ID A0A232FA77_9HYME Unreviewed; 908 AA.
AC A0A232FA77;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=TSAR_008725 {ECO:0000313|EMBL:OXU27380.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU27380.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU27380.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU27380.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU27380.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Thiolase family.
CC {ECO:0000256|ARBA:ARBA00010982}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXU27380.1}.
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DR EMBL; NNAY01000615; OXU27380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232FA77; -.
DR STRING; 543379.A0A232FA77; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
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; 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; PS00098; THIOLASE_1; 1.
DR PROSITE; PS00737; THIOLASE_2; 1.
DR PROSITE; PS00099; THIOLASE_3; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..908
FT /note="acetyl-CoA C-acetyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012104648"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 368..385
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 531..777
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 785..907
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 908 AA; 101319 MW; 63F9BCBB8E4F4E14 CRC64;
MHECKIRLLM LIFCTKYSTS AEWSHSVIGE IVNEIKPYEI LLFHNQTSSP SSFKKLNKIV
EHIPTKSLND FSHHFTHSSF KTLHVLLFNA DNDNDLAALR WILFDFFDRT SIRTKPKCLV
IIVTKNYLSQ SYTSFILHFG WTKKFLDLTI LNIVADGGES SDVVIKLFYD PFREIYTKEP
WNSNGNLFPN KLSNMYGFPL KVPIYHIPPY LSIIRNSDGS VRDLQGIHYK YLLVLSDFLN
FSITHYKEYE FSKSVSPLKT ELHRWLQDNE VNMLPIPMYL TIIGNLSSFP IEFVNLYPLV
PVQPSEHLVL PQSLSVDFFI VCAIYVLIMS IAYILKFDRT FWSSGNIEQL LLGFSISLHK
LRNSAERIFF ISVVLVSCIY TNNAFQELLN IKVITESKSF DSFEKISNSG LDVYVEYPAF
NNIFPYYDVH AQKIKSRATK IQNMTFCFDK MLEKNDGCIC LASGRIWEYL FKNAKNYDSK
RTKLAEFNIP FTYLAFVYEK ASPFVGRFDQ ILYRVLQSGI NRVWYSNEIT VRSFCGSLSS
LKASDLGSIV IKESLARANL KPTDVSEVIM GQGLTAGQGQ NPARQASIQA GLPITVPAYL
VSMLCGSGLK SIMNGYQAIK SGESEVIVAG GQESMSKAPH AIHLRDGVKM GDATMVDTML
VDGLTDVFHN IHMGVTAENL AKKYAISREE QDEFAARSQN KAEIAMTKGY FDKEIIPVPV
TIRRKTTIVS KDEFPKPGTT AKDLAGLKPV FVKDGTVTPG NASGINDGAA AVVLMSSETA
TKKGLKPMAR IVAMTVVGLE PDIMGYGPVP AVELLLKKAQ WKKEEVDLFE LNEAFAAQSI
ACERNLGVDP EKVNICGGAI ALGHPIGASG ARIVVTLLYL LERTGGKKGV ASLCIGGGMG
IAIAVERL
//