ID A0A0S7E3X8_9EURO Unreviewed; 465 AA.
AC A0A0S7E3X8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ALT_009634 {ECO:0000313|EMBL:GIM44408.1};
OS Aspergillus lentulus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=293939 {ECO:0000313|EMBL:GIM44408.1};
RN [1] {ECO:0000313|EMBL:GIM44408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IFM 54703 {ECO:0000313|EMBL:GIM44408.1};
RA Kusuya Y., Sakai K., Kamei K., Takahashi H., Yaguchi T.;
RT "Draft Genome sequence of the pathogenic filamentous fungus Aspergillus
RT lentulus IFM 54703T.";
RL Genome Announc. 4:e01568-15(2016).
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:GIM44408.1}.
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DR EMBL; BCLY01000017; GIM44408.1; -; Genomic_DNA.
DR STRING; 293939.A0A0S7E3X8; -.
DR VEuPathDB; FungiDB:TMP_alenIFM54703_9880; -.
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}.
SQ SEQUENCE 465 AA; 50303 MW; 34DB63CACD1A6803 CRC64;
MAAETRGNAY VLGVGMAAFL KPRATRMYTE LAFEAGVKAM LDAHVTYDDV EAGVACYAFG
PTCSGQRAFY QFGMTEIPIY NVNNACATGS TGIYMARNLV RSGMHDCVLV VGFEQMNAGP
LVSTVTDRPT PFDLSMRLME ATRGADKTPK NPQMFGNAGR EYMERFGATA DDFAEIARIS
HEHSSRNPYA QFRTVYTLDE IRNAPMIYYP MTKLQCSPTS DGAAAAVIVS QRFLDARPEL
KDHAILIAGQ SMKSDSPSLY SGGAMDMVGY EMTRSATAAA LMDAKESIHD IKVCELHDCF
SANELISLDA MGFSQKGQAH QLVRSGDITY GGRGPIINPS GGLISKGHPL GATGLAQCAE
LVWQLRGWAN NGRLVANTRV ALQHNIGLGG AIVVTVYRRT DGRTNTASQP TEGEIANYSG
LGYNPAVEAR YVTRAQAESV RSKSARCDYA LDKTLDLIEG RRGKL
//
