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Acetyl-CoA acetyltransferase, cytosolic 1 (EC 2.3.1.9) (Cytosolic acetoacetyl-CoA thiolase 1) (Thiolase 1) (Protein EMBRYO DEFECTIVE 1276)

 THIC1_ARATH             Reviewed;         403 AA.
Q8S4Y1; Q93YW6; Q9LUB1;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
25-APR-2018, entry version 116.
RecName: Full=Acetyl-CoA acetyltransferase, cytosolic 1;
EC=2.3.1.9;
AltName: Full=Cytosolic acetoacetyl-CoA thiolase 1;
Short=Thiolase 1;
AltName: Full=Protein EMBRYO DEFECTIVE 1276;
Name=AAT1; Synonyms=EMB1276; OrderedLocusNames=At5g48230;
ORFNames=MIF21.12;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Ahumada I., Boronat A., Campos N.;
"Arabidopsis thaliana mRNA encoding cytosolic acetoacetyl-CoA
thiolase, the first enzyme of the mevalonate pathway for isoprenoid
biosynthesis.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17951448; DOI=10.1105/tpc.107.050989;
Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T.,
Antonicelli G.E., Rasche N., Lueder F., Weckwerth W., Jahn O.;
"Proteome analysis of Arabidopsis leaf peroxisomes reveals novel
targeting peptides, metabolic pathways, and defense mechanisms.";
Plant Cell 19:3170-3193(2007).
-!- CATALYTIC ACTIVITY: 2 acetyl-CoA = CoA + acetoacetyl-CoA.
{ECO:0000255|PROSITE-ProRule:PRU10020}.
-!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8S4Y1-1; Sequence=Displayed;
Name=2;
IsoId=Q8S4Y1-2; Sequence=VSP_015461;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
-!- SIMILARITY: Belongs to the thiolase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA97003.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF364059; AAM00280.1; -; mRNA.
EMBL; AB023039; BAA97003.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002688; AED95638.1; -; Genomic_DNA.
EMBL; CP002688; AED95639.1; -; Genomic_DNA.
EMBL; AY059736; AAL24148.1; -; mRNA.
EMBL; AY091271; AAM14210.1; -; mRNA.
RefSeq; NP_568694.2; NM_124198.4. [Q8S4Y1-1]
RefSeq; NP_851154.1; NM_180823.3. [Q8S4Y1-2]
UniGene; At.24167; -.
UniGene; At.49143; -.
ProteinModelPortal; Q8S4Y1; -.
SMR; Q8S4Y1; -.
BioGrid; 20123; 4.
IntAct; Q8S4Y1; 1.
STRING; 3702.AT5G48230.2; -.
PaxDb; Q8S4Y1; -.
PRIDE; Q8S4Y1; -.
EnsemblPlants; AT5G48230.1; AT5G48230.1; AT5G48230. [Q8S4Y1-2]
EnsemblPlants; AT5G48230.2; AT5G48230.2; AT5G48230. [Q8S4Y1-1]
GeneID; 834876; -.
Gramene; AT5G48230.1; AT5G48230.1; AT5G48230. [Q8S4Y1-2]
Gramene; AT5G48230.2; AT5G48230.2; AT5G48230. [Q8S4Y1-1]
KEGG; ath:AT5G48230; -.
Araport; AT5G48230; -.
TAIR; locus:2164778; AT5G48230.
eggNOG; KOG1390; Eukaryota.
eggNOG; COG0183; LUCA.
HOGENOM; HOG000012238; -.
InParanoid; Q8S4Y1; -.
KO; K00626; -.
OMA; WDVYNKF; -.
OrthoDB; EOG09360EGX; -.
PhylomeDB; Q8S4Y1; -.
BRENDA; 2.3.1.9; 399.
Reactome; R-ATH-70895; Branched-chain amino acid catabolism.
Reactome; R-ATH-77108; Utilization of Ketone Bodies.
Reactome; R-ATH-77111; Synthesis of Ketone Bodies.
UniPathway; UPA00058; UER00101.
PRO; PR:Q8S4Y1; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q8S4Y1; baseline and differential.
Genevisible; Q8S4Y1; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005777; C:peroxisome; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IDA:TAIR.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006635; P:fatty acid beta-oxidation; IBA:GO_Central.
GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009846; P:pollen germination; IMP:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0016125; P:sterol metabolic process; IMP:TAIR.
CDD; cd00751; thiolase; 1.
Gene3D; 3.40.47.10; -; 4.
InterPro; IPR002155; Thiolase.
InterPro; IPR016039; Thiolase-like.
InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
InterPro; IPR020610; Thiolase_AS.
InterPro; IPR020617; Thiolase_C.
InterPro; IPR020613; Thiolase_CS.
InterPro; IPR020616; Thiolase_N.
Pfam; PF02803; Thiolase_C; 1.
Pfam; PF00108; Thiolase_N; 1.
PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
SUPFAM; SSF53901; SSF53901; 2.
TIGRFAMs; TIGR01930; AcCoA-C-Actrans; 1.
PROSITE; PS00098; THIOLASE_1; 1.
PROSITE; PS00737; THIOLASE_2; 1.
PROSITE; PS00099; THIOLASE_3; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome; Cytoplasm;
Isoprene biosynthesis; Metal-binding; Potassium; Reference proteome;
Transferase.
CHAIN 1 403 Acetyl-CoA acetyltransferase, cytosolic
1.
/FTId=PRO_0000206411.
REGION 232 234 Coenzyme A binding. {ECO:0000250}.
ACT_SITE 97 97 Acyl-thioester intermediate.
{ECO:0000250}.
ACT_SITE 359 359 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
ACT_SITE 389 389 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10020}.
METAL 254 254 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 255 255 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 257 257 Potassium; via carbonyl oxygen.
{ECO:0000250}.
METAL 355 355 Potassium; via carbonyl oxygen.
{ECO:0000250}.
BINDING 237 237 Coenzyme A. {ECO:0000250}.
BINDING 258 258 Coenzyme A. {ECO:0000250}.
VAR_SEQ 1 11 MAHTSESVNPR -> MNVDES (in isoform 2).
{ECO:0000303|PubMed:14593172}.
/FTId=VSP_015461.
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


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