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Database: UniProt
Entry: A0A3Q0R263_AMPCI
LinkDB: A0A3Q0R263_AMPCI
Original site: A0A3Q0R263_AMPCI 
ID   A0A3Q0R263_AMPCI        Unreviewed;       676 AA.
AC   A0A3Q0R263;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Acetoacetyl-CoA synthetase {ECO:0000256|ARBA:ARBA00015326, ECO:0000256|RuleBase:RU367019};
DE            EC=6.2.1.16 {ECO:0000256|ARBA:ARBA00012988, ECO:0000256|RuleBase:RU367019};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000004186.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000004186.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Converts acetoacetate to acetoacetyl-CoA in the cytosol.
CC       {ECO:0000256|RuleBase:RU367019}.
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:0000256|RuleBase:RU367019};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|RuleBase:RU367019}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432, ECO:0000256|RuleBase:RU367019}.
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DR   STRING; 61819.ENSACIP00000004186; -.
DR   Ensembl; ENSACIT00000004322.1; ENSACIP00000004186.1; ENSACIG00000003283.1.
DR   GeneTree; ENSGT00940000156044; -.
DR   OMA; MPNTWQT; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030729; F:acetoacetate-CoA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU367019};
KW   Cytoplasm {ECO:0000256|RuleBase:RU367019};
KW   Fatty acid metabolism {ECO:0000256|RuleBase:RU367019};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU367019};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU367019};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU367019}.
FT   DOMAIN          49..106
FT                   /note="Acetyl-coenzyme A synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16177"
FT   DOMAIN          113..491
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
SQ   SEQUENCE   676 AA;  75299 MW;  93DDBF38755F718C CRC64;
     MSKDTEGKSE KIMDMESKVL WYPDSKRNTQ MDKFRIQVNE DYGLNLANYS DLYQWSVDSY
     PEFWTEVWRF CGIVSSKPYE EVVDVSKRIS DVPEWFKGAR LNXAENLLKH ADHDKVALYA
     AKEANEEIVK VTFGELRRDV ALFAAAMRRM GVQTGDRVVG YLPNGIHAVE AMLAAASIGA
     IWSSTSVDFG VNGVLDRFSQ IQPKLIFSVA AVVYNGKTHD HMEKLTSVVK GLPDLQKVVV
     IPYARARHET DLSKIPNSVF IDDFLASGRG EGDQFPQLEF EQLPFNHPLF IMYSSGTTGA
     PKCMVHSAGG TLIQHLKEHI LHGNMTSSDV IIYYTTTGWM MWNWLVSSLA VGASVVLYDG
     SPLMPTPNVL WNLTDQLGIT IFGTGAKWLA VLQERNLKPS ETHNLQSLHT ILSTGSPLKP
     QSYDYVYRCI KSTVMLGSIS GGTDIVSCFM GQNPTVPVYR GEIQSRNLGM AVEAWNPDGK
     PVWGESGELV CLKPIPCQPT HFWNDENGSK YHKAYFSTFP GVWAHGDYCK INPKTRGIVM
     LGRSDGTLNP NGVRFGSSEI YNIVEAFEEV SDSLCVPQYN ADGEERVILF LKMAPGKPFC
     PELVAKIKGA IRKALSARHI PALLLETRDI PYTISGKKVE VAVKQVIAGR EVTQRGAFSN
     PDSLDLYKNI PELQNY
//
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