FATA1_ARATH
ID FATA1_ARATH Reviewed; 362 AA.
AC Q42561;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Oleoyl-acyl carrier protein thioesterase 1, chloroplastic;
DE EC=3.1.2.14;
DE AltName: Full=18:0-acyl-carrier protein thioesterase;
DE Short=18:0-ACP thioesterase;
DE AltName: Full=Acyl-[acyl-carrier-protein] hydrolase;
DE Flags: Precursor;
GN Name=FATA; Synonyms=FATA1; OrderedLocusNames=At3g25110; ORFNames=MJL12.5;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Root;
RX PubMed=7840673; DOI=10.1006/abbi.1995.1081;
RA Dormann P., Voelker T.A., Ohlrogge J.B.;
RT "Cloning and expression in Escherichia coli of a novel thioesterase from
RT Arabidopsis thaliana specific for long-chain acyl-acyl carrier proteins.";
RL Arch. Biochem. Biophys. 316:612-618(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12061798; DOI=10.1016/s0003-9861(02)00017-6;
RA Salas J.J., Ohlrogge J.B.;
RT "Characterization of substrate specificity of plant FatA and FatB acyl-ACP
RT thioesterases.";
RL Arch. Biochem. Biophys. 403:25-34(2002).
RN [6]
RP FUNCTION.
RX PubMed=22002626; DOI=10.1007/s00425-011-1534-5;
RA Moreno-Perez A.J., Venegas-Caleron M., Vaistij F.E., Salas J.J.,
RA Larson T.R., Garces R., Graham I.A., Martinez-Force E.;
RT "Reduced expression of FatA thioesterases in Arabidopsis affects the oil
RT content and fatty acid composition of the seeds.";
RL Planta 235:629-639(2012).
CC -!- FUNCTION: Plays an essential role in chain termination during de novo
CC fatty acid synthesis. Possesses high thioesterase activity for oleoyl-
CC ACP versus other acyl-ACPs. Substrate preference is 18:1 > 18:0 > 16:1.
CC {ECO:0000269|PubMed:12061798, ECO:0000269|PubMed:22002626}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) +
CC holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14;
CC Evidence={ECO:0000269|PubMed:12061798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.9 uM for myristoyl-ACP (14:0-ACP)
CC {ECO:0000269|PubMed:12061798};
CC KM=8.9 uM for myristoleoyl-ACP (14:1-ACP)
CC {ECO:0000269|PubMed:12061798};
CC KM=4.9 uM for palmitoyl-ACP (16:0-ACP) {ECO:0000269|PubMed:12061798};
CC KM=4.9 uM for palmitoleoyl-ACP (16:1-ACP)
CC {ECO:0000269|PubMed:12061798};
CC KM=5.0 uM for stearoyl-ACP (18:0-ACP) {ECO:0000269|PubMed:12061798};
CC KM=3.1 uM for oleoyl-ACP (18:1-ACP) {ECO:0000269|PubMed:12061798};
CC Note=The catalytic efficiency for 18:1 is at least 20-fold higher
CC than for other substrates.;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; Z36912; CAA85389.1; -; mRNA.
DR EMBL; AB026647; BAB02069.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76980.1; -; Genomic_DNA.
DR EMBL; AK176105; BAD43868.1; -; mRNA.
DR PIR; S69197; S69197.
DR RefSeq; NP_189147.1; NM_113415.4.
DR AlphaFoldDB; Q42561; -.
DR SMR; Q42561; -.
DR STRING; 3702.AT3G25110.1; -.
DR PaxDb; Q42561; -.
DR PRIDE; Q42561; -.
DR ProteomicsDB; 231016; -.
DR EnsemblPlants; AT3G25110.1; AT3G25110.1; AT3G25110.
DR GeneID; 822102; -.
DR Gramene; AT3G25110.1; AT3G25110.1; AT3G25110.
DR KEGG; ath:AT3G25110; -.
DR Araport; AT3G25110; -.
DR TAIR; locus:2090285; AT3G25110.
DR eggNOG; ENOG502QTE3; Eukaryota.
DR HOGENOM; CLU_045466_1_2_1; -.
DR OMA; TRRDWIM; -.
DR OrthoDB; 602729at2759; -.
DR PhylomeDB; Q42561; -.
DR BioCyc; ARA:AT3G25110-MON; -.
DR BioCyc; MetaCyc:AT3G25110-MON; -.
DR PRO; PR:Q42561; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q42561; baseline and differential.
DR Genevisible; Q42561; AT.
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; IDA:TAIR.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IGI:UniProtKB.
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 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..38
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 39..362
FT /note="Oleoyl-acyl carrier protein thioesterase 1,
FT chloroplastic"
FT /id="PRO_0000418153"
FT REGION 312..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 264
FT /evidence="ECO:0000255"
FT ACT_SITE 266
FT /evidence="ECO:0000255"
FT ACT_SITE 301
FT /evidence="ECO:0000255"
SQ SEQUENCE 362 AA; 40819 MW; CD877DCCC0972C01 CRC64;
MLKLSCNVTD SKLQRSLLFF SHSYRSDPVN FIRRRIVSCS QTKKTGLVPL RAVVSADQGS
VVQGLATLAD QLRLGSLTED GLSYKEKFVV RSYEVGSNKT ATVETIANLL QEVGCNHAQS
VGFSTDGFAT TTTMRKLHLI WVTARMHIEI YKYPAWGDVV EIETWCQSEG RIGTRRDWIL
KDSVTGEVTG RATSKWVMMN QDTRRLQKVS DDVRDEYLVF CPQEPRLAFP EENNRSLKKI
PKLEDPAQYS MIGLKPRRAD LDMNQHVNNV TYIGWVLESI PQEIVDTHEL QVITLDYRRE
CQQDDVVDSL TTTTSEIGGT NGSATSGTQG HNDSQFLHLL RLSGDGQEIN RGTTLWRKKP
SS