstPublicDate":"2020-06-17","lastAnnotationUpdateDate":"2025-04-09","lastSequenceUpdateDate":"2011-11-16","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Acyl-[acyl-carrier-protein] hydrolase FATB2, chloroplastic"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"CvFatB2"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"value":"3.1.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Myristoyl-[acyl-carrier-protein] thioesterase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Palmitoyl-[acyl-carrier-protein] thioesterase"}}],"flag":"Fragment,Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"FATB2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Plays an essential role in chain termination during de novo fatty acid synthesis (Probable). Possesses thioesterase activity for medium chain acyl-ACPs. Substrate preference is 14:0 > 16:0 > 16:1 (PubMed:21831316, PubMed:29491418, PubMed:30409825)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tetradecanoyl-[ACP] + H2O = tetradecanoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30123"},{"database":"Rhea","id":"RHEA-COMP:9648"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30807"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78477"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30124"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexadecanoyl-[ACP] + H2O = hexadecanoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41932"},{"database":"Rhea","id":"RHEA-COMP:9652"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:7896"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78483"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:41933"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the acyl-ACP thioesterase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"OUTSIDE"},"end":{"value":46,"modifier":"EXACT"}},"description":"Chloroplast","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Acyl-[acyl-carrier-protein] hydrolase FATB2, chloroplastic","featureId":"PRO_0000450102"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Mutagenesis","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"Loss of thioesterase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A","E","N"]}},{"type":"Mutagenesis","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"Loss of thioesterase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"Loss of thioesterase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"Loss of thioesterase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A","D","Q"]}},{"type":"Mutagenesis","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Decreases thioesterase activity 2-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Increases thioesterase activity 2-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["S"]}},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"21831316","citationType":"journal article","authors":["Jing F.","Cantu D.C.","Tvaruzkova J.","Chipman J.P.","Nikolau B.J.","Yandeau-Nelson M.D.","Reilly P.J."],"citationCrossReferences":[{"database":"PubMed","id":"21831316"},{"database":"DOI","id":"10.1186/1471-2091-12-44"}],"title":"Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity.","publicationDate":"2011","journal":"BMC Biochem.","firstPage":"44","lastPage":"44","volume":"12"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","FUNCTION","CATALYTIC ACTIVITY"]},{"referenceNumber":2,"citation":{"id":"29491418","citationType":"journal article","authors":["Jing F.","Zhao L.","Yandeau-Nelson M.D.","Nikolau B.J."],"citationCrossReferences":[{"database":"PubMed","id":"29491418"},{"database":"DOI","id":"10.1038/s41467-018-03310-z"}],"title":"Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase.","publicationDate":"2018","journal":"Nat. Commun.","firstPage":"860","lastPage":"860","volume":"9"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"]},{"referenceNumber":3,"citation":{"id":"30409825","citationType":"journal article","authors":["Jing F.","Yandeau-Nelson M.D.","Nikolau B.J."],"citationCrossReferences":[{"database":"PubMed","id":"30409825"},{"database":"DOI","id":"10.1042/bcj20180470"}],"title":"Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase.","publicationDate":"2018","journal":"Biochem. J.","firstPage":"3861","lastPage":"3873","volume":"475"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF ASP-309; ASN-311; HIS-313; GLU-347 AND CYS-348"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JF338907","properties":[{"key":"ProteinId","value":"AEM72523.