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
//