FATA2_ARATH
ID FATA2_ARATH Reviewed; 367 AA.
AC Q9SV64; Q8GWU8;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Oleoyl-acyl carrier protein thioesterase 2, 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=FATA2; OrderedLocusNames=At4g13050; ORFNames=F25G13.140;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
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. {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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; AL079349; CAB45504.1; -; Genomic_DNA.
DR EMBL; AL161535; CAB78347.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83224.1; -; Genomic_DNA.
DR EMBL; BT024746; ABD59084.1; -; mRNA.
DR EMBL; AK118624; BAC43222.1; -; mRNA.
DR PIR; T10207; T10207.
DR RefSeq; NP_193041.1; NM_117374.4.
DR AlphaFoldDB; Q9SV64; -.
DR SMR; Q9SV64; -.
DR STRING; 3702.AT4G13050.1; -.
DR PaxDb; Q9SV64; -.
DR PRIDE; Q9SV64; -.
DR ProteomicsDB; 230966; -.
DR EnsemblPlants; AT4G13050.1; AT4G13050.1; AT4G13050.
DR GeneID; 826919; -.
DR Gramene; AT4G13050.1; AT4G13050.1; AT4G13050.
DR KEGG; ath:AT4G13050; -.
DR Araport; AT4G13050; -.
DR TAIR; locus:2123256; AT4G13050.
DR eggNOG; ENOG502QTE3; Eukaryota.
DR HOGENOM; CLU_045466_1_2_1; -.
DR InParanoid; Q9SV64; -.
DR OMA; HELSWII; -.
DR OrthoDB; 602729at2759; -.
DR PhylomeDB; Q9SV64; -.
DR BioCyc; ARA:AT4G13050-MON; -.
DR PRO; PR:Q9SV64; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SV64; baseline and differential.
DR Genevisible; Q9SV64; 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; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Hydrolase;
KW Lipid biosynthesis; Lipid metabolism; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..367
FT /note="Oleoyl-acyl carrier protein thioesterase 2,
FT chloroplastic"
FT /id="PRO_0000418154"
FT ACT_SITE 263
FT /evidence="ECO:0000255"
FT ACT_SITE 265
FT /evidence="ECO:0000255"
FT ACT_SITE 300
FT /evidence="ECO:0000255"
SQ SEQUENCE 367 AA; 42231 MW; C1CCD6CF159A4CC4 CRC64;
MLKLSCNVTD HIHNLFSNSR RIFVPVHRQT RPISCFQLKK EPLRAILSAD HGNSSVRVAD
TVSGTSPADR LRFGRLMEDG FSYKEKFIVR SYEVGINKTA TIETIANLLQ EVACNHVQNV
GFSTDGFATT LTMRKLHLIW VTARMHIEIY KYPAWSDVVE IETWCQSEGR IGTRRDWILK
DCATGEVIGR ATSKWVMMNQ DTRRLQRVTD EVRDEYLVFC PPEPRLAFPE ENNSSLKKIP
KLEDPAQYSM LGLKPRRADL DMNQHVNNVT YIGWVLESIP QEIIDTHELK VITLDYRREC
QQDDIVDSLT TSETPNEVVS KLTGTNGSTT SSKREHNESH FLHILRLSEN GQEINRGRTQ
WRKKSSR
