ID   FATB_CINCA              Reviewed;         382 AA.
AC   Q39473;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Dodecanoyl-[acyl-carrier-protein] hydrolase, chloroplastic {ECO:0000305};
DE            EC=3.1.2.21 {ECO:0000269|PubMed:7479856};
DE   AltName: Full=14:0-acyl-carrier protein thioesterase;
DE            Short=14:0-ACP thioesterase;
DE   AltName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE   AltName: Full=CcFatB1 {ECO:0000303|PubMed:7479856};
DE   AltName: Full=Myristoyl-acyl carrier protein thioesterase;
DE   Flags: Precursor;
GN   Name=FATB1 {ECO:0000303|PubMed:7479856};
OS   Cinnamomum camphora (Camphor tree) (Laurus camphora).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Cinnamomum.
OX   NCBI_TaxID=13429;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Seed;
RX   PubMed=7479856; DOI=10.1073/pnas.92.23.10639;
RA   Yuan L., Voelker T.A., Hawkins D.J.;
RT   "Modification of the substrate specificity of an acyl-acyl carrier protein
RT   thioesterase by protein engineering.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10639-10643(1995).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: Plays an essential role in chain termination during de novo
CC       fatty acid synthesis. High thioesterase activity for myristoyl-ACP.
CC       {ECO:0000269|PubMed:7479856}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-[ACP] + H2O = dodecanoate + H(+) + holo-[ACP];
CC         Xref=Rhea:RHEA:30119, Rhea:RHEA-COMP:9644, Rhea:RHEA-COMP:9685,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:65264; EC=3.1.2.21;
CC         Evidence={ECO:0000269|PubMed:7479856};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:Q41635}.
CC   -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR   EMBL; U31813; AAC49151.1; -; mRNA.
DR   AlphaFoldDB; Q39473; -.
DR   SMR; Q39473; -.
DR   PRIDE; Q39473; -.
DR   BRENDA; 3.1.2.14; 1390.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0047381; F:dodecanoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
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..83
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000250|UniProtKB:Q41635"
FT   CHAIN           84..382
FT                   /note="Dodecanoyl-[acyl-carrier-protein] hydrolase,
FT                   chloroplastic"
FT                   /id="PRO_0000000592"
FT   ACT_SITE        283
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        285
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        320
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   382 AA;  42675 MW;  857F673424FA018E CRC64;
     MATTSLASAF CSMKAVMLAR DGRGMKPRSS DLQLRAGNAQ TSLKMINGTK FSYTESLKKL
     PDWSMLFAVI TTIFSAAEKQ WTNLEWKPKP NPPQLLDDHF GPHGLVFRRT FAIRSYEVGP
     DRSTSIVAVM NHLQEAALNH AKSVGILGDG FGTTLEMSKR DLIWVVKRTH VAVERYPAWG
     DTVEVECWVG ASGNNGRRHD FLVRDCKTGE ILTRCTSLSV MMNTRTRRLS KIPEEVRGEI
     GPAFIDNVAV KDEEIKKPQK LNDSTADYIQ GGLTPRWNDL DINQHVNNIK YVDWILETVP
     DSIFESHHIS SFTIEYRREC TMDSVLQSLT TVSGGSSEAG LVCEHLLQLE GGSEVLRAKT
     EWRPKLTDSF RGISVIPAES SV