FATB1_CUPVI
ID FATB1_CUPVI Reviewed; 419 AA.
AC G3ESU9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Acyl-[acyl-carrier-protein] hydrolase FATB1, chloroplastic {ECO:0000305};
DE Short=CvFatB1 {ECO:0000303|PubMed:21831316};
DE EC=3.1.2.- {ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418, ECO:0000269|PubMed:30409825};
DE AltName: Full=Decanoyl-[acyl-carrier-protein] thioesterase {ECO:0000305|PubMed:21831316};
DE AltName: Full=Octanoyl-[acyl-carrier-protein] thioesterase {ECO:0000305|PubMed:21831316};
DE Flags: Precursor;
GN Name=FATB1 {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 ASN-315; HIS-317; GLU-351
RP AND CYS-352.
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 short chain acyl-ACPs. Substrate preference is 8:0 > 10:0
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 + octanoyl-[ACP] = H(+) + holo-[ACP] + octanoate;
CC Xref=Rhea:RHEA:30131, Rhea:RHEA-COMP:9636, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78463;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30132;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-[ACP] + H2O = decanoate + H(+) + holo-[ACP];
CC Xref=Rhea:RHEA:30115, Rhea:RHEA-COMP:9640, Rhea:RHEA-COMP:9685,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78468;
CC Evidence={ECO:0000269|PubMed:21831316, ECO:0000269|PubMed:29491418,
CC ECO:0000269|PubMed:30409825};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30116;
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}.
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; JF338906; AEM72522.1; -; mRNA.
DR AlphaFoldDB; G3ESU9; -.
DR SMR; G3ESU9; -.
DR BRENDA; 3.1.2.14; 16463.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IEA:InterPro.
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..419
FT /note="Acyl-[acyl-carrier-protein] hydrolase FATB1,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000450101"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000250|UniProtKB:Q41635"
FT ACT_SITE 317
FT /evidence="ECO:0000250|UniProtKB:Q41635"
FT ACT_SITE 352
FT /evidence="ECO:0000255"
FT MUTAGEN 315
FT /note="N->A: Reduces thioesterase activity 7-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 317
FT /note="H->A: Loss of thioesterase activity."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 351
FT /note="E->A: Reduces thioesterase activity 18-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 351
FT /note="E->D: Reduces thioesterase activity 9-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
FT MUTAGEN 352
FT /note="C->A,S: Reduces thioesterase activity 1.5-fold."
FT /evidence="ECO:0000269|PubMed:30409825"
SQ SEQUENCE 419 AA; 46360 MW; 5DBB71BB930F52A1 CRC64;
MVAAAATSAF FPVPAPGTSP KPGKSGNWPS SLSPTFKPKS IPNGGFQVKA NASAHPKANG
SAVNLKSGSL NTQEDTSSSP PPRAFLNQLP DWSMLLTAIT TVFVAAEKQW TMLDRKSKRP
DMLVDSVGLK SIVRDGLVSR HSFSIRSYEI GADRTASIET LMNHLQETTI NHCKSLGLHN
DGFGRTPGMC KNDLIWVLTK MQIMVNRYPT WGDTVEINTW FSQSGKIGMA SDWLISDCNT
GEILIRATSV WAMMNQKTRR FSRLPYEVRQ ELTPHFVDSP HVIEDNDQKL RKFDVKTGDS
IRKGLTPRWN DLDVNQHVSN VKYIGWILES MPIEVLETQE LCSLTVEYRR ECGMDSVLES
VTAVDPSENG GRSQYKHLLR LEDGTDIVKS RTEWRPKNAG TNGAISTSTA KTSNGNSVS