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"G3ESV0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G3ESV0","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.1.2.14","properties":[{"key":"OrganismId","value":"16463"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000036","properties":[{"key":"GoTerm","value":"F:acyl carrier activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00586","properties":[{"key":"EntryName","value":"4HBT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000014","properties":[{"key":"EntryName","value":"Acyl-[acyl-carrier-protein] hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021113","properties":[{"key":"EntryName","value":"Acyl-ACP-thioesterase_N"}]},{"database":"InterPro","id":"IPR049427","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"}]},{"database":"InterPro","id":"IPR002864","properties":[{"key":"EntryName","value":"Acyl-ACP_thioesterase_NHD"}]},{"database":"InterPro","id":"IPR045023","properties":[{"key":"EntryName","value":"FATA/B"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"PANTHER","id":"PTHR31727","properties":[{"key":"EntryName","value":"OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31727:SF2","properties":[{"key":"EntryName","value":"PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01643","properties":[{"key":"EntryName","value":"Acyl-ACP_TE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20791","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12590","properties":[{"key":"EntryName","value":"Acyl-thio_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"TAASSAFFPVPSADTSSRPGKLGNGPSSFSPLKPKSIPNGGLQVKASASAPPKINGSSVGLKSGGLKTHDDAPSAPPPRTFINQLPDWSMLLAAITTAFLAAEKQWMMLDRKPKRLDMLEDPFGLGRVVQDGLVFRQNFSIRSYEIGADRTASIETVMNHLQETALNHVKTAGLSNDGFGRTPEMYKRDLIWVVAKMQVMVNRYPTWGDTVEVNTWVAKSGKNGMRRDWLISDCNTGEILTRASSVWVMMNQKTRKLSKIPDEVRREIEPHFVDSAPVIEDDDRKLPKLDEKSADSIRKGLTPRWNDLDVNQHVNNAKYIGWILESTPPEVLETQELCSLTLEYRRECGRESVLESLTAVDPSGEGYGSQFQHLLRLEDGGEIVKGRTEWRPKNAGINGVVPSEESSPGDYS","length":412,"molWeight":45564,"crc64":"EDECD381C92F981F","md5":"4F82DC4A8451A145C6B7569D2B97FD4C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transit peptide":1,"Chain":1,"Region":1,"Compositional bias":2,"Active site":3,"Mutagenesis":6,"Non-terminal residue":1},"uniParcId":"UPI0002290327"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G3ESU9","uniProtkbId":"FATB1_CUPVI","entryAudit":{"firstPublicDate":"2020-06-17","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"2011-11-16","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Acyl-[acyl-carrier-protein] hydrolase FATB1, chloroplastic"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"CvFatB1"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"value":"3.1.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Decanoyl-[acyl-carrier-protein] thioesterase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Octanoyl-[acyl-carrier-protein] thioesterase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"FATB1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Plays an essential role in chain termination during de novo fatty acid synthesis (Probable). Possesses thioesterase activity for short chain acyl-ACPs. Substrate preference is 8:0 > 10:0 (PubMed:21831316, PubMed:29491418, PubMed:30409825)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octanoyl-[ACP] + H2O = octanoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30131"},{"database":"Rhea","id":"RHEA-COMP:9636"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:25646"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78463"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30132"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-[ACP] + H2O = decanoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30115"},{"database":"Rhea","id":"RHEA-COMP:9640"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:27689"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78468"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30116"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29491418"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the acyl-ACP thioesterase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Chloroplast","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Acyl-[acyl-carrier-protein] hydrolase FATB1, chloroplastic","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":"PRO_0000450101"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Mutagenesis","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Reduces thioesterase activity 7-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Loss of thioesterase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"Reduces thioesterase activity 18-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"Reduces thioesterase activity 9-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Reduces thioesterase activity 1.5-fold.