ID K7F639_PELSI Unreviewed; 631 AA.
AC K7F639;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
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};
GN Name=AACS {ECO:0000313|Ensembl:ENSPSIP00000003499.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000003499.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000003499.1}
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 EMBL; AGCU01163827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01163835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7F639; -.
DR STRING; 13735.ENSPSIP00000003499; -.
DR Ensembl; ENSPSIT00000003516.1; ENSPSIP00000003499.1; ENSPSIG00000003310.1.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000156044; -.
DR HOGENOM; CLU_000022_3_3_1; -.
DR OMA; MPNTWQT; -.
DR TreeFam; TF354241; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:UP000007267}.
FT DOMAIN 6..63
FT /note="Acetyl-coenzyme A synthetase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16177"
FT DOMAIN 69..449
FT /note="AMP-dependent synthetase/ligase"
FT /evidence="ECO:0000259|Pfam:PF00501"
SQ SEQUENCE 631 AA; 70525 MW; C0645DA75E498974 CRC64;
LLLVNYNELY QWSVESYSDF WAEFWKFSGI VYSRLYDEVV DPSKGIADVP EWFKGSRLNY
AENLLKHKEK EKIALYAAKE GKEEILKVTF EELRQDVALY ASAMRKMGVK IGDRVVGYLP
NSIHAVEAML AAASIGAIWS STSPDFGING VLDRFSQIQP KLIFSVEAVI YNGKEHNHME
KLHNVVKGLP DLRKVVVIPY VSSRETIDIS KIPNSVFLED FLATGKGEQA PQLELEQLPF
SHPLFIMYSS GTTGAPKCMV HSAGGTLIQH LKEHILHGNM TSNDIIMYYT TTGWMMWNWL
VSALSTGASV VLYDGSPLVP SPNVLWDLVD RLGITILGTG AKWLAVLEEK NLKPCDTHNL
HTLHTILSTG SPLKSQSYEY VYKHIKSSVL LGSISGGTDI ISCFMGQNVT IPVYKGEIQA
RNLGMAVEAW NDEGKPVWGE SGELVCTKPM PCQPTHFWND ENGNKYRKAY FSKFPGVWAH
GDYCKINPET GGIVMLGRSD GTLNPNGVRF GSSEIYNIVE AFEEVSDSLC VPQYNKEGEE
RVILFLKMAS DQVFTQHLVK RIRDAIRIAL SARHVPSIIL ETKGIPYTIN GKKVEVAVKQ
IIAGKEVDQQ GSFSNPETLD LYQNIPELQN F
//
