ID E3RS82_PYRTT Unreviewed; 433 AA.
AC E3RS82;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Acetyl-acetyltransferase protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PTT_11734 {ECO:0000313|EMBL:EFQ91414.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ91414.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ91414.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
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; GL534769; EFQ91414.1; -; Genomic_DNA.
DR RefSeq; XP_003300487.1; XM_003300439.1.
DR AlphaFoldDB; E3RS82; -.
DR STRING; 861557.E3RS82; -.
DR EnsemblFungi; EFQ91414; EFQ91414; PTT_11734.
DR KEGG; pte:PTT_11734; -.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_0_0_1; -.
DR OrthoDB; 5481312at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00751; thiolase; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR002155; Thiolase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR InterPro; IPR020617; Thiolase_C.
DR InterPro; IPR020616; Thiolase_N.
DR NCBIfam; TIGR01930; AcCoA-C-Actrans; 1.
DR PANTHER; PTHR18919:SF156; ACETYL-COA ACETYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR18919; ACETYL-COA C-ACYLTRANSFERASE; 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.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 41..297
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 308..427
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT ACT_SITE 123
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 386
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT ACT_SITE 414
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ SEQUENCE 433 AA; 45815 MW; 7BC677F5EED29E1B CRC64;
MSSAAIRASM RMASRPQQRL ASIQRQFSSS SPQRKEIRDA YIISASRTPT AFNGNFTTVS
ATQLGATAIK SALDKSKVPI SSIDAVYMGN VLSAGVGQAP ARQAAIFAGL PTNIEATTIN
KVCASGLKAV NIAASTIELG QAEAQVAGGM ENMTRVPYYL NRASQQPAFG HQKLQDGLIA
DGLWDVYNQI HMGNCAENTA KKYQVSRQDQ DDYAIETYKR AQQAYKDGLF KDEIVPVTVK
SKKGEVIISE DEQYNKLKLD KVSTLKPAFD KGPDASVTAA NSSPLSDGAS ALVLGSKEIA
QKYGKDSRVL AKVVTYADAS LDPIDFPVAP ASCVEKLLKQ SGLSKNDISI WEFNEAFAAV
IKANAKILGL GTDNVNPRGG AIALGHALGS SGSRILVTLL HQLEVGQYGA AVICNGGGAA
SGIIVQRVSA DQL
//
