ID A1CWK1_NEOFI Unreviewed; 419 AA.
AC A1CWK1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=NFIA_104910 {ECO:0000313|EMBL:EAW25003.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW25003.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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DR EMBL; DS027685; EAW25003.1; -; Genomic_DNA.
DR RefSeq; XP_001266900.1; XM_001266899.1.
DR AlphaFoldDB; A1CWK1; -.
DR STRING; 331117.A1CWK1; -.
DR EnsemblFungi; EAW25003; EAW25003; NFIA_104910.
DR GeneID; 4593854; -.
DR KEGG; nfi:NFIA_104910; -.
DR VEuPathDB; FungiDB:NFIA_104910; -.
DR eggNOG; KOG1389; Eukaryota.
DR HOGENOM; CLU_031026_1_1_1; -.
DR OMA; MTAFPEP; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000006702; 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:UP000006702};
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; 43520 MW; 8CA35E1CE7DE6ECD CRC64;
MSSAQQRLSQ VSSHFTSGGK KGVAAITEKH PDDIVVTCAL RTALTKGGKG GFKDTAAADL
LAGVFKGVID RSGIDPKVVE DVAVGSVLAP GGGATEFRAA ALVAGFPEST AVKSLNRQCS
SGLQAIVDMA NAIKSGMIEV GIGAGVESMS SQYGPGAVTE FSELLESHPE SANCKVPMGV
LSEQMAKDRN ISRAVQDAFA ASSYQKAVKA QKAGLFNEEI VPLQVKWTDP KTGEEKTITV
KADDGIRDGI TPESLGKIRP AFAKDGSIHA GNASQISDGA AAVLLMKRST AERLGQKIIG
KYVAASVVGV KPLLMGIGPW KAIPVALEKA GITKDEVDIY EINEAFASQC VWCVNELGLP
HEKINPKGGA IAFGHPLGCT GARQISTLLT ELKRTNKKVG VTSMCVGTGM GMAAVWVAE
//
