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Database: UniProt
Entry: K9F6N9_PEND2
LinkDB: K9F6N9_PEND2
Original site: K9F6N9_PEND2 
ID   K9F6N9_PEND2            Unreviewed;       419 AA.
AC   K9F6N9;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE            EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN   ORFNames=PDIG_87260 {ECO:0000313|EMBL:EKV04734.1};
OS   Penicillium digitatum (strain PHI26 / CECT 20796) (Green mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1170229 {ECO:0000313|EMBL:EKV04734.1, ECO:0000313|Proteomes:UP000009882};
RN   [1] {ECO:0000313|Proteomes:UP000009882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI26 / CECT 20796 {ECO:0000313|Proteomes:UP000009882};
RX   PubMed=23171342; DOI=10.1186/1471-2164-13-646;
RA   Marcet-Houben M., Ballester A.-R., de la Fuente B., Harries E.,
RA   Marcos J.F., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome sequence of the necrotrophic fungus Penicillium digitatum, the main
RT   postharvest pathogen of citrus.";
RL   BMC Genomics 13:646-646(2012).
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, 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:EKV04734.1}.
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DR   EMBL; AKCT01000320; EKV04734.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9F6N9; -.
DR   STRING; 1170229.K9F6N9; -.
DR   eggNOG; KOG1389; Eukaryota.
DR   HOGENOM; CLU_031026_1_1_1; -.
DR   InParanoid; K9F6N9; -.
DR   OMA; MTAFPEP; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000009882; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd00751; thiolase; 1.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR002155; Thiolase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
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   PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW   Potassium {ECO:0000256|ARBA:ARBA00022958};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009882};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          34..289
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          297..415
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        119
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        375
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        405
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   419 AA;  43160 MW;  45506487E78E2461 CRC64;
     MSNAQQRLNQ VSSHLSLGGK KGAAAILEKH PDDIVVTCAL RTALTKGGKG GFKDTAGADL
     LAGVFKAILN KSGIDPSAVQ DIAVGSVLAP GGGATEFRAA ALVAGFPEST AVKSLNRQCS
     SGLQAIADIA NAIQSGMIDV GIGAGVESMS SQYGPGAVTE FSDLLESHPE SANCKVPMGV
     LSENMAKDRG VTRASQDAFA ARSYQKALAA QKAGLFDEEI APLDVKWTDP KTGEEKTITV
     KADDGIRPGI TAESLGKIKP AFAKDGSIHA GNASQISDGA AAVLLMKRST AERLGQTILG
     KYVAASVVGV KPLLMGIGPW KAIPVALEKA GITKDDVDIY EINEAFASQC VWCVHELGIP
     AEKVNPKGGA IAFGHPLGCT GARQVSTLFT ELKRTSKKIG VTSMCIGTGM GMAAVWVSE
//
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