FATB_ARATH
ID FATB_ARATH Reviewed; 412 AA.
AC Q9SJE2; Q42558; Q42562;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=Acyl-acyl carrier protein thioesterase B1 {ECO:0000303|PubMed:10859193};
DE Short=AtFATB1 {ECO:0000303|PubMed:10859193};
DE Flags: Precursor;
GN Name=FATB; Synonyms=FATB1; OrderedLocusNames=At1g08510; ORFNames=T27G7.19;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Col-2;
RX PubMed=10859193; DOI=10.1104/pp.123.2.637;
RA Doermann P., Voelker T.A., Ohlrogge J.B.;
RT "Accumulation of palmitate in Arabidopsis mediated by the acyl-acyl carrier
RT protein thioesterase FATB1.";
RL Plant Physiol. 123:637-644(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Columbia;
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 [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=12671095; DOI=10.1105/tpc.008946;
RA Bonaventure G., Salas J.J., Pollard M.R., Ohlrogge J.B.;
RT "Disruption of the FATB gene in Arabidopsis demonstrates an essential role
RT of saturated fatty acids in plant growth.";
RL Plant Cell 15:1020-1033(2003).
RN [8]
RP FUNCTION, 3D-STRUCTURE MODELING, AND MUTAGENESIS OF ARG-259; ASN-315 AND
RP ASN-320.
RC STRAIN=cv. Columbia;
RX PubMed=15531590; DOI=10.1074/jbc.m411351200;
RA Mayer K.M., Shanklin J.;
RT "A structural model of the plant acyl-acyl carrier protein thioesterase
RT FatB comprises two helix/4-stranded sheet domains, the N-terminal domain
RT containing residues that affect specificity and the C-terminal domain
RT containing catalytic residues.";
RL J. Biol. Chem. 280:3621-3627(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18326828; DOI=10.1105/tpc.107.054858;
RA Raffaele S., Vailleau F., Leger A., Joubes J., Miersch O., Huard C.,
RA Blee E., Mongrand S., Domergue F., Roby D.;
RT "A MYB transcription factor regulates very-long-chain fatty acid
RT biosynthesis for activation of the hypersensitive cell death response in
RT Arabidopsis.";
RL Plant Cell 20:752-767(2008).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=18263779; DOI=10.1104/pp.107.115220;
RA Lu Y., Savage L.J., Ajjawi I., Imre K.M., Yoder D.W., Benning C.,
RA Dellapenna D., Ohlrogge J.B., Osteryoung K.W., Weber A.P., Wilkerson C.G.,
RA Last R.L.;
RT "New connections across pathways and cellular processes: industrialized
RT mutant screening reveals novel associations between diverse phenotypes in
RT Arabidopsis.";
RL Plant Physiol. 146:1482-1500(2008).
CC -!- FUNCTION: Plays an essential role in chain termination during de novo
CC fatty acid synthesis. Possesses high thioesterase activity for
CC palmitoyl-ACP versus other acyl-ACPs. Substrate preference is 16:0 >
CC 18:1 > 18:0 > 16:1. Plays an essential role in the supply of saturated
CC fatty acids necessary for plant growth and seed development.
CC Contributes to 16:0 production particularly in flowers. May be involved
CC in the synthesis of long chain fatty acid.
CC {ECO:0000269|PubMed:10859193, ECO:0000269|PubMed:12061798,
CC ECO:0000269|PubMed:12671095, ECO:0000269|PubMed:15531590,
CC ECO:0000269|PubMed:18263779, ECO:0000269|PubMed:18326828,
CC ECO:0000269|PubMed:7840673}.
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:12061798, ECO:0000269|PubMed:7840673};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 uM for myristoyl-ACP (14:0-ACP) {ECO:0000269|PubMed:12061798};
CC KM=4.0 uM for myristoleoyl-ACP (14:1-ACP)
CC {ECO:0000269|PubMed:12061798};
CC KM=3.8 uM for palmitoyl-ACP (16:0-ACP) {ECO:0000269|PubMed:12061798};
CC KM=2.6 uM for palmitoleoyl-ACP (16:1-ACP)
CC {ECO:0000269|PubMed:12061798};
CC KM=3.0 uM for stearoyl-ACP (18:0-ACP) {ECO:0000269|PubMed:12061798};
CC KM=2.6 uM for oleoyl-ACP (18:1-ACP) {ECO:0000269|PubMed:12061798};
CC Note=The catalytic efficiency for 16:0 is at least 2-fold higher than
CC for other substrates.;
CC pH dependence:
CC Optimum pH is 9.7. {ECO:0000269|PubMed:7840673};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed in roots,
CC leaves, stems, siliques and seeds. {ECO:0000269|PubMed:10859193,
CC ECO:0000269|PubMed:7840673}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth, deformed seeds with low rate of
CC germination and reduced levels of palmitate and stearate.
