ID A0A3Q2WNL6_HAPBU Unreviewed; 676 AA.
AC A0A3Q2WNL6;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000027561.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000027561.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 RefSeq; XP_005924578.1; XM_005924516.2.
DR AlphaFoldDB; A0A3Q2WNL6; -.
DR STRING; 8153.ENSHBUP00000027561; -.
DR Ensembl; ENSHBUT00000000485.1; ENSHBUP00000027561.1; ENSHBUG00000010853.1.
DR GeneID; 102301425; -.
DR CTD; 65985; -.
DR GeneTree; ENSGT00940000156044; -.
DR OMA; MPNTWQT; -.
DR OrthoDB; 45466at2759; -.
DR Proteomes; UP000264840; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT DOMAIN 49..106
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 113..490
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 676 AA; 75222 MW; 80BC115FAB8D1DB3 CRC64;
MSKDTEGKSE KIMDMESKVL WYPDSKRNTQ MDKFRIQVNQ DYGLNLANYS DLYQWSVDSY
PEFWGEIWRF CGVVSSKPYE EVVDVSKRIS DVPEWFKGAR LNYAENLLKH ADHDKVALYA
AKEANEEIVK VTFGELRRDV ALFAAAMRKM GVQTGDRVVG YLPNGIHAVE AMLAAASIGA
IWSSTSVDFG VNGVLDRFSQ IQPKLIFSVA AVVYNGKTHD HMEKLISVVK GLPDLQKVIV
IPYARTKHET DLSKIPNSVF MDDFLASGRG EGDQFPQLEF EQLPFNHPLF IMYSSGTTGA
PKCMVHSAGG SLIQHLKEHI LHGNMTSSDV IIYYTTTGWM MWNWLVSALA VGASVVLYDG
SPLMPTPNVL WNLTDQLGIT IFGTGAKWLS VLQERNLTPS ETHNLQSLHT ILSTGSPLKP
QIYDYVYRCI KSTVLLGSIS GGTDIVSCFM GQNPTVPVYR GEIQSRNLGM AVEAWSPDGK
PVWGESGELV CLKPIPCQPT HFWNDENQSK YHKAYFSTYP GVWAHGDYCK INPKTGGIVM
LGRSDGTLNP NGVRFGSSEI YNIVEAFEEV SDSLCVPQYN ADGEERVILF LKMAPGKPFS
PELVAKIKGA IRKALSARHV PALLLETRDI PYTISGKKVE VAVKQVIAGR EVTQRGAFSN
PDSLDLYKNI PELQNY
//