ID E4ZSK9_LEPMJ Unreviewed; 795 AA.
AC E4ZSK9;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=LEMA_P121530.1 {ECO:0000313|EMBL:CBX94389.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA;
CC Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000617};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000256|ARBA:ARBA00004872}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
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DR EMBL; FP929122; CBX94389.1; -; Genomic_DNA.
DR RefSeq; XP_003837833.1; XM_003837785.1.
DR AlphaFoldDB; E4ZSK9; -.
DR STRING; 985895.E4ZSK9; -.
DR EnsemblFungi; CBX94389; CBX94389; LEMA_P121530.1.
DR GeneID; 13290924; -.
DR eggNOG; KOG1389; Eukaryota.
DR eggNOG; KOG3294; Eukaryota.
DR HOGENOM; CLU_353385_0_0_1; -.
DR InParanoid; E4ZSK9; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR CDD; cd13214; PH-GRAM_WBP2; 1.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020610; Thiolase_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020613; Thiolase_CS.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR43853; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR PANTHER; PTHR43853:SF8; 3-KETOACYL-COA THIOLASE, PEROXISOMAL; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 410..665
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 674..791
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT REGION 204..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 795 AA; 84693 MW; 1D773CBDF9AEDFBB CRC64;
MGRAKEDVKK FKANGRNSWV MLAESGGYTP LPGEQTLYQS PPRTTLSLQT SHGHAPAESY
SQQCKSGVIY LTNRRANKSV QLIYLPISPT PTLQSFAVPI LNVIDSRVTA PWFGANKWEA
VVQPVPGGGI PPQHAELELV MEFKEGGAFD FASIFERLKE RLRQAVDVAR ETGAHVVDSR
TGTAAPLDMN TVHLDDLPAY EDSGRHERVS VADAPDPPVL AAPVPQSPAV RHASVERSPP
RQDRFQAPAP PNEAPPGYEE VQRGSIADEL ERQMRDSRTR GDEDEEGEAS PSHPGAGQTS
AKEEIASVKR LVAWVHQLST SSAALCLCLS SITVLFAFWL SACTLVVEKW ISWLTRHRVK
ECMDGEEADE LYTVQERLTQ VEAHLTGSSA KSGAGIKGKA GMLEKHDDDV VVTCALRTPF
TKGGKGGFKD TQASDLLHGA FKALIQRSGI DPSLVEDIAV GAVLAPGGGA TEFRAAALAA
GFPVTTAVKS LNRQCSSGLQ ACVDIANAIK SGMIEVGIGA GAESMSTQYG PNAVSEFSEL
LDSHPEAKNC KVPMGVLSEQ MAKAKGIPRS EQDKFAASSF QKAVAAQKQG LFDEEIAPLT
VKWTDPKTDE TKTITVSQDD GIRPNITAES LSKIRPAFSK DGSIHAGNAS QISDGAAAVL
LMKRSTARRL GQPIIGKFVQ ASIVGVPPLL MGVGPAAAIP VVLEKTGLSK ADVDIFEINE
AFASQCLYCI NELGIEQEKI NPKGGAIAFG HPLGVTGARQ VSTLLTELKR RGEKVGVTSM
CIGTGMGMAA VWVAE
//
