ID   KAT1_PETHY              Reviewed;         462 AA.
AC   C8YNG6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   03-AUG-2022, entry version 40.
DE   RecName: Full=3-ketoacyl CoA thiolase 1, peroxisomal {ECO:0000303|PubMed:19659733};
DE            Short=PhKAT1 {ECO:0000303|PubMed:19659733};
DE            EC=2.3.1.16;
DE   Flags: Precursor;
GN   Name=KAT1 {ECO:0000303|PubMed:19659733};
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC
RP   ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Mitchell;
RX   PubMed=19659733; DOI=10.1111/j.1365-313x.2009.03953.x;
RA   Van Moerkercke A., Schauvinhold I., Pichersky E., Haring M.A.,
RA   Schuurink R.C.;
RT   "A plant thiolase involved in benzoic acid biosynthesis and volatile
RT   benzenoid production.";
RL   Plant J. 60:292-302(2009).
CC   -!- FUNCTION: Component of the floral volatile benzenoid/phenylpropanoid
CC       (FVBP) biosynthetic pathway (PubMed:19659733). Thiolase that catalyzes
CC       the conversion of 3-oxo-3-phenylpropionyl-CoA (benzoylacetyl-CoA) to
CC       benzoyl-CoA (PubMed:19659733). {ECO:0000269|PubMed:19659733}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC         Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC         Evidence={ECO:0000269|PubMed:19659733};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:19659733}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q56WD9}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:19659733}.
CC   -!- DISRUPTION PHENOTYPE: Strongly reduced benzoic acid (BA) levels and
CC       lower benzenoid formation. {ECO:0000269|PubMed:19659733}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000305}.
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DR   EMBL; FJ657663; ACV70032.1; -; mRNA.
DR   AlphaFoldDB; C8YNG6; -.
DR   SMR; C8YNG6; -.
DR   UniPathway; UPA00199; -.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019438; P:aromatic compound biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:UniProtKB.
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   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; Peroxisome; Transferase; Transit peptide.
FT   TRANSIT         1..34
FT                   /note="Peroxisome"
FT                   /evidence="ECO:0000305"
FT   CHAIN           35..462
FT                   /note="3-ketoacyl CoA thiolase 1, peroxisomal"
FT                   /id="PRO_0000451518"
FT   ACT_SITE        138
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   ACT_SITE        393
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   ACT_SITE        425
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:I6XHI4"
SQ   SEQUENCE   462 AA;  48866 MW;  7CE59F50A71B8AD1 CRC64;
     MEKAIQRQRV LLEHLQPIRH HTHDHSSSLT TSICAAGDSA AYQRTAAFGD DVVIVAAYRT
     AICKSKRGGF KDTLSDDLLA PVLKAVIEKT NLDPKEVGDI VVGTVLAPGS IRAMECRMAA
     FYAGFPETVP IRTVNRQCSS GLQAVADVAA SIKAGFYDIG IGAGLELMTV DNIGRVQQRN
     TKVDTFAQAR DCLLPMGITS ENVAQRFGVT RLEQDQAAVN SHQRAAAATA SGKFKDEIIP
     VLTKIVDPQT GKEKPVVISV DDGIRPNTNL TSLGKLKPAF KNDGTTTAGN ASQVSDGAAA
     VLLMKRSVAM KKGLPILGVF RSFAAVGVDP AVMGIGPAVA IPPAVKSAGL DLDDIDLYEI
     NEAFASQFVY CQKKLNLDPE KVNVNGGAMA LGHPLGATGA RCVATLLHEM KRRGKDCRFG
     VISMCIGSGM GAAAVFERGD AVDDLCNARV SNNNSFLSKD AK