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30409825"}],"alternativeSequence":{"originalSequence":"C","alternativeSequences":["A","S"]}}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"21831316","citationType":"journal article","authors":["Jing F.","Cantu D.C.","Tvaruzkova J.","Chipman J.P.","Nikolau B.J.","Yandeau-Nelson M.D.","Reilly P.J."],"citationCrossReferences":[{"database":"PubMed","id":"21831316"},{"database":"DOI","id":"10.1186/1471-2091-12-44"}],"title":"Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity.","publicationDate":"2011","journal":"BMC Biochem.","firstPage":"44","lastPage":"44","volume":"12"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","FUNCTION","CATALYTIC ACTIVITY"]},{"referenceNumber":2,"citation":{"id":"29491418","citationType":"journal article","authors":["Jing F.","Zhao L.","Yandeau-Nelson M.D.","Nikolau B.J."],"citationCrossReferences":[{"database":"PubMed","id":"29491418"},{"database":"DOI","id":"10.1038/s41467-018-03310-z"}],"title":"Two distinct domains contribute to the substrate acyl chain length selectivity of plant acyl-ACP thioesterase.","publicationDate":"2018","journal":"Nat. Commun.","firstPage":"860","lastPage":"860","volume":"9"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"]},{"referenceNumber":3,"citation":{"id":"30409825","citationType":"journal article","authors":["Jing F.","Yandeau-Nelson M.D.","Nikolau B.J."],"citationCrossReferences":[{"database":"PubMed","id":"30409825"},{"database":"DOI","id":"10.1042/bcj20180470"}],"title":"Identification of active site residues implies a two-step catalytic mechanism for acyl-ACP thioesterase.","publicationDate":"2018","journal":"Biochem. J.","firstPage":"3861","lastPage":"3873","volume":"475"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","MUTAGENESIS OF ASN-315; HIS-317; GLU-351 AND CYS-352"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JF338906","properties":[{"key":"ProteinId","value":"AEM72522.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"G3ESU9","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G3ESU9","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.1.2.14","properties":[{"key":"OrganismId","value":"16463"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000036","properties":[{"key":"GoTerm","value":"F:acyl carrier activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00586","properties":[{"key":"EntryName","value":"4HBT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000014","properties":[{"key":"EntryName","value":"Acyl-[acyl-carrier-protein] hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021113","properties":[{"key":"EntryName","value":"Acyl-ACP-thioesterase_N"}]},{"database":"InterPro","id":"IPR049427","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"}]},{"database":"InterPro","id":"IPR002864","properties":[{"key":"EntryName","value":"Acyl-ACP_thioesterase_NHD"}]},{"database":"InterPro","id":"IPR045023","properties":[{"key":"EntryName","value":"FATA/B"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"PANTHER","id":"PTHR31727","properties":[{"key":"EntryName","value":"OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31727:SF2","properties":[{"key":"EntryName","value":"PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01643","properties":[{"key":"EntryName","value":"Acyl-ACP_TE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20791","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12590","properties":[{"key":"EntryName","value":"Acyl-thio_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MVAAAATSAFFPVPAPGTSPKPGKSGNWPSSLSPTFKPKSIPNGGFQVKANASAHPKANGSAVNLKSGSLNTQEDTSSSPPPRAFLNQLPDWSMLLTAITTVFVAAEKQWTMLDRKSKRPDMLVDSVGLKSIVRDGLVSRHSFSIRSYEIGADRTASIETLMNHLQETTINHCKSLGLHNDGFGRTPGMCKNDLIWVLTKMQIMVNRYPTWGDTVEINTWFSQSGKIGMASDWLISDCNTGEILIRATSVWAMMNQKTRRFSRLPYEVRQELTPHFVDSPHVIEDNDQKLRKFDVKTGDSIRKGLTPRWNDLDVNQHVSNVKYIGWILESMPIEVLETQELCSLTVEYRRECGMDSVLESVTAVDPSENGGRSQYKHLLRLEDGTDIVKSRTEWRPKNAGTNGAISTSTAKTSNGNSVS","length":419,"molWeight":46360,"crc64":"5DBB71BB930F52A1","md5":"BD2727576475492FC6399C62DC9605E3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transit peptide":1,"Chain":1,"Region":2,"Compositional bias":2,"Active site":3,"Mutagenesis":5},"uniParcId":"UPI0002290326"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G3ESV1","uniProtkbId":"FATB3_CUPVI","entryAudit":{"firstPublicDate":"2020-06-17","lastAnnotationUpdateDate":"2025-04-09","lastSequenceUpdateDate":"2011-11-16","entryVersion":31,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Acyl-[acyl-carrier-protein] hydrolase FATB3, chloroplastic"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"CvFatB3"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"}],"value":"3.1.2.