ID   AACS_MACFA              Reviewed;         672 AA.
AC   Q9N0E1; Q4R4U8; Q9BE28;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Acetoacetyl-CoA synthetase;
DE            EC=6.2.1.16 {ECO:0000250|UniProtKB:Q9JMI1};
GN   Name=AACS; ORFNames=QccE-10783, QccE-14415, QflA-13650;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Frontal cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AB045989; BAB01571.1; -; mRNA.
DR   EMBL; AB060214; BAB41151.1; -; mRNA.
DR   EMBL; AB169796; BAE01877.1; -; mRNA.
DR   RefSeq; NP_001270939.1; NM_001284010.1.
DR   AlphaFoldDB; Q9N0E1; -.
DR   SMR; Q9N0E1; -.
DR   STRING; 9541.XP_005572665.1; -.
DR   Ensembl; ENSMFAT00000063482; ENSMFAP00000013533; ENSMFAG00000028497.
DR   GeneID; 102145658; -.
DR   CTD; 65985; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   GeneTree; ENSGT00940000156044; -.
DR   OrthoDB; 899666at2759; -.
DR   Proteomes; UP000233100; Chromosome 11.
DR   Bgee; ENSMFAG00000028497; Expressed in frontal cortex and 13 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
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   ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..672
FT                   /note="Acetoacetyl-CoA synthetase"
FT                   /id="PRO_0000315785"
FT   CONFLICT        7
FT                   /note="P -> A (in Ref. 1; BAB41151)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110
FT                   /note="E -> D (in Ref. 2; BAE01877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="A -> V (in Ref. 2; BAE01877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="M -> V (in Ref. 2; BAE01877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        400
FT                   /note="S -> G (in Ref. 1; BAB41151 and 2; BAE01877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        505
FT                   /note="S -> N (in Ref. 1; BAB41151 and 2; BAE01877)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        578
FT                   /note="F -> Y (in Ref. 2; BAE01877)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   672 AA;  75046 MW;  DF31672A8E204528 CRC64;
     MSKEERPGRE EILECQVMWE PDSKKNTQMD RFRAAVGAAC GLALENYDDL YRWSVESYSD
     FWAEFWKFSG IVFSRAYDEV VDTSKGIADV PEWFKGSRLN YAENLLRHKE NDRVALYVAR
     EGKEEIVKVT FEELRQEVAL FAAAMRKMGV KKGDRVVGYL PNSEHAVEAM LAAASIGAIW
     SSTSPDFGVN GVLDRFSQIQ PKLIFSVEAV VYNGKEHSHM EKLQQVVKGL PDLKKVVVIP
     YVSSREKIDL SKIPNSVFLD DFLATGTSEQ APQLEFEQLP FSHPLFIMFS SGTTGAPKCM
     VHSAGGTLIQ HLKEHLLHGN MTSSDILLCY TTAGWMMWNW MVSILATGAA MVLYDGSPLV
     PTPNVLWDLV DRIGITVLVT GAKWLSVLEE KAMKPVETHS LQMLHTILST GSPLKAQSYE
     YVYRCIKSSI LLGSISGGTD IISCFMGHNF SLPVYKGEIQ ARNLGMAVEA WNEEGKAVWG
     ESGELVCTKP IPCQPTHFWN DENGSKYRKA YFSKFPGIWA HGDYCRINPK TGGIIMLGRS
     DGTLNPNGVR FGSSEIYNIV ESFEEVEDSL CVPQYNKFRE ERVILFLKMA SGHAFQPDLV
     KRIRDAIRVG LSARHVPSLI LETKGIPYTL NGKKVEVAVK QIIAGKAVEQ GGAFSNPETL
     DLYRDIPELQ GF