CC {ECO:0000269|PubMed:12671095, ECO:0000269|PubMed:18263779,
CC ECO:0000269|PubMed:18326828}.
CC -!- MISCELLANEOUS: Plants silencing FATB, show reduced level of palmitate
CC in flowers and seeds. {ECO:0000305|PubMed:10859193}.
CC -!- SIMILARITY: Belongs to the acyl-ACP thioesterase family. {ECO:0000305}.
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DR EMBL; Z36910; CAA85387.1; -; mRNA.
DR EMBL; Z36911; CAA85388.1; -; mRNA.
DR EMBL; AC006932; AAF22899.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28300.1; -; Genomic_DNA.
DR EMBL; AY054679; AAK96870.1; -; mRNA.
DR EMBL; AY059827; AAL24309.1; -; mRNA.
DR EMBL; AY064652; AAL47363.1; -; mRNA.
DR EMBL; BT008505; AAP37864.1; -; mRNA.
DR PIR; S69195; A59034.
DR RefSeq; NP_172327.1; NM_100724.3.
DR AlphaFoldDB; Q9SJE2; -.
DR SMR; Q9SJE2; -.
DR STRING; 3702.AT1G08510.1; -.
DR PaxDb; Q9SJE2; -.
DR PRIDE; Q9SJE2; -.
DR ProteomicsDB; 230797; -.
DR EnsemblPlants; AT1G08510.1; AT1G08510.1; AT1G08510.
DR GeneID; 837372; -.
DR Gramene; AT1G08510.1; AT1G08510.1; AT1G08510.
DR KEGG; ath:AT1G08510; -.
DR Araport; AT1G08510; -.
DR TAIR; locus:2201786; AT1G08510.
DR eggNOG; ENOG502QQHW; Eukaryota.
DR HOGENOM; CLU_045466_0_0_1; -.
DR InParanoid; Q9SJE2; -.
DR OMA; WILEVVI; -.
DR OrthoDB; 602729at2759; -.
DR PhylomeDB; Q9SJE2; -.
DR BioCyc; ARA:AT1G08510-MON; -.
DR BioCyc; MetaCyc:AT1G08510-MON; -.
DR BRENDA; 3.1.2.14; 399.
DR PRO; PR:Q9SJE2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SJE2; baseline and differential.
DR Genevisible; Q9SJE2; AT.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; TAS:TAIR.
DR GO; GO:0000036; F:acyl carrier activity; IDA:TAIR.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IDA:TAIR.
DR GO; GO:0016296; F:palmitoyl-[acyl-carrier-protein] hydrolase activity; IEA:RHEA.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IMP:TAIR.
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..49
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 50..412
FT /note="Palmitoyl-acyl carrier protein thioesterase,
FT chloroplastic"
FT /id="PRO_0000418155"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /evidence="ECO:0000255"
FT ACT_SITE 317
FT /evidence="ECO:0000255"
FT ACT_SITE 352
FT /evidence="ECO:0000255"
FT MUTAGEN 259
FT /note="R->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15531590"
FT MUTAGEN 315
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15531590"
FT MUTAGEN 320
FT /note="N->Y: No effect on activity."
FT /evidence="ECO:0000269|PubMed:15531590"
FT CONFLICT 38
FT /note="A -> T (in Ref. 1; CAA85388)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="K -> R (in Ref. 1; CAA85387/CAA85388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 45687 MW; 8BE5A4AB3884D2B4 CRC64;
MVATSATSSF FPVPSSSLDP NGKGNKIGST NLAGLNSAPN SGRMKVKPNA QAPPKINGKK
VGLPGSVDIV RTDTETSSHP APRTFINQLP DWSMLLAAIT TIFLAAEKQW MMLDWKPRRS
DMLVDPFGIG RIVQDGLVFR QNFSIRSYEI GADRSASIET VMNHLQETAL NHVKTAGLLG
DGFGSTPEMF KKNLIWVVTR MQVVVDKYPT WGDVVEVDTW VSQSGKNGMR RDWLVRDCNT
GETLTRASSV WVMMNKLTRR LSKIPEEVRG EIEPYFVNSD PVLAEDSRKL TKIDDKTADY
VRSGLTPRWS DLDVNQHVNN VKYIGWILES APVGIMERQK LKSMTLEYRR ECGRDSVLQS
LTAVTGCDIG NLATAGDVEC QHLLRLQDGA EVVRGRTEWS SKTPTTTWGT AP