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Myristoyl-[acyl-carrier-protein] thioesterase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21831316"}],"value":"FATB3"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"21831316"}],"value":"Plays an essential role in chain termination during de novo fatty acid synthesis (Probable). Possesses thioesterase activity for medium chain acyl-ACPs. Main substrate is 14:0 (PubMed:21831316)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tetradecanoyl-[ACP] + H2O = tetradecanoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30123"},{"database":"Rhea","id":"RHEA-COMP:9648"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30807"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78477"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:30124"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21831316"}]}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the acyl-ACP thioesterase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transit peptide","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Chloroplast","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Acyl-[acyl-carrier-protein] hydrolase FATB3, chloroplastic","featureId":"PRO_0000450103"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q41635"}]},{"type":"Active site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]}],"keywords":[{"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"21831316","citationType":"journal article","authors":["Jing F.","Cantu D.C.","Tvaruzkova J.","Chipman J.P.","Nikolau B.J.","Yandeau-Nelson M.D.","Reilly P.J."],"citationCrossReferences":[{"database":"PubMed","id":"21831316"},{"database":"DOI","id":"10.1186/1471-2091-12-44"}],"title":"Phylogenetic and experimental characterization of an acyl-ACP thioesterase family reveals significant diversity in enzymatic specificity and activity.","publicationDate":"2011","journal":"BMC Biochem.","firstPage":"44","lastPage":"44","volume":"12"},"referencePositions":["NUCLEOTIDE SEQUENCE [MRNA]","FUNCTION","CATALYTIC ACTIVITY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JF338908","properties":[{"key":"ProteinId","value":"AEM72524.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"G3ESV1","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G3ESV1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000036","properties":[{"key":"GoTerm","value":"F:acyl carrier activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00586","properties":[{"key":"EntryName","value":"4HBT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000014","properties":[{"key":"EntryName","value":"Acyl-[acyl-carrier-protein] hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021113","properties":[{"key":"EntryName","value":"Acyl-ACP-thioesterase_N"}]},{"database":"InterPro","id":"IPR049427","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"}]},{"database":"InterPro","id":"IPR002864","properties":[{"key":"EntryName","value":"Acyl-ACP_thioesterase_NHD"}]},{"database":"InterPro","id":"IPR045023","properties":[{"key":"EntryName","value":"FATA/B"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"PANTHER","id":"PTHR31727","properties":[{"key":"EntryName","value":"OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31727:SF2","properties":[{"key":"EntryName","value":"PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01643","properties":[{"key":"EntryName","value":"Acyl-ACP_TE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20791","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12590","properties":[{"key":"EntryName","value":"Acyl-thio_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MVAAAASSAFFSFPTPGTSPKPGKFGNWPSSLSIPFNPKSNHNGGIQVKANASAHPKANGSAVSLKAGSLETQEDTSSPSPPPRTFISQLPDWSMLVSAITTVFVAAEKQWTMLDRKSKRPDVLVEPFVQDGVSFRQSFSIRSYEIGVDRTASIETLMNIFQETSLNHCKSLGLLNDGFGRTPEMCKRDLIWVVTKMQIEVNRYPTWGDTIEVTTWVSESGKNGMSRDWLISDCHSGEILIRATSVWAMMNQKTRRLSKIPDEVRQEIVPYFVDSAPVIEDDRKLHKLDVKTGDSIRNGLTPRWNDFDVNQHVNNVKYIAWLLKSVPTEVFETQELCGLTLEYRRECRRDSVLESVTAMDPSKEGDRSLYQHLLRLENGADIALGRTEWRPKNAGATGAVSTGKTSNGNSVS","length":412,"molWeight":45787,"crc64":"530044630C0E9260","md5":"F487B427864C568765609DA4CFDFBB8C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transit peptide":1,"Chain":1,"Region":2,"Compositional bias":3,"Active site":3},"uniParcId":"UPI0002290328"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0S1TKL1","uniProtkbId":"A0A0S1TKL1_CUPVI","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-02-17","entryVersion":22,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ALM22867.