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Database: UniProt
Entry: A0A194PSL1_PAPXU
LinkDB: A0A194PSL1_PAPXU
Original site: A0A194PSL1_PAPXU 
ID   A0A194PSL1_PAPXU        Unreviewed;       514 AA.
AC   A0A194PSL1;
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=RR46_06561 {ECO:0000313|EMBL:KPI94110.1};
OS   Papilio xuthus (Asian swallowtail butterfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC   Papilionidae; Papilioninae; Papilio.
OX   NCBI_TaxID=66420 {ECO:0000313|EMBL:KPI94110.1, ECO:0000313|Proteomes:UP000053268};
RN   [1] {ECO:0000313|EMBL:KPI94110.1, ECO:0000313|Proteomes:UP000053268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ya'a_city_454_Px {ECO:0000313|EMBL:KPI94110.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KPI94110.1};
RX   PubMed=26354079; DOI=10.1038/ncomms9212;
RA   Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA   Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA   Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA   Wang W.;
RT   "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL   Nat. Commun. 6:8212-8212(2015).
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; KQ459600; KPI94110.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A194PSL1; -.
DR   STRING; 66420.A0A194PSL1; -.
DR   Proteomes; UP000053268; 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:UP000053268};
KW   Transferase {ECO:0000256|RuleBase:RU003557, ECO:0000313|EMBL:KPI94110.1}.
FT   DOMAIN          36..293
FT                   /note="Thiolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00108"
FT   DOMAIN          302..421
FT                   /note="Thiolase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02803"
SQ   SEQUENCE   514 AA;  55590 MW;  39C92C69542E3B91 CRC64;
     MLLFKGTNLI TFKICIGGTI LKTMSRSLSN VTLNEVVIAS AVRTPMGSFR GSLASLSASE
     LGAVAVKAAI ERAGIPKEEV KEVYIGNVCS ANLGQAPARQ AVIFAGLPKS TICTTVNKVC
     ASGMKSIMLA AQGLQTGAQD VMLAGGMESM SNVPFYLKRG ETTYGGLQLV DGIVFDGLTD
     VYNKFHMGNC AENTAKKLEI SRKDQDDYAI SSYKRSAAAY EQKAFADELV PVPVPQKRGA
     PPVIFEEDEE YKRVNFEKFT KLSTVFQKEN GTVTAGNAST LNDGAAALVL MTADAAKRLN
     VTPIAKVVGF ADGECDPIDF PIAPAVAIPK LLEKTGVNKD DVALWEINEA FSVVAVANQK
     LLGLDPAKIN VHGGAVSLGH PIGMSGARIV VHLCHALKKG EKGVASICNG GGGASSIMIE
     KLPEAIKRPP TLTFYTKDPC PLCDIALEDL EPFRNRVKVE KVYITEKENL RWLRLYRNDI
     PVIFLNGKFL CMHKLNKDLL ERRLQLIENE YEMK
//
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