FATB2_CUPVI
ID FATB2_CUPVI Reviewed; 412 AA.
AC G3ESV0;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 23.
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase FATB2, chloroplastic {ECO:0000305};
DE Short=CvFatB2 {ECO:0000303|PubMed:21831316};
DE EC=3.1.2.- {ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418, ECO:0000269|PubMed:30409825};
DE AltName: Full=Myristoyl-[acyl-carrier-protein] thioesterase {ECO:0000305|PubMed:21831316};
DE AltName: Full=Palmitoyl-[acyl-carrier-protein] thioesterase {ECO:0000305|PubMed:21831316};
DE Flags: Precursor; Fragment;
GN Name=FATB2 {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).
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29491418; DOI=10.1038/s41467-018-03310-z;
RA Jing F., Zhao L., Yandeau-Nelson M.D., Nikolau B.J.;
RT "Two distinct domains contribute to the substrate acyl chain length
RT selectivity of plant acyl-ACP thioesterase.";
RL Nat. Commun. 9:860-860(2018).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-309; ASN-311; HIS-313;
RP GLU-347 AND CYS-348.
RX PubMed=30409825; DOI=10.1042/bcj20180470;
RA Jing F., Yandeau-Nelson M.D., Nikolau B.J.;
RT "Identification of active site residues implies a two-step catalytic
RT mechanism for acyl-ACP thioesterase.";
RL Biochem. J. 475:3861-3873(2018).
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. Substrate preference is 14:0 > 16:0 > 16:1
CC (PubMed:21831316, PubMed:29491418, PubMed:30409825).
CC {ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825, 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, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30124;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-[ACP] = H(+) + hexadecanoate + holo-[ACP];
CC Xref=Rhea:RHEA:41932, Rhea:RHEA-COMP:9652, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78483;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41933;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; JF338907; AEM72523.1; -; mRNA.
DR AlphaFoldDB; G3ESV0; -.
DR SMR; G3ESV0; -.
DR BRENDA; 3.1.2.14; 16463.
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:0016296; F:palmitoyl-[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..46
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 47..412
FT /note="Acyl-[acyl-carrier-protein] hydrolase FATB2,
FT chloroplastic"
FT /id="PRO_0000450102"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 311
FT /evidence="ECO:0000250|UniProtKB:Q41635"
FT ACT_SITE 313
FT /evidence="ECO:0000250|UniProtKB:Q41635"
FT ACT_SITE 348
FT /evidence="ECO:0000255"
FT MUTAGEN 309
FT /note="D->A,E,N: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 311
FT /note="N->A: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 313
FT /note="H->A: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 347
FT /note="E->A,D,Q: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 348
FT /note="C->A: Decreases thioesterase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 348
FT /note="C->S: Increases thioesterase activity 2-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
FT NON_TER 1
SQ SEQUENCE 412 AA; 45564 MW; EDECD381C92F981F CRC64;
TAASSAFFPV PSADTSSRPG KLGNGPSSFS PLKPKSIPNG GLQVKASASA PPKINGSSVG
LKSGGLKTHD DAPSAPPPRT FINQLPDWSM LLAAITTAFL AAEKQWMMLD RKPKRLDMLE
DPFGLGRVVQ DGLVFRQNFS IRSYEIGADR TASIETVMNH LQETALNHVK TAGLSNDGFG
RTPEMYKRDL IWVVAKMQVM VNRYPTWGDT VEVNTWVAKS GKNGMRRDWL ISDCNTGEIL
TRASSVWVMM NQKTRKLSKI PDEVRREIEP HFVDSAPVIE DDDRKLPKLD EKSADSIRKG
LTPRWNDLDV NQHVNNAKYI GWILESTPPE VLETQELCSL TLEYRRECGR ESVLESLTAV
DPSGEGYGSQ FQHLLRLEDG GEIVKGRTEW RPKNAGINGV VPSEESSPGD YS
