ID A0A1Y2W0V4_9PEZI Unreviewed; 458 AA.
AC A0A1Y2W0V4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=M426DRAFT_321642 {ECO:0000313|EMBL:OTB03492.1};
OS Hypoxylon sp. CI-4A.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Hypoxylaceae; Hypoxylon.
OX NCBI_TaxID=1001833 {ECO:0000313|EMBL:OTB03492.1, ECO:0000313|Proteomes:UP000242955};
RN [1] {ECO:0000313|EMBL:OTB03492.1, ECO:0000313|Proteomes:UP000242955}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CI-4A {ECO:0000313|EMBL:OTB03492.1,
RC ECO:0000313|Proteomes:UP000242955};
RX PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA Henrissat B., Gladden J.M.;
RT "Characterization of four endophytic fungi as potential consolidated
RT bioprocessing hosts for conversion of lignocellulose into advanced
RT biofuels.";
RL Appl. Microbiol. Biotechnol. 101:2603-2618(2017).
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}.
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DR EMBL; KZ111558; OTB03492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2W0V4; -.
DR STRING; 1001833.A0A1Y2W0V4; -.
DR InParanoid; A0A1Y2W0V4; -.
DR OrthoDB; 1799125at2759; -.
DR Proteomes; UP000242955; 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:UP000242955};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 9..231
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 276..365
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 458 AA; 49487 MW; 7DAA15D399A876C8 CRC64;
MPAKQKQPVY ILGVGMTKFI KPRGKVDYTE LGFEAGVKAM LDAQITYDDV EQGVACYCYG
DSTCGQRVFY QFGMTQIPIL NVNNNCSTGS TGLFMARNTI AYGGADCVLV VGFEKMMPGS
LNSFFNDREN PLGTTHKMMV ETRGFEKGPG AAQMFGNAGR EYMEKFGAKL EDFAEIARIN
HAHSTKNPYS QFQDVYTLDQ IQKAPMIHSP LTKLQCCPTS DGGAAAVLVS QDFLDARPHL
RDRAILIAGQ SLATDSPSLF SRSAIDLVGF EMTRRAAETA CEEAGVRPED AQVVELHDCF
SANELVTLDG LGLCAPGKAH EMVRAGDITY GGKFVVNPSG GLISKGHPLG ATGIAQAAEL
VWHLRGWANN RAAPRTRYGL QHNLGLGGAA VVSVYCRPDR SVAPLLSDAE IGSRNGLGYN
PAVEAKGFTK QQCGAVLSRN ASSDWARQDT ERKVEARF
//
