ID   FATB3_CUPVI             Reviewed;         412 AA.
AC   G3ESV1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=Acyl-[acyl-carrier-protein] hydrolase FATB3, chloroplastic {ECO:0000305};
DE            Short=CvFatB3 {ECO:0000303|PubMed:21831316};
DE            EC=3.1.2.- {ECO:0000269|PubMed:21831316};
DE   AltName: Full=Myristoyl-[acyl-carrier-protein] thioesterase {ECO:0000305|PubMed:21831316};
DE   Flags: Precursor;
GN   Name=FATB3 {ECO:0000303|PubMed:21831316};
OS   Cuphea viscosissima (Blue waxweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Cuphea.
OX   NCBI_TaxID=857185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21831316; DOI=10.1186/1471-2091-12-44;
RA   Jing F., Cantu D.C., Tvaruzkova J., Chipman J.P., Nikolau B.J.,
RA   Yandeau-Nelson M.D., Reilly P.J.;
RT   "Phylogenetic and experimental characterization of an acyl-ACP thioesterase
RT   family reveals significant diversity in enzymatic specificity and
RT   activity.";
RL   BMC Biochem. 12:44-44(2011).
CC   -!- FUNCTION: Plays an essential role in chain termination during de novo
CC       fatty acid synthesis (Probable). Possesses thioesterase activity for
CC       medium chain acyl-ACPs. Main substrate is 14:0 (PubMed:21831316).
CC       {ECO:0000269|PubMed:21831316, ECO:0000305|PubMed:21831316}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + tetradecanoyl-[ACP] = H(+) + holo-[ACP] +
CC         tetradecanoate; Xref=Rhea:RHEA:30123, Rhea:RHEA-COMP:9648, Rhea:RHEA-
CC         COMP:9685, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:78477;
CC         Evidence={ECO:0000269|PubMed:21831316};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC         Evidence={ECO:0000269|PubMed:21831316};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JF338908; AEM72524.1; -; mRNA.
DR   AlphaFoldDB; G3ESV1; -.
DR   SMR; G3ESV1; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR021113; Acyl-ACP-thioesterase_N.
DR   InterPro; IPR002864; Acyl-ACP_thioesterase.
DR   InterPro; IPR045023; FATA/B.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   PANTHER; PTHR31727; PTHR31727; 1.
DR   Pfam; PF01643; Acyl-ACP_TE; 1.
DR   Pfam; PF12590; Acyl-thio_N; 1.
DR   SUPFAM; SSF54637; SSF54637; 2.
PE   1: Evidence at protein level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW   Lipid biosynthesis; Lipid metabolism; Plastid; Transit peptide.
FT   TRANSIT         1..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..412
FT                   /note="Acyl-[acyl-carrier-protein] hydrolase FATB3,
FT                   chloroplastic"
FT                   /id="PRO_0000450103"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..412
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000250|UniProtKB:Q41635"
FT   ACT_SITE        312
FT                   /evidence="ECO:0000250|UniProtKB:Q41635"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   412 AA;  45787 MW;  530044630C0E9260 CRC64;
     MVAAAASSAF FSFPTPGTSP KPGKFGNWPS SLSIPFNPKS NHNGGIQVKA NASAHPKANG
     SAVSLKAGSL ETQEDTSSPS PPPRTFISQL PDWSMLVSAI TTVFVAAEKQ WTMLDRKSKR
     PDVLVEPFVQ DGVSFRQSFS IRSYEIGVDR TASIETLMNI FQETSLNHCK SLGLLNDGFG
     RTPEMCKRDL IWVVTKMQIE VNRYPTWGDT IEVTTWVSES GKNGMSRDWL ISDCHSGEIL
     IRATSVWAMM NQKTRRLSKI PDEVRQEIVP YFVDSAPVIE DDRKLHKLDV KTGDSIRNGL
     TPRWNDFDVN QHVNNVKYIA WLLKSVPTEV FETQELCGLT LEYRRECRRD SVLESVTAMD
     PSKEGDRSLY QHLLRLENGA DIALGRTEWR PKNAGATGAV STGKTSNGNS VS