GenomeNet

Database: UniProt
Entry: G2WT47_VERDV
LinkDB: G2WT47_VERDV
Original site: G2WT47_VERDV 
ID   G2WT47_VERDV            Unreviewed;       400 AA.
AC   G2WT47;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE            EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN   ORFNames=VDAG_00970 {ECO:0000313|EMBL:EGY17288.1};
OS   Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS   (Verticillium wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY17288.1, ECO:0000313|Proteomes:UP000001611};
RN   [1] {ECO:0000313|Proteomes:UP000001611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC   {ECO:0000313|Proteomes:UP000001611};
RX   PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA   Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA   Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA   Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA   Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA   Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA   Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT   "Comparative genomics yields insights into niche adaptation of plant
RT   vascular wilt pathogens.";
RL   PLoS Pathog. 7:E1002137-E1002137(2011).
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC       biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00037924}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC       {ECO:0000256|ARBA:ARBA00010982, ECO:0000256|RuleBase:RU003557}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DS572696; EGY17288.1; -; Genomic_DNA.
DR   RefSeq; XP_009648151.1; XM_009649856.1.
DR   AlphaFoldDB; G2WT47; -.
DR   STRING; 498257.G2WT47; -.
DR   EnsemblFungi; EGY17288; EGY17288; VDAG_00970.
DR   GeneID; 20702433; -.
DR   KEGG; vda:VDAG_00970; -.
DR   eggNOG; KOG1390; Eukaryota.
DR   HOGENOM; CLU_031026_0_1_1; -.
DR   InParanoid; G2WT47; -.
DR   OMA; ICPSIAI; -.
DR   OrthoDB; 5481312at2759; -.
DR   Proteomes; UP000001611; Chromosome 1.
DR   GO; GO:0003988; F:acetyl-CoA C-acyltransferase activity; IEA:UniProtKB-EC.
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; 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; PTHR18919:SF171; ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC; 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.
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:UP000001611};
KW   Transferase {ECO:0000256|RuleBase:RU003557}.
FT   DOMAIN          7..268
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          277..397
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
FT   ACT_SITE        92
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        355
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
FT   ACT_SITE        385
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000429-1"
SQ   SEQUENCE   400 AA;  41372 MW;  E2608F10598544E9 CRC64;
     MANLPSVYIV SAARTPVGSF LGSLSSLSAV DLGAHAIKAA VERVPEIKPE DVEEVFYGNV
     LSANLGQAPA RQCAIGAGLS QGVVATTVNK VCASGLKAII LGAQTIITGN ASIVVAGGTE
     SMSNVPHYLP TLRNGAKYGH QTLVDGVLQD GLTDAYGKKE HMGMQGELCA QDHSITREEQ
     DAYAIQTYKR AQAATEAGVF AKEITPVEVS GGRGKPNVKV DRDDEVKNLN EAKLKAMRPA
     FQPNGGTITA PNAAPINDGA AAVVLMSEAK VKELGVTPIA KIRGWGDAAR EPERFTIAPT
     LAIPKAIAHA GLTADDVDFY EINEAFSVVA LANMKILGLS DDKVNVFGGS VAIGHPLGCS
     GARIVTTLTT VLREKKAKIG VAGICNGGGG ASALVIENLQ
//
DBGET integrated database retrieval system