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013211"}],"value":"1-acylglycerol-3-phosphate O-acyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013211"}],"value":"2.3.1.51"}]}},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19709"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57970"},{"database":"ChEBI","id":"CHEBI:58342"},{"database":"ChEBI","id":"CHEBI:58608"}],"ecNumber":"2.3.1.51","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001141"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004728"}],"value":"Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008655"}],"value":"Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"Phospholipid/glycerol acyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00563"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ALM22867.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ALM22867.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"26505880","citationType":"journal article","authors":["Kim H.J.","Silva J.E.","Iskandarov U.","Andersson M.","Cahoon R.E.","Mockaitis K.","Cahoon E.B."],"citationCrossReferences":[{"database":"PubMed","id":"26505880"},{"database":"DOI","id":"10.1111/tpj.13063"}],"title":"Structurally divergent lysophosphatidic acid acyltransferases with high selectivity for saturated medium chain fatty acids from Cuphea seeds.","publicationDate":"2015","journal":"Plant J.","firstPage":"1021","lastPage":"1033","volume":"84"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ALM22867.1"}]},{"referenceNumber":2,"citation":{"id":"CI-592ENSC4F38GP","citationType":"submission","authors":["Jackson K.R.","Lunt B.L.","Fisher J.N.B.","Gardner A.V.","Bailey M.E.","Deus L.M.","Earl A.S.","Gibby P.D.","Hartmann K.A.","Liu J.E.","Manci A.M.","Nielsen D.A.","Solomon M.B.","Breakwell D.P.","Burnett S.H.","Grose J.H."],"publicationDate":"SEP-2015","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ALM22867.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KT694310","properties":[{"key":"ProteinId","value":"ALM22867.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"A0A0S1TKL1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00557","properties":[{"key":"RectionId","value":"UER00613"}]},{"database":"GO","id":"GO:0012505","properties":[{"key":"GoTerm","value":"C:endomembrane system"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003841","properties":[{"key":"GoTerm","value":"F:1-acylglycerol-3-phosphate O-acyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016024","properties":[{"key":"GoTerm","value":"P:CDP-diacylglycerol biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd07990","properties":[{"key":"EntryName","value":"LPLAT_LCLAT1-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR032098","properties":[{"key":"EntryName","value":"Acyltransf_C"}]},{"database":"InterPro","id":"IPR002123","properties":[{"key":"EntryName","value":"Plipid/glycerol_acylTrfase"}]},{"database":"PANTHER","id":"PTHR10983","properties":[{"key":"EntryName","value":"1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10983:SF24","properties":[{"key":"EntryName","value":"1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 3, ISOFORM E-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16076","properties":[{"key":"EntryName","value":"Acyltransf_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01553","properties":[{"key":"EntryName","value":"Acyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00563","properties":[{"key":"EntryName","value":"PlsC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69593","properties":[{"key":"EntryName","value":"Glycerol-3-phosphate (1)-acyltransferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAIAAAAVIFLFGLIFFASGLIINLFQALCFVLIRPLSKNAYRRINRVFAELLLSELLCLFDWWAGAKLKLFTDPETFRLMGKEHALVIINHMTELDWMVGWVMGQHFGCLGSIISVAKKSTKFLPVLGWSMWFSEYLYLERSWAKDKSTLKSHIERLIDYPLPFWLVIFVEGTRFTRTKLLAAQQYAVSSGLPVPRNVLIPRTKGFVSCVSHMRSFVPAVYDVTVAFPKTSPPPTLLNLFEGQSIMLHVHIKRHAMKDLPESDDAVAEWCRDKFVEKDALLDKHNAEDTFSGQEVRHTGSRQLKSLLVVISWVVVTTFGALKFLQWSSWKGKAFSAIGLGIVTLLMHVLILSSQAERSNPAEVAQAKLKTGLSISKKVTDKEN","length":384,"molWeight":43348,"crc64":"1C38CD8F82179988","md5":"AA77D9364851E42D409C7B78FBE133A8"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":2,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":3,"Domain":1},"uniParcId":"UPI00071FDB2A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"K9JGV7","uniProtkbId":"K9JGV7_CUPVI","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2013-03-06","entryVersion":27,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51160.