ID A0A3S4AL90_9PEZI Unreviewed; 467 AA.
AC A0A3S4AL90;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=TT172_LOCUS2840 {ECO:0000313|EMBL:SPQ20421.1};
OS Thermothielavioides terrestris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothielavioides.
OX NCBI_TaxID=2587410 {ECO:0000313|EMBL:SPQ20421.1, ECO:0000313|Proteomes:UP000289323};
RN [1] {ECO:0000313|EMBL:SPQ20421.1, ECO:0000313|Proteomes:UP000289323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Huttner S., Dainat J.;
RL Submitted (APR-2018) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; OUUZ01000004; SPQ20421.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S4AL90; -.
DR Proteomes; UP000289323; 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 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 276..372
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 467 AA; 49985 MW; AF917215883BBFCC CRC64;
MAPKQKQACY VLGVGMTKFV KPRGKIDYTE LGYEAGIKAM LDAHITYDDV EQGIACYCYG
DSTCGQRVFY QFGMTQIPIY NVNNNCSTGS TGLAMARNMI AAGGADCILV VGFEKMMPGS
LQSFWNDRES PLGTTYAMMA ATRGVTKAPG AAQMFGNAGR EYMEKYGAKA EDFAEIARIN
HQHSVNNPYS QFQDVYTLDE ILASPMIHEP LTKLQCCPTS DGGAAAVLVS QAFLDARPHL
RGQAVLIAGQ CLATDGPSLF SRSAIDLVGR EMTQRAARVA MAEAGVTPAD FAVCELHDCF
SANEMVLLDA LGLAEPGKAH ELVRAGGITY GSGKGGRREL VVNPSGGLIS KGHPLGATGI
AQCAELVWHL RGWSNNRAVP GTKWALQHNL GLGGAAVVTV YRRADGQEAP VVDSAEVGRL
NGLGYNPAVE ARGFTEEQAR RVRSKDKTNE WARTATLPMM KAAQAKV
//
