ID   AACS_DANRE              Reviewed;         673 AA.
AC   A3QK15; Q7ZU87;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acetoacetyl-CoA synthetase;
DE            EC=6.2.1.16 {ECO:0000250|UniProtKB:Q9JMI1};
GN   Name=aacs; ORFNames=si:dkey-215k6.2, zgc:56105;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=SJD;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol (By
CC       similarity). Ketone body-utilizing enzyme, responsible for the
CC       synthesis of cholesterol and fatty acids (By similarity).
CC       {ECO:0000250|UniProtKB:Q9D2R0, ECO:0000250|UniProtKB:Q9JMI1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetoacetate + ATP + CoA = acetoacetyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:16117, ChEBI:CHEBI:13705,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57286,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; EC=6.2.1.16;
CC         Evidence={ECO:0000250|UniProtKB:Q9JMI1};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16118;
CC         Evidence={ECO:0000250|UniProtKB:Q9JMI1};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q9JMI1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A3QK15-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A3QK15-2; Sequence=VSP_030703;
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CR759959; CAM56650.1; -; Genomic_DNA.
DR   EMBL; BC050501; AAH50501.1; -; mRNA.
DR   RefSeq; NP_957303.1; NM_201009.1.
DR   RefSeq; XP_005165133.1; XM_005165076.3. [A3QK15-1]
DR   AlphaFoldDB; A3QK15; -.
DR   SMR; A3QK15; -.
DR   STRING; 7955.ENSDARP00000002180; -.
DR   PaxDb; A3QK15; -.
DR   PeptideAtlas; A3QK15; -.
DR   Ensembl; ENSDART00000010101; ENSDARP00000002180; ENSDARG00000012468. [A3QK15-1]
DR   Ensembl; ENSDART00000099434; ENSDARP00000090207; ENSDARG00000012468. [A3QK15-2]
DR   GeneID; 393984; -.
DR   KEGG; dre:393984; -.
DR   CTD; 65985; -.
DR   ZFIN; ZDB-GENE-040426-903; aacs.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000156044; -.
DR   HOGENOM; CLU_000022_3_3_1; -.
DR   InParanoid; A3QK15; -.
DR   OMA; WYSSTGW; -.
DR   OrthoDB; 899666at2759; -.
DR   PhylomeDB; A3QK15; -.
DR   TreeFam; TF354241; -.
DR   Reactome; R-DRE-77111; Synthesis of Ketone Bodies.
DR   PRO; PR:A3QK15; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000012468; Expressed in zone of skin and 30 other tissues.
DR   ExpressionAtlas; A3QK15; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IBA:GO_Central.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR005914; Acac_CoA_synth.
DR   InterPro; IPR032387; ACAS_N.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   Pfam; PF16177; ACAS_N; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   TIGRFAMs; TIGR01217; ac_ac_CoA_syn; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Fatty acid metabolism;
KW   Ligase; Lipid metabolism; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..673
FT                   /note="Acetoacetyl-CoA synthetase"
FT                   /id="PRO_0000315789"
FT   VAR_SEQ         346..359
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_030703"
FT   CONFLICT        164
FT                   /note="V -> I (in Ref. 2; AAH50501)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        431
FT                   /note="V -> M (in Ref. 2; AAH50501)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   673 AA;  74967 MW;  71CACCD9B2049782 CRC64;
     MSKDTEAKSE EIMESKVLWY PDSKRNTQTD RFRTLVNREF GLNLANYNDL YQWSVDSYPE
     FWAQVWKFCG ITCSKMYEEV VDVSKRISDV PEWFKGSRLN YAENLLKHKD QDKVALYAAS
     EAKEEIVKVT FGELRRDVAL FAAAMRKMGI KIGDRVVGYL PNGVHAVEAM LAAASIGAIW
     SSTSPDFGVN GVLDRISQIQ PKLIFSVAAV VYNGKQHDHM EKLQNVVKGL PDLKKVVVIP
     YVRSRQETDL SKIPNSVFLE DFLATGKEGD QDPQLEFEQL PFSHPLFIMY SSGTTGAPKC
     MVHSAGGTLI QHLKEHILHG NMTFNDVIIY YTTTGWMMWN WLISSLAVGA SVVLYDGSPL
     VPSANVLWDL VDRLGITIFG TGAKWLAVLE ERDQKPASTH SLQTLHTLLS TGSPLKPQSY
     EYVYSCIKNN VLLGSISGGT DIISCFMGQN MTVPVYRGEI QARNLGMAVE SWSCEGKPVW
     GESGELVCLK PIPCQPTHFW NDENGSKYHK AYFSTFPGVW AHGDYCKINP KTGGVVMLGR
     SDGTLNPNGV RFGSSEIYNI VEAFDEVSDS LCVPQYNSDG EERVILFLKM GPNKSFSQEL
     VGKIRGAIRV ALSARHVPAL ILETKDIPYT ISGKKVEVAV KQVIAGKEVT QRGAFSNPDS
     LDLYKNLPEL QNF