ID A0A195ERW0_9HYME Unreviewed; 499 AA.
AC A0A195ERW0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=acetyl-CoA C-acetyltransferase {ECO:0000256|ARBA:ARBA00012705};
DE EC=2.3.1.9 {ECO:0000256|ARBA:ARBA00012705};
GN ORFNames=ALC56_14728 {ECO:0000313|EMBL:KYN30916.1};
OS Trachymyrmex septentrionalis.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN30916.1, ECO:0000313|Proteomes:UP000078541};
RN [1] {ECO:0000313|EMBL:KYN30916.1, ECO:0000313|Proteomes:UP000078541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN30916.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN30916.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex septentrionalis WGS genome.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; KQ981993; KYN30916.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195ERW0; -.
DR STRING; 34720.A0A195ERW0; -.
DR Proteomes; UP000078541; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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 Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR008554; Glutaredoxin-like.
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 InterPro; IPR036249; Thioredoxin-like_sf.
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; PF05768; Glrx-like; 1.
DR Pfam; PF02803; Thiolase_C; 1.
DR Pfam; PF00108; Thiolase_N; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KYN30916.1}.
FT DOMAIN 18..275
FT /note="Thiolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00108"
FT DOMAIN 283..403
FT /note="Thiolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02803"
SQ SEQUENCE 499 AA; 54058 MW; 27CC35F60805A850 CRC64;
MNFMSKRLYS SKVKLNDVVI VSAVRTPMGS FLGSLSSMSA TKLGAIAIQA AIERAGIAKE
QVKEIYMGNV CQAFLGQAPT RQAALFAGLP TSTICTTVNK VCASGMKSVM LASQSLQCGH
QEIVLAGGME SMSNVPYYLS RGETSYGGVK LEDGIVFDGL TDVYNKCHMG NCAENTAKKL
NITRQQQDEY AISSYKRSAA AYDNNVFKDE LVSVNVPQKK GKPDVSFTAD EEYKRVNFEK
FSKLNTVFQK ENGTVTAGNA STLNDGAAAL ILMTSDVAQK LNLKPLARIV AFQDAATDPI
DFPIAPAFAV PSLLQNAGVN KNDIALWEIN EAFSAVVVAN QKLLDIDPAK VNVHGGAVSL
GHPIGMSGAR IIVHLAHALK AGEKGVASIC NGGGGASSIL IEKLSHPISS PPKLTLYTKS
PCLLCDVLKN ELRLRFADRY QLEEVDIAAQ GNEQYFQLYK YDIPVLFLEG QYLCKHRLDA
DLLERRLDEL VSRKDKCTH
//
