ID   AACS_CHICK              Reviewed;         667 AA.
AC   Q5ZLG0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Acetoacetyl-CoA synthetase;
DE            EC=6.2.1.16 {ECO:0000250|UniProtKB:Q9JMI1};
GN   Name=AACS; ORFNames=RCJMB04_6g9;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ719774; CAG31433.1; -; mRNA.
DR   RefSeq; NP_001006184.1; NM_001006184.1.
DR   AlphaFoldDB; Q5ZLG0; -.
DR   SMR; Q5ZLG0; -.
DR   STRING; 9031.ENSGALP00000004568; -.
DR   PaxDb; Q5ZLG0; -.
DR   PRIDE; Q5ZLG0; -.
DR   GeneID; 416811; -.
DR   KEGG; gga:416811; -.
DR   CTD; 65985; -.
DR   VEuPathDB; HostDB:geneid_416811; -.
DR   eggNOG; KOG1175; Eukaryota.
DR   HOGENOM; CLU_1418071_0_0_1; -.
DR   InParanoid; Q5ZLG0; -.
DR   OrthoDB; 899666at2759; -.
DR   PhylomeDB; Q5ZLG0; -.
DR   PRO; PR:Q5ZLG0; -.
DR   Proteomes; UP000000539; Unplaced.
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   ATP-binding; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..667
FT                   /note="Acetoacetyl-CoA synthetase"
FT                   /id="PRO_0000315788"
SQ   SEQUENCE   667 AA;  74370 MW;  17B6EE7757E85366 CRC64;
     MSREPEIMES QVMWEPDSKR NTHMDRFRAA VAGSCGLRLA NYNDLYQWSV ESFADFWAEF
     WKYSNIVCSR LYDEVVDTSK SIADVPEWFK GSRLNYAENL LKHKDNDKIA LYAAKEGKEE
     ILKVTFEELR QAVALYAAAM RKMGVKIGDR VVGYLPNSIH AVEAMLAAAS IGAIWSSTSP
     DFGINGVLDR FSQIQPKLIF SVEAVVYNGK EHNHLEKLLS VVKGLPDLKK VVVIPYVSSR
     ETIDISKIPN SVFLEDFLAT GKGDQAPQLE FEQLPFSHPL FIMYSSGTTG APKCMVHSAG
     GTLIQHLKEH ILHGNMSSND IIMYYTTTGW MMWNWLVTAL ATGASVVLYD GSPLVPSPNV
     LWDLIDRLGI TILGTGAKWL AVLEEKNLKP CETHNLQTLH TILSTGSPLK SQSYEYVYKH
     IKSSVLLGSI SGGTDIISCF MGQNVTIPVY KGEIQARNLG MAVEAWNDEG KPVWGESGEL
     VCTKPIPCQP THFWNDENGS KYRKAYFSKF PGVWAHGDYC KINPKTGGIV MLGRSDGTLN
     PNGVRFGSSE IYNIVEAFEE VSDSLCVPQY NKDGEERVIL FLKMASNHAF SEDLVKRIRD
     AIRVALSARH VPSLILETKG IPYTINGKKV EVAVKQIIAG KEVEQRGAFS NPETLDLYQN
     IPELQNF