ID A0A1B8D6W5_9PEZI Unreviewed; 408 AA.
AC A0A1B8D6W5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=acetyl-CoA C-acyltransferase {ECO:0000256|ARBA:ARBA00024073};
DE EC=2.3.1.16 {ECO:0000256|ARBA:ARBA00024073};
GN ORFNames=VE04_04890 {ECO:0000313|EMBL:OBT54897.1};
OS Pseudogymnoascus sp. 24MN13.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622150 {ECO:0000313|EMBL:OBT54897.1, ECO:0000313|Proteomes:UP000092157};
RN [1] {ECO:0000313|EMBL:OBT54897.1, ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|EMBL:OBT54897.1,
RC ECO:0000313|Proteomes:UP000092157};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|Proteomes:UP000092157};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00001958};
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; KV456248; OBT54897.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8D6W5; -.
DR STRING; 1622150.A0A1B8D6W5; -.
DR Proteomes; UP000092157; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:SF12; ACETYL-COA C-ACETYLTRANSFERASE; 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:UP000092157};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 22..277
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 287..404
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 106
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 363
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 408 AA; 42918 MW; 3F1EAC9A11E3B6FD CRC64;
MGHLGSPADG KARLLQKNPD DIVITLAIRT PLTKARKGGL KDTPIDDLLI AILTQVREKS
KLEPSLVEDV CVGNCLGSGQ AYVARSAVLA AGFPITTAAS IVNRFCSSGL LAIQGIANQI
SAGSIDVGVA VGAESMSTTP DGGAPKMSDK IMNHPIASQN QMSMGYTSEE VAGQFDVSRQ
AMDQFAAESY QKAEKAQKEG WFDDEITPII VTIKDPKTGE AKQVTVSKDD GIRYGTTAES
LGKIRNAFPQ WKPSRTTGGN ASQITDGAAA VLLMKRSRAI ELGQPIVGKF AGSTVVGLEP
RIMGIGPSYA IPKILGKVGL AKEDIDVFEI NEAFASMGVY CVEKLALDKA KVNPRGGAIA
LGHPLGCTGT RQVVTALSEL RRQDKRIAVT SMCVGTGMGM AGIFVSEH
//
