THIC2_ARATH
ID THIC2_ARATH Reviewed; 415 AA.
AC Q9FIK7; Q3E710; Q3E8F1;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Probable acetyl-CoA acetyltransferase, cytosolic 2;
DE EC=2.3.1.9;
DE AltName: Full=Cytosolic acetoacetyl-CoA thiolase 2;
DE Short=Thiolase 2;
GN OrderedLocusNames=At5g47720; ORFNames=MCA23.4;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
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] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FIK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FIK7-2; Sequence=VSP_018140;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000305}.
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DR EMBL; AB016886; BAB11319.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95558.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95559.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95560.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95561.1; -; Genomic_DNA.
DR EMBL; AY088740; AAM67058.1; -; mRNA.
DR RefSeq; NP_199583.1; NM_124146.3. [Q9FIK7-1]
DR RefSeq; NP_851150.1; NM_180819.3. [Q9FIK7-2]
DR RefSeq; NP_974900.1; NM_203171.2. [Q9FIK7-2]
DR RefSeq; NP_974901.2; NM_203172.4. [Q9FIK7-1]
DR AlphaFoldDB; Q9FIK7; -.
DR SMR; Q9FIK7; -.
DR BioGRID; 20071; 2.
DR STRING; 3702.AT5G47720.4; -.
DR PaxDb; Q9FIK7; -.
DR PRIDE; Q9FIK7; -.
DR ProteomicsDB; 234342; -. [Q9FIK7-1]
DR EnsemblPlants; AT5G47720.1; AT5G47720.1; AT5G47720. [Q9FIK7-2]
DR EnsemblPlants; AT5G47720.2; AT5G47720.2; AT5G47720. [Q9FIK7-1]
DR EnsemblPlants; AT5G47720.3; AT5G47720.3; AT5G47720. [Q9FIK7-2]
DR EnsemblPlants; AT5G47720.4; AT5G47720.4; AT5G47720. [Q9FIK7-1]
DR GeneID; 834823; -.
DR Gramene; AT5G47720.1; AT5G47720.1; AT5G47720. [Q9FIK7-2]
DR Gramene; AT5G47720.2; AT5G47720.2; AT5G47720. [Q9FIK7-1]
DR Gramene; AT5G47720.3; AT5G47720.3; AT5G47720. [Q9FIK7-2]
DR Gramene; AT5G47720.4; AT5G47720.4; AT5G47720. [Q9FIK7-1]
DR KEGG; ath:AT5G47720; -.
DR Araport; AT5G47720; -.
DR TAIR; locus:2160887; AT5G47720.
DR eggNOG; KOG1390; Eukaryota.
DR InParanoid; Q9FIK7; -.
DR OMA; TNVCCTT; -.
DR PhylomeDB; Q9FIK7; -.
DR BRENDA; 2.3.1.9; 399.
DR PRO; PR:Q9FIK7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FIK7; baseline and differential.
DR Genevisible; Q9FIK7; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
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; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Cytoplasm; Metal-binding; Potassium;
KW Reference proteome; Transferase.
FT CHAIN 1..415
FT /note="Probable acetyl-CoA acetyltransferase, cytosolic 2"
FT /id="PRO_0000206412"
FT ACT_SITE 99
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10020"
FT BINDING 234..236
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 239
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 256
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 259
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250"
FT VAR_SEQ 406..415
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_018140"
SQ SEQUENCE 415 AA; 43292 MW; 04098F25AB18482A CRC64;
MAPPVSDDSL QPRDVCVVGV ARTPIGDFLG SLSSLTATRL GSIAIQAALK RAHVDPALVE
EVFFGNVLTA NLGQAPARQA ALGAGIPYSV ICTTINKVCA AGMKSVMLAS QSIQLGLNDI
VVAGGMESMS NVPKYLPDAR RGSRLGHDTV VDGMMKDGLW DVYNDFGMGV CGEICADQYR
ITREEQDAYA IQSFERGIAA QNTQLFAWEI VPVEVSTGRG RPSVVIDKDE GLGKFDAAKL
KKLRPSFKED GGSVTAGNAS SISDGAAALV LVSGEKALEL GLHVIAKIRG YADAAQAPEL
FTTTPALAIP KAIKRAGLDA SQVDYYEINE AFSVVALANQ KLLGLDPERL NAHGGAVSLG
HPLGCSGARI LVTLLGVLRA KKGKYGVASI CNGGGGASAL VLEFMSEKTI GYSAL
