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 27-MAR-2024, entry version 103.
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; 7955-ENSDARP00000002180; -.
DR PeptideAtlas; A3QK15; -.
DR GeneID; 393984; -.
DR KEGG; dre:393984; -.
DR AGR; ZFIN:ZDB-GENE-040426-903; -.
DR CTD; 65985; -.
DR ZFIN; ZDB-GENE-040426-903; aacs.
DR eggNOG; KOG1175; Eukaryota.
DR HOGENOM; CLU_000022_3_3_1; -.
DR InParanoid; A3QK15; -.
DR OMA; MPNTWQT; -.
DR OrthoDB; 45466at2759; -.
DR PhylomeDB; A3QK15; -.
DR TreeFam; TF354241; -.
DR Reactome; R-DRE-77111; Synthesis of Ketone Bodies.
DR PRO; PR:A3QK15; -.
DR Proteomes; UP000000437; Chromosome 5.
DR Bgee; ENSDARG00000012468; Expressed in zone of skin and 30 other cell types or tissues.
DR ExpressionAtlas; A3QK15; baseline.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 CDD; cd05943; AACS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR NCBIfam; TIGR01217; ac_ac_CoA_syn; 1.
DR PANTHER; PTHR42921; ACETOACETYL-COA SYNTHETASE; 1.
DR PANTHER; PTHR42921:SF1; ACETOACETYL-COA SYNTHETASE; 1.
DR Pfam; PF16177; ACAS_N; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 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
//
