ID G3J9Z3_CORMM Unreviewed; 457 AA.
AC G3J9Z3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=CCM_02487 {ECO:0000313|EMBL:EGX94216.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX94216.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX94216.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX94216.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126400; EGX94216.1; -; Genomic_DNA.
DR RefSeq; XP_006667702.1; XM_006667639.1.
DR AlphaFoldDB; G3J9Z3; -.
DR STRING; 983644.G3J9Z3; -.
DR GeneID; 18164514; -.
DR KEGG; cmt:CCM_02487; -.
DR VEuPathDB; FungiDB:CCM_02487; -.
DR eggNOG; KOG1406; Eukaryota.
DR HOGENOM; CLU_035425_0_1_1; -.
DR InParanoid; G3J9Z3; -.
DR OMA; PSLYAMM; -.
DR OrthoDB; 1799125at2759; -.
DR Proteomes; UP000001610; 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:UP000001610};
KW Transferase {ECO:0000256|RuleBase:RU003557};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 8..230
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 273..364
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 457 AA; 49029 MW; AD1DBB7EAE552DE9 CRC64;
MPRPLAPVYI LGVGMTKFIK PRGNVDYTEL GFEAGVKALL DAHITYDDVD QGVACYCYGD
STCGQRVFYQ FGMTKVPIYN VNNNCATGST GLAMGRTFVA SGAADCVLVV GFEKMMAGSL
QSFFNDRENP LGTTVNMMVE TRGFEPAPGA PQMFGNGGRE YKEKFGATNE DFAEIARVNH
AHSPNNPYSQ FQQVYTQEQI LKSPMIFDPL TKLQCCPTSD GGAAAVLVSQ EFLDARPHLK
SQAVLIAGQC LATDAPSLFS KSSIDLLGFE MTQYAKDVAF KQAGITAADV KVVELHDCFS
ANEMLVLDAL GLCEHGKAHE MVRRGDITYG GKYLVNPSGG LISKGHPLGA TGIAQAAELV
WHLRGWANNR EVPDTKYALQ HNLGLGGAVV VSVLARADGK AAPKLSNQEV GKINGLGYNP
ATEAKGFTAA QATSVRSKKH SSAWALQDTE EKVTANF
//