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Acyl-[acyl-carrier-protein] hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"3.1.2.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51160.1"}],"value":"FATB2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Plays an essential role in chain termination during de novo fatty acid synthesis"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004229"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006500"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Belongs to the acyl-ACP thioesterase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Acyl-ACP-thioesterase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12590"}]},{"type":"Domain","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Acyl-ACP thioesterase N-terminal hotdog","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01643"}]},{"type":"Domain","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Acyl-ACP thioesterase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20791"}]},{"type":"Region","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CRTQD87NOV7F3","citationType":"submission","authors":["Darias M.J.","Fernandez I.","Andree K.","Gisbert E."],"title":"Gene expression in developing Sparus aurata larvae.","publicationDate":"NOV-2009","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51160.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"GU225693","properties":[{"key":"ProteinId","value":"ADR51160.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"K9JGV7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000036","properties":[{"key":"GoTerm","value":"F:acyl carrier activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00586","properties":[{"key":"EntryName","value":"4HBT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000014","properties":[{"key":"EntryName","value":"Acyl-[acyl-carrier-protein] hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021113","properties":[{"key":"EntryName","value":"Acyl-ACP-thioesterase_N"}]},{"database":"InterPro","id":"IPR049427","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"}]},{"database":"InterPro","id":"IPR002864","properties":[{"key":"EntryName","value":"Acyl-ACP_thioesterase_NHD"}]},{"database":"InterPro","id":"IPR045023","properties":[{"key":"EntryName","value":"FATA/B"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"PANTHER","id":"PTHR31727","properties":[{"key":"EntryName","value":"OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31727:SF2","properties":[{"key":"EntryName","value":"PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01643","properties":[{"key":"EntryName","value":"Acyl-ACP_TE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20791","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12590","properties":[{"key":"EntryName","value":"Acyl-thio_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MVLPLQVLHSSPCHLPTPSSRPGKLGNGPSSFSPLKPKSIPNGGLQVKASASAPPKINGSSVGLKSGGLKTHDDAPSAPPPRTFINQLPDWSMLLAAITTAFLAAEKQWMMLDWKPKRLDMLEDPFGLGRIVQDGLVFRQNFSIRSYEIGADRTASIETVMNHLQETALNHVKTAGLSNDGFGRTPEMYKRDLIWVVAKMQVMVNRYPTWGDTVEVNTWVAKSGKNGMRRDWLISDCNTGEILTRASSVWVMMNQKTRKLSKIPDEGRREIEPHFVDSAPVIEDDDRKLPKLDEKSADSIRKGLTPRWNDLDVNQHVNNVKYIGWILESTPPEVLETQELCSLTLEYRRECGRESVLESLTAVDPSGEGYGSQFQHLLRLEDGGEIVKGRTEWRPKNAGINGVVP","length":405,"molWeight":45055,"crc64":"5AA0733CE4BF66E1","md5":"0F9E7B122C35A8EC84E9DC1F4FB829B7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Region":1,"Compositional bias":1},"uniParcId":"UPI0002A7CA04"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"K9JHH6","uniProtkbId":"K9JHH6_CUPVI","entryAudit":{"firstPublicDate":"2013-03-06","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2013-03-06","entryVersion":27,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Cuphea viscosissima","commonName":"Blue waxweed","taxonId":857185,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51159.1"}],"lineage":["Eukaryota","Viridiplantae","Streptophyta","Embryophyta","Tracheophyta","Spermatophyta","Magnoliopsida","eudicotyledons","Gunneridae","Pentapetalae","rosids","malvids","Myrtales","Lythraceae","Cuphea"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Acyl-[acyl-carrier-protein] hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"3.1.2.