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Database: UniProt
Entry: A0A232FA77_9HYME
LinkDB: A0A232FA77_9HYME
Original site: A0A232FA77_9HYME 
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
//
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