FATB_GOSHI
ID FATB_GOSHI Reviewed; 413 AA.
AC Q9SQI3; Q9ZTT9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Palmitoyl-acyl carrier protein thioesterase, chloroplastic;
DE EC=3.1.2.-;
DE AltName: Full=16:0-acyl-carrier protein thioesterase;
DE Short=16:0-ACP thioesterase;
DE AltName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE AltName: Full=PATE;
DE Flags: Precursor;
GN Name=FATB1;
OS Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=3635;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Acala SJ5;
RX PubMed=10524217; DOI=10.1016/s0167-4781(99)00115-3;
RA Yoder D.W., Nampaisansuk M., Pirtle I.L., Chapman K.D., Pirtle R.M.;
RT "Molecular cloning and nucleotide sequence of a gene encoding a cotton
RT palmitoyl-acyl carrier protein thioesterase.";
RL Biochim. Biophys. Acta 1446:403-413(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-413, AND CHARACTERIZATION.
RC STRAIN=cv. Deltapine 62;
RX PubMed=10202811; DOI=10.1093/oxfordjournals.pcp.a029523;
RA Pirtle R.M., Yoder D.W., Huynh T.T., Nampaisansuk M., Pirtle I.L.,
RA Chapman K.D.;
RT "Characterization of a palmitoyl-acyl carrier protein thioesterase (FatB1)
RT in cotton.";
RL Plant Cell Physiol. 40:155-163(1999).
CC -!- FUNCTION: Plays an essential role in chain termination during de novo
CC fatty acid synthesis. High thioesterase activity for palmitoyl-ACP
CC versus other acyl-ACPs.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; AF076535; AAF02215.1; -; Genomic_DNA.
DR EMBL; AF034266; AAD01982.1; -; mRNA.
DR RefSeq; XP_016720478.1; XM_016864989.1.
DR RefSeq; XP_016720479.1; XM_016864990.1.
DR AlphaFoldDB; Q9SQI3; -.
DR SMR; Q9SQI3; -.
DR GeneID; 107932873; -.
DR KEGG; ghi:107932873; -.
DR OMA; WILEVVI; -.
DR BRENDA; 3.1.2.14; 2499.
DR Proteomes; UP000189702; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IBA:GO_Central.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
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; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..57
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 58..413
FT /note="Palmitoyl-acyl carrier protein thioesterase,
FT chloroplastic"
FT /id="PRO_0000000594"
FT REGION 12..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /evidence="ECO:0000255"
FT ACT_SITE 312
FT /evidence="ECO:0000255"
FT ACT_SITE 347
FT /evidence="ECO:0000255"
SQ SEQUENCE 413 AA; 45646 MW; FF745A07BE5ADB45 CRC64;
MVATAVTSAF FPVTSSPDSS DSKNKKLGSI KSKPSVSSGS LQVKANAQAP PKINGTVAST
TPVEGSKNDD GASSPPPRTF INQLPDWSML LAAITTIFLA AEKQWMMLDW KPRRPDMVID
PFGIGKIVQD GLVFSQNFSI RSYEIGADQT ASIETLMNHL QETAINHCRS AGLLGEGFGA
TPEMCKKNLI WVVTRMQVVV DRYPTWGDVV QVDTWVSASG KNGMRRDWLV SNSETGEILT
RATSVWVMMN KLTRRLSKIP EEVRGEIEPF FMNSDPVLAE DSQKLVKLDD STAEHVCKGL
TPKWSDLDVN QHVNNVKYIG WILESAPLPI LESHELSALT LEYRRECGRD SVLQSLTTVS
DSNTENAVNV GEFNCQHLLR LDDGAEIVRG RTRWRPKHAK SSANMDQITA KRA
