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Database: UniProt
Entry: A0A0M8PGX9_9EURO
LinkDB: A0A0M8PGX9_9EURO
Original site: A0A0M8PGX9_9EURO 
ID   A0A0M8PGX9_9EURO        Unreviewed;       458 AA.
AC   A0A0M8PGX9;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00012352};
DE            EC=2.3.1.176 {ECO:0000256|ARBA:ARBA00012352};
DE   AltName: Full=Propanoyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00032316};
GN   ORFNames=ACN38_g582 {ECO:0000313|EMBL:KOS48434.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS48434.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS48434.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS48434.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOS48434.1}.
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DR   EMBL; LHQQ01000005; KOS48434.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8PGX9; -.
DR   STRING; 229535.A0A0M8PGX9; -.
DR   OrthoDB; 1799125at2759; -.
DR   Proteomes; UP000037696; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd00829; SCP-x_thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   PANTHER; PTHR42870; ACETYL-COA C-ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR42870:SF1; NON-SPECIFIC LIPID-TRANSFER PROTEIN-LIKE 2; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW   Transferase {ECO:0000256|RuleBase:RU003557};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          11..231
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          274..365
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   458 AA;  49176 MW;  1B35BEFB4078102F CRC64;
     MGKKQGTPAY VLGVGMTKFI KPRGKVDYHE LGYEAGIKAM LDAKINYDEV DQGVACYVYG
     DSTCGQRVFY QFGQTSIPIY NVNNNCSTGS TGLAMGRTLV SHGAADCVLV VGFEKMNPGS
     LQSMYNDREN PTGLFGTMMA ETRGVTNAPG AAQMFGNAGV EYKEKYGAKN EDFAEIARIN
     HEHSKRNPYS QFQTEYTLEQ IMKAPMIHEP LTKLQCCPTS DGGAAAVIVS QDFLDARPHL
     KEHAILIAGQ CLATDTDTVY SQSSIDLMGF GMSRQACRTA AAEAGVNVKD IKVCELHDCF
     SANEMITIDA LELCEPGQAH EMVRRGDITY GGKMVINPSG GLISKGHPLG ATGIAQCAEL
     VWHLRGWANN RLIDGTSAAL QHNLGLGGAV VVTVYKRTDG KVAAAVPSDV VGKINGLGYN
     PAVEAKGFTA EQAKSVVSKT HSSQYALSDT QERVVARF
//
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