ID U9TQK2_RHIID Unreviewed; 220 AA.
AC U9TQK2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
DE Flags: Fragment;
GN ORFNames=GLOINDRAFT_202383 {ECO:0000313|EMBL:ESA09717.1};
OS Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194)
OS (Arbuscular mycorrhizal fungus) (Glomus intraradices).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=747089 {ECO:0000313|EMBL:ESA09717.1};
RN [1] {ECO:0000313|EMBL:ESA09717.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DAOM 197198 {ECO:0000313|EMBL:ESA09717.1};
RG DOE Joint Genome Institute;
RA Tisserant E., Malbreil M., Kuo A., Kohler A., Symeonidi A., Balestrini R.,
RA Charron P., Duensing N., Frei-dit-Frey N., Gianinazzi-Pearson V.,
RA Gilbert B., Handa Y., Hijri M., Kaul R., Kawaguchi M., Krajinski F.,
RA Lammers P., Lapierre D., Masclaux F.G., Murat C., Morin E., Ndikumana S.,
RA Pagni M., Petitpierre D., Requena N., Rosikiewicz P., Riley R., Saito K.,
RA San Clemente H., Shapiro H., van Tuinen D., Becard G., Bonfante P.,
RA Paszkowski U., Shachar-Hill Y., Young J.P., Sanders I.R., Henrissat B.,
RA Rensing S.A., Grigoriev I.V., Corradi N., Roux C., Martin F.;
RT "The genome of an arbuscular mycorrhizal fungus provides insights into the
RT evolution of the oldest plant symbiosis.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KI287802; ESA09717.1; -; Genomic_DNA.
DR AlphaFoldDB; U9TQK2; -.
DR eggNOG; KOG1390; Eukaryota.
DR HOGENOM; CLU_031026_3_0_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; 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 SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003557};
KW Transferase {ECO:0000256|RuleBase:RU003557}.
FT DOMAIN 2..87
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 97..218
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ESA09717.1"
SQ SEQUENCE 220 AA; 22765 MW; 02B9B1E26F07E2C6 CRC64;
KDDYAISSYQ RAQQAFADGV YENEIVPVTV SGGRGKPNKV ITQDDEISNL NVDKLRAVRP
AFTEKGSVTA PNSSPLSDGA AAIVLISGEK VKELGIKTLA KINGWGDAAQ TPSKFTTSPS
LAIPKALAHA GNIPISQVDY FEINEAFSVV ALANLKLLEL SKDKVNVFGG AVAMGHPLGC
SGARIICTLI SVLQNKNGKT GVASVCNGGG GASAIVISLQ
//
