THIC1_ARATH
ID THIC1_ARATH Reviewed; 403 AA.
AC Q8S4Y1; Q93YW6; Q9LUB1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Acetyl-CoA acetyltransferase, cytosolic 1;
DE EC=2.3.1.9;
DE AltName: Full=Cytosolic acetoacetyl-CoA thiolase 1;
DE Short=Thiolase 1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1276;
GN Name=AAT1; Synonyms=EMB1276; OrderedLocusNames=At5g48230;
GN ORFNames=MIF21.12;
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] (ISOFORM 1).
RA Ahumada I., Boronat A., Campos N.;
RT "Arabidopsis thaliana mRNA encoding cytosolic acetoacetyl-CoA thiolase, the
RT first enzyme of the mevalonate pathway for isoprenoid biosynthesis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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] (ISOFORM 2).
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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT peptides, metabolic pathways, and defense mechanisms.";
RL Plant Cell 19:3170-3193(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036,
CC ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S4Y1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S4Y1-2; Sequence=VSP_015461;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF364059; AAM00280.1; -; mRNA.
DR EMBL; AB023039; BAA97003.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95638.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95639.1; -; Genomic_DNA.
DR EMBL; AY059736; AAL24148.1; -; mRNA.
DR EMBL; AY091271; AAM14210.1; -; mRNA.
DR RefSeq; NP_568694.2; NM_124198.4. [Q8S4Y1-1]
DR RefSeq; NP_851154.1; NM_180823.3. [Q8S4Y1-2]
DR AlphaFoldDB; Q8S4Y1; -.
DR SMR; Q8S4Y1; -.
DR BioGRID; 20123; 6.
DR IntAct; Q8S4Y1; 1.
DR STRING; 3702.AT5G48230.2; -.
DR PaxDb; Q8S4Y1; -.
DR PRIDE; Q8S4Y1; -.
DR ProteomicsDB; 246414; -. [Q8S4Y1-1]
DR EnsemblPlants; AT5G48230.1; AT5G48230.1; AT5G48230. [Q8S4Y1-2]
DR EnsemblPlants; AT5G48230.2; AT5G48230.2; AT5G48230. [Q8S4Y1-1]
DR GeneID; 834876; -.
DR Gramene; AT5G48230.1; AT5G48230.1; AT5G48230. [Q8S4Y1-2]
DR Gramene; AT5G48230.2; AT5G48230.2; AT5G48230. [Q8S4Y1-1]
DR KEGG; ath:AT5G48230; -.
DR Araport; AT5G48230; -.
DR TAIR; locus:2164778; AT5G48230.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_0_0_1; -.
DR InParanoid; Q8S4Y1; -.
DR OMA; ICPSIAI; -.
DR PhylomeDB; Q8S4Y1; -.
DR BRENDA; 2.3.1.9; 399.
DR UniPathway; UPA00058; UER00101.
DR PRO; PR:Q8S4Y1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8S4Y1; baseline and differential.
DR Genevisible; Q8S4Y1; AT.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009846; P:pollen germination; IMP:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0016125; P:sterol metabolic process; IMP:TAIR.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
DR PROSITE; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Isoprene biosynthesis;
KW Metal-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..403
FT /note="Acetyl-CoA acetyltransferase, cytosolic 1"
FT /id="PRO_0000206411"
FT ACT_SITE 97
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 359
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 389
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT BINDING 232..234
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..11
FT /note="MAHTSESVNPR -> MNVDES (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_015461"
SQ SEQUENCE 403 AA; 41412 MW; 113A349257F7FC98 CRC64;
MAHTSESVNP RDVCIVGVAR TPMGGFLGSL SSLPATKLGS LAIAAALKRA NVDPALVQEV
VFGNVLSANL GQAPARQAAL GAGIPNSVIC TTVNKVCASG MKAVMIAAQS IQLGINDVVV
AGGMESMSNT PKYLAEARKG SRFGHDSLVD GMLKDGLWDV YNDCGMGSCA ELCAEKFQIT
REQQDDYAVQ SFERGIAAQE AGAFTWEIVP VEVSGGRGRP STIVDKDEGL GKFDAAKLRK
LRPSFKENGG TVTAGNASSI SDGAAALVLV SGEKALQLGL LVLAKIKGYG DAAQEPEFFT
TAPALAIPKA IAHAGLESSQ VDYYEINEAF AVVALANQKL LGIAPEKVNV NGGAVSLGHP
LGCSGARILI TLLGILKKRN GKYGVGGVCN GGGGASALVL ELL