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51159.1"}],"value":"FATB1"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Plays an essential role in chain termination during de novo fatty acid synthesis"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004229"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Plastid, chloroplast","id":"SL-0049"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006500"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"value":"Belongs to the acyl-ACP thioesterase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Acyl-ACP-thioesterase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12590"}]},{"type":"Domain","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Acyl-ACP thioesterase N-terminal hotdog","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01643"}]},{"type":"Domain","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Acyl-ACP thioesterase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20791"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022528"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0150","category":"Cellular component","name":"Chloroplast"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022640"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363096"}],"id":"KW-0934","category":"Cellular component","name":"Plastid"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CRTQD87NOV7F3","citationType":"submission","authors":["Darias M.J.","Fernandez I.","Andree K.","Gisbert E."],"title":"Gene expression in developing Sparus aurata larvae.","publicationDate":"NOV-2009","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ADR51159.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"GU225692","properties":[{"key":"ProteinId","value":"ADR51159.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"mRNA"}]},{"database":"AlphaFoldDB","id":"K9JHH6","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0009507","properties":[{"key":"GoTerm","value":"C:chloroplast"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000036","properties":[{"key":"GoTerm","value":"F:acyl carrier activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00586","properties":[{"key":"EntryName","value":"4HBT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000014","properties":[{"key":"EntryName","value":"Acyl-[acyl-carrier-protein] hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR021113","properties":[{"key":"EntryName","value":"Acyl-ACP-thioesterase_N"}]},{"database":"InterPro","id":"IPR049427","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"}]},{"database":"InterPro","id":"IPR002864","properties":[{"key":"EntryName","value":"Acyl-ACP_thioesterase_NHD"}]},{"database":"InterPro","id":"IPR045023","properties":[{"key":"EntryName","value":"FATA/B"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"PANTHER","id":"PTHR31727","properties":[{"key":"EntryName","value":"OLEOYL-ACYL CARRIER PROTEIN THIOESTERASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31727:SF2","properties":[{"key":"EntryName","value":"PALMITOYL-ACYL CARRIER PROTEIN THIOESTERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01643","properties":[{"key":"EntryName","value":"Acyl-ACP_TE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20791","properties":[{"key":"EntryName","value":"Acyl-ACP_TE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12590","properties":[{"key":"EntryName","value":"Acyl-thio_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MVATAASSAFFPLPSPDTSSRPGKLGNGSSSLSPLKPKFVANAGLKVKASASAPPKINGSSVGLKSGSLKTQEDTPSVPPPRTFINQLPDWSMLLAAITTVFLAAEKQWMMLDWKPKRPDMLVDPFGLGSIVQGGLVFRQNFSIRSYEIGADRTASIETVMNHLQETALNHVKSAGLLNDGFGRTPEMFKRDLIWVVAKMQVMVNRYPTWGDTVEVNTWVAKSGKNGMRRDWLISDCNTGEIPTRASSVWVMMNQKTRKLSKIPDEVRHEIEPHFIDCAPVIEDDDRKLRKLDEKTADSIRKGLTPKWNDLDVNQHVNNVKYIGWILESTPQEVLESQELSSLTLEYRRECGRESVLESLTAVDPAGKGFGSQFQHLLRLEDGGEIVKGRTEWRPKTAGVNGAIASGETSHGDS","length":414,"molWeight":45671,"crc64":"FBAA2263118F3EC6","md5":"C52CE27832960B5815D4714EFAB5DB71"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Region":2,"Compositional bias":2},"uniParcId":"UPI0002A88DA1"}